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Q9JI03

- CO5A1_RAT

UniProt

Q9JI03 - CO5A1_RAT

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Protein
Collagen alpha-1(V) chain
Gene
Col5a1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 3 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.

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: InterPro
  2. heparin binding Source: RGD
Complete GO annotation...

Keywords - Ligandi

Heparin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(V) chain
Gene namesi
Name:Col5a1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi70920. Col5a1.

Subcellular locationi

GO - Cellular componenti

  1. collagen type V trimer Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030 Reviewed prediction
Add
BLAST
Chaini31 – 18401810Collagen alpha-1(V) chain
PRO_0000041762Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei234 – 2341Sulfotyrosine Reviewed prediction
Modified residuei236 – 2361Sulfotyrosine Reviewed prediction
Modified residuei240 – 2401Sulfotyrosine Reviewed prediction
Modified residuei262 – 2621Sulfotyrosine Reviewed prediction
Modified residuei263 – 2631Sulfotyrosine Reviewed prediction
Modified residuei336 – 3361Sulfotyrosine Reviewed prediction
Modified residuei338 – 3381Sulfotyrosine Reviewed prediction
Modified residuei344 – 3441Sulfotyrosine Reviewed prediction
Modified residuei572 – 57214-hydroxyproline By similarity
Modified residuei578 – 57814-hydroxyproline By similarity
Modified residuei623 – 62314-hydroxyproline By similarity
Modified residuei629 – 62915-hydroxylysine By similarity
Modified residuei641 – 64114-hydroxyproline By similarity
Modified residuei644 – 64415-hydroxylysine By similarity
Modified residuei650 – 65014-hydroxyproline By similarity
Modified residuei656 – 65614-hydroxyproline By similarity
Modified residuei659 – 65914-hydroxyproline By similarity
Modified residuei677 – 67714-hydroxyproline By similarity
Modified residuei680 – 68014-hydroxyproline By similarity
Modified residuei682 – 68213-hydroxyproline By similarity
Modified residuei688 – 68813-hydroxyproline By similarity
Modified residuei692 – 69214-hydroxyproline By similarity
Modified residuei698 – 69814-hydroxyproline By similarity
Modified residuei707 – 70714-hydroxyproline By similarity
Modified residuei710 – 71015-hydroxylysine By similarity
Modified residuei719 – 71914-hydroxyproline By similarity
Modified residuei722 – 72214-hydroxyproline By similarity
Modified residuei728 – 72814-hydroxyproline By similarity
Modified residuei734 – 73414-hydroxyproline By similarity
Modified residuei746 – 74615-hydroxylysine By similarity
Modified residuei752 – 75214-hydroxyproline By similarity
Modified residuei758 – 75814-hydroxyproline By similarity
Modified residuei764 – 76414-hydroxyproline By similarity
Modified residuei767 – 76714-hydroxyproline By similarity
Modified residuei773 – 77314-hydroxyproline By similarity
Modified residuei776 – 77615-hydroxylysine By similarity
Modified residuei782 – 78214-hydroxyproline By similarity
Modified residuei791 – 79114-hydroxyproline By similarity
Modified residuei797 – 79715-hydroxylysine By similarity
Modified residuei806 – 80615-hydroxylysine By similarity
Modified residuei809 – 80915-hydroxylysine By similarity
Modified residuei812 – 81215-hydroxylysine By similarity
Modified residuei818 – 81814-hydroxyproline By similarity
Modified residuei821 – 82115-hydroxylysine By similarity
Modified residuei836 – 83614-hydroxyproline By similarity
Modified residuei848 – 84815-hydroxylysine By similarity
Modified residuei866 – 86615-hydroxylysine By similarity
Modified residuei872 – 87214-hydroxyproline By similarity
Modified residuei875 – 87514-hydroxyproline By similarity
Modified residuei878 – 87814-hydroxyproline By similarity
Modified residuei884 – 88415-hydroxylysine By similarity
Modified residuei890 – 89014-hydroxyproline By similarity
Modified residuei893 – 89314-hydroxyproline By similarity
Modified residuei899 – 89915-hydroxylysine By similarity
Modified residuei905 – 90514-hydroxyproline By similarity
Modified residuei908 – 90814-hydroxyproline By similarity
Modified residuei932 – 93214-hydroxyproline By similarity
Modified residuei947 – 94714-hydroxyproline By similarity
Modified residuei1019 – 101914-hydroxyproline By similarity
Modified residuei1022 – 102214-hydroxyproline By similarity
Modified residuei1025 – 102514-hydroxyproline By similarity
Modified residuei1031 – 103114-hydroxyproline By similarity
Modified residuei1223 – 122314-hydroxyproline By similarity
Modified residuei1226 – 122614-hydroxyproline By similarity
Modified residuei1469 – 146914-hydroxyproline By similarity
Modified residuei1472 – 147214-hydroxyproline By similarity
Modified residuei1603 – 16031Sulfotyrosine Reviewed prediction
Modified residuei1606 – 16061Sulfotyrosine Reviewed prediction

