ID A0A8C1RXV7_CYPCA Unreviewed; 922 AA.
AC A0A8C1RXV7;
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:ENSCCRP00010121626.1};
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:ENSCCRP00010121626.1, ECO:0000313|Proteomes:UP000694427};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00010121626.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00010121626.1}
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; A0A8C1RXV7; -.
DR Ensembl; ENSCCRT00010135081.1; ENSCCRP00010121626.1; 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..922
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034166655"
FT DOMAIN 34..222
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 221..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..694
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 386..402
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..595
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..664
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..689
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 922 AA; 97138 MW; 783786534F12159E 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 VSTSGPPGPP GPPGKPGPPG PNGPLRSLLP GPPGAPGKDG
RDGQPGLPGV PGQDGLIGQQ GPKGAKGEQG RDGLSIIGLP GPPGPPGPII NFQDLLLNDT
AAKLNLTKIR GPPGPMGPEG LPGRAGFPGP RGPKGEVGFP GIQGPPGLKG EKGEPGVSIA
