ID A0A1S3G2Y8_DIPOR Unreviewed; 1481 AA.
AC A0A1S3G2Y8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Collagen alpha-2(V) chain {ECO:0000313|RefSeq:XP_012883030.1};
GN Name=Col5a2 {ECO:0000313|RefSeq:XP_012883030.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012883030.1};
RN [1] {ECO:0000313|RefSeq:XP_012883030.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012883030.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_012883030.1; XM_013027576.1.
DR STRING; 10020.ENSDORP00000017854; -.
DR GeneID; 105994143; -.
DR KEGG; dord:105994143; -.
DR CTD; 1290; -.
DR InParanoid; A0A1S3G2Y8; -.
DR OMA; CESPQVP; -.
DR OrthoDB; 2970887at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005588; C:collagen type V trimer; IEA:Ensembl.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046332; F:SMAD binding; IEA:Ensembl.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0048592; P:eye morphogenesis; IEA:Ensembl.
DR GO; GO:1903225; P:negative regulation of endodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
DR GO; GO:0043588; P:skin development; IEA:Ensembl.
DR Gene3D; 2.60.120.1000; -; 1.
DR Gene3D; 6.20.200.20; -; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF58; COLLAGEN ALPHA-1(II) CHAIN; 1.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 10.
DR Pfam; PF00093; VWC; 1.
DR SMART; SM00038; COLFI; 1.
DR SMART; SM00214; VWC; 1.
DR SUPFAM; SSF57603; FnI-like domain; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_012883030.1};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1481
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010175252"
FT DOMAIN 39..97
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 1248..1481
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000259|PROSITE:PS51461"
FT REGION 107..1251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..183
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..671
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..917
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1026
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1209
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1481 AA; 143487 MW; 7EFE47A74BEBB21E CRC64;
MMANWVEARP LLILTVLLGQ SVSITAQEEG DNDVFDEEIA CTQHGQMYLN RDVWKPSPCE
ICVCDNGAIL CDKIECLEML TCANPVRPSG ECCATCPGTG GDGNNNFGRG RKGQKGEPGL
VPVVTGIRGR PGPAGPPGSQ GPRGERGPKG RPGPRGPQGI DGEPGVPGQP GAPGPPGHPS
HPGPDGMSRP FSAQMAGLDE KSGLGSQVGL MPGSVGPVGP RGPQGLQGQQ GGTGPAGPPG
EPGEPGPMGP IGARGPEGPP GKPGEDGARG FPGAPGLPGL KGHRGHKGLE GPKGEIGATG
SKGEAGPTGP MGAMGPLGPR GMPGERGRLG PQGAPGQRGA HGMPGKPGPM GPLGIPGSSG
FPGNPGMKGE AGPTGARGPE GPQGQRGETG PPGPAGSQGL PGTMGTDGTP GAKGPTGSAG
TSGPPGLSGP PGSPGPQGST GPQGIRGQPG DPGVPGFKGE AGPKGEPGPH GIQGPIGPPG
EEGKRGPRGD PGTVGPPGPM GERGAPGNRG FPGSDGLPGP KGAQGERGPV GSSGPKGGQG
DPGRPGEPGL PGARGLTGNP GVQGPEGKLG PLGASGEDGR PGPPGSIGIR GQPGSMGLPG
PKGSSGDPGK PGEAGNAGVP GQRGAPGKDG EVGPSGPVGP PGLAGERGEQ GPPGPTGFQG
LPGPPGPPGE GGKPGDQGVP GDPGAVGPLG PRGERGNPGE RGEPGITGLP GEKGMAGGHG
PDGPKGSPGP SGTVGDTGPP GLQGMPGERG IAGTPGPKGD RGGIGEKGAE GTAGNDGARG
LPGPLGPPGP AGPTGEKGEP GPRGLVGPPG SRGNPGSRGE NGPTGAVGFA GPQGPDGQPG
VKGEPGEPGQ KGDAGSPGPQ GLAGSPGPHG PHGVPGLKGG RGTQGPPGAT GFPGSAGRVG
PPGPAGAPGP AGPIGEPGKE GPPGLRGDPG SHGRVGDRGP AGPPGGPGDK GDPGEDGQPG
PDGPPGPAGT TGQRGIVGMP GQRGERGMPG LPGPAGTPGK VGPTGATGDK GPPGPVGPPG
SNGPVGEPGP EGPAGNDGTP GRDGAVGERG DRGDPGPAGL PGSQGAPGTP GPVGSPGDAG
QRGEPGSRGP IGPPGRAGKR GLPGPQGPRG DKGDHGDRGD RGQKGHRGFT GLQGLPGPPG
PNGEQGSAGI PGPFGPRGPP GPVGPSGKEG NPGPLGPIGP PGVRGSVGEA GPEGPPGEPG
PPGPPGPPGH LTAALGDIMG HYDENMPDPL PEFTEDQAAP DDTNKTDPGV HATLKSLSSQ
IETMRSPDGS KKHPARTCDD LKLCHSTKQS GEYWIDPNQG SAEDAIKVYC NMDTGETCIS
ANPSSIPRKT WWASKSPDNK PVWYGLDMNR GSQFTYGDYQ SPNTAVTQMT FLRLLSKEAS
QNITYICKNS IGYMDDQTKS LKKAVVLKGS NDLEIKGEGN IRFRYTVLHD TCSKRNGNVG
KTVFEYRTQN VARLPIIDLA PVDIGSTDQE FGVEIGPVCF M
//
