CO5A1_RAT
ID CO5A1_RAT Reviewed; 1840 AA.
AC Q9JI03;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Collagen alpha-1(V) chain;
DE Flags: Precursor;
GN Name=Col5a1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND HEPARIN-BINDING.
RC STRAIN=Sprague-Dawley; TISSUE=Schwann cell;
RX PubMed=10852920; DOI=10.1074/jbc.m003922200;
RA Chernousov M.A., Rothblum K., Tyler W.A., Stahl R.C., Carey D.J.;
RT "Schwann cells synthesize type V collagen that contains a novel alpha 4
RT chain. Molecular cloning, biochemical characterization, and high affinity
RT heparin binding of alpha 4(V) collagen.";
RL J. Biol. Chem. 275:28208-28215(2000).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Type V collagen is a member of group I collagen (fibrillar
CC forming collagen). It is a minor connective tissue component of nearly
CC ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate,
CC thrombospondin, heparin, and insulin (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Trimers of two alpha 1(V) and one alpha 2(V) chains in most
CC tissues and trimers of one alpha 1(V), one alpha 2(V), and one alpha
CC 3(V) chains in placenta. Interacts with CSPG4 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- TISSUE SPECIFICITY: A high molecular weight form was detected in
CC Schwann cells and peripheral nerve. A lower, probably processed form,
CC is detected in all other tissues tested (at protein level).
CC {ECO:0000269|PubMed:10852920}.
CC -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000250}.
CC -!- PTM: Sulfated on 40% of tyrosines. {ECO:0000250}.
CC -!- PTM: Hydroxylation on proline residues within the sequence motif, GXPG,
CC is most likely to be 4-hydroxy as this fits the requirement for 4-
CC hydroxylation in vertebrates. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
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DR EMBL; AF272662; AAF76433.1; -; mRNA.
DR RefSeq; NP_604447.1; NM_134452.1.
DR AlphaFoldDB; Q9JI03; -.
DR SMR; Q9JI03; -.
DR BioGRID; 250110; 1.
DR IntAct; Q9JI03; 1.
DR STRING; 10116.ENSRNOP00000012334; -.
DR jPOST; Q9JI03; -.
DR PaxDb; Q9JI03; -.
DR PRIDE; Q9JI03; -.
DR GeneID; 85490; -.
DR KEGG; rno:85490; -.
DR UCSC; RGD:70920; rat.
DR CTD; 1289; -.
DR RGD; 70920; Col5a1.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; Q9JI03; -.
DR OrthoDB; 199083at2759; -.
DR PhylomeDB; Q9JI03; -.
DR Reactome; R-RNO-1442490; Collagen degradation.
DR Reactome; R-RNO-1474244; Extracellular matrix organization.
DR Reactome; R-RNO-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-RNO-186797; Signaling by PDGF.
DR Reactome; R-RNO-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR Reactome; R-RNO-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-RNO-3000178; ECM proteoglycans.
DR Reactome; R-RNO-419037; NCAM1 interactions.
DR Reactome; R-RNO-8874081; MET activates PTK2 signaling.
DR Reactome; R-RNO-8948216; Collagen chain trimerization.
DR PRO; PR:Q9JI03; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005604; C:basement membrane; ISO:RGD.
DR GO; GO:0005581; C:collagen trimer; ISO:RGD.
DR GO; GO:0005588; C:collagen type V trimer; ISO:RGD.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; ISO:RGD.
DR GO; GO:0008201; F:heparin binding; IDA:RGD.
DR GO; GO:0048407; F:platelet-derived growth factor binding; ISO:RGD.
DR GO; GO:0043394; F:proteoglycan binding; ISO:RGD.
DR GO; GO:0001568; P:blood vessel development; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0032964; P:collagen biosynthetic process; ISO:RGD.
DR GO; GO:0030199; P:collagen fibril organization; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0048592; P:eye morphogenesis; ISO:RGD.
DR GO; GO:0003007; P:heart morphogenesis; ISO:RGD.
DR GO; GO:0045112; P:integrin biosynthetic process; ISO:RGD.
DR GO; GO:1903225; P:negative regulation of endodermal cell differentiation; ISO:RGD.
DR GO; GO:0051128; P:regulation of cellular component organization; ISO:RGD.
DR GO; GO:0043588; P:skin development; ISO:RGD.
DR GO; GO:0097435; P:supramolecular fiber organization; ISO:RGD.
DR GO; GO:0035989; P:tendon development; ISO:RGD.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; ISO:RGD.
DR CDD; cd00110; LamG; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 6.
DR Pfam; PF02210; Laminin_G_2; 1.
