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UniProtKB/Swiss-Prot entry P08519


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name APOA_HUMAN
Primary accession number P08519
Secondary accession number Q5VTD7
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on August 1, 1988 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 99)
Name and origin of the protein
Protein name Apolipoprotein(a) [Precursor]
Synonyms Apo(a)
Lp(a)
EC 3.4.21.-
Gene name
Name: LPA
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND POLYMORPHISM.
DOI=10.1038/330132a0; PubMed=3670400 [NCBI, ExPASy, EBI, Israel, Japan]
McLean J.W., Tomlison J.E., Kuang W.-J., Eaton D.L., Chen E.Y., Fless G.M., Scanu A.M., Lawn R.M.;
"cDNA sequence of human apolipoprotein(a) is homologous to plasminogen.";
Nature 330:132-137(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[3]
FUNCTION AS A SERINE PROTEASE.
PubMed=2531657 [NCBI, ExPASy, EBI, Israel, Japan]
Salonen E.-M., Jauhiainen M., Zardi L., Vaheri A., Ehnholm C.;
"Lipoprotein(a) binds to fibronectin and has serine proteinase activity capable of cleaving it.";
EMBO J. 8:4035-4040(1989).
[4]
REVIEW.
DOI=10.1126/science.2530631; PubMed=2530631 [NCBI, ExPASy, EBI, Israel, Japan]
Utermann G.;
"The mysteries of lipoprotein(a).";
Science 246:904-910(1989).
[5]
STRUCTURE OF N-LINKED AND O-LINKED CARBOHYDRATES, AND MASS SPECTROMETRY.
DOI=10.1074/jbc.M102150200; PubMed=11294842 [NCBI, ExPASy, EBI, Israel, Japan]
Garner B., Merry A.H., Royle L., Harvey D.J., Rudd P.M., Thillet J.;
"Structural elucidation of the N- and O-glycans of human apolipoprotein(a): role of o-glycans in conferring protease resistance.";
J. Biol. Chem. 276:22200-22208(2001).
[6]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 4121-4208.
DOI=10.1006/jmbi.1996.0122; PubMed=8642595 [NCBI, ExPASy, EBI, Israel, Japan]
Mikol V., Lograsso P.V., Boettcher B.R.;
"Crystal structures of apolipoprotein(a) kringle IV37 free and complexed with 6-aminohexanoic acid and with p-aminomethylbenzoic acid: existence of novel and expected binding modes.";
J. Mol. Biol. 256:751-761(1996).
[7]
VARIANT ARG-4193.
DOI=10.1016/0925-4439(94)90104-X; PubMed=7918682 [NCBI, ExPASy, EBI, Israel, Japan]
Scanu A.M., Pfaffinger D., Lee J.C., Hinman J.;
"A single point mutation (Trp72-->Arg) in human apo(a) kringle 4-37 associated with a lysine binding defect in Lp(a).";
Biochim. Biophys. Acta 1227:41-45(1994).
Comments
  • FUNCTION: Apo(a) is the main constituent of lipoprotein(a) (Lp(a)). It has serine proteinase activity and is able of autoproteolysis. Inhibits tissue-type plasminogen activator 1. Lp(a) may be a ligand for megalin/Gp 330.
  • SUBUNIT: Disulfide-linked to apo-B100. Binds to fibronectin and decorin.
  • PTM: N- and O-glycosylated. The N-glycans are complex biantennary structures present in either a mono- or disialylated state. The O-glycans are mostly (80%) represented by the monosialylated core type I structure, NeuNAcalpha2-3Galbeta1-3GalNAc, with smaller amounts of disialylated and non-sialylated O-glycans also detected.
  • POLYMORPHISM: The genome version encodes a variant that contains 16 Kringle domains and that lack residues 533 to 3040.
  • DISEASE: Elevated plasma concentrations of apo(a) and its naturally occurring proteolytic fragments are correlated with atherosclerosis. Homology with plasminogen kringles IV and V is thought to underlie the atherogenicity of the protein, because the fragments are competing with plasminogen for fibrin(ogen) binding.
  • MISCELLANEOUS: Apo(a) is known to be proteolytically cleaved, leading to the formation of the so-called mini-Lp(a). Apo(a) fragments accumulate in atherosclerotic lesions, where they may promote thrombogenesis. O-glycosylation may limit the extent of proteolytic fragmentation.
  • SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily [view classification].
  • SIMILARITY: Contains 38 kringle domains.
  • SIMILARITY: Contains 1 peptidase S1 domain [view classification].
  • WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and polymorphism database; URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=APOA";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X06290; CAA29618.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL596089; CAH73590.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL109933; CAH73590.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL109933; CAI22905.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL596089; CAI22905.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00029168; -.
PIR S00657; S00657.
UniGene Hs.520120
3D structure databases
PDB
1I71; X-ray; 1.45 A; A=3781-3863.[ExPASy / RCSB / EBI]
1JFN; NMR; -; A=3665-3770.[ExPASy / RCSB / EBI]
1KIV; X-ray; 2.10 A; A=4124-4201.[ExPASy / RCSB / EBI]
2FEB; NMR; -; A=3885-3980.[ExPASy / RCSB / EBI]
3KIV; X-ray; 1.80 A; A=4123-4201.[ExPASy / RCSB / EBI]
4KIV; X-ray; 2.20 A; A=4123-4201.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1I71; -.
1JFN; -.
1KIV; -.
2FEB; -.
3KIV; -.
4KIV; -.
SMR P08519; 4312-4548.
ModBase P08519.
Protein family/group databases
MEROPS S01.999; -.
PTM databases
GlycoSuiteDB P08519; -.
Enzyme and pathway databases
Pathway_Interaction_DB amb2_neutrophils_pathway; amb2 Integrin signaling.
Organism-specific databases
GeneCards GC06M160872; -.
H-InvDB HIX0042093; -.
HIX0057735; -.
HGNC HGNC:6667; LPA.
GenAtlas LPA.
MIM 152200; gene+phenotype. [NCBI / EBI]
PharmGKB PA30432; -.
Gene expression databases
ArrayExpress P08519; -.
Bgee P08519; -.
CleanEx HS_LPA; -.
GermOnline ENSG00000198670; Homo sapiens.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (non-traceable author statement from UniProtKB).
GO:0034185; Molecular function: apolipoprotein binding (inferred from physical interaction from UniProtKB).
GO:0004866; Molecular function: endopeptidase inhibitor activity (traceable author statement from ProtInc).
GO:0004252; Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0008015; Biological process: blood circulation (traceable author statement from ProtInc).
GO:0006629; Biological process: lipid metabolic process (non-traceable author statement from ProtInc).
GO:0006869; Biological process: lipid transport (inferred from electronic annotation from UniProtKB-KW).
GO:0006508; Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000001; Kringle.
IPR018056; Kringle_CS.
IPR018059; Kringle_sub.
IPR018114; Peptidase_S1/S6_AS.
IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
Graphical view of domain structure.
Gene3D G3DSA:2.40.20.10; Kringle; 38.
Pfam PF00051; Kringle; 38.
PF00089; Trypsin; 1.
Pfam graphical view of domain structure.
PRINTS PR00722; CHYMOTRYPSIN.
PR00018; KRINGLE.
ProDom PD000395; Kringle; 38.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00130; KR; 38.
SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.
PROSITE PS00021; KRINGLE_1; 38.
PS50070; KRINGLE_2; 38.
PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P08519; -.
Genome annotation databases
Ensembl ENSG00000198670; Homo sapiens. [Contig view]
Phylogenomic databases
HOGENOM P08519; -.
HOVERGEN P08519; -.
Other
DrugBank DB00513; Aminocaproic Acid.
SOURCE LPA; Homo sapiens.
ProtoNet P08519.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Atherosclerosis; Disulfide bond; Glycoprotein; Hydrolase; Kringle; Lipid transport; Polymorphism; Protease; Repeat; Serine protease; Signal; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
SIGNAL   1     19  19      
CHAIN   20   4548  4529     Apolipoprotein(a). PRO_0000028097
DOMAIN   20    130  111     Kringle 1. 
