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P25940

- CO5A3_HUMAN

UniProt

P25940 - CO5A3_HUMAN

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Protein

Collagen alpha-3(V) chain

Gene

COL5A3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. collagen binding Source: UniProtKB
  2. extracellular matrix structural constituent Source: UniProtKB
  3. heparin binding Source: Ensembl

GO - Biological processi

  1. axon guidance Source: Reactome
  2. cell-matrix adhesion Source: Ensembl
  3. collagen catabolic process Source: Reactome
  4. collagen fibril organization Source: UniProtKB
  5. extracellular matrix disassembly Source: Reactome
  6. extracellular matrix organization Source: Reactome
  7. skin development Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_118779. Extracellular matrix organization.
REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_13552. Integrin cell surface interactions.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150401. Collagen degradation.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_163942. Syndecan interactions.
REACT_16888. Signaling by PDGF.
REACT_18312. NCAM1 interactions.
REACT_197897. Syndecan interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-3(V) chain
Gene namesi
Name:COL5A3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:14864. COL5A3.

Subcellular locationi

Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

GO - Cellular componenti

  1. collagen type V trimer Source: UniProtKB
  2. endoplasmic reticulum lumen Source: Reactome
  3. extracellular region Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26726.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence AnalysisAdd
BLAST
Chaini30 – 17451716Collagen alpha-3(V) chainPRO_0000005845Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi102 – 1021N-linked (GlcNAc...)1 Publication
Glycosylationi141 – 1411N-linked (GlcNAc...)1 Publication
Disulfide bondi1544 – 1544InterchainPROSITE-ProRule annotation
Disulfide bondi1567 – 1567InterchainPROSITE-ProRule annotation
Disulfide bondi1576 – 1576InterchainPROSITE-ProRule annotation
Disulfide bondi1585 ↔ 1742PROSITE-ProRule annotation
Disulfide bondi1651 ↔ 1696PROSITE-ProRule annotation

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiP25940.
PRIDEiP25940.

PTM databases

PhosphoSiteiP25940.

Expressioni

Gene expression databases

BgeeiP25940.
CleanExiHS_COL5A3.
GenevestigatoriP25940.

Organism-specific databases

HPAiHPA048256.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

STRINGi9606.ENSP00000264828.

Structurei

3D structure databases

ProteinModelPortaliP25940.
SMRiP25940. Positions 1533-1743.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini62 – 224163Laminin G-likeAdd
BLAST
Domaini391 – 44050Collagen-like 1Add
BLAST
Domaini482 – 53857Collagen-like 2Add
BLAST
Domaini824 – 87754Collagen-like 3Add
BLAST
Domaini905 – 95046Collagen-like 4Add
BLAST
Domaini951 – 98939Collagen-like 5Add
BLAST
Domaini1430 – 148859Collagen-like 6Add
BLAST
Domaini1514 – 1744231Fibrillar collagen NC1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni211 – 391181Nonhelical regionAdd
BLAST
Regioni392 – 14891098Triple-helical regionAdd
BLAST

Sequence similaritiesi

Belongs to the fibrillar collagen family.PROSITE-ProRule annotation
Contains 6 collagen-like domains.Curated
Contains 1 fibrillar collagen NC1 domain.PROSITE-ProRule annotation
Contains 1 laminin G-like domain.Curated

