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UniProtKB/Swiss-Prot entry P08253


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

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Entry information
Entry name MMP2_HUMAN
Primary accession number P08253
Secondary accession numbers B2R6U1 Q9UCJ8
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on February 1, 1991 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 129)
Name and origin of the protein
Protein name 72 kDa type IV collagenase [Precursor]
Synonyms EC 3.4.24.24
72 kDa gelatinase
Matrix metalloproteinase-2
MMP-2
Gelatinase A
TBE-1
Gene name
Name: MMP2
Synonyms: CLG4A
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 [GENOMIC DNA].
PubMed=2162831 [NCBI, ExPASy, EBI, Israel, Japan]
Huhtala P., Chow L.T., Tryggvason K.;
"Structure of the human type IV collagenase gene.";
J. Biol. Chem. 265:11077-11082(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0888-7543(91)90408-7; PubMed=1851724 [NCBI, ExPASy, EBI, Israel, Japan]
Collier I.E., Bruns G.A.P., Goldberg G.I., Gerhard D.S.;
"On the structure and chromosome location of the 72- and 92-kDa human type IV collagenase genes.";
Genomics 9:429-434(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Teratocarcinoma;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-447 AND LEU-621.
NIEHS SNPs program;
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51.
DOI=10.1016/0888-7543(90)90486-E; PubMed=2158484 [NCBI, ExPASy, EBI, Israel, Japan]
Huhtala P., Eddy R.L., Fan Y.S., Byers M.G., Shows T.B., Tryggvason K.;
"Completion of the primary structure of the human type IV collagenase preproenzyme and assignment of the gene (CLG4) to the q21 region of chromosome 16.";
Genomics 6:554-559(1990).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 19-660, AND PARTIAL PROTEIN SEQUENCE.
PubMed=2834383 [NCBI, ExPASy, EBI, Israel, Japan]
Collier I.E., Wilhelm S.M., Eisen A.Z., Marmer B.L., Grant G.A., Seltzer J.L., Kronberger A., He C., Bauer E.A., Goldberg G.I.;
"H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen.";
J. Biol. Chem. 263:6579-6587(1988).
[8]
PROTEIN SEQUENCE OF 30-44.
TISSUE=Melanoma;
PubMed=1480041 [NCBI, ExPASy, EBI, Israel, Japan]
Stetler-Stevenson W.G., Krutzsch H.C., Liotta L.A.;
"TIMP-2: identification and characterization of a new member of the metalloproteinase inhibitor family.";
Matrix Suppl. 1:299-306(1992).
[9]
ENZYME REGULATION.
DOI=10.1128/IAI.69.3.1402-1408.2001; PubMed=11179305 [NCBI, ExPASy, EBI, Israel, Japan]
Gusman H., Travis J., Helmerhorst E.J., Potempa J., Troxler R.F., Oppenheim F.G.;
"Salivary histatin 5 is an inhibitor of both host and bacterial enzymes implicated in periodontal disease.";
Infect. Immun. 69:1402-1408(2001).
[10]
PROTEOLYTIC PROCESSING OF KISS1.
DOI=10.1038/sj.onc.1206542; PubMed=12879005 [NCBI, ExPASy, EBI, Israel, Japan]
Takino T., Koshikawa N., Miyamori H., Tanaka M., Sasaki T., Okada Y., Seiki M., Sato H.;
"Cleavage of metastasis suppressor gene product KiSS-1 protein/metastin by matrix metalloproteinases.";
Oncogene 22:4617-4626(2003).
[11]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 443-660.
DOI=10.1038/nsb1195-938; PubMed=7583664 [NCBI, ExPASy, EBI, Israel, Japan]
Libson A.M., Gittis A.G., Collier I.E., Marmer B.L., Goldberg G.I., Lattman E.E.;
"Crystal structure of the haemopexin-like C-terminal domain of gelatinase A.";
Nat. Struct. Biol. 2:938-942(1995).
[12]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 458-660.
DOI=10.1016/0014-5793(95)01435-7; PubMed=8549817 [NCBI, ExPASy, EBI, Israel, Japan]
Gohlke U., Gomis-Rueth F.-X., Crabbe T., Murphy G., Docherty A.J., Bode W.;
"The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its function.";
FEBS Lett. 378:126-130(1996).
[13]
VARIANT TORG-WINCHESTER SYNDROME HIS-101, AND VARIANT TYR-210.
DOI=10.1038/90100; PubMed=11431697 [NCBI, ExPASy, EBI, Israel, Japan]
