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Protein

Collagen alpha-1(V) chain

Gene

Col5a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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

  • extracellular matrix structural constituent Source: InterPro
  • 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
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi70920. Col5a1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Sequence analysisAdd BLAST30
ChainiPRO_000004176231 – 1840Collagen alpha-1(V) chainAdd BLAST1810

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei234SulfotyrosineSequence analysis1
Modified residuei236SulfotyrosineSequence analysis1
Modified residuei240SulfotyrosineSequence analysis1
Modified residuei262SulfotyrosineSequence analysis1
Modified residuei263SulfotyrosineSequence analysis1
Modified residuei336SulfotyrosineSequence analysis1
Modified residuei338SulfotyrosineSequence analysis1
Modified residuei344SulfotyrosineSequence analysis1
Modified residuei5724-hydroxyprolineBy similarity1
Modified residuei5784-hydroxyprolineBy similarity1
Modified residuei6234-hydroxyprolineBy similarity1
Modified residuei6295-hydroxylysineBy similarity1
Modified residuei6414-hydroxyprolineBy similarity1
Modified residuei6445-hydroxylysineBy similarity1
Modified residuei6504-hydroxyprolineBy similarity1
Modified residuei6564-hydroxyprolineBy similarity1
Modified residuei6594-hydroxyprolineBy similarity1
Modified residuei6774-hydroxyprolineBy similarity1
Modified residuei6804-hydroxyprolineBy similarity1
Modified residuei6823-hydroxyprolineBy similarity1
Modified residuei6883-hydroxyprolineBy similarity1
Modified residuei6924-hydroxyprolineBy similarity1
Modified residuei6984-hydroxyprolineBy similarity1
Modified residuei7074-hydroxyprolineBy similarity1
Modified residuei7105-hydroxylysineBy similarity1
Modified residuei7194-hydroxyprolineBy similarity1
Modified residuei7224-hydroxyprolineBy similarity1
Modified residuei7284-hydroxyprolineBy similarity1
Modified residuei7344-hydroxyprolineBy similarity1
Modified residuei7465-hydroxylysineBy similarity1
Modified residuei7524-hydroxyprolineBy similarity1
Modified residuei7584-hydroxyprolineBy similarity1
Modified residuei7644-hydroxyprolineBy similarity1
Modified residuei7674-hydroxyprolineBy similarity1
Modified residuei7734-hydroxyprolineBy similarity1
Modified residuei7765-hydroxylysineBy similarity1
Modified residuei7824-hydroxyprolineBy similarity1
Modified residuei7914-hydroxyprolineBy similarity1
Modified residuei7975-hydroxylysineBy similarity1
Modified residuei8065-hydroxylysineBy similarity1
Modified residuei8095-hydroxylysineBy similarity1
Modified residuei8125-hydroxylysineBy similarity1
Modified residuei8184-hydroxyprolineBy similarity1
Modified residuei8215-hydroxylysineBy similarity1
Modified residuei8364-hydroxyprolineBy similarity1
Modified residuei8485-hydroxylysineBy similarity1
Modified residuei8665-hydroxylysineBy similarity1
Modified residuei8724-hydroxyprolineBy similarity1
Modified residuei8754-hydroxyprolineBy similarity1
Modified residuei8784-hydroxyprolineBy similarity1
Modified residuei8845-hydroxylysineBy similarity1
Modified residuei8904-hydroxyprolineBy similarity1
Modified residuei8934-hydroxyprolineBy similarity1
Modified residuei8995-hydroxylysineBy similarity1
Modified residuei9054-hydroxyprolineBy similarity1
Modified residuei9084-hydroxyprolineBy similarity1
Modified residuei9324-hydroxyprolineBy similarity1
Modified residuei9474-hydroxyprolineBy similarity1
Modified residuei10194-hydroxyprolineBy similarity1
Modified residuei10224-hydroxyprolineBy similarity1
Modified residuei10254-hydroxyprolineBy similarity1
Modified residuei10314-hydroxyprolineBy similarity1
Modified residuei12234-hydroxyprolineBy similarity1
Modified residuei12264-hydroxyprolineBy similarity1
Modified residuei14694-hydroxyprolineBy similarity1
Modified residuei14724-hydroxyprolineBy similarity1
Modified residuei1603SulfotyrosineSequence analysis1
Modified residuei1606SulfotyrosineSequence analysis1

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

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 interactor.
STRINGi10116.ENSRNOP00000012334.

Structurei

3D structure databases

ProteinModelPortaliQ9JI03.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini72 – 244Laminin G-likeAdd BLAST173
Domaini1611 – 1839Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST229

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni231 – 445Nonhelical regionBy similarityAdd BLAST215
Regioni446 – 560Interrupted collagenous regionBy similarityAdd BLAST115
Regioni561 – 1572Triple-helical regionBy similarityAdd BLAST1012
Regioni1573 – 1607Nonhelical 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.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiQ9JI03.
KOiK19721.
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.

Q9JI03-1 [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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AF272662 mRNA. Translation: AAF76433.1.
RefSeqiNP_604447.1. NM_134452.1.
UniGeneiRn.117.

3D structure databases

ProteinModelPortaliQ9JI03.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JI03. 1 interactor.
STRINGi10116.ENSRNOP00000012334.

Proteomic databases

PaxDbiQ9JI03.
PRIDEiQ9JI03.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1289.
RGDi70920. Col5a1.

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiQ9JI03.
KOiK19721.
PhylomeDBiQ9JI03.

Miscellaneous databases

PROiQ9JI03.

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]
ProtoNetiSearch...

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 5, 2016
This is version 100 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

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.