ID A0A9J8CVI0_CYPCA Unreviewed; 969 AA.
AC A0A9J8CVI0;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 28-JAN-2026, entry version 14.
DE SubName: Full=Collagen, type XV, alpha 1b {ECO:0000313|Ensembl:ENSCCRP00000169155.1};
OS Cyprinus carpio carpio.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=630221 {ECO:0000313|Ensembl:ENSCCRP00000169155.1, ECO:0000313|Proteomes:UP001108240};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00000169155.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00000169155.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
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DR AlphaFoldDB; A0A9J8CVI0; -.
DR Ensembl; ENSCCRT00000146936.1; ENSCCRP00000169155.1; ENSCCRG00000061532.1.
DR GeneTree; ENSGT00940000164061; -.
DR Proteomes; UP001108240; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR050149; Collagen_superfamily.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP001108240};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..969
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039917038"
FT DOMAIN 34..222
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 221..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..331
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..355
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..405
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..482
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..642
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..711
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..736
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 969 AA; 102318 MW; 29581375FB4BA65B CRC64;
MKLWLLSWLV GAHLALGSLS SAPHVMEERG SKGHLVLTEL VGVPLPPSVS FITGYEGFPA
YNFGPHANVG RLTQSFVPEP FFKDFAIIVT VKPSNSRGGV LFAITDPSQK IVHLGLALTP
VEDKTQRIEL YYSQPGLADT MEVASFKVPD MTQQWNRFTL MVEQEEVRLY MDCEEYHSTP
LKRSQQPLSF KPGSGIFVAN AGSTGLERFV GSIQQLVIKQ DPRAAEEQCE EDEPSLQSSS
DGSGEADYDY EEEHGRREVI FGRTNEREDK ETTHRPTFPV QAPPTVLPDM DEGEVSGHVT
PIDERLLRGE RGEPGPEGPP GPPGPPGPSL PPIHSAQPGQ RGPQGPVGPP GSQGRPGKDG
QPYGFDSLGS GFGDVNIDTE LLRVSTSGPP GPPGPPGKPG PPGPNGPLRS LLPGPPGAPG
KDGRDGQPGL PVSMFSFRLN QLLKKGLQKR KKKGENGDPG PIGPIGPRGV PGPPGPPGPP
GPLSNNFMTD TLKGEQGRDG LSIIGLPGPP GPPGPIINFQ DLLLNDTAAK LNLTKIRGPP
GPMGPEGLPG RAGFPGPRGP KGEVGFPGIQ GPPGLKGEKG EPGVSIAADG SLITGLRGPR
GPKGMKGDIG PSGQPGIVGP IGPPGQKGEY GLPGRPGRPG IAGRKGDKGH SSGPPVLWVS
KGTKGDNGYK GQKGEKGDPG LPGPPGLPGR RGLVGPKGDS IIGPPGDTGY PGHPGPPGFG
RPGPQGPPGP PGPPGTPSVR TYKNTQTLIR ETSQCAEGTL AYVIDKSELY FRELKSFLPG
NHVFPQHAHS VPALHLVALN APFSGDMHGI RGADYQCYQQ ARARGLTSTY RAFLSSHLQD
LSSIVKKGDH FSLPVVNLKG DVLFSSWISM FSGNGAVFDP LTPIYSFDGR NVMTDQAWPQ
KLVWHGSNTA GIRMTTNYCE AWRTHDMAVT GQASLLQTGR LLGQHTRSCS NHFIVLCIEN
SYIQSPKRN
//