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00760000118776.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiP25940.
KOiK06236.
OMAiKGDVGQD.
OrthoDBiEOG7XPZ4W.
PhylomeDBiP25940.
TreeFamiTF323987.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008160. Collagen.
IPR013320. ConA-like_dom.
IPR000885. Fib_collagen_C.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 6 hits.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS51461. NC1_FIB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25940 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGNRRDLGQP RAGLCLLLAA LQLLPGTQAD PVDVLKALGV QGGQAGVPEG
60 70 80 90 100
PGFCPQRTPE GDRAFRIGQA STLGIPTWEL FPEGHFPENF SLLITLRGQP
110 120 130 140 150
ANQSVLLSIY DERGARQLGL ALGPALGLLG DPFRPLPQQV NLTDGRWHRV
160 170 180 190 200
AVSIDGEMVT LVADCEAQPP VLGHGPRFIS IAGLTVLGTQ DLGEKTFEGD
210 220 230 240 250
IQELLISPDP QAAFQACERY LPDCDNLAPA ATVAPQGEPE TPRPRRKGKG
260 270 280 290 300
KGRKKGRGRK GKGRKKNKEI WTSSPPPDSA ENQTSTDIPK TETPAPNLPP
310 320 330 340 350
TPTPLVVTST VTTGLNATIL ERSLDPDSGT ELGTLETKAA REDEEGDDST
360 370 380 390 400
MGPDFRAAEY PSRTQFQIFP GAGEKGAKGE PAVIEKGQQF EGPPGAPGPQ
410 420 430 440 450
GVVGPSGPPG PPGFPGDPGP PGPAGLPGIP GIDGIRGPPG TVIMMPFQFA
460 470 480 490 500
GGSFKGPPVS FQQAQAQAVL QQTQLSMKGP PGPVGLTGRP GPVGLPGHPG
510 520 530 540 550
LKGEEGAEGP QGPRGLQGPH GPPGRVGKMG RPGADGARGL PGDTGPKGDR
560 570 580 590 600
GFDGLPGLPG EKGQRGDFGH VGQPGPPGED GERGAEGPPG PTGQAGEPGP
610 620 630 640 650
RGLLGPRGSP GPTGRPGVTG IDGAPGAKGN VGPPGEPGPP GQQGNHGSQG
660 670 680 690 700
LPGPQGLIGT PGEKGPPGNP GIPGLPGSDG PLGHPGHEGP TGEKGAQGPP
710 720 730 740 750
GSAGPPGYPG PRGVKGTSGN RGLQGEKGEK GEDGFPGFKG DVGLKGDQGK
760 770 780 790 800
PGAPGPRGED GPEGPKGQAG QAGEEGPPGS AGEKGKLGVP GLPGYPGRPG
810 820 830 840 850
PKGSIGFPGP LGPIGEKGKS GKTGQPGLEG ERGPPGSRGE RGQPGATGQP
860 870 880 890 900
GPKGDVGQDG APGIPGEKGL PGLQGPPGFP GPKGPPGHQG KDGRPGHPGQ
910 920 930 940 950
RGELGFQGQT GPPGPAGVLG PQGKTGEVGP LGERGPPGPP GPPGEQGLPG
960 970 980 990 1000
LEGREGAKGE LGPPGPLGKE GPAGLRGFPG PKGGPGDPGP TGLKGDKGPP
1010 1020 1030 1040 1050
GPVGANGSPG ERGPLGPAGG IGLPGQSGSE GPVGPAGKKG SRGERGPPGP
1060 1070 1080 1090 1100
TGKDGIPGPL GPLGPPGAAG PSGEEGDKGD VGAPGHKGSK GDKGDAGPPG
1110 1120 1130 1140 1150
QPGIRGPAGH PGPPGADGAQ GRRGPPGLFG QKGDDGVRGF VGVIGPPGLQ
1160 1170 1180 1190 1200
GLPGPPGEKG EVGDVGSMGP HGAPGPRGPQ GPTGSEGTPG LPGGVGQPGA
1210 1220 1230 1240 1250
VGEKGERGDA GDPGPPGAPG IPGPKGDIGE KGDSGPSGAA GPPGKKGPPG
1260 1270 1280 1290 1300
EDGAKGSVGP TGLPGDLGPP GDPGVSGIDG SPGEKGDPGD VGGPGPPGAS
1310 1320 1330 1340 1350
GEPGAPGPPG KRGPSGHMGR EGREGEKGAK GEPGPDGPPG RTGPMGARGP
1360 1370 1380 1390 1400
PGRVGPEGLR GIPGPVGEPG LLGAPGQMGP PGPLGPSGLP GLKGDTGPKG
1410 1420 1430 1440 1450
EKGHIGLIGL IGPPGEAGEK GDQGLPGVQG PPGPKGDPGP PGPIGSLGHP
1460 1470 1480 1490 1500
GPPGVAGPLG QKGSKGSPGS MGPRGDTGPA GPPGPPGAPA ELHGLRRRRR
1510 1520 1530 1540 1550
FVPVPLPVVE GGLEEVLASL TSLSLELEQL RRPPGTAERP GLVCHELHRN
1560 1570 1580 1590 1600
HPHLPDGEYW IDPNQGCARD SFRVFCNFTA GGETCLYPDK KFEIVKLASW
1610 1620 1630 1640 1650
SKEKPGGWYS TFRRGKKFSY VDADGSPVNV VQLNFLKLLS ATARQNFTYS
1660 1670 1680 1690 1700
CQNAAAWLDE ATGDYSHSAR FLGTNGEELS FNQTTAATVS VPQDGCRLRK
1710 1720 1730 1740
GQTKTLFEFS SSRAGFLPLW DVAATDFGQT NQKFGFELGP VCFSS
Length:1,745
Mass (Da):172,121
Last modified:December 15, 2009 - v3
Checksum:i4F5644D2A919D864
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1687 – 16871A → T in AAF59902. (PubMed:10722718)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti134 – 1341R → H.
Corresponds to variant rs2303098 [ dbSNP | Ensembl ].
VAR_020015
Natural varianti322 – 3221R → G.1 Publication
Corresponds to variant rs2287803 [ dbSNP | Ensembl ].
VAR_060789
Natural varianti1042 – 10421R → P.
Corresponds to variant rs2161468 [ dbSNP | Ensembl ].
VAR_055678
Natural varianti1207 – 12071R → P.
Corresponds to variant rs2287813 [ dbSNP | Ensembl ].
VAR_020016
Natural varianti1428 – 14281V → M.
Corresponds to variant rs3815746 [ dbSNP | Ensembl ].
VAR_020017
Natural varianti1488 – 14881A → P.
Corresponds to variant rs3745584 [ dbSNP | Ensembl ].
VAR_055679
Natural varianti1594 – 15941I → M.
Corresponds to variant rs3745581 [ dbSNP | Ensembl ].
VAR_020018
Natural varianti1691 – 16911V → I.
Corresponds to variant rs2277969 [ dbSNP | Ensembl ].
VAR_020019

