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Protein

Collagen alpha-2(V) chain

Gene

Col5a2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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. Type V collagen is a key determinant in the assembly of tissue-specific matrices.By similarity3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi1312CalciumBy similarity1
Metal bindingi1314CalciumBy similarity1
Metal bindingi1315Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1320CalciumBy similarity1

GO - Molecular functioni

  • extracellular matrix structural constituent Source: InterPro
  • metal ion binding Source: UniProtKB-KW
  • SMAD binding Source: MGI

GO - Biological processi

  • cellular response to amino acid stimulus Source: MGI
  • collagen fibril organization Source: UniProtKB
  • eye morphogenesis Source: MGI
  • negative regulation of endodermal cell differentiation Source: MGI
  • ossification Source: Ensembl
  • skeletal system development Source: MGI
  • skin development Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-1442490. Collagen degradation.
R-MMU-1474244. Extracellular matrix organization.
R-MMU-1650814. Collagen biosynthesis and modifying enzymes.
R-MMU-186797. Signaling by PDGF.
R-MMU-2022090. Assembly of collagen fibrils and other multimeric structures.
R-MMU-216083. Integrin cell surface interactions.
R-MMU-3000171. Non-integrin membrane-ECM interactions.
R-MMU-3000178. ECM proteoglycans.
R-MMU-419037. NCAM1 interactions.
R-MMU-8874081. MET activates PTK2 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-2(V) chain
Gene namesi
Name:Col5a2Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:88458. Col5a2.

Subcellular locationi

GO - Cellular componenti

  • collagen trimer Source: MGI
  • collagen type V trimer Source: MGI
  • extracellular matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
ChainiPRO_000028376827 – 1227Collagen alpha-2(V) chainSequence analysisAdd BLAST1201
PropeptideiPRO_00002837691228 – 1497C-terminal propeptideSequence analysisAdd BLAST270

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2884-hydroxyprolineBy similarity1
Modified residuei2914-hydroxyprolineBy similarity1
Modified residuei2944-hydroxyprolineBy similarity1
Modified residuei6094-hydroxyprolineBy similarity1
Modified residuei6154-hydroxyprolineBy similarity1
Glycosylationi1260N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1294 ↔ 1326PROSITE-ProRule annotation
Disulfide bondi1334 ↔ 1495PROSITE-ProRule annotation
Glycosylationi1398N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1403 ↔ 1448PROSITE-ProRule annotation

Post-translational modificationi

Prolines at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Probably 3-hydroxylated on prolines by LEPREL1.
Hydroxylation on proline residues within the sequence motif, GXPG, is most likely to be 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

MaxQBiQ3U962.
PaxDbiQ3U962.
PeptideAtlasiQ3U962.
PRIDEiQ3U962.

PTM databases

PhosphoSitePlusiQ3U962.

Expressioni

Developmental stagei

Expressed in embryos from 9 days of gestation onward. In 12.5 dpc embryos, low and diffuse level of expression was observed in the peritoneal membranes and intestinal and craniofacial mesenchymes. By 16.5 dpc, expression is higher and exhibits a more restricted accumulation in primary ossified regions, perichondrium, joints, tendon, atrioventricular valve of heart, and in selected portions of the head.1 Publication

Gene expression databases

BgeeiENSMUSG00000026042.
CleanExiMM_COL5A2.
GenevisibleiQ3U962. MM.

Interactioni

Subunit structurei

Trimers of two alpha 1(V) and one alpha 2(V) chains expressed in most tissues and trimers of one alpha 1(V), one alpha 2(V), and one alpha 3(V) chains with a more limited distribution of expression.By similarity1 Publication

GO - Molecular functioni

  • SMAD binding Source: MGI

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000083620.

Structurei

3D structure databases

ProteinModelPortaliQ3U962.
SMRiQ3U962.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini38 – 96VWFCPROSITE-ProRule annotationAdd BLAST59
Domaini1264 – 1497Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST234

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi141 – 143Cell attachment siteSequence analysis3
Motifi504 – 506Cell attachment siteSequence analysis3
Motifi942 – 944Cell attachment siteSequence analysis3
Motifi1065 – 1067Cell attachment siteSequence analysis3
Motifi1068 – 1070Cell attachment siteSequence analysis3
Motifi1125 – 1127Cell attachment siteSequence analysis3
Motifi1134 – 1136Cell attachment siteSequence analysis3

Domaini

The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function (By similarity).By similarity

Sequence similaritiesi

Belongs to the fibrillar collagen family.PROSITE-ProRule annotation
Contains 1 fibrillar collagen NC1 domain.PROSITE-ProRule annotation
Contains 1 VWFC domain.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG4110XTV. LUCA.
GeneTreeiENSGT00840000129673.
HOVERGENiHBG004933.
InParanoidiQ3U962.
KOiK19721.
OMAiIGIRGQP.
OrthoDBiEOG091G03LV.
PhylomeDBiQ3U962.
TreeFamiTF344135.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR001007. VWF_dom.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 6 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEiPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q3U962-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMANWVGARP LLILSVLLGY CVSIKAQEQE NDEYDEEIAC TQHGQMYLNR
60 70 80 90 100
DIWKPSPCQI CVCDNGAILC DKIECPEVLN CANPITPTGE CCPVCPQTGG
110 120 130 140 150
GDTSFGRGRK GQKGEPGLVP VVTGIRGRPG PAGPPGSQGP RGDRGPKGRP
160 170 180 190 200
GPRGPQGIDG EPGVPGQPGA PGPPGHPSHP GPDGMSRPFS AQMAGLDEKS
210 220 230 240 250
GLGSQVGLMP GSVGPVGPRG PQGLQGQQGG VGPAGPPGEP GEPGPMGPIG
260 270 280 290 300
SRGPEGPPGK PGEDGEPGRN GNTGEVGFSG SPGARGFPGA PGLPGLKGHR
310 320 330 340 350
GHKGLEGPKG EIGAPGAKGE AGPTGPMGAM GPLGPRGMPG ERGRLGPQGA
360 370 380 390 400
PGKRGAHGMP GKPGPMGPLG IPGSSGFPGN PGMKGEAGPT GARGPEGPQG
410 420 430 440 450
QRGETGPPGP AGSQGLPGAV GTDGTPGAKG PTGSAGTSGP PGLAGPPGSP
460 470 480 490 500
GPQGSTGPQG IRGQSGDPGV PGFKGEAGPK GEPGPHGIQG PIGPPGEEGK
510 520 530 540 550
RGPRGDPGTV GPPGPMGERG APGNRGFPGS DGLPGPKGAQ GERGPVGSSG
560 570 580 590 600
PKGGQGDPGR PGEPGLPGAR GLTGNPGVQG PEGKLGPLGA PGEDGRPGPP
610 620 630 640 650
GSIGIRGQPG SMGLPGPKGS SGDLGKPGEA GNAGVPGQRG APGKDGEVGP
660 670 680 690 700
SGPVGPPGLA GERGEQGPPG PTGFQGLPGP PGPPGEGGKA GDQGVPGEPG
710 720 730 740 750
AVGPLGPRGE RGNPGERGEP GITGLPGEKG MAGGHGPDGP KGNPGPTGTI
760 770 780 790 800
GDTGPPGLQG MPGERGIAGT PGPKGDRGGI GEKGAEGTAG NDGARGLPGP
810 820 830 840 850
LGPPGPAGPT GEKGEPGPRG LVGPPGSRGN PGSRGENGPT GAVGFAGPQG
860 870 880 890 900
PDGQPGVKGE PGEPGQKGDA GSPGPQGLAG SPGPHGPHGV PGLKGGRGTQ
910 920 930 940 950
GPPGATGFPG SAGRVGPPGP AGAPGPAGPA GEPGKEGPPG LRGDPGSHGR
960 970 980 990 1000
VGDRGPAGPP GSPGDKGDPG EDGQPGPDGP PGPAGTTGQR GIVGMPGQRG
1010 1020 1030 1040 1050
ERGMPGLPGP AGTPGKVGPT GATGDKGPPG PVGPPGSNGP VGEPGPEGPA
1060 1070 1080 1090 1100
GNDGTPGRDG AVGERGDRGD PGPAGLPGSQ GAPGTPGPVG APGDAGQRGE
1110 1120 1130 1140 1150
PGSRGPVGPP GRAGKRGLPG PQGPRGDKGD NGDRGDRGQK GHRGFTGLQG
1160 1170 1180 1190 1200
LPGPPGPNGE QGSAGIPGPF GPRGPPGPVG PSGKEGNPGP LGPIGPPGVR
1210 1220 1230 1240 1250
GSVGEAGPEG PPGEPGPPGP PGPPGHLTAA LGDIMGHYDE NMPDPLPEFT
1260 1270 1280 1290 1300
EDQAAPDDTN KTDPGIHVTL KSLSSQIETM RSPDGSKKHP ARTCDDLKLC
1310 1320 1330 1340 1350
HPTKQSGEYW IDPNQGSAED AIKVYCNMET GETCISANPA SVPRKTWWAS
1360 1370 1380 1390 1400
KSPDNKPVWY GLDMNRGSQF TYGDYQSPNT AITQMTFLRL LSKEASQNLT
1410 1420 1430 1440 1450
YICRNTVGYM DDQAKNLKKA VVLKGSNDLE IKGEGNIRFR YTVLQDTCSK
1460 1470 1480 1490
RNGNVGKTIF EYRTQNVARL PIIDVGPVDI GNADQEFGLD IGPVCFM
Length:1,497
Mass (Da):145,018
Last modified:October 11, 2005 - v1
Checksum:iCAAE15514984DB41
GO

