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P25940 (CO5A3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-3(V) chain
Gene names
Name:COL5A3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1745 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin.

Subunit structure

Trimers of two alpha 1(V) and one alpha 2(V) chains in most tissues and trimers of one alpha 1(V), one alpha 2(V), and one alpha 3(V) chains in placenta.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Post-translational modification

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.

Sequence similarities

Belongs to the fibrillar collagen family.

Contains 6 collagen-like domains.

Contains 1 fibrillar collagen NC1 domain.

Contains 1 laminin G-like domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 17451716Collagen alpha-3(V) chain
PRO_0000005845

Regions

Domain62 – 224163Laminin G-like
Domain391 – 44050Collagen-like 1
Domain482 – 53857Collagen-like 2
Domain824 – 87754Collagen-like 3
Domain905 – 95046Collagen-like 4
Domain951 – 98939Collagen-like 5
Domain1430 – 148859Collagen-like 6
Domain1514 – 1744231Fibrillar collagen NC1
Region211 – 391181Nonhelical region
Region392 – 14891098Triple-helical region

Amino acid modifications

Glycosylation1021N-linked (GlcNAc...) Ref.4
Glycosylation1411N-linked (GlcNAc...) Ref.4
Disulfide bond1544Interchain By similarity
Disulfide bond1567Interchain By similarity
Disulfide bond1576Interchain By similarity
Disulfide bond1585 ↔ 1742 By similarity
Disulfide bond1651 ↔ 1696 By similarity

Natural variations

Natural variant1341R → H.
Corresponds to variant rs2303098 [ dbSNP | Ensembl ].
VAR_020015
Natural variant3221R → G. Ref.1
Corresponds to variant rs2287803 [ dbSNP | Ensembl ].
VAR_060789
Natural variant10421R → P.
Corresponds to variant rs2161468 [ dbSNP | Ensembl ].
VAR_055678
Natural variant12071R → P.
Corresponds to variant rs2287813 [ dbSNP | Ensembl ].
VAR_020016
Natural variant14281V → M.
Corresponds to variant rs3815746 [ dbSNP | Ensembl ].
VAR_020017
Natural variant14881A → P.
Corresponds to variant rs3745584 [ dbSNP | Ensembl ].
VAR_055679
Natural variant15941I → M.
Corresponds to variant rs3745581 [ dbSNP | Ensembl ].
VAR_020018
Natural variant16911V → I.
Corresponds to variant rs2277969 [ dbSNP | Ensembl ].
VAR_020019

Experimental info

Sequence conflict16871A → T in AAF59902. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P25940 [UniParc].

Last modified December 15, 2009. Version 3.
Checksum: 4F5644D2A919D864

FASTA1,745172,121
        10         20         30         40         50         60 
MGNRRDLGQP RAGLCLLLAA LQLLPGTQAD PVDVLKALGV QGGQAGVPEG PGFCPQRTPE 

        70         80         90        100        110        120 
GDRAFRIGQA STLGIPTWEL FPEGHFPENF SLLITLRGQP ANQSVLLSIY DERGARQLGL 

       130        140        150        160        170        180 
ALGPALGLLG DPFRPLPQQV NLTDGRWHRV AVSIDGEMVT LVADCEAQPP VLGHGPRFIS 

       190        200        210        220        230        240 
IAGLTVLGTQ DLGEKTFEGD IQELLISPDP QAAFQACERY LPDCDNLAPA ATVAPQGEPE 

       250        260        270        280        290        300 
TPRPRRKGKG KGRKKGRGRK GKGRKKNKEI WTSSPPPDSA ENQTSTDIPK TETPAPNLPP 

       310        320        330        340        350        360 
TPTPLVVTST VTTGLNATIL ERSLDPDSGT ELGTLETKAA REDEEGDDST MGPDFRAAEY 

       370        380        390        400        410        420 
PSRTQFQIFP GAGEKGAKGE PAVIEKGQQF EGPPGAPGPQ GVVGPSGPPG PPGFPGDPGP 

       430        440        450        460        470        480 
PGPAGLPGIP GIDGIRGPPG TVIMMPFQFA GGSFKGPPVS FQQAQAQAVL QQTQLSMKGP 

       490        500        510        520        530        540 
PGPVGLTGRP GPVGLPGHPG LKGEEGAEGP QGPRGLQGPH GPPGRVGKMG RPGADGARGL 

       550        560        570        580        590        600 
PGDTGPKGDR GFDGLPGLPG EKGQRGDFGH VGQPGPPGED GERGAEGPPG PTGQAGEPGP 

       610        620        630        640        650        660 
RGLLGPRGSP GPTGRPGVTG IDGAPGAKGN VGPPGEPGPP GQQGNHGSQG LPGPQGLIGT 

       670        680        690        700        710        720 
PGEKGPPGNP GIPGLPGSDG PLGHPGHEGP TGEKGAQGPP GSAGPPGYPG PRGVKGTSGN 

       730        740        750        760        770        780 
RGLQGEKGEK GEDGFPGFKG DVGLKGDQGK PGAPGPRGED GPEGPKGQAG QAGEEGPPGS 

       790        800        810        820        830        840 
AGEKGKLGVP GLPGYPGRPG PKGSIGFPGP LGPIGEKGKS GKTGQPGLEG ERGPPGSRGE 

       850        860        870        880        890        900 
RGQPGATGQP GPKGDVGQDG APGIPGEKGL PGLQGPPGFP GPKGPPGHQG KDGRPGHPGQ 

