ID A0A8C1RXE5_CYPCA Unreviewed; 984 AA.
AC A0A8C1RXE5;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 14.
DE SubName: Full=Collagen, type XV, alpha 1b {ECO:0000313|Ensembl:ENSCCRP00010121623.1};
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:ENSCCRP00010121623.1, ECO:0000313|Proteomes:UP000694427};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00010121623.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00010121623.1}
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; A0A8C1RXE5; -.
DR Ensembl; ENSCCRT00010135078.1; ENSCCRP00010121623.1; ENSCCRG00010053102.1.
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:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 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: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..984
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034909139"
FT DOMAIN 34..222
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 221..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..328
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..352
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..398
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..616
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..685
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..710
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 984 AA; 104052 MW; CF970620DBC2B8AE 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 EKPTFPVQAP PTVLPDMDEG EVSGHVTPID
ERLLRGERGE PGPEGPPGPP GPPGPSLPPI HSAQPGQRGP QGPVGPPGSQ GRPGKDGQPY
GFDSLGSGFG DVNIDTELLR GPPGPPGPPG KPGPPGPNGP LRSLLPGPPG APGKDGRDGQ
PGLPVSMFSF RLNQLLKKGL QKRKKKGEPG SPGKDGIQGS AGFPGARGEQ GRDGLSIIGL
PGPPGPPGPI INFQDLLLND TAAKLNLTKI RGPPGPMGPE GLPGRAGFPG PRGPKGEVGF
PGIQGPPGLK GEKGEPGVSI AADGSLITGL RGPRGPKGMK GDIGPSGQPG IVGPIGPPGQ
KGEYGLPGRP GRPGIAGRKG DKGHSSGPPV LWVSKGTKGD NGYKGQKGEK GDPGLPGPPG
LPGRRGLVGP KGDSIIGPPG DTGYPGHPGP PGFGRPGPQG PPGPPGPPGT PSVRTYKNTQ
TLIRETSQCA EGTLAYVIDK SELYFRVRGG WKKLGELIPV PQDSSTSDLS QGLSRPSDHS
VPKVHSQELK SFLPGNHVFP QHAHSVPALH LVALNAPFSG DMHGIRGADY QCYQQARARG
LTSTYRAFLS SHLQDLSSIV KKGDHFSLPV VNLKGDVLFS SWISMFSGNG AVFDPLTPIY
SFDGRNVMTD QAWPQKLVWH GSNTAGIRMT TNYCEAWRTH DMAVTGQASL LQTGRLLGQH
TRSCSNHFIV LCIENSYIQS PKRN
//