Martignetti J.A., Aqeel A.A., Sewairi W.A., Boumah C.E., Kambouris M., Mayouf S.A., Sheth K.V., Eid W.A., Dowling O., Harris J., Glucksman M.J., Bahabri S., Meyer B.F., Desnick R.J.;
"Mutation of the matrix metalloproteinase 2 gene (MMP2) causes a multicentric osteolysis and arthritis syndrome.";
Nat. Genet. 28:261-265(2001).
[14]
VARIANT TORG-WINCHESTER SYNDROME LYS-404.
DOI=10.1111/j.1399-0004.2004.00402.x; PubMed=15691365 [NCBI, ExPASy, EBI, Israel, Japan]
Zankl A., Bonafe L., Calcaterra V., Di Rocco M., Superti-Furga A.;
"Winchester syndrome caused by a homozygous mutation affecting the active site of matrix metalloproteinase 2.";
Clin. Genet. 67:261-266(2005).
[15]
VARIANT TORG-WINCHESTER SYNDROME VAL-400 DEL.
DOI=10.1111/j.1399-0004.2006.00584.x; PubMed=16542393 [NCBI, ExPASy, EBI, Israel, Japan]
Rouzier C., Vanatka R., Bannwarth S., Philip N., Coussement A., Paquis-Flucklinger V., Lambert J.-C.;
"A novel homozygous MMP2 mutation in a family with Winchester syndrome.";
Clin. Genet. 69:271-276(2006).
[16]
VARIANTS [LARGE SCALE ANALYSIS] THR-228; MET-498 AND ILE-644.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
Comments
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
M55593; AAA52028.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M58552; AAA52028.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M55582; AAA52028.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M55583; AAA52028.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M55584; AAA52028.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M55585; AAA52028.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M55586; AAA52028.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M55587; AAA52028.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M55588; AAA52028.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M55589; AAA52028.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M55590; AAA52028.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M55591; AAA52028.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M55592; AAA52028.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK312711; BAG35588.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY738117; AAU10089.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002576; AAH02576.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M33789; AAA52027.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J03210; AAA35701.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00027780; -.
PIR A28153; A28153.
RefSeq NP_001121363.1; -.
NP_004521.1; -.
UniGene Hs.513617
3D structure databases
PDB
1CK7; X-ray; 2.80 A; A=30-660.[ExPASy / RCSB / EBI]
1CXW; NMR; -; A=278-336.[ExPASy / RCSB / EBI]
1EAK; X-ray; 2.66 A; A/B/C/D=32-452.[ExPASy / RCSB / EBI]
1GEN; X-ray; 2.15 A; A=443-660.[ExPASy / RCSB / EBI]
1GXD; X-ray; 3.10 A; A/B=30-660.[ExPASy / RCSB / EBI]
1HOV; NMR; -; A=110-446.[ExPASy / RCSB / EBI]
1J7M; NMR; -; A=337-394.[ExPASy / RCSB / EBI]
1KS0; NMR; -; A=223-282.[ExPASy / RCSB / EBI]
1QIB; X-ray; 2.80 A; A=115-449.[ExPASy / RCSB / EBI]
1RTG; X-ray; 2.60 A; A=451-660.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1CK7; -.
1CXW; -.
1EAK; -.
1GEN; -.
1GXD; -.
1HOV; -.
1J7M; -.
1KS0; -.
1QIB; -.
1RTG; -.
ModBase P08253.
Protein-protein interaction databases
DIP DIP:26N; -.
IntAct P08253; 2.
Protein family/group databases
MEROPS M10.003; -.
PTM databases
PhosphoSite P08253; -.
Enzyme and pathway databases
BRENDA 3.4.24.24; 247.
Pathway_Interaction_DB amb2_neutrophils_pathway; amb2 Integrin signaling.
foxm1pathway; FOXM1 transcription factor network.
lysophospholipid_pathway; LPA receptor mediated events.
avb3_opn_pathway; Osteopontin-mediated events.
er_nongenomic_pathway; Plasma membrane estrogen receptor signaling.
syndecan_2_pathway; Syndecan-2-mediated signaling events.
Organism-specific databases
GeneCards GC16P054070; -.
H-InvDB HIX0013041; -.
HIX0040455; -.
HGNC HGNC:7166; MMP2.
GenAtlas MMP2.
HPA CAB002788; -.
HPA001939; -.
MIM 120360; gene. [NCBI / EBI]