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF177941 mRNA. Translation: AAF59902.1.
AC008742 Genomic DNA. No translation available.
CCDSiCCDS12222.1.
PIRiS20375.
RefSeqiNP_056534.2. NM_015719.3.
UniGeneiHs.235368.

Genome annotation databases

EnsembliENST00000264828; ENSP00000264828; ENSG00000080573.
GeneIDi50509.
KEGGihsa:50509.
UCSCiuc002mmq.1. human.

Polymorphism databases

DMDMi281185497.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF177941 mRNA. Translation: AAF59902.1 .
AC008742 Genomic DNA. No translation available.
CCDSi CCDS12222.1.
PIRi S20375.
RefSeqi NP_056534.2. NM_015719.3.
UniGenei Hs.235368.

3D structure databases

ProteinModelPortali P25940.
SMRi P25940. Positions 1533-1743.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000264828.

Chemistry

ChEMBLi CHEMBL2364188.

PTM databases

PhosphoSitei P25940.

Polymorphism databases

DMDMi 281185497.

Proteomic databases

PaxDbi P25940.
PRIDEi P25940.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264828 ; ENSP00000264828 ; ENSG00000080573 .
GeneIDi 50509.
KEGGi hsa:50509.
UCSCi uc002mmq.1. human.

Organism-specific databases

CTDi 50509.
GeneCardsi GC19M010071.
H-InvDB HIX0039977.
HIX0040299.
HGNCi HGNC:14864. COL5A3.
HPAi HPA048256.
MIMi 120216. gene.
neXtProti NX_P25940.
PharmGKBi PA26726.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00760000118776.
HOGENOMi HOG000085654.
HOVERGENi HBG004933.
InParanoidi P25940.
KOi K06236.
OMAi KGDVGQD.
OrthoDBi EOG7XPZ4W.
PhylomeDBi P25940.
TreeFami TF323987.

Enzyme and pathway databases

Reactomei REACT_118779. Extracellular matrix organization.
REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_13552. Integrin cell surface interactions.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150401. Collagen degradation.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_163942. Syndecan interactions.
REACT_16888. Signaling by PDGF.
REACT_18312. NCAM1 interactions.
REACT_197897. Syndecan interactions.

Miscellaneous databases

GeneWikii COL5A3.
GenomeRNAii 50509.
NextBioi 53078.
PROi P25940.
SOURCEi Search...

Gene expression databases

Bgeei P25940.
CleanExi HS_COL5A3.
Genevestigatori P25940.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR008160. Collagen.
IPR013320. ConA-like_dom.
IPR000885. Fib_collagen_C.
IPR001791. Laminin_G.
[Graphical view ]
Pfami PF01410. COLFI. 1 hit.
PF01391. Collagen. 6 hits.
[Graphical view ]
ProDomi PD002078. Fib_collagen_C. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00038. COLFI. 1 hit.
SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
PROSITEi PS51461. NC1_FIB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiCO5A3_HUMAN
AccessioniPrimary (citable) accession number: P25940
Secondary accession number(s): Q9NZQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: December 15, 2009
Last modified: October 29, 2014
This is version 136 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3