Sequence cautioni

The sequence BAE23896 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti20Y → D in BAE23896 (PubMed:16141072).Curated1
Sequence conflicti88T → P in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti160G → R in BAE27850 (PubMed:16141072).Curated1
Sequence conflicti164V → M in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti222Q → V in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti231V → A in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti387A → R in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti390T → H in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti428A → R in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti431P → A in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti614L → V in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti614L → V in AAH55077 (PubMed:15489334).Curated1
Sequence conflicti666Q → A in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti809 – 813PTGEK → LLGAP in AAA37440 (PubMed:1297453).Curated5
Sequence conflicti851P → S in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti1001 – 1002ER → VT in AAA37440 (PubMed:1297453).Curated2
Sequence conflicti1013T → A in AAH55077 (PubMed:15489334).Curated1
Sequence conflicti1063G → V in BAE21154 (PubMed:16141072).Curated1
Sequence conflicti1181P → S in AAA37440 (PubMed:1297453).Curated1
Sequence conflicti1337A → T in AAH55077 (PubMed:15489334).Curated1
Sequence conflicti1388L → F in AAA37440 (PubMed:1297453).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02918 mRNA. Translation: AAA37440.1.
AK132413 mRNA. Translation: BAE21154.1.
AK139130 mRNA. Translation: BAE23896.1. Different initiation.
AK147220 mRNA. Translation: BAE27775.1.
AK147328 mRNA. Translation: BAE27850.1.
AK151929 mRNA. Translation: BAE30805.1.
AK160008 mRNA. Translation: BAE35556.1.
BC043696 mRNA. Translation: AAH43696.1.
BC055077 mRNA. Translation: AAH55077.1.
CCDSiCCDS35555.1.
PIRiI49607.
RefSeqiNP_031763.2. NM_007737.2.
UniGeneiMm.10299.

Genome annotation databases

EnsembliENSMUST00000086430; ENSMUSP00000083620; ENSMUSG00000026042.
GeneIDi12832.
KEGGimmu:12832.
UCSCiuc007awr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02918 mRNA. Translation: AAA37440.1.
AK132413 mRNA. Translation: BAE21154.1.
AK139130 mRNA. Translation: BAE23896.1. Different initiation.
AK147220 mRNA. Translation: BAE27775.1.
AK147328 mRNA. Translation: BAE27850.1.
AK151929 mRNA. Translation: BAE30805.1.
AK160008 mRNA. Translation: BAE35556.1.
BC043696 mRNA. Translation: AAH43696.1.
BC055077 mRNA. Translation: AAH55077.1.
CCDSiCCDS35555.1.
PIRiI49607.
RefSeqiNP_031763.2. NM_007737.2.
UniGeneiMm.10299.

3D structure databases

ProteinModelPortaliQ3U962.
SMRiQ3U962.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000083620.

PTM databases

PhosphoSitePlusiQ3U962.

Proteomic databases

MaxQBiQ3U962.
PaxDbiQ3U962.
PeptideAtlasiQ3U962.
PRIDEiQ3U962.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000086430; ENSMUSP00000083620; ENSMUSG00000026042.
GeneIDi12832.
KEGGimmu:12832.
UCSCiuc007awr.1. mouse.

Organism-specific databases

CTDi1290.
MGIiMGI:88458. Col5a2.

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG4110XTV. LUCA.
GeneTreeiENSGT00840000129673.
HOVERGENiHBG004933.
InParanoidiQ3U962.
KOiK19721.
OMAiIGIRGQP.
OrthoDBiEOG091G03LV.
PhylomeDBiQ3U962.
TreeFamiTF344135.

Enzyme and pathway databases

ReactomeiR-MMU-1442490. Collagen degradation.
R-MMU-1474244. Extracellular matrix organization.
R-MMU-1650814. Collagen biosynthesis and modifying enzymes.
R-MMU-186797. Signaling by PDGF.
R-MMU-2022090. Assembly of collagen fibrils and other multimeric structures.
R-MMU-216083. Integrin cell surface interactions.
R-MMU-3000171. Non-integrin membrane-ECM interactions.
R-MMU-3000178. ECM proteoglycans.
R-MMU-419037. NCAM1 interactions.
R-MMU-8874081. MET activates PTK2 signaling.

Miscellaneous databases

ChiTaRSiCol5a2. mouse.
PROiQ3U962.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026042.
CleanExiMM_COL5A2.
GenevisibleiQ3U962. MM.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR001007. VWF_dom.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 6 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEiPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCO5A2_MOUSE
AccessioniPrimary (citable) accession number: Q3U962
Secondary accession number(s): Q3TVR2
, Q3UHK7, Q3UTT4, Q3V1J6, Q61431, Q7TMS0, Q80VS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: October 11, 2005
Last modified: November 30, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Mice homozygous for the targeted deletion of the N-terminal telopeptide segment of the COL5A2 chain show poor survival rates, possibly because of complications from spinal deformities, and exhibit skin and eye abnormalities caused by disorganized type I collagen fibrils.3 Publications
The alpha 1(V)-alpha 1(V)-alpha 2(V) heterotrimer makes a critical contribution to fibrillogenesis, basement membrane organization, and cell viability, and may play a possible role in the development of a functional skin matrix.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.