CO5A1_CRILO
ID CO5A1_CRILO Reviewed; 1840 AA.
AC Q60467;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Collagen alpha-1(V) chain;
DE Flags: Precursor;
GN Name=COL5A1;
OS Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10030;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=1722213; DOI=10.1016/s0021-9258(18)54290-3;
RA Greenspan D.S., Cheng W., Hoffman G.G.;
RT "The pro-alpha-1(V) collagen chain: complete primary structure,
RT distribution of expression, and comparison with the pro-alpha-1(XI)
RT collagen chain.";
RL J. Biol. Chem. 266:24727-24733(1991).
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: Ubiquitously expressed.
CC {ECO:0000269|PubMed:1722213}.
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 -!- PTM: Sulfated on 40% of tyrosines. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
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DR EMBL; M76730; AAA37002.1; -; mRNA.
DR AlphaFoldDB; Q60467; -.
DR SMR; Q60467; -.
DR PRIDE; Q60467; -.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
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; 8.
DR SMART; SM00038; COLFI; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
PE 2: Evidence at transcript level;
KW Collagen; Extracellular matrix; Heparin-binding; Hydroxylation; Repeat;
KW Secreted; Signal; Sulfation.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..1840
FT /note="Collagen alpha-1(V) chain"
FT /id="PRO_0000041760"
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 242..523
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 528..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 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 271
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; 184176 MW; 32C56821EF64CE75 CRC64;
MDVHTRWKDR LPVGPAAVPP LLLLLLLLWA PPQSRAAQPT DLLEMLDFHN LPSGVTKTTG
FCATRRSSRG PDVAYRVSKD AQLSMPRKQL YPDSDFAEDF SILTTVKAKK GSQAFLVSVY
NEQGIQQVGM ELGRSPVFLY EDHTGKPGPE EYPLFPGINL SDGKWHRIAI SVYRKNVTLI
LDCKKKVVKF LNRSDHPIID VNGIIMFGSR ILDDEIFEGD IQQLLFVSDH RAAYDYCEHY
SPDCDTAVPD TPQSQDPNPD EYYPEGDGET YYYEYPYYED PEDLGKEPAP TQKPVEAARE
TTEVPEEQTQ PPPEAPTVPE TSDPAGKEDD PGFGDYDYVP TDDYYTPAPY EDLGYGEGVE
NPDQPTNPDS GAEVPTSTII TSNTSNPAPS PGEDKDDLGG EFTEETIKNL EENYYDPYFD
PDSDSNVSPS EIGPGMPANQ DTIYEGIGGP RGEKGQKGEP AIIEPGMLIE GPPGPEGPAG
LPGPPGTTGP TGQVGDPGER 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 PGVAGKEGTK GDPGPAGLPG KDGPPGLRGF PGDRGLPGPV GALGLKGSEG
PPGPPGPAGS PGERGPAGAA GPIGIPGRPG PQGPPGPAGE KGVPGEKGPQ GPAGRDGLQG
PVGLPGPAGP VGPPGEDGDK GEIGEPGQKG SKGDKGEQGP PGPTGPQGPI GQPGPSGADG
EPGPRGQQGL FGQKGDEGSR GFPGPPGPVG LQGLPGPPGE KGETGDVGQM GPPGPPGPRG
PSGAPGADGP QGPPGGIGNP GAVGEKGEPG EAGEPGLPGE GGPLGPKGER GEKGEVGPSG
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 ESYLDYADGM EEIFGSLNSL
KLEIEQMKRP LGTQQNPART CKDLQLCHPD FPDGEYWVDP NQGCSRDSFK VYCNFTAGGS
TCVFPDKKSE GARITSWPKE NPGSWFSEFK RGKLLSYVDA EGNPVGVVQM TFLRLLSASA
HQNITYNCYQ SVAWQDAATG SYDKAIRFLG SNDEEMSYDN NPYIRALVDG CATKKGYQKT
VLEIDTPKVE QVPIVDIMFN DFGEASQKFG FEVGPACFLG
