ID A0A8C1I904_CYPCA Unreviewed; 890 AA.
AC A0A8C1I904;
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:ENSCCRP00010007994.1};
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:ENSCCRP00010007994.1, ECO:0000313|Proteomes:UP000694427};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00010007994.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00010007994.1}
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; A0A8C1I904; -.
DR Ensembl; ENSCCRT00010008700.1; ENSCCRP00010007994.1; 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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..890
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034428335"
FT DOMAIN 31..219
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 219..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..453
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..478
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..545
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..568
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..588
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..610
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..681
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 890 AA; 94202 MW; 31846D0D7EFC65A3 CRC64;
MLLSWLLGAH LALSYRSSAL HVMEERGSKG HLVLTELVGV PLPPSVSFVT GYEGFPAYSF
GPNANVGRLT QSFVLEPFFM DFAIIVTVKP SNSRGGVLFA ITDPSQTIVQ LGLALTPVED
KTQRIVLYYS EPGLADTMEV ASFKVPDMTQ QWNRFTLTVE HEEVRLYMDC EEYHSAPLKR
SQQPLSFKQG SGIFVANAGS TGLERFVGSI QQLVIKPDPR AAEEQCEEDD PSVSASGDRS
GDGSGGGGDY DDEEEHGRHE VISGQTNTHR PTYPVQAPPT VSPDMDEGEF SGHVTPIDER
LLRGTYKTDE TGESTGDGER GRDGLSITGP RGPPGPPGPT INFQDLLLND TAAKLNLTKI
RGPPGPMVCK AAHCFPLKSF LRCLTWIGEK GESGVSIAAD GSVIPGLRGP RGPNGMKGDI
GPSGQPGIMG PIGPPGQKGE YGLPGRPGRA GIAGRKGDKG DTSGPPGPPG PPGPPGPPGR
VIGLNRVKQL QFHFVHVMVD IAVVDSVECV YLKGAKGDNG YKGQKGEKGD PGLPGSSGLP
GRTGLVGPKG DSIVGPPGNT GPPGPPGLPG YGIPGPQGPP GPPGPPGTPS AYGSAVSLPG
PAGPQGPPGA PGHGNPVRTY KNSQTLIRET SQAAEGTLAY VIDKSELYIR VRGGWKKVEL
GELIPVPQDS SSSALSQGLS RPSDRSVPRV HSQELKSSLP DYHVFLQNAH SMPALHLVAL
NAPFTGDMHG IRGADYQCYQ QARARGLTST YRAFLSSHLQ DLSSIVKKGD RFGMPVVNLK
GDVLFGSWMA MFSGDGAVFD PLTPIYSFDG RNVMSDQAWP QKLVWHGSDT AGIRMTTSYC
EAWRTGDMAV TGQASLLQTG RLLGQHARSC SNHFIVLCIE NSYIQNPGRN
//
