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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).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

Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

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 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 18401810Collagen alpha-1(V) chainPRO_0000041762Add
BLAST

Amino acid modifications

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

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).By similarity

Protein-protein interaction databases

IntActiQ9JI03. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9JI03.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini72 – 244173Laminin G-likeAdd
BLAST
Domaini1611 – 1839229Fibrillar collagen NC1PROSITE-ProRule annotationAdd
BLAST

Region

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

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

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

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.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDVHTRWKAP RPGAPLLSSP LLLLLLLLWA PPPSRAAQPT DLLEMLDFHN
60 70 80 90 100
LPSGVTKTTG FCATRRSSKE PDVAYRVSKD AQLSMPTKQL YPESDFPEDF
110 120 130 140 150
SILTTVKAKK GSQAFLVSVY NEQGIQQLGL ELGRSPVFLY EDHTGKPGPE
160 170 180 190 200
EYPLFPGINL SDGKWHRIAI SVYKKNVTLI LDCKKKITKF LNRGDHPIID
210 220 230 240 250
VNGIIMFGSR ILDDEIFEGD IQQLLFVSDH RAAYDYCEHY SPDCDTAVPD
260 270 280 290 300
TPQSQDPNPD EYYPEGEGET YYYEYPYYED PEDPGKEPAP SQKPVEAARE
310 320 330 340 350
TTEVPEEQTQ PPSEAPTVPE TSDTAGKEDN PGIGDYDYVP TDDYYTTSPY
360 370 380 390 400
EDFGYGEGVE NPDQPTNPDS GAEIPTSTSV TSNSSNPAPS PEEGKDDLGG
410 420 430 440 450
EFTEETIKNL DENYYDPYFD PDSDSNVSPS EIGPGMPANQ DTIYEGIGGP
460 470 480 490 500
RGEKGQKGEP AIIEPGMLIE GPPGPEGPAG LPGPPGTTGP TGQMGDPGER
510 520 530 540 550
GPPGRPGLPG ADGLPGPPGT MLMLPFRFGG GGDAGSKGPM VSAQESQAQA
560 570 580 590 600
ILQQARLALR GPAGPMGLTG RPGPMGPPGS GGLKGEPGDM GPQGPRGVQG
610 620 630 640 650
PPGPTGKPGR RGRAGSDGAR GMPGQTGPKG DRGFDGLAGL PGEKGHRGDP
660 670 680 690 700
GPSGPPGLPG DDGERGDDGE VGPRGLPGEP GPRGLLGPKG PPGPPGPPGV
710 720 730 740 750
TGMDGQPGPK GNVGPQGEPG PPGQQGNPGA QGLPGPQGAI GPPGEKGPLG
760 770 780 790 800
KPGLPGMPGA DGPPGHPGKE GPPGEKGGQG PPGPQGPIGY PGPRGVKGAD
810 820 830 840 850
GIRGLKGTKG EKGEDGFPGF KGDMGIKGDR GEIGPPGPRG EDGPEGPKGR
860 870 880 890 900
GGPNGDPGPL GPTGEKGKLG VPGLPGYPGR QGPKGSIGFP GFPGANGEKG
910 920 930 940 950
GRGTPGKPGP RGQRGPTGPR GERGPRGITG KPGPKGNSGG DGPAGPPGER
960 970 980 990 1000
GPNGPQGPTG FPGPKGPPGP PGKDGLPGHP GQRGETGFQG KTGPPGPPGV
1010 1020 1030 1040 1050
VGPQGPTGET GPMGERGHPG PPGPPGEQGL PGAAGKEGTK GDPGPAGLPG
1060 1070 1080 1090 1100
KDGPPGLRGF PGDRGLPGPV GALGLKGSEG PPGPPGPAGS PGERGPAGAA
1110 1120 1130 1140 1150
GPIGIPGRPG PQGPPGPAGE KGVPGEEGPQ GPAGRDGLQG PVGLPGPAGP
1160 1170 1180 1190 1200
VGPPGEDGDK GEIGEPGQKG SKGDKGEQGP PGPTGPQGPT GQPGPSGADG
1210 1220 1230 1240 1250
EPGPRGQQGL FGQKGDEGSR GFPGPPGPVG LQGLPGPPGE KGETGDVGQM
1260 1270 1280 1290 1300
GPPGPPGPRG PSGAPGADGP QGPPGGIGNP GAVGEKGEPG EAGEPGLPGE
1310 1320 1330 1340 1350
GGPLGPKGER GEKGEAGPSG AAGPPGPKGP PGDDGPKGSP GPVGFPGDPG
1360 1370 1380 1390 1400
PPGEPGPAGQ DGPPGDKGDD GEPGQTGSPG PTGEPGPSGP PGKRGPPGPA
1410 1420 1430 1440 1450
GPEGRQGEKG AKGEAGLEGP PGKTGPIGPQ GAPGKPGPDG LRGIPGPVGE
1460 1470 1480 1490 1500
QGLPGSPGPD GPPGPMGPPG LPGLKGDSGP KGEKGHPGLI GLIGPPGEQG
1510 1520 1530 1540 1550
EKGDRGLPGP QGSSGPKGEQ GITGPSGPLG PPGPPGLPGP PGPKGAKGSS
1560 1570 1580 1590 1600
GPTGPKGEAG HPGLPGPPGP PGEVIQPLPI QASRTRRNID ASQLLDDGAG
1610 1620 1630 1640 1650
ESYVDYADGM EEIFGSLNSL KLEIEQMKRP LGTQQNPART CKDLQLCHPD
1660 1670 1680 1690 1700
FPDGEYWVDP NQGCSRDSFK VYCNFTAGGS TCVFPDKKSE GARITSWPKE
1710 1720 1730 1740 1750
NPGSWFSEFK RGKLLSYVDA EGNPVGVVQM TFLRLLSASA QQNITYNCYQ
1760 1770 1780 1790 1800
SVAWQDAATG SYDKAIRFLG SNDEEMSYDN NPYIRALVDG CATKKGYQKT
1810 1820 1830 1840
VLEIDTPKVE QVPIVDIMFT DFGEASQKFG FEVGPACFLG
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.
IPR013320. ConA-like_dom.
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: October 29, 2014
This is version 91 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