DOMAIN   131    244  114     Kringle 2. 
DOMAIN   245    358  114     Kringle 3. 
DOMAIN   359    472  114     Kringle 4. 
DOMAIN   473    586  114     Kringle 5. 
DOMAIN   587    700  114     Kringle 6. 
DOMAIN   701    814  114     Kringle 7. 
DOMAIN   815    928  114     Kringle 8. 
DOMAIN   929   1042  114     Kringle 9. 
DOMAIN   1043   1156  114     Kringle 10. 
DOMAIN   1157   1270  114     Kringle 11. 
DOMAIN   1271   1384  114     Kringle 12. 
DOMAIN   1385   1498  114     Kringle 13. 
DOMAIN   1499   1612  114     Kringle 14. 
DOMAIN   1613   1726  114     Kringle 15. 
DOMAIN   1727   1840  114     Kringle 16. 
DOMAIN   1841   1954  114     Kringle 17. 
DOMAIN   1955   2068  114     Kringle 18. 
DOMAIN   2069   2182  114     Kringle 19. 
DOMAIN   2183   2296  114     Kringle 20. 
DOMAIN   2297   2410  114     Kringle 21. 
DOMAIN   2411   2524  114     Kringle 22. 
DOMAIN   2525   2638  114     Kringle 23. 
DOMAIN   2639   2752  114     Kringle 24. 
DOMAIN   2753   2866  114     Kringle 25. 
DOMAIN   2867   2980  114     Kringle 26. 
DOMAIN   2981   3094  114     Kringle 27. 
DOMAIN   3095   3208  114     Kringle 28. 
DOMAIN   3209   3322  114     Kringle 29. 
DOMAIN   3323   3436  114     Kringle 30. 
DOMAIN   3437   3550  114     Kringle 31. 
DOMAIN   3551   3664  114     Kringle 32. 
DOMAIN   3665   3770  106     Kringle 33. 
DOMAIN   3771   3884  114     Kringle 34. 
DOMAIN   3885   3998  114     Kringle 35. 
DOMAIN   3999   4112  114     Kringle 36. 
DOMAIN   4113   4226  114     Kringle 37. 
DOMAIN   4227   4327  101     Kringle 38. 
DOMAIN   4328   4546  219     Peptidase S1. 
ACT_SITE   4369   4369        Charge relay system. 
ACT_SITE   4412   4412        Charge relay system. 
ACT_SITE   4498   4498        Charge relay system. 
CARBOHYD   61     61        N-linked (GlcNAc...) (Potential). 
CARBOHYD   101    101        N-linked (GlcNAc...) (Potential). 
CARBOHYD   215    215        N-linked (GlcNAc...) (Potential). 
CARBOHYD   329    329        N-linked (GlcNAc...) (Potential). 
CARBOHYD   443    443        N-linked (GlcNAc...) (Potential). 
CARBOHYD   557    557        N-linked (GlcNAc...) (Potential). 
CARBOHYD   671    671        N-linked (GlcNAc...) (Potential). 
CARBOHYD   785    785        N-linked (GlcNAc...) (Potential). 
CARBOHYD   899    899        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1013   1013        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1127   1127        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1241   1241        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1355   1355        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1469   1469        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1583   1583        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1697   1697        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1811   1811        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1925   1925        N-linked (GlcNAc...) (Potential). 
CARBOHYD   2039   2039        N-linked (GlcNAc...) (Potential). 
CARBOHYD   2153   2153        N-linked (GlcNAc...) (Potential). 
CARBOHYD   2267   2267        N-linked (GlcNAc...) (Potential). 
CARBOHYD   2381   2381        N-linked (GlcNAc...) (Potential). 
CARBOHYD   2495   2495        N-linked (GlcNAc...) (Potential). 
CARBOHYD   2609   2609        N-linked (GlcNAc...) (Potential). 
CARBOHYD   2723   2723        N-linked (GlcNAc...) (Potential). 
CARBOHYD   2837   2837        N-linked (GlcNAc...) (Potential). 
CARBOHYD   2951   2951        N-linked (GlcNAc...) (Potential). 
CARBOHYD   3065   3065        N-linked (GlcNAc...) (Potential). 
CARBOHYD   3179   3179        N-linked (GlcNAc...) (Potential). 
CARBOHYD   3293   3293        N-linked (GlcNAc...) (Potential). 
