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Protein

Collagen alpha-2(V) chain

Gene

Col5a2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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

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

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: GO_Central
  • extracellular matrix structural constituent conferring tensile strength Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • SMAD binding Source: MGI

GO - Biological processi

Keywordsi

LigandCalcium, 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
R-MMU-8948216 Collagen chain trimerization

Names & Taxonomyi

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

Organism-specific databases

MGIiMGI:88458 Col5a2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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...) asparagineSequence analysis1
Disulfide bondi1294 ↔ 1326PROSITE-ProRule annotation
Disulfide bondi1334 ↔ 1495PROSITE-ProRule annotation
Glycosylationi1398N-linked (GlcNAc...) asparagineSequence 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

iPTMnetiQ3U962
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 Expressed in 303 organ(s), highest expression level in vault of skull
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

Protein-protein interaction databases

ComplexPortaliCPX-2962 Collagen type V trimer variant 1
CPX-2963 Collagen type V trimer variant 2
CPX-2976 Collagen type XI trimer variant 2
CPX-2977 Collagen type XI trimer variant 3
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

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3544 Eukaryota
ENOG4110XTV LUCA
GeneTreeiENSGT00900000140789
HOVERGENiHBG004933
InParanoidiQ3U962
KOiK19721
OMAiPNAAITQ
OrthoDBiEOG091G03LV
PhylomeDBiQ3U962
TreeFamiTF344135

Family and domain databases

InterProiView protein in InterPro
IPR008160 Collagen
IPR000885 Fib_collagen_C
IPR001007 VWF_dom
PfamiView protein in Pfam
PF01410 COLFI, 1 hit
PF01391 Collagen, 6 hits
PF00093 VWC, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD002078 Fib_collagen_C, 1 hit
SMARTiView protein in SMART
SM00038 COLFI, 1 hit
SM00214 VWC, 1 hit
PROSITEiView protein in PROSITE
PS51461 NC1_FIB, 1 hit
PS01208 VWFC_1, 1 hit
PS50184 VWFC_2, 1 hit

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

Similar proteinsi

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

ComplexPortaliCPX-2962 Collagen type V trimer variant 1
CPX-2963 Collagen type V trimer variant 2
CPX-2976 Collagen type XI trimer variant 2
CPX-2977 Collagen type XI trimer variant 3
STRINGi10090.ENSMUSP00000083620

PTM databases

iPTMnetiQ3U962
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
GeneTreeiENSGT00900000140789
HOVERGENiHBG004933
InParanoidiQ3U962
KOiK19721
OMAiPNAAITQ
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
R-MMU-8948216 Collagen chain trimerization

Miscellaneous databases

ChiTaRSiCol5a2 mouse
PROiPR:Q3U962
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026042 Expressed in 303 organ(s), highest expression level in vault of skull
CleanExiMM_COL5A2
GenevisibleiQ3U962 MM

Family and domain databases

InterProiView protein in InterPro
IPR008160 Collagen
IPR000885 Fib_collagen_C
IPR001007 VWF_dom
PfamiView protein in Pfam
PF01410 COLFI, 1 hit
PF01391 Collagen, 6 hits
PF00093 VWC, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD002078 Fib_collagen_C, 1 hit
SMARTiView protein in SMART
SM00038 COLFI, 1 hit
SM00214 VWC, 1 hit
PROSITEiView protein in PROSITE
PS51461 NC1_FIB, 1 hit
PS01208 VWFC_1, 1 hit
PS50184 VWFC_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCO5A2_MOUSE
AccessioniPrimary (citable) accession number: Q3U962
Secondary accession number(s): Q3TVR2
, Q3UHK7, Q3UTT4, Q3V1J6, Q61431, Q7TMS0, Q80VS8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: October 11, 2005
Last modified: November 7, 2018
This is version 100 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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Main funding by: National Institutes of Health

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