       910        920        930        940        950        960 
RGELGFQGQT GPPGPAGVLG PQGKTGEVGP LGERGPPGPP GPPGEQGLPG LEGREGAKGE 

       970        980        990       1000       1010       1020 
LGPPGPLGKE GPAGLRGFPG PKGGPGDPGP TGLKGDKGPP GPVGANGSPG ERGPLGPAGG 

      1030       1040       1050       1060       1070       1080 
IGLPGQSGSE GPVGPAGKKG SRGERGPPGP TGKDGIPGPL GPLGPPGAAG PSGEEGDKGD 

      1090       1100       1110       1120       1130       1140 
VGAPGHKGSK GDKGDAGPPG QPGIRGPAGH PGPPGADGAQ GRRGPPGLFG QKGDDGVRGF 

      1150       1160       1170       1180       1190       1200 
VGVIGPPGLQ GLPGPPGEKG EVGDVGSMGP HGAPGPRGPQ GPTGSEGTPG LPGGVGQPGA 

      1210       1220       1230       1240       1250       1260 
VGEKGERGDA GDPGPPGAPG IPGPKGDIGE KGDSGPSGAA GPPGKKGPPG EDGAKGSVGP 

      1270       1280       1290       1300       1310       1320 
TGLPGDLGPP GDPGVSGIDG SPGEKGDPGD VGGPGPPGAS GEPGAPGPPG KRGPSGHMGR 

      1330       1340       1350       1360       1370       1380 
EGREGEKGAK GEPGPDGPPG RTGPMGARGP PGRVGPEGLR GIPGPVGEPG LLGAPGQMGP 

      1390       1400       1410       1420       1430       1440 
PGPLGPSGLP GLKGDTGPKG EKGHIGLIGL IGPPGEAGEK GDQGLPGVQG PPGPKGDPGP 

      1450       1460       1470       1480       1490       1500 
PGPIGSLGHP GPPGVAGPLG QKGSKGSPGS MGPRGDTGPA GPPGPPGAPA ELHGLRRRRR 

      1510       1520       1530       1540       1550       1560 
FVPVPLPVVE GGLEEVLASL TSLSLELEQL RRPPGTAERP GLVCHELHRN HPHLPDGEYW 

      1570       1580       1590       1600       1610       1620 
IDPNQGCARD SFRVFCNFTA GGETCLYPDK KFEIVKLASW SKEKPGGWYS TFRRGKKFSY 

      1630       1640       1650       1660       1670       1680 
VDADGSPVNV VQLNFLKLLS ATARQNFTYS CQNAAAWLDE ATGDYSHSAR FLGTNGEELS 

      1690       1700       1710       1720       1730       1740 
FNQTTAATVS VPQDGCRLRK GQTKTLFEFS SSRAGFLPLW DVAATDFGQT NQKFGFELGP 


VCFSS 

« Hide

References

« Hide 'large scale' references
[1]"The pro-alpha3 (V) collagen chain. Complete primary structure, expression domains in adult and developing tissues, and comparison to the structures and expression domains of the other types V and XI procollagen chains."
Imamura Y., Scott I.C., Greenspan D.S.
J. Biol. Chem. 275:8749-8759(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-322.
Tissue: Heart and Placenta.
[2]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Isolation of the alpha 3-chain of human type V collagen and characterization by partial sequencing."
Mann K.
Biol. Chem. Hoppe-Seyler 373:69-75(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 479-564; 665-709; 723-758; 787-816; 922-1008; 1054-1088; 1248-1287 AND 1313-1334.
Tissue: Placenta.
[4]"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-102 AND ASN-141.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF177941 mRNA. Translation: AAF59902.1.
AC008742 Genomic DNA. No translation available.
CCDSCCDS12222.1.
PIRS20375.
RefSeqNP_056534.2. NM_015719.3.
UniGeneHs.235368.

3D structure databases

ProteinModelPortalP25940.
SMRP25940. Positions 1533-1743.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000264828.

Chemistry

ChEMBLCHEMBL2364188.

PTM databases

PhosphoSiteP25940.

Polymorphism databases

DMDM281185497.

Proteomic databases

PaxDbP25940.
PRIDEP25940.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264828; ENSP00000264828; ENSG00000080573.
GeneID50509.
KEGGhsa:50509.
UCSCuc002mmq.1. human.

Organism-specific databases

CTD50509.
GeneCardsGC19M010071.
H-InvDBHIX0039977.
HIX0040299.
HGNCHGNC:14864. COL5A3.
HPAHPA048256.
MIM120216. gene.
neXtProtNX_P25940.
PharmGKBPA26726.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000085654.
HOVERGENHBG004933.
InParanoidP25940.
KOK06236.
OMAKGDVGQD.
OrthoDBEOG7XPZ4W.
PhylomeDBP25940.
TreeFamTF323987.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.
REACT_196873. Extracellular matrix organization.

Gene expression databases

BgeeP25940.
CleanExHS_COL5A3.
GenevestigatorP25940.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008160. Collagen.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000885. Fib_collagen_C.
IPR001791. Laminin_G.
[Graphical view]
PfamPF01410. COLFI. 1 hit.
PF01391. Collagen. 6 hits.
[Graphical view]
ProDomPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00038. COLFI. 1 hit.
SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS51461. NC1_FIB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCOL5A3.
GenomeRNAi50509.
NextBio53078.
PROP25940.
SOURCESearch...

Entry information

Entry nameCO5A3_HUMAN
AccessionPrimary (citable) accession number: P25940
Secondary accession number(s): Q9NZQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: December 15, 2009
Last modified: July 9, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM