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Protein

Collagen alpha-1(V) chain

Gene

Col5a1

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 (By similarity). Transcriptionally activated by CEBPZ, which recognizes a CCAAT-like motif, CAAAT in the COL5A1 promoter.By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

  • blood vessel development Source: MGI
  • cell adhesion Source: MGI
  • cell migration Source: MGI
  • collagen biosynthetic process Source: MGI
  • collagen fibril organization Source: MGI
  • extracellular fibril organization Source: MGI
  • eye morphogenesis Source: MGI
  • heart morphogenesis Source: MGI
  • integrin biosynthetic process Source: MGI
  • negative regulation of endodermal cell differentiation Source: MGI
  • regulation of cellular component organization Source: MGI
  • skin development Source: MGI
  • tendon development Source: MGI
  • wound healing, spreading of epidermal cells Source: MGI
Complete GO annotation...

Keywords - Ligandi

Heparin-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-1(V) chain
Gene namesi
Name:Col5a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:88457. Col5a1.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: MGI
  • collagen trimer Source: MGI
  • collagen type V trimer Source: MGI
  • extracellular exosome Source: MGI
  • extracellular matrix Source: UniProtKB
  • proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 36Sequence analysisAdd BLAST36
ChainiPRO_000004176137 – 1838Collagen alpha-1(V) chainAdd BLAST1802

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei234SulfotyrosineSequence analysis1
Modified residuei236SulfotyrosineSequence analysis1
Modified residuei240SulfotyrosineSequence analysis1
Modified residuei262SulfotyrosineSequence analysis1
Modified residuei263SulfotyrosineSequence analysis1
Modified residuei5704-hydroxyprolineBy similarity1
Modified residuei5764-hydroxyprolineBy similarity1
Modified residuei6214-hydroxyprolineBy similarity1
Modified residuei6275-hydroxylysineBy similarity1
Modified residuei6394-hydroxyprolineBy similarity1
Modified residuei6425-hydroxylysineBy similarity1
Modified residuei6484-hydroxyprolineBy similarity1
Modified residuei6544-hydroxyprolineBy similarity1
Modified residuei6574-hydroxyprolineBy similarity1
Modified residuei6754-hydroxyprolineBy similarity1
Modified residuei6784-hydroxyprolineBy similarity1
Modified residuei6803-hydroxyprolineBy similarity1
Modified residuei6863-hydroxyprolineBy similarity1
Modified residuei6904-hydroxyprolineBy similarity1
Modified residuei6964-hydroxyprolineBy similarity1
Modified residuei7054-hydroxyprolineBy similarity1
Modified residuei7085-hydroxylysineBy similarity1
Modified residuei7174-hydroxyprolineBy similarity1
Modified residuei7204-hydroxyprolineBy similarity1
Modified residuei7264-hydroxyprolineBy similarity1
Modified residuei7324-hydroxyprolineBy similarity1
Modified residuei7445-hydroxylysineBy similarity1
Modified residuei7504-hydroxyprolineBy similarity1
Modified residuei7564-hydroxyprolineBy similarity1
Modified residuei7624-hydroxyprolineBy similarity1
Modified residuei7654-hydroxyprolineBy similarity1
Modified residuei7714-hydroxyprolineBy similarity1
Modified residuei7745-hydroxylysineBy similarity1
Modified residuei7804-hydroxyprolineBy similarity1
Modified residuei7894-hydroxyprolineBy similarity1
Modified residuei7955-hydroxylysineBy similarity1
Modified residuei8045-hydroxylysineBy similarity1
Modified residuei8075-hydroxylysineBy similarity1
Modified residuei8105-hydroxylysineBy similarity1
Modified residuei8164-hydroxyprolineBy similarity1
Modified residuei8195-hydroxylysineBy similarity1
Modified residuei8344-hydroxyprolineBy similarity1
Modified residuei8465-hydroxylysineBy similarity1
Modified residuei8645-hydroxylysineBy similarity1
Modified residuei8704-hydroxyprolineBy similarity1
Modified residuei8734-hydroxyprolineBy similarity1
Modified residuei8764-hydroxyprolineBy similarity1
Modified residuei8825-hydroxylysineBy similarity1
Modified residuei8884-hydroxyprolineBy similarity1
Modified residuei8914-hydroxyprolineBy similarity1
Modified residuei8975-hydroxylysineBy similarity1
Modified residuei9034-hydroxyprolineBy similarity1
Modified residuei9064-hydroxyprolineBy similarity1
Modified residuei9304-hydroxyprolineBy similarity1
Modified residuei9454-hydroxyprolineBy similarity1
Modified residuei10174-hydroxyprolineBy similarity1
Modified residuei10204-hydroxyprolineBy similarity1
Modified residuei10234-hydroxyprolineBy similarity1
Modified residuei10294-hydroxyprolineBy similarity1
Modified residuei12214-hydroxyprolineBy similarity1
Modified residuei12244-hydroxyprolineBy similarity1
Modified residuei14674-hydroxyprolineBy similarity1
Modified residuei14704-hydroxyprolineBy similarity1
Modified residuei1601SulfotyrosineSequence analysis1
Modified residuei1604SulfotyrosineSequence analysis1

Post-translational modificationi

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
Sulfated on 40% of tyrosines.By similarity

Keywords - PTMi

Hydroxylation, Sulfation

Proteomic databases

MaxQBiO88207.
PaxDbiO88207.
PeptideAtlasiO88207.
PRIDEiO88207.

PTM databases

iPTMnetiO88207.
PhosphoSitePlusiO88207.

Expressioni

Tissue specificityi

Expressed in limbs, vertebrae, heart, brain, liver, intestine, tongue, tail, skin, calvaria, lung and kidney of E18 embryos.1 Publication

Developmental stagei

Detected at E11, E12, E14, E16 and E18.1 Publication

Gene expression databases

BgeeiENSMUSG00000026837.
CleanExiMM_COL5A1.
ExpressionAtlasiO88207. baseline and differential.
GenevisibleiO88207. MM.

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. Interacts with CSPG4 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198821. 5 interactors.
IntActiO88207. 1 interactor.
STRINGi10090.ENSMUSP00000028280.

Structurei

3D structure databases

ProteinModelPortaliO88207.
SMRiO88207.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini72 – 244Laminin G-likeAdd BLAST173
Domaini1609 – 1837Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST229

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni231 – 443Nonhelical regionBy similarityAdd BLAST213
Regioni444 – 558Interrupted collagenous regionBy similarityAdd BLAST115
Regioni559 – 1570Triple-helical regionBy similarityAdd BLAST1012
Regioni1571 – 1605Nonhelical regionBy similarityAdd BLAST35

Sequence similaritiesi

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

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
GeneTreeiENSGT00840000129673.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiO88207.
KOiK19721.
OMAiPIGVVQM.
OrthoDBiEOG091G01AE.
PhylomeDBiO88207.
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. 4 hits.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 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.

O88207-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVHTRWKAA RPGALLLSSP LLLFLLLLWA PPSSRAAQPA DLLEMLDFHN
60 70 80 90 100
LPSGVTKTTG FCATRRSSSE PDVAYRVSKD AQLSMPTKQL YPESGFPEDF
110 120 130 140 150
SILTTVKAKK GSQAFLVSIY NEQGIQQLGL ELGRSPVFLY EDHTGKPGPE
160 170 180 190 200
EYPLFPGINL SDGKWHRIAL SVYKKNVTLI LDCKKKITKF LSRSDHPIID
210 220 230 240 250
TNGIVMFGSR ILDDEIFEGD IQQLLFVSDN RAAYDYCEHY SPDCDTAVPD
260 270 280 290 300
TPQSQDPNPD EYYPEGEGET YYYEYPYYED PEDPGKEPAP TQKPVEAARE
310 320 330 340 350
TTEVPEEQTQ PLPEAPTVPE TSDTADKEDS LGIGDYDYVP PDDYYTPPPY
360 370 380 390 400
EDFGYGEGVE NPDQPTNPDS GAEVPTSTTV TSNTSNPAPG EGKDDLGGEF
410 420 430 440 450
TEETIKNLEE NYYDPYFDPD SDSSVSPSEI GPGMPANQDT IFEGIGGPRG
460 470 480 490 500
EKGQKGEPAI IEPGMLIEGP PGPEGPAGLP GPPGTTGPTG QMGDPGERGP
510 520 530 540 550
PGRPGLPGAD GLPGPPGTML MLPFRFGGGG DAGSKGPMVS AQESQAQAIL
560 570 580 590 600
QQARLALRGP AGPMGLTGRP GPMGPPGSGG LKGEPGDMGP QGPRGVQGPP
610 620 630 640 650
GPTGKPGRRG RAGSDGARGM PGQTGPKGDR GFDGLAGLPG EKGHRGDPGP
660 670 680 690 700
SGPPGIPGDD GERGDDGEVG PRGLPGEPGP RGLLGPKGPP GPPGPPGVTG
710 720 730 740 750
MDGQPGPKGN VGPQGEPGPP GQQGNPGAQG LPGPQGAIGP PGEKGPLGKP
760 770 780 790 800
GLPGMPGADG PPGHPGKEGP PGEKGGQGPP GPQGPIGYPG PRGVKGADGI
810 820 830 840 850
RGLKGTKGEK GEDGFPGFKG DMGIKGDRGE IGPPGPRGED GPEGPKGRGG
860 870 880 890 900
PNGDPGPLGP TGEKGKLGVP GLPGYPGRQG PKGSIGFPGF PGANGEKGGR
910 920 930 940 950
GTPGKPGPRG QRGPTGPRGE RGPRGITGKP GPKGNSGGDG PAGPPGERGP
960 970 980 990 1000
NGPQGPTGFP GPKGPPGPPG KDGLPGHPGQ RGETGFQGKT GPPGPPGVVG
1010 1020 1030 1040 1050
PQGPTGETGP MGERGHPGPP GPPGEQGLPG AAGKEGTKGD PGPAGLPGKD
1060 1070 1080 1090 1100
GPPGLRGFPG DRGLPGPVGA LGLKGSEGPP GPPGPAGSPG ERGPAGAAGP
1110 1120 1130 1140 1150
IGIPGRPGPQ GPPGPAGEKG LPGEKGPQGP AGRDGLQGPV GLPGPAGPVG
1160 1170 1180 1190 1200
PPGEDGDKGE IGEPGQKGSK GDKGEQGPPG PTGPQGPIGQ PGPSGADGEP
1210 1220 1230 1240 1250
GPRGQQGLFG QKGDEGSRGF PGPPGPVGLQ GLPGPPGEKG ETGDVGQMGP
1260 1270 1280 1290 1300
PGPPGPRGPS GAPGADGPQG PPGGIGNPGA VGEKGEPGEA GDPGLPGEGG
1310 1320 1330 1340 1350
PLGPKGERGE KGEAGPSGAA GPPGPKGPPG DDGPKGSPGP VGFPGDPGPP
1360 1370 1380 1390 1400
GEPGPAGQDG PPGDKGDDGE PGQTGSPGPT GEPGPSGPPG KRGPPGPAGP
1410 1420 1430 1440 1450
EGRQGEKGAK GEAGLEGPPG KTGPIGPQGA PGKPGPDGLR GIPGPVGEQG
1460 1470 1480 1490 1500
LPGSPGPDGP PGPMGPPGLP GLKGDSGPKG EKGHPGLIGL IGPPGEQGEK
1510 1520 1530 1540 1550
GDRGLPGPQG SSGPKGDQGI TGPSGPLGPP GPPGLPGPPG PKGAKGSSGP
1560 1570 1580 1590 1600
TGPKGEAGHP GLPGPPGPPG EVIQPLPIQA SRTRRNIDAS QLLDDGAGES
1610 1620 1630 1640 1650
YVDYADGMEE IFGSLNSLKL EIEQMKRPLG TQQNPARTCK DLQLCHPDFP
1660 1670 1680 1690 1700
DGEYWVDPNQ GCSRDSFKVY CNFTAGGSTC VFPDKKSEGA RITSWPKENP
1710 1720 1730 1740 1750
GSWFSEFKRG KLLSYVDAEG NPVGVVQMTF LRLLSASAHQ NVTYNCYQSV
1760 1770 1780 1790 1800
AWQDAATGSY DKAIRFLGSN DEEMSYDNNP YIRALVDGCA TKKGYQKTVL
1810 1820 1830
EIDTPKVEQV PIVDIMFNDF GEASQKFGFE VGPACFLG
Length:1,838
Mass (Da):183,677
Last modified:February 6, 2007 - v2
Checksum:iD20F4E5198A09ECF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1097A → S in BAA28786 (PubMed:9582436).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009993 mRNA. Translation: BAA28786.1.
AL731778, AL732513 Genomic DNA. Translation: CAM46247.1.
AB098608 Genomic DNA. Translation: BAD26732.1.
AK148055 mRNA. Translation: BAE28315.1.
CCDSiCCDS15831.1.
RefSeqiNP_056549.2. NM_015734.2.
UniGeneiMm.7281.

Genome annotation databases

EnsembliENSMUST00000028280; ENSMUSP00000028280; ENSMUSG00000026837.
GeneIDi12831.
KEGGimmu:12831.
UCSCiuc008ixt.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009993 mRNA. Translation: BAA28786.1.
AL731778, AL732513 Genomic DNA. Translation: CAM46247.1.
AB098608 Genomic DNA. Translation: BAD26732.1.
AK148055 mRNA. Translation: BAE28315.1.
CCDSiCCDS15831.1.
RefSeqiNP_056549.2. NM_015734.2.
UniGeneiMm.7281.

3D structure databases

ProteinModelPortaliO88207.
SMRiO88207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198821. 5 interactors.
IntActiO88207. 1 interactor.
STRINGi10090.ENSMUSP00000028280.

PTM databases

iPTMnetiO88207.
PhosphoSitePlusiO88207.

Proteomic databases

MaxQBiO88207.
PaxDbiO88207.
PeptideAtlasiO88207.
PRIDEiO88207.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028280; ENSMUSP00000028280; ENSMUSG00000026837.
GeneIDi12831.
KEGGimmu:12831.
UCSCiuc008ixt.2. mouse.

Organism-specific databases

CTDi1289.
MGIiMGI:88457. Col5a1.

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
GeneTreeiENSGT00840000129673.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiO88207.
KOiK19721.
OMAiPIGVVQM.
OrthoDBiEOG091G01AE.
PhylomeDBiO88207.
TreeFamiTF323987.

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

ChiTaRSiCol5a1. mouse.
PROiO88207.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026837.
CleanExiMM_COL5A1.
ExpressionAtlasiO88207. baseline and differential.
GenevisibleiO88207. MM.

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. 4 hits.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS51461. NC1_FIB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCO5A1_MOUSE
AccessioniPrimary (citable) accession number: O88207
Secondary accession number(s): A3KGE3, Q3UG94, Q6F6B0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: February 6, 2007
Last modified: November 30, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.