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 By similarity.
Sulfated on 40% of tyrosines By similarity.
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

Hydroxylation, Sulfation

Proteomic databases

PaxDbiQ9JI03.
PRIDEiQ9JI03.

Expressioni

Tissue specificityi

A high molecular weight form was detected in Schwann cells and peripheral nerve. A lower, probably processed form, is detected in all other tissues tested (at protein level).1 Publication

Gene expression databases

GenevestigatoriQ9JI03.

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.

Protein-protein interaction databases

IntActiQ9JI03. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9JI03.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini72 – 244173Laminin G-like
Add
BLAST
Domaini1611 – 1839229Fibrillar collagen NC1
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni231 – 445215Nonhelical region By similarity
Add
BLAST
Regioni446 – 560115Interrupted collagenous region By similarity
Add
BLAST
Regioni561 – 15721012Triple-helical region By similarity
Add
BLAST
Regioni1573 – 160735Nonhelical region By similarity
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiQ9JI03.
KOiK06236.
PhylomeDBiQ9JI03.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008160. Collagen.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000885. Fib_collagen_C.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 6 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.
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.

Q9JI03-1 [UniParc]FASTAAdd to Basket

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MDVHTRWKAP RPGAPLLSSP LLLLLLLLWA PPPSRAAQPT DLLEMLDFHN     50
LPSGVTKTTG FCATRRSSKE PDVAYRVSKD AQLSMPTKQL YPESDFPEDF 100
SILTTVKAKK GSQAFLVSVY NEQGIQQLGL ELGRSPVFLY EDHTGKPGPE 150
EYPLFPGINL SDGKWHRIAI SVYKKNVTLI LDCKKKITKF LNRGDHPIID 200
VNGIIMFGSR ILDDEIFEGD IQQLLFVSDH RAAYDYCEHY SPDCDTAVPD 250
TPQSQDPNPD EYYPEGEGET YYYEYPYYED PEDPGKEPAP SQKPVEAARE 300
TTEVPEEQTQ PPSEAPTVPE TSDTAGKEDN PGIGDYDYVP TDDYYTTSPY 350
EDFGYGEGVE NPDQPTNPDS GAEIPTSTSV TSNSSNPAPS PEEGKDDLGG 400
EFTEETIKNL DENYYDPYFD PDSDSNVSPS EIGPGMPANQ DTIYEGIGGP 450
RGEKGQKGEP AIIEPGMLIE GPPGPEGPAG LPGPPGTTGP TGQMGDPGER 500
GPPGRPGLPG ADGLPGPPGT MLMLPFRFGG GGDAGSKGPM VSAQESQAQA 550
ILQQARLALR GPAGPMGLTG RPGPMGPPGS GGLKGEPGDM GPQGPRGVQG 600
PPGPTGKPGR RGRAGSDGAR GMPGQTGPKG DRGFDGLAGL PGEKGHRGDP 650
GPSGPPGLPG DDGERGDDGE VGPRGLPGEP GPRGLLGPKG PPGPPGPPGV 700
TGMDGQPGPK GNVGPQGEPG PPGQQGNPGA QGLPGPQGAI GPPGEKGPLG 750
KPGLPGMPGA DGPPGHPGKE GPPGEKGGQG PPGPQGPIGY PGPRGVKGAD 800
GIRGLKGTKG EKGEDGFPGF KGDMGIKGDR GEIGPPGPRG EDGPEGPKGR 850
GGPNGDPGPL GPTGEKGKLG VPGLPGYPGR QGPKGSIGFP GFPGANGEKG 900
GRGTPGKPGP RGQRGPTGPR GERGPRGITG KPGPKGNSGG DGPAGPPGER 950
GPNGPQGPTG FPGPKGPPGP PGKDGLPGHP GQRGETGFQG KTGPPGPPGV 1000
VGPQGPTGET GPMGERGHPG PPGPPGEQGL PGAAGKEGTK GDPGPAGLPG 1050
KDGPPGLRGF PGDRGLPGPV GALGLKGSEG PPGPPGPAGS PGERGPAGAA 1100
