P02743 (SAMP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serum amyloid P-component
Short name=SAP

Alternative name(s):
9.5S alpha-1-glycoprotein

Cleaved into the following chain:

1. Serum amyloid P-component(1-203)

Gene names

Name:	APCS
Synonyms:	PTX2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	223 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. May also function as a calcium-dependent lectin.
Cofactor	Binds 2 calcium ions per subunit.
Subunit structure	Homopentamer. Pentaxin (or pentraxin) have a discoid arrangement of 5 non-covalently bound subunits.
Subcellular location	Secreted.
Tissue specificity	Found in serum and urine. Ref.10
Post-translational modification	N-glycosylated with a complex biantennary oligosaccharide chain with a sialic acid at the end (disialo-SAP). Monosialo-SAP as well as asioalo-SAP are also detected (Ref.10). Ref.9
Involvement in disease	SAP is a precursor of amyloid component P which is found in basement membrane and associated with amyloid deposits.
Sequence similarities	Belongs to the pentaxin family. Contains 1 pentaxin domain.
Mass spectrometry	Molecular mass is 25462.5±1.1 Da from positions 20 - 223. Determined by ESI. Ref.9 Molecular mass is 25463±3 Da from positions 20 - 223. Determined by MALDI. Ref.10 Molecular mass is 1285.78 Da from positions 213 - 223. Determined by MALDI. Ref.10 Molecular mass is 1186.71 Da from positions 213 - 222. Determined by MALDI. Ref.10

Ontologies

Keywords
Cellular component	Amyloid Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Calcium Lectin Metal-binding
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	acute-phase response Traceable author statement Ref.1. Source: ProtInc chaperone-mediated protein complex assembly Traceable author statement PubMed 10972085. Source: ProtInc protein folding Traceable author statement PubMed 10812074. Source: ProtInc
Cellular_component	extracellular space Inferred from direct assay PubMed 20551380. Source: BHF-UCL protein complex Inferred from electronic annotation. Source: Compara
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW unfolded protein binding Traceable author statement PubMed 10812074. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Ref.7 Ref.8

Chain

20 – 223

204

Serum amyloid P-component

PRO_0000023540

Chain

20 – 222

203

Serum amyloid P-component(1-203)

PRO_0000023541

Regions

Domain

20 – 223

204

Pentaxin

Sites

Metal binding

77

1

Calcium 1

Metal binding

78

1

Calcium 1

Metal binding

155

1

Calcium 1

Metal binding

155

1

Calcium 2

Metal binding

156

1

Calcium 1; via carbonyl oxygen

Metal binding

157

1

Calcium 1

Metal binding

157

1

Calcium 2

Metal binding

167

1

Calcium 2

Amino acid modifications

Glycosylation

51

1

N-linked (GlcNAc...) Ref.11 Ref.12

CAR_000169

Disulfide bond

55 ↔ 114

Ref.7

Natural variations

Natural variant

141

1

G → S in a breast cancer sample; somatic mutation. Ref.16

VAR_035814

Natural variant

155

1

E → G.

VAR_006054

Natural variant

158

1

S → G.

VAR_006055

Experimental info

Sequence conflict

101

1

S → P in AAA60302. Ref.1

Secondary structure

1

.

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223

Helix Strand Turn

Details...

Beta strand

26 – 30

5

Beta strand

38 – 42

5

Beta strand

49 – 59

11

Beta strand

66 – 73

8

Beta strand

76 – 86

11

Beta strand

89 – 94

6

Beta strand

97 – 102

6

Beta strand

111 – 118

8

Turn

119 – 121

3

Beta strand

123 – 128

6

Beta strand

149 – 154

6

Beta strand

157 – 160

4

Helix

165 – 167

3

Beta strand

171 – 181

11

Helix

185 – 193

9

Beta strand

200 – 203

4

Helix

204 – 206

3

Beta strand

208 – 214

7

Beta strand

216 – 219

4

Sequences

	Sequence		Length	Mass (Da)
	P02743 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: 6C88A515FE88B393	FASTA	223	25,387
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human serum amyloid P component. cDNA isolation, complete sequence of pre-serum amyloid P component, and localization of the gene to chromosome 1." Mantzouranis E.C., Dowton S.B., Whitehead A.S., Edge M.D., Bruns G.A.P., Colten H.R. J. Biol. Chem. 260:7752-7756(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Isolation and characterization of the complete complementary and genomic DNA sequences of human serum amyloid P component." Ohnishi S., Maeda S., Shimada K., Arao T. J. Biochem. 100:849-858(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The DNA sequence and biological annotation of human chromosome 1." 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. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skeletal muscle.
[7]	"The primary structure of human tissue amyloid P component from a patient with primary idiopathic amyloidosis." Prelli F., Pras M., Frangione B. J. Biol. Chem. 260:12895-12898(1985) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-223.
[8]	"Human plasma P component: isolation and characterization." Thompson A.R., Enfield D.L. Biochemistry 17:4304-4311(1978) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-49.
[9]	"Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure." 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. Proc. Natl. Acad. Sci. U.S.A. 91:5602-5606(1994) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATE, MASS SPECTROMETRY.
[10]	"Proteomic characterization of novel serum amyloid P component variants from human plasma and urine." Kiernan U.A., Nedelkov D., Tubbs K.A., Niederkofler E.E., Nelson R.W. Proteomics 4:1825-1829(2004) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, MASS SPECTROMETRY.
[11]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-51, MASS SPECTROMETRY. Tissue: Plasma.
[12]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-51, MASS SPECTROMETRY. Tissue: Liver.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"Structure of pentameric human serum amyloid P component." Emsley J., White H.E., O'Hara B., Oliva G., Srinivasan N., Tickle I.J., Blundell T.L., Pepys M.B., Wood S.P. Nature 367:338-345(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[15]	"Crystal structure of a decameric complex of human serum amyloid P component with bound dAMP." Hohenester E., Hutchinson W.L., Pepys M.B., Wood S.P. J. Mol. Biol. 269:570-578(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[16]	"The consensus coding sequences of human breast and colorectal cancers." 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. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-141.
+	Additional computationally mapped references.

Web resources

Wikipedia

Serum amyloid P component entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D00097 Genomic DNA. Translation: BAA00060.1.
M10944 mRNA. Translation: AAA60302.1.
X04608 mRNA. Translation: CAA28275.1.
CR450313 mRNA. Translation: CAG29309.1.
AL445528 Genomic DNA. Translation: CAH73651.1.
BT006750 mRNA. Translation: AAP35396.1.
BC007039 mRNA. Translation: AAH07039.1.
BC007058 mRNA. Translation: AAH07058.1.

IPI

IPI00022391.

PIR

YLHUP. A25503.

RefSeq

NP_001630.1. NM_001639.3.

UniGene

Hs.507080.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GYK	X-ray	2.20	A/B/C/D/E	20-223	[»]
1LGN	X-ray	2.80	A/B/C/D/E	20-223	[»]
1SAC	X-ray	2.00	A/B/C/D/E	20-223	[»]
2A3W	X-ray	2.20	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T	20-223	[»]
2A3X	X-ray	3.00	A/B/C/D/E/F/G/H/I/J	20-223	[»]
2A3Y	X-ray	2.00	A/B/C/D/E	20-223	[»]
2W08	X-ray	1.70	A/B/C/D/E	20-223	[»]
3D5O	X-ray	2.80	A/B/C/D/E	20-223	[»]
3KQR	X-ray	1.50	A/B/C/D/E	20-223	[»]

ProteinModelPortal

P02743.

ModBase

Search...

Protein-protein interaction databases

IntAct

P02743. 3 interactions.

STRING

9606.ENSP00000255040.

Protein family/group databases

TCDB

1.C.92.1.2. pentraxin family.

PTM databases

GlycoSuiteDB

P02743.

PhosphoSite

P02743.

Polymorphism databases

DMDM

730704.

2D gel databases

DOSAC-COBS-2DPAGE

P02743.

OGP

P02743.

REPRODUCTION-2DPAGE

IPI00022391.
P02743.

SWISS-2DPAGE

P02743.

Proteomic databases

PaxDb

P02743.

PeptideAtlas

P02743.

PRIDE

P02743.

Protocols and materials databases

DNASU

325.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000255040; ENSP00000255040; ENSG00000132703.

GeneID

325.

KEGG

hsa:325.

UCSC

uc001ftv.3. human.

Organism-specific databases

CTD

325.

GeneCards

GC01P159557.

HGNC

HGNC:584. APCS.

HPA

CAB007817.

MIM

104770. gene.

neXtProt

NX_P02743.

PharmGKB

PA24877.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG44770.

HOGENOM

HOG000247043.

HOVERGEN

HBG005405.

InParanoid

P02743.

OMA

AEFWING.

OrthoDB

EOG4R23VS.

PhylomeDB

P02743.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.

Gene expression databases

Bgee

P02743.

CleanEx

HS_APCS.

Genevestigator

P02743.

GermOnline

ENSG00000132703. Homo sapiens.

Family and domain databases

Gene3D

2.60.120.200. 1 hit.

InterPro

IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR001759. Pentaxin.
[Graphical view]

Pfam

PF00354. Pentaxin. 1 hit.
[Graphical view]

PRINTS

PR00895. PENTAXIN.

SMART

SM00159. PTX. 1 hit.
[Graphical view]

SUPFAM

SSF49899. ConA_like_lec_gl. 1 hit.

PROSITE

PS00289. PENTAXIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL4929.

EvolutionaryTrace

P02743.

GenomeRNAi

325.

NextBio

1333.

SOURCE

Search...

Entry information

Entry name

SAMP_HUMAN

Accession

Primary (citable) accession number: P02743

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 156 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.