259600; phenotype. [NCBI / EBI]
Orphanet 85196; Nodulosis-arthropathy-osteolysis syndrome.
3460; Winchester disease.
PharmGKB PA30877; -.
Gene expression databases
ArrayExpress P08253; -.
Bgee P08253; -.
CleanEx HS_MMP2; -.
GermOnline ENSG00000087245; Homo sapiens.
Ontologies
GO
GO:0005615; Cellular component: extracellular space (inferred from direct assay from MGI).
GO:0043231; Cellular component: intracellular membrane-bounded organelle (inferred from direct assay from HPA).
GO:0005578; Cellular component: proteinaceous extracellular matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004222; Molecular function: metalloendopeptidase activity (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0008270; Molecular function: zinc ion binding (traceable author statement from ProtInc).
GO:0030574; Biological process: collagen catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0006508; Biological process: proteolysis (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000562; FN_type2_col_bd.
IPR000585; Hemopexin/matrixin.
IPR018486; Hemopexin/matrixin_CS.
IPR018487; Hemopexin/matrixin_repeat.
IPR001818; Pept_M10A_M12B.
IPR006025; Pept_M_Zn_BS.
IPR006026; Peptidase_M.
IPR002477; Peptidoglycan-bd-like.
Graphical view of domain structure.
Gene3D G3DSA:2.110.10.10; Hemopexin; 1.
Pfam PF00040; fn2; 3.
PF00045; Hemopexin; 4.
PF00413; Peptidase_M10; 1.
PF01471; PG_binding_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00013; FNTYPEII.
PR00138; MATRIXIN.
ProDom PD000995; FN_Type_II; 2.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00059; FN2; 3.
SM00120; HX; 4.
SM00235; ZnMc; 1.
SMART graphical view of domain structure.
PROSITE PS00546; CYSTEINE_SWITCH; 1.
PS00023; FN2_1; 3.
PS51092; FN2_2; 3.
PS00024; HEMOPEXIN; 1.
PS00142; ZINC_PROTEASE; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas P08253; -.
PRIDE P08253; -.
Genome annotation databases
Ensembl ENSG00000087245; Homo sapiens. [Contig view]
GeneID 4313; -.
NMPDR fig|9606.3.peg.12256; -.
Phylogenomic databases
HOGENOM P08253; -.
HOVERGEN P08253; -.
OMA P08253; DDDRKWG.
Other
DrugBank DB00786; Marimastat.
DB00605; Sulindac.
NextBio 16973; -.
PMAP-CutDB P08253; -.
SOURCE MMP2; Homo sapiens.
ProtoNet P08253.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calcium; Collagen degradation; Direct protein sequencing; Disease mutation; Disulfide bond; Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Polymorphism; Protease; Repeat; Secreted; Signal; Zinc; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    29  29     Potential. 
PROPEP   30   109  80     Activation peptide. PRO_0000028714
CHAIN   110   660  551     72 kDa type IV collagenase. PRO_0000028715
DOMAIN   228   276  49     Fibronectin type-II 1. 
DOMAIN   286   334  49     Fibronectin type-II 2. 
DOMAIN   344   392  49     Fibronectin type-II 3. 
DOMAIN   475   518  44     Hemopexin-like 1. 
DOMAIN   520   563  44     Hemopexin-like 2. 
DOMAIN   568   615  48     Hemopexin-like 3. 
DOMAIN   617   660  44     Hemopexin-like 4. 
REGION   110   221  112     Collagenase-like 1. 
REGION   222   396  175     Collagen-binding. 
REGION   397   465  69     Collagenase-like 2. 
MOTIF   100   107  8     Cysteine switch (By similarity). 
ACT_SITE   404   404        By similarity. 
METAL   102   102        Zinc 2; in inhibited form (By similarity). 
METAL   134   134        Calcium 1 (By similarity). 
METAL   168   168        Calcium 2 (By similarity). 
METAL   178   178        Zinc 1 (By similarity). 
METAL   180   180        Zinc 1 (By similarity). 
METAL   185   185        Calcium 3 (By similarity). 
METAL   186   186        Calcium 3; via carbonyl oxygen (By similarity). 
METAL   193   193        Zinc 1 (By similarity). 
METAL   200   200        Calcium 2; via carbonyl oxygen (By similarity). 
METAL   202   202        Calcium 2; via carbonyl oxygen (By similarity). 
METAL   204   204        Calcium 2 (By similarity). 