GPIGIPGRPG PQGPPGPAGE KGVPGEEGPQ GPAGRDGLQG PVGLPGPAGP 1150
VGPPGEDGDK GEIGEPGQKG SKGDKGEQGP PGPTGPQGPT GQPGPSGADG 1200
EPGPRGQQGL FGQKGDEGSR GFPGPPGPVG LQGLPGPPGE KGETGDVGQM 1250
GPPGPPGPRG PSGAPGADGP QGPPGGIGNP GAVGEKGEPG EAGEPGLPGE 1300
GGPLGPKGER GEKGEAGPSG AAGPPGPKGP PGDDGPKGSP GPVGFPGDPG 1350
PPGEPGPAGQ DGPPGDKGDD GEPGQTGSPG PTGEPGPSGP PGKRGPPGPA 1400
GPEGRQGEKG AKGEAGLEGP PGKTGPIGPQ GAPGKPGPDG LRGIPGPVGE 1450
QGLPGSPGPD GPPGPMGPPG LPGLKGDSGP KGEKGHPGLI GLIGPPGEQG 1500
EKGDRGLPGP QGSSGPKGEQ GITGPSGPLG PPGPPGLPGP PGPKGAKGSS 1550
GPTGPKGEAG HPGLPGPPGP PGEVIQPLPI QASRTRRNID ASQLLDDGAG 1600
ESYVDYADGM EEIFGSLNSL KLEIEQMKRP LGTQQNPART CKDLQLCHPD 1650
FPDGEYWVDP NQGCSRDSFK VYCNFTAGGS TCVFPDKKSE GARITSWPKE 1700
NPGSWFSEFK RGKLLSYVDA EGNPVGVVQM TFLRLLSASA QQNITYNCYQ 1750
SVAWQDAATG SYDKAIRFLG SNDEEMSYDN NPYIRALVDG CATKKGYQKT 1800
VLEIDTPKVE QVPIVDIMFT DFGEASQKFG FEVGPACFLG 1840
Length:1,840
Mass (Da):183,987
Last modified:October 1, 2000 - v1
Checksum:iAD38F5FF886B923C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF272662 mRNA. Translation: AAF76433.1.
RefSeqiNP_604447.1. NM_134452.1.
UniGeneiRn.117.

Genome annotation databases

GeneIDi85490.
KEGGirno:85490.
UCSCiRGD:70920. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF272662 mRNA. Translation: AAF76433.1 .
RefSeqi NP_604447.1. NM_134452.1.
UniGenei Rn.117.

3D structure databases

ProteinModelPortali Q9JI03.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9JI03. 1 interaction.

Proteomic databases

PaxDbi Q9JI03.
PRIDEi Q9JI03.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 85490.
KEGGi rno:85490.
UCSCi RGD:70920. rat.

Organism-specific databases

CTDi 1289.
RGDi 70920. Col5a1.

Phylogenomic databases

eggNOGi NOG12793.
HOGENOMi HOG000085654.
HOVERGENi HBG004933.
InParanoidi Q9JI03.
KOi K06236.
PhylomeDBi Q9JI03.

Miscellaneous databases

NextBioi 617576.

Gene expression databases

Genevestigatori Q9JI03.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR008160. Collagen.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000885. Fib_collagen_C.
IPR001791. Laminin_G.
[Graphical view ]
Pfami PF01410. COLFI. 1 hit.
PF01391. Collagen. 6 hits.
PF02210. Laminin_G_2. 1 hit.
[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

  1. "Schwann cells synthesize type V collagen that contains a novel alpha 4 chain. Molecular cloning, biochemical characterization, and high affinity heparin binding of alpha 4(V) collagen."
    Chernousov M.A., Rothblum K., Tyler W.A., Stahl R.C., Carey D.J.
    J. Biol. Chem. 275:28208-28215(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, HEPARIN-BINDING.
    Strain: Sprague-Dawley.
    Tissue: Schwann cell.

Entry informationi

Entry nameiCO5A1_RAT
AccessioniPrimary (citable) accession number: Q9JI03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 89 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi