ID A0A8C1GF07_CYPCA Unreviewed; 888 AA.
AC A0A8C1GF07;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 15.
DE SubName: Full=Collagen, type XV, alpha 1b {ECO:0000313|Ensembl:ENSCCRP00010007985.1};
OS Cyprinus carpio (Common carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=7962 {ECO:0000313|Ensembl:ENSCCRP00010007985.1, ECO:0000313|Proteomes:UP000694427};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00010007985.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00010007985.1}
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; A0A8C1GF07; -.
DR Ensembl; ENSCCRT00010008688.1; ENSCCRP00010007985.1; ENSCCRG00010003372.1.
DR Proteomes; UP000694427; 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; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 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; 1.
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:UP000694427};
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..888
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034388695"
FT DOMAIN 34..222
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 222..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..456
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..481
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..543
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..566
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..586
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..608
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..679
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 888 AA; 94033 MW; 1EBA24B3BF07C635 CRC64;
MKLWLLSWLL GAHLALSYRS SALHVMEERG SKGHLVLTEL VGVPLPPSVS FVTGYEGFPA
YSFGPNANVG RLTQSFVLEP FFMDFAIIVT VKPSNSRGGV LFAITDPSQT IVQLGLALTP
VEDKTQRIVL YYSEPGLADT MEVASFKVPD MTQQWNRFTL TVEHEEVRLY MDCEEYHSAP
LKRSQQPLSF KQGSGIFVAN AGSTGLERFV GSIQQLVIKP DPRAAEEQCE EDDPSVSASG
DRSGDGSGGG GDYDDEEEHG RHEVISGQTN THRPTYPVQA PPTVSPDMDE GEFSGHVTPI
DERLLRGTYK TDETGESTGD GERGRDGLSI TGPRGPPGPP GPTINFQDLL LNDTAAKLNL
TKIRGPPGPM VCKAAHCFPL KSFLRCLTWI GEKGESGVSI AADGSVIPGL RGPRGPNGMK
GDIGPSGQPG IMGPIGPPGQ KGEYGLPGRP GRAGIAGRKG DKGDTSGPPG PPGPPGPPGP
PGRVIGLNRF HFVHVMVDIA VVDSVECVYL KGAKGDNGYK GQKGEKGDPG LPGSSGLPGR
TGLVGPKGDS IVGPPGNTGP PGPPGLPGYG IPGPQGPPGP PGPPGTPSAY GSAVSLPGPA
GPQGPPGAPG HGNPVRTYKN SQTLIRETSQ AAEGTLAYVI DKSELYIRVR GGWKKVELGE
LIPVPQDSSS SALSQGLSRP SDRSVPRVHS QELKSSLPDY HVFLQNAHSM PALHLVALNA
PFTGDMHGIR GADYQCYQQA RARGLTSTYR AFLSSHLQDL SSIVKKGDRF GMPVVNLKGD
VLFGSWMAMF SGDGAVFDPL TPIYSFDGRN VMSDQAWPQK LVWHGSDTAG IRMTTSYCEA
WRTGDMAVTG QASLLQTGRL LGQHARSCSN HFIVLCIENS YIQNPGRN
//