METAL   206   206        Zinc 1 (By similarity). 
METAL   208   208        Calcium 3 (By similarity). 
METAL   209   209        Calcium 1 (By similarity). 
METAL   211   211        Calcium 3 (By similarity). 
METAL   403   403        Zinc 2; catalytic (By similarity). 
METAL   407   407        Zinc 2; catalytic (By similarity). 
METAL   413   413        Zinc 2; catalytic (By similarity). 
METAL   476   476        Calcium 4; via carbonyl oxygen. 
METAL   521   521        Calcium 4; via carbonyl oxygen. 
METAL   569   569        Calcium 4; via carbonyl oxygen. 
METAL   618   618        Calcium 4; via carbonyl oxygen. 
CARBOHYD   573   573        N-linked (GlcNAc...) (Potential). 
CARBOHYD   642   642        N-linked (GlcNAc...) (Potential). 
DISULFID   233   259        By similarity. 
DISULFID   247   274        By similarity. 
DISULFID   291   317        By similarity. 
DISULFID   305   332        By similarity. 
DISULFID   349   375        By similarity. 
DISULFID   363   390        By similarity. 
DISULFID   469   660         
VARIANT   101   101  1     R -> H (in Torg-Winchester syndrome). VAR_032423 
VARIANT   210   210  1     D -> Y. VAR_032424 
VARIANT   228   228  1     A -> T (in a colorectal cancer sample; somatic mutation). VAR_036136 
VARIANT   400   400  1     Missing (in Torg-Winchester syndrome). VAR_054996
VARIANT   404   404  1     E -> K (in Torg-Winchester syndrome). VAR_032425 
VARIANT   447   447  1     A -> V (in dbSNP:rs17859943 [NCBI]). VAR_020616 
VARIANT   498   498  1     T -> M (in a colorectal cancer sample; somatic mutation). VAR_036137 
VARIANT   621   621  1     V -> L (in dbSNP:rs16955280 [NCBI]). VAR_020617 
VARIANT   644   644  1     S -> I (in a colorectal cancer sample; somatic mutation). VAR_036138 
CONFLICT   546   546        S -> G (in Ref. 3; BAG35588). 
CONFLICT   618   618        D -> G (in Ref. 3; BAG35588). 
HELIX   46    57  12      
TURN   62    64  3      
HELIX   67    81  15      
HELIX   91    96  6      
STRAND   111   113  3      
STRAND   122   128  7      
HELIX   137   152  16      
STRAND   158   161  4      
STRAND   163   165  3      
STRAND   168   174  7      
STRAND   179   181  3      
STRAND   186   190  5      
STRAND   192   194  3      
STRAND   197   199  3      
TURN   200   203  4      
STRAND   205   208  4      
STRAND   213   218  6      
TURN   227   230  4      
STRAND   235   239  5      
STRAND   242   246  5      
STRAND   258   264  7      
HELIX   265   268  4      
STRAND   271   273  3      
TURN   277   279  3      
STRAND   282   286  5      
STRAND   293   296  4      
STRAND   301   304  4      
STRAND   316   322  7      
HELIX   323   326  4      
STRAND   329   331  3      
TURN   342   346  5      
STRAND   351   355  5      
STRAND   358   362  5      
STRAND   374   380  7      
HELIX   381   384  4      
STRAND   387   389  3      
HELIX   397   409  13      
STRAND   422   424  3      
HELIX   435   444  10      
TURN   468   470  3      
STRAND   476   481  6      
STRAND   484   489  6      
STRAND   492   498  7      
STRAND   504   508  5      
HELIX   509   511  3      
STRAND   521   526  6      
TURN   527   530  4      
STRAND   531   536  6      
STRAND   539   544  6      
STRAND   553   555  3      
HELIX   556   559  4      
STRAND   569   573  5      
TURN   575   577  3      
STRAND   580   584  5      
STRAND   587   592  6      
TURN   593   596  4      
HELIX   606   609  4      
STRAND   610   612  3      
STRAND   618   622  5      
TURN   624   626  3      
STRAND   628   633  6      
STRAND   636   641  6      
STRAND   644   652  9      
HELIX   653   656  4      
Sequence information
Length: 660 AA [This is the length of the unprocessed precursor] Molecular weight: 73882 Da [This is the MW of the unprocessed precursor] CRC64: BC7147DC8B49F289 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEALMARGAL TGPLRALCLL GCLLSHAAAA PSPIIKFPGD VAPKTDKELA VQYLNTFYGC 

        70         80         90        100        110        120 
PKESCNLFVL KDTLKKMQKF FGLPQTGDLD QNTIETMRKP RCGNPDVANY NFFPRKPKWD 

       130        140        150        160        170        180 
KNQITYRIIG YTPDLDPETV DDAFARAFQV WSDVTPLRFS RIHDGEADIM INFGRWEHGD 

       190        200        210        220        230        240 
GYPFDGKDGL LAHAFAPGTG VGGDSHFDDD ELWTLGEGQV VRVKYGNADG EYCKFPFLFN 

       250        260        270        280        290        300 
GKEYNSCTDT GRSDGFLWCS TTYNFEKDGK YGFCPHEALF TMGGNAEGQP CKFPFRFQGT 

       310        320        330        340        350        360 
SYDSCTTEGR TDGYRWCGTT EDYDRDKKYG FCPETAMSTV GGNSEGAPCV FPFTFLGNKY 

       370        380        390        400        410        420 
ESCTSAGRSD GKMWCATTAN YDDDRKWGFC PDQGYSLFLV AAHEFGHAMG LEHSQDPGAL 

       430        440        450        460        470        480 
MAPIYTYTKN FRLSQDDIKG IQELYGASPD IDLGTGPTPT LGPVTPEICK QDIVFDGIAQ 

       490        500        510        520        530        540 
IRGEIFFFKD RFIWRTVTPR DKPMGPLLVA TFWPELPEKI DAVYEAPQEE KAVFFAGNEY 

       550        560        570        580        590        600 
WIYSASTLER GYPKPLTSLG LPPDVQRVDA AFNWSKNKKT YIFAGDKFWR YNEVKKKMDP 

       610        620        630        640        650        660 
GFPKLIADAW NAIPDNLDAV VDLQGGGHSY FFKGAYYLKL ENQSLKSVKF GSIKSDWLGC 

P08253 in FASTA format

View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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