DR SMART; SM00038; COLFI; 1.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
PE 1: Evidence at protein level;
KW Collagen; Extracellular matrix; Heparin-binding; Hydroxylation;
KW Reference proteome; Repeat; Secreted; Signal; Sulfation.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..1840
FT /note="Collagen alpha-1(V) chain"
FT /id="PRO_0000041762"
FT DOMAIN 72..244
FT /note="Laminin G-like"
FT DOMAIN 1611..1839
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 231..445
FT /note="Nonhelical region"
FT /evidence="ECO:0000250"
FT REGION 241..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..560
FT /note="Interrupted collagenous region"
FT /evidence="ECO:0000250"
FT REGION 561..1576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..1572
FT /note="Triple-helical region"
FT /evidence="ECO:0000250"
FT REGION 1573..1607
FT /note="Nonhelical region"
FT /evidence="ECO:0000250"
FT COMPBIAS 304..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..485
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..702
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..975
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1359
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1383..1398
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1456..1470
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1527..1542
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1561..1575
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 234
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 236
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 240
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 262
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 263
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 336
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 338
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 344
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 572
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 578
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 623
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 629
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 641
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 644
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 650
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 656
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 659
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 677
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 680
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 682
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 688
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 692
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 698
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 707
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 710
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 719
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 722
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 728
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 734
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 746
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 752
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 758
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 764
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 767
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 773
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 776
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 782
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 791
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 797
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 806
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 809
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 812
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 818
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 821
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 836
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 848
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 866
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 872
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 875
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 878
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 884
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 890
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 893
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 899
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 905
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 908
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 932
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 947
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 1019
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 1022
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 1025
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 1031
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 1223
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 1226
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 1469
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 1472
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 1603
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1606
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1840 AA; 183987 MW; AD38F5FF886B923C CRC64;
MDVHTRWKAP RPGAPLLSSP LLLLLLLLWA PPPSRAAQPT DLLEMLDFHN LPSGVTKTTG
FCATRRSSKE PDVAYRVSKD AQLSMPTKQL YPESDFPEDF SILTTVKAKK GSQAFLVSVY
NEQGIQQLGL ELGRSPVFLY EDHTGKPGPE EYPLFPGINL SDGKWHRIAI SVYKKNVTLI
LDCKKKITKF LNRGDHPIID VNGIIMFGSR ILDDEIFEGD IQQLLFVSDH RAAYDYCEHY
SPDCDTAVPD TPQSQDPNPD EYYPEGEGET YYYEYPYYED PEDPGKEPAP SQKPVEAARE
TTEVPEEQTQ PPSEAPTVPE TSDTAGKEDN PGIGDYDYVP TDDYYTTSPY EDFGYGEGVE
NPDQPTNPDS GAEIPTSTSV TSNSSNPAPS PEEGKDDLGG EFTEETIKNL DENYYDPYFD
PDSDSNVSPS EIGPGMPANQ DTIYEGIGGP RGEKGQKGEP AIIEPGMLIE GPPGPEGPAG
LPGPPGTTGP TGQMGDPGER GPPGRPGLPG ADGLPGPPGT MLMLPFRFGG GGDAGSKGPM
VSAQESQAQA ILQQARLALR GPAGPMGLTG RPGPMGPPGS GGLKGEPGDM GPQGPRGVQG
PPGPTGKPGR RGRAGSDGAR GMPGQTGPKG DRGFDGLAGL PGEKGHRGDP GPSGPPGLPG
DDGERGDDGE VGPRGLPGEP GPRGLLGPKG PPGPPGPPGV TGMDGQPGPK GNVGPQGEPG
PPGQQGNPGA QGLPGPQGAI GPPGEKGPLG KPGLPGMPGA DGPPGHPGKE GPPGEKGGQG
PPGPQGPIGY PGPRGVKGAD GIRGLKGTKG EKGEDGFPGF KGDMGIKGDR GEIGPPGPRG
EDGPEGPKGR GGPNGDPGPL GPTGEKGKLG VPGLPGYPGR QGPKGSIGFP GFPGANGEKG
GRGTPGKPGP RGQRGPTGPR GERGPRGITG KPGPKGNSGG DGPAGPPGER GPNGPQGPTG
FPGPKGPPGP PGKDGLPGHP GQRGETGFQG KTGPPGPPGV VGPQGPTGET GPMGERGHPG
PPGPPGEQGL PGAAGKEGTK GDPGPAGLPG KDGPPGLRGF PGDRGLPGPV GALGLKGSEG
PPGPPGPAGS PGERGPAGAA GPIGIPGRPG PQGPPGPAGE KGVPGEEGPQ GPAGRDGLQG
PVGLPGPAGP VGPPGEDGDK GEIGEPGQKG SKGDKGEQGP PGPTGPQGPT GQPGPSGADG
EPGPRGQQGL FGQKGDEGSR GFPGPPGPVG LQGLPGPPGE KGETGDVGQM GPPGPPGPRG
PSGAPGADGP QGPPGGIGNP GAVGEKGEPG EAGEPGLPGE GGPLGPKGER GEKGEAGPSG
AAGPPGPKGP PGDDGPKGSP GPVGFPGDPG PPGEPGPAGQ DGPPGDKGDD GEPGQTGSPG
PTGEPGPSGP PGKRGPPGPA GPEGRQGEKG AKGEAGLEGP PGKTGPIGPQ GAPGKPGPDG
LRGIPGPVGE QGLPGSPGPD GPPGPMGPPG LPGLKGDSGP KGEKGHPGLI GLIGPPGEQG
EKGDRGLPGP QGSSGPKGEQ GITGPSGPLG PPGPPGLPGP PGPKGAKGSS GPTGPKGEAG
HPGLPGPPGP PGEVIQPLPI QASRTRRNID ASQLLDDGAG ESYVDYADGM EEIFGSLNSL
KLEIEQMKRP LGTQQNPART CKDLQLCHPD FPDGEYWVDP NQGCSRDSFK VYCNFTAGGS
TCVFPDKKSE GARITSWPKE NPGSWFSEFK RGKLLSYVDA EGNPVGVVQM TFLRLLSASA
QQNITYNCYQ SVAWQDAATG SYDKAIRFLG SNDEEMSYDN NPYIRALVDG CATKKGYQKT
VLEIDTPKVE QVPIVDIMFT DFGEASQKFG FEVGPACFLG
