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UniProtKB/Swiss-Prot entry P02743


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

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Entry information
Entry name SAMP_HUMAN
Primary accession number P02743
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on February 1, 1995 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 121)
Name and origin of the protein
Protein name Serum amyloid P-component [Precursor]
Synonyms SAP
9.5S alpha-1-glycoprotein
Contains Serum amyloid P-component(1-203)
Gene name
Name: APCS
Synonyms: PTX2
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].
PubMed=2987268 [NCBI, ExPASy, EBI, Israel, Japan]
Mantzouranis E.C., Dowton S.B., Whitehead A.S., Edge M.D., Bruns G.A.P., Colten H.R.;
"Human serum amyloid P component. cDNA isolation, complete sequence of pre-serum amyloid P component, and localization of the gene to chromosome 1.";
J. Biol. Chem. 260:7752-7756(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3029048 [NCBI, ExPASy, EBI, Israel, Japan]
Ohnishi S., Maeda S., Shimada K., Arao T.;
"Isolation and characterization of the complete complementary and genomic DNA sequences of human serum amyloid P component.";
J. Biochem. 100:849-858(1986).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle;
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).
[7]
PROTEIN SEQUENCE OF 20-223.
PubMed=4055725 [NCBI, ExPASy, EBI, Israel, Japan]
Prelli F., Pras M., Frangione B.;
"The primary structure of human tissue amyloid P component from a patient with primary idiopathic amyloidosis.";
J. Biol. Chem. 260:12895-12898(1985).
[8]
PROTEIN SEQUENCE OF 20-49.
DOI=10.1021/bi00613a030; PubMed=81686 [NCBI, ExPASy, EBI, Israel, Japan]
Thompson A.R., Enfield D.L.;
"Human plasma P component: isolation and characterization.";
Biochemistry 17:4304-4311(1978).
[9]
STRUCTURE OF CARBOHYDRATE, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.91.12.5602; PubMed=8202534 [NCBI, ExPASy, EBI, Israel, Japan]
Pepys M.B., Rademacher T.W., Amatayakul-Chantler S., Williams P., Noble G.E., Hutchinson W.L., Hawkins P.N., Nelson S.R., Gallimore J.R., Herbert J., Hutton T., Dwek R.A.;
"Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure.";
Proc. Natl. Acad. Sci. U.S.A. 91:5602-5606(1994).
[10]
TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
DOI=10.1002/pmic.200300690; PubMed=15174148 [NCBI, ExPASy, EBI, Israel, Japan]
Kiernan U.A., Nedelkov D., Tubbs K.A., Niederkofler E.E., Nelson R.W.;
"Proteomic characterization of novel serum amyloid P component variants from human plasma and urine.";
Proteomics 4:1825-1829(2004).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-51, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-51, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1021/pr8008012; PubMed=19159218 [NCBI, ExPASy, EBI, Israel, Japan]
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[13]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
DOI=10.1038/367338a0; PubMed=8114934 [NCBI, ExPASy, EBI, Israel, Japan]
Emsley J., White H.E., O'Hara B., Oliva G., Srinivasan N., Tickle I.J., Blundell T.L., Pepys M.B., Wood S.P.;
"Structure of pentameric human serum amyloid P component.";
Nature 367:338-345(1994).
[14]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
DOI=10.1006/jmbi.1997.1075; PubMed=9217261 [NCBI, ExPASy, EBI, Israel, Japan]
Hohenester E., Hutchinson W.L., Pepys M.B., Wood S.P.;
"Crystal structure of a decameric complex of human serum amyloid P component with bound dAMP.";
J. Mol. Biol. 269:570-578(1997).
[15]
VARIANT [LARGE SCALE ANALYSIS] SER-141.
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
D00097; BAA00060.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M10944; AAA60302.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04608; CAA28275.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR450313; CAG29309.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL445528; CAH73651.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006750; AAP35396.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007039; AAH07039.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007058; AAH07058.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00022391; -.
PIR A25503; YLHUP.
RefSeq NP_001630.1; -.
UniGene Hs.507080
3D structure databases
PDB
1GYK; X-ray; 2.20 A; A/B/C/D/E=20-223.[ExPASy / RCSB / EBI]
1LGN; X-ray; 2.80 A; A/B/C/D/E=20-223.[ExPASy / RCSB / EBI]
1SAC; X-ray; 2.00 A; A/B/C/D/E=20-223.[ExPASy / RCSB / EBI]
2A3W; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=20-223.[ExPASy / RCSB / EBI]
2A3X; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J=20-223.[ExPASy / RCSB / EBI]
2A3Y; X-ray; 2.00 A; A/B/C/D/E=20-223.[ExPASy / RCSB / EBI]
2W08; X-ray; 1.70 A; A/B/C/D/E=20-223.[ExPASy / RCSB / EBI]
3D5O; X-ray; 2.80 A; A/B/C/D/E=20-223.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1GYK; -.
1LGN; -.
1SAC; -.
2A3W; -.
2A3X; -.
2A3Y; -.
2W08; -.
3D5O; -.
ModBase P02743.
Protein-protein interaction databases
IntAct P02743; 1.
Protein family/group databases
TCDB 1.C.92.1.2; pentraxin family.
PTM databases
GlycoSuiteDB P02743; -.
2D gel databases
SWISS-2DPAGE P02743; -.
Cornea-2DPAGE P02743; -.
DOSAC-COBS-2DPAGE P02743; -.
OGP P02743; -.
REPRODUCTION-2DPAGE IPI00022391; -.
P02743; -.
Organism-specific databases
GeneCards GC01P157824; -.
H-InvDB HIX0001200; -.
HGNC HGNC:584; APCS.
GenAtlas APCS.
HPA CAB007817; -.
MIM 104770; gene. [NCBI / EBI]
PharmGKB PA24877; -.
Gene expression databases
ArrayExpress P02743; -.
Bgee P02743; -.
CleanEx HS_APCS; -.
GermOnline ENSG00000132703; Homo sapiens.
Ontologies
GO
GO:0005615; Cellular component: extracellular space (traceable author statement from ProtInc).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005529; Molecular function: sugar binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051082; Molecular function: unfolded protein binding (traceable author statement from ProtInc).
GO:0006953; Biological process: acute-phase response (traceable author statement from ProtInc).
GO:0051131; Biological process: chaperone-mediated protein complex assembly (traceable author statement from ProtInc).
GO:0006457; Biological process: protein folding (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR013320; ConA-like_subgrp.
IPR001759; Pentaxin.
Graphical view of domain structure.
Gene3D G3DSA:2.60.120.200; ConA_like_subgrp; 1.
Pfam PF00354; Pentaxin; 1.
Pfam graphical view of domain structure.
PRINTS PR00895; PENTAXIN.
ProDom PD002153; Pentaxin; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00159; PTX; 1.
SMART graphical view of domain structure.
PROSITE PS00289; PENTAXIN; 1.
Proteomic databases
PeptideAtlas P02743; -.
PRIDE P02743; -.
Genome annotation databases
Ensembl ENSG00000132703; Homo sapiens. [Contig view]
GeneID 325; -.
KEGG hsa:325; -.
Phylogenomic databases
HOGENOM P02743; -.
HOVERGEN P02743; -.
OMA P02743; KIVLGQE.
Other
NextBio 1333; -.
SOURCE APCS; Homo sapiens.
ProtoNet P02743.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Amyloid; Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein; Lectin; Metal-binding; Polymorphism; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    19  19      
CHAIN   20   223  204     Serum amyloid P-component. PRO_0000023540
CHAIN   20   222  203     Serum amyloid P-component(1-203). PRO_0000023541
DOMAIN   20   223  204     Pentaxin. 
METAL   77    77        Calcium 1. 
METAL   78    78        Calcium 1. 
METAL   155   155        Calcium 1. 
METAL   155   155        Calcium 2. 
METAL   156   156        Calcium 1; via carbonyl oxygen. 
METAL   157   157        Calcium 1. 
METAL   157   157        Calcium 2. 
METAL   167   167        Calcium 2. 
CARBOHYD   51    51        N-linked (GlcNAc...) [GlycoSuiteDB]. CAR_000169
DISULFID   55   114         
VARIANT   141   141  1     G -> S (in a breast cancer sample; somatic mutation). VAR_035814 [3D]
VARIANT   155   155  1     E -> G. VAR_006054 [3D]
VARIANT   158   158  1     S -> G. VAR_006055 [3D]
CONFLICT   101   101        S -> P (in Ref. 1; AAA60302). 
STRAND   26    30  5      
STRAND   39    41  3      
STRAND   49    59  11      
STRAND   66    73  8      
STRAND   76    86  11      
STRAND   89    94  6      
STRAND   97   102  6      
STRAND   111   118  8      
TURN   119   121  3      
STRAND   123   128  6      
STRAND   149   154  6      
STRAND   157   160  4      
HELIX   165   167  3      
STRAND   171   181  11      
HELIX   185   192  8      
STRAND   200   202  3      
STRAND   209   211  3      
STRAND   216   219  4      
Sequence information
Length: 223 AA [This is the length of the unprocessed precursor] Molecular weight: 25387 Da [This is the MW of the unprocessed precursor] CRC64: 6C88A515FE88B393 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNKPLLWISV LTSLLEAFAH TDLSGKVFVF PRESVTDHVN LITPLEKPLQ NFTLCFRAYS 

        70         80         90        100        110        120 
DLSRAYSLFS YNTQGRDNEL LVYKERVGEY SLYIGRHKVT SKVIEKFPAP VHICVSWESS 

       130        140        150        160        170        180 
SGIAEFWING TPLVKKGLRQ GYFVEAQPKI VLGQEQDSYG GKFDRSQSFV GEIGDLYMWD 

       190        200        210        220 
SVLPPENILS AYQGTPLPAN ILDWQALNYE IRGYVIIKPL VWV 

P02743 in FASTA format

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