CARBOHYD   3407   3407        N-linked (GlcNAc...) (Potential). 
CARBOHYD   3521   3521        N-linked (GlcNAc...) (Potential). 
CARBOHYD   3635   3635        N-linked (GlcNAc...) (Potential). 
CARBOHYD   3749   3749        N-linked (GlcNAc...) (Potential). 
CARBOHYD   3855   3855        N-linked (GlcNAc...) (Potential). 
CARBOHYD   3889   3889        N-linked (GlcNAc...) (Potential). 
CARBOHYD   3969   3969        N-linked (GlcNAc...) (Potential). 
CARBOHYD   4083   4083        N-linked (GlcNAc...) (Potential). 
CARBOHYD   4197   4197        N-linked (GlcNAc...) (Potential). 
DISULFID   28    105        By similarity. 
DISULFID   49     88        By similarity. 
DISULFID   77    100        By similarity. 
DISULFID   142    219        By similarity. 
DISULFID   163    202        By similarity. 
DISULFID   191    214        By similarity. 
DISULFID   256    333        By similarity. 
DISULFID   277    316        By similarity. 
DISULFID   305    328        By similarity. 
DISULFID   370    447        By similarity. 
DISULFID   391    430        By similarity. 
DISULFID   419    442        By similarity. 
DISULFID   484    561        By similarity. 
DISULFID   505    544        By similarity. 
DISULFID   533    556        By similarity. 
DISULFID   598    675        By similarity. 
DISULFID   619    658        By similarity. 
DISULFID   647    670        By similarity. 
DISULFID   712    789        By similarity. 
DISULFID   733    772        By similarity. 
DISULFID   761    784        By similarity. 
DISULFID   826    903        By similarity. 
DISULFID   847    886        By similarity. 
DISULFID   875    898        By similarity. 
DISULFID   940   1017        By similarity. 
DISULFID   961   1000        By similarity. 
DISULFID   989   1012        By similarity. 
DISULFID   1054   1131        By similarity. 
DISULFID   1075   1114        By similarity. 
DISULFID   1103   1126        By similarity. 
DISULFID   1168   1245        By similarity. 
DISULFID   1189   1228        By similarity. 
DISULFID   1217   1240        By similarity. 
DISULFID   1282   1359        By similarity. 
DISULFID   1303   1342        By similarity. 
DISULFID   1331   1354        By similarity. 
DISULFID   1396   1473        By similarity. 
DISULFID   1417   1456        By similarity. 
DISULFID   1445   1468        By similarity. 
DISULFID   1510   1587        By similarity. 
DISULFID   1531   1570        By similarity. 
DISULFID   1559   1582        By similarity. 
DISULFID   1624   1701        By similarity. 
DISULFID   1645   1684        By similarity. 
DISULFID   1673   1696        By similarity. 
DISULFID   1738   1815        By similarity. 
DISULFID   1759   1798        By similarity. 
DISULFID   1787   1810        By similarity. 
DISULFID   1852   1929        By similarity. 
DISULFID   1873   1912        By similarity. 
DISULFID   1901   1924        By similarity. 
DISULFID   1966   2043        By similarity. 
DISULFID   1987   2026        By similarity. 
DISULFID   2015   2038        By similarity. 
DISULFID   2080   2157        By similarity. 
DISULFID   2101   2140        By similarity. 
DISULFID   2129   2152        By similarity. 
DISULFID   2194   2271        By similarity. 
DISULFID   2215   2254        By similarity. 
DISULFID   2243   2266        By similarity. 
DISULFID   2308   2385        By similarity. 
DISULFID   2329   2368        By similarity. 
DISULFID   2357   2380        By similarity. 
DISULFID   2422   2499        By similarity. 
DISULFID   2443   2482        By similarity. 
DISULFID   2471   2494        By similarity. 
DISULFID   2536   2613        By similarity. 
DISULFID   2557   2596        By similarity. 
DISULFID   2585   2608        By similarity. 
DISULFID   2650   2727        By similarity. 
DISULFID   2671   2710        By similarity. 
DISULFID   2699   2722        By similarity. 
DISULFID   2764   2841        By similarity. 
DISULFID   2785   2824        By similarity. 
DISULFID   2813   2836        By similarity. 
DISULFID   2878   2955        By similarity. 
DISULFID   2899   2938        By similarity. 
DISULFID   2927   2950        By similarity. 
DISULFID   2992   3069        By similarity. 
DISULFID   3013   3052        By similarity. 
DISULFID   3041   3064        By similarity. 
DISULFID   3106   3183        By similarity. 
DISULFID   3127   3166        By similarity. 
DISULFID   3155   3178        By similarity. 
DISULFID   3220   3297        By similarity. 
DISULFID   3241   3280        By similarity. 
DISULFID   3269   3292        By similarity. 
DISULFID   3334   3411        By similarity. 
DISULFID   3355   3394        By similarity. 
DISULFID   3383   3406        By similarity. 
DISULFID   3448   3525        By similarity. 
DISULFID   3469   3508        By similarity. 
DISULFID   3497   3520        By similarity. 
DISULFID   3562   3639        By similarity. 
DISULFID   3583   3622        By similarity. 
DISULFID   3611   3634        By similarity. 
DISULFID   3676   3753         
DISULFID   3697   3736         
DISULFID   3725   3748         
DISULFID   3782   3859         
DISULFID   3803   3842         
DISULFID   3831   3854         
DISULFID   3896   3973        By similarity. 
DISULFID   3917   3956        By similarity. 
DISULFID   3945   3968        By similarity. 
DISULFID   4010   4087        By similarity. 
DISULFID   4031   4070        By similarity. 
DISULFID   4059   4082        By similarity. 
DISULFID   4124   4201        By similarity. 
DISULFID   4145   4184        By similarity. 
DISULFID   4173   4196        By similarity. 
DISULFID   4228   4307        By similarity. 
DISULFID   4249   4290        By similarity. 
DISULFID   4278   4302        By similarity. 
DISULFID   4354   4370        By similarity. 
DISULFID   4446   4504        By similarity. 
DISULFID   4476   4483        By similarity. 
DISULFID   4494   4522        By similarity. 
VARIANT   3498   3498  1     R -> Q (in dbSNP:rs41259144 [NCBI]). VAR_047293 
VARIANT   3866   3866  1     L -> V (in dbSNP:rs7765803 [NCBI]). VAR_047294 
VARIANT   3880   3880  1     L -> V (in dbSNP:rs7765781 [NCBI]). VAR_047295 
VARIANT   3907   3907  1     T -> P (in dbSNP:rs41272110 [NCBI]). VAR_047296 
VARIANT   3929   3929  1     R -> Q (in dbSNP:rs41272112 [NCBI]). VAR_047297 
VARIANT   4106   4106  1     M -> T (in dbSNP:rs41264308 [NCBI]). VAR_047298 
VARIANT   4187   4187  1     M -> T (in dbSNP:rs1801693 [NCBI]). VAR_047299 
VARIANT   4193   4193  1     W -> R (loss of lysine-sepharose binding). VAR_006633 
VARIANT   4330   4330  1     G -> A (in dbSNP:rs41265936 [NCBI]). VAR_047300 
VARIANT   4399   4399  1     I -> M (in dbSNP:rs3798220 [NCBI]). VAR_047301 
VARIANT   4524   4524  1     R -> C (in dbSNP:rs3124784 [NCBI]). VAR_047302 
STRAND   3665   3667  3      
TURN   3679   3683  5      
STRAND   3704   3706  3      
HELIX   3712   3714  3      
TURN   3716   3718  3      
STRAND   3735   3740  6      
STRAND   3745   3749  5      
TURN   3818   3820  3      
TURN   3822   3825  4      
STRAND   3834   3836  3      
STRAND   3841   3846  6      
STRAND   3851   3855  5      
STRAND   4129   4131  3      
STRAND   4152   4154  3      
TURN   4160   4162  3      
STRAND   4183   4187  5      
STRAND   4193   4197  5      
Sequence information
Length: 4548 AA [This is the length of the unprocessed precursor] Molecular weight: 501319 Da [This is the MW of the unprocessed precursor] CRC64: 96921BE96A465C5F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEHKEVVLLL LLFLKSAAPE QSHVVQDCYH GDGQSYRGTY STTVTGRTCQ AWSSMTPHQH 

        70         80         90        100        110        120 
NRTTENYPNA GLIMNYCRNP DAVAAPYCYT RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP 

       130        140        150        160        170        180 
VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY 

       190        200        210        220        230        240 
YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA 

       250        260        270        280        290        300 
PSEQAPTEQR PGVQECYHGN GQSYRGTYST TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL 

       310        320        330        340        350        360 
IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP 

       370        380        390        400        410        420 
TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR 

       430        440        450        460        470        480 
NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG 

       490        500        510        520        530        540 
VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA 

       550        560        570        580        590        600 
APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA PPTVTPVPSL EAPSEQAPTE QRPGVQECYH 

       610        620        630        640        650        660 
GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT 

       670        680        690        700        710        720 
RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY 

       730        740        750        760        770        780 
RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR 

       790        800        810        820        830        840 
WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA PSEQAPTEQR PGVQECYHGN GQSYRGTYST 

       850        860        870        880        890        900 
TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL 

       910        920        930        940        950        960 
TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT 

       970        980        990       1000       1010       1020 
CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA 

      1030       1040       1050       1060       1070       1080 
EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS 

      1090       1100       1110       1120       1130       1140 
MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA 

      1150       1160       1170       1180       1190       1200 
PPTVTPVPSL EAPSEQAPTE QRPGVQECYH GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH 

      1210       1220       1230       1240       1250       1260 
SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP 

      1270       1280       1290       1300       1310       1320 
VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY 

      1330       1340       1350       1360       1370       1380 
YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA 

      1390       1400       1410       1420       1430       1440 
PSEQAPTEQR PGVQECYHGN GQSYRGTYST TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL 

      1450       1460       1470       1480       1490       1500 
IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP 

      1510       1520       1530       1540       1550       1560 
TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR 

      1570       1580       1590       1600       1610       1620 
NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG 

      1630       1640       1650       1660       1670       1680 
VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA 

      1690       1700       1710       1720       1730       1740 
APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA PPTVTPVPSL EAPSEQAPTE QRPGVQECYH 

      1750       1760       1770       1780       1790       1800 
GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT 

      1810       1820       1830       1840       1850       1860 
RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY 

      1870       1880       1890       1900       1910       1920 
RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR 

      1930       1940       1950       1960       1970       1980 
WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA PSEQAPTEQR PGVQECYHGN GQSYRGTYST 

      1990       2000       2010       2020       2030       2040 
TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL 

      2050       2060       2070       2080       2090       2100 
TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT 

      2110       2120       2130       2140       2150       2160 
CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA 

      2170       2180       2190       2200       2210       2220 
EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS 

      2230       2240       2250       2260       2270       2280 
MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA 

      2290       2300       2310       2320       2330       2340 
PPTVTPVPSL EAPSEQAPTE QRPGVQECYH GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH 

      2350       2360       2370       2380       2390       2400 
SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP 

      2410       2420       2430       2440       2450       2460 
VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY 

      2470       2480       2490       2500       2510       2520 
YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA 

      2530       2540       2550       2560       2570       2580 
PSEQAPTEQR PGVQECYHGN GQSYRGTYST TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL 

      2590       2600       2610       2620       2630       2640 
IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP 

      2650       2660       2670       2680       2690       2700 
TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR 

      2710       2720       2730       2740       2750       2760 
NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG 

      2770       2780       2790       2800       2810       2820 
VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA 

      2830       2840       2850       2860       2870       2880 
APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA PPTVTPVPSL EAPSEQAPTE QRPGVQECYH 

      2890       2900       2910       2920       2930       2940 
GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT 

      2950       2960       2970       2980       2990       3000 
RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY 

      3010       3020       3030       3040       3050       3060 
RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR 

      3070       3080       3090       3100       3110       3120 
WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA PSEQAPTEQR PGVQECYHGN GQSYRGTYST 

      3130       3140       3150       3160       3170       3180 
TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL 

      3190       3200       3210       3220       3230       3240 
TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT 

      3250       3260       3270       3280       3290       3300 
CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA 

      3310       3320       3330       3340       3350       3360 
EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS 

      3370       3380       3390       3400       3410       3420 
MTPHSHSRTP EYYPNAGLIM NYCRNPDPVA APYCYTRDPS VRWEYCNLTQ CSDAEGTAVA 

      3430       3440       3450       3460       3470       3480 
PPTITPIPSL EAPSEQAPTE QRPGVQECYH GNGQSYQGTY FITVTGRTCQ AWSSMTPHSH 

      3490       3500       3510       3520       3530       3540 
SRTPAYYPNA GLIKNYCRNP DPVAAPWCYT TDPSVRWEYC NLTRCSDAEW TAFVPPNVIL 

      3550       3560       3570       3580       3590       3600 
APSLEAFFEQ ALTEETPGVQ DCYYHYGQSY RGTYSTTVTG RTCQAWSSMT PHQHSRTPEN 

      3610       3620       3630       3640       3650       3660 
YPNAGLTRNY CRNPDAEIRP WCYTMDPSVR WEYCNLTQCL VTESSVLATL TVVPDPSTEA 

      3670       3680       3690       3700       3710       3720 
SSEEAPTEQS PGVQDCYHGD GQSYRGSFST TVTGRTCQSW SSMTPHWHQR TTEYYPNGGL 

      3730       3740       3750       3760       3770       3780 
TRNYCRNPDA EISPWCYTMD PNVRWEYCNL TQCPVTESSV LATSTAVSEQ APTEQSPTVQ 

      3790       3800       3810       3820       3830       3840 
DCYHGDGQSY RGSFSTTVTG RTCQSWSSMT PHWHQRTTEY YPNGGLTRNY CRNPDAEIRP 

      3850       3860       3870       3880       3890       3900 
WCYTMDPSVR WEYCNLTQCP VMESTLLTTP TVVPVPSTEL PSEEAPTENS TGVQDCYRGD 

      3910       3920       3930       3940       3950       3960 
GQSYRGTLST TITGRTCQSW SSMTPHWHRR IPLYYPNAGL TRNYCRNPDA EIRPWCYTMD 

      3970       3980       3990       4000       4010       4020 
PSVRWEYCNL TRCPVTESSV LTTPTVAPVP STEAPSEQAP PEKSPVVQDC YHGDGRSYRG 

      4030       4040       4050       4060       4070       4080 
ISSTTVTGRT CQSWSSMIPH WHQRTPENYP NAGLTENYCR NPDSGKQPWC YTTDPCVRWE 

      4090       4100       4110       4120       4130       4140 
YCNLTQCSET ESGVLETPTV VPVPSMEAHS EAAPTEQTPV VRQCYHGNGQ SYRGTFSTTV 

      4150       4160       4170       4180       4190       4200 
TGRTCQSWSS MTPHRHQRTP ENYPNDGLTM NYCRNPDADT GPWCFTMDPS IRWEYCNLTR 

      4210       4220       4230       4240       4250       4260 
CSDTEGTVVA PPTVIQVPSL GPPSEQDCMF GNGKGYRGKK ATTVTGTPCQ EWAAQEPHRH 

      4270       4280       4290       4300       4310       4320 
STFIPGTNKW AGLEKNYCRN PDGDINGPWC YTMNPRKLFD YCDIPLCASS SFDCGKPQVE 

      4330       4340       4350       4360       4370       4380 
PKKCPGSIVG GCVAHPHSWP WQVSLRTRFG KHFCGGTLIS PEWVLTAAHC LKKSSRPSSY 

      4390       4400       4410       4420       4430       4440 
KVILGAHQEV NLESHVQEIE VSRLFLEPTQ ADIALLKLSR PAVITDKVMP ACLPSPDYMV 

      4450       4460       4470       4480       4490       4500 
TARTECYITG WGETQGTFGT GLLKEAQLLV IENEVCNHYK YICAEHLARG TDSCQGDSGG 

      4510       4520       4530       4540 
PLVCFEKDKY ILQGVTSWGL GCARPNKPGV YARVSRFVTW IEGMMRNN 

P08519 in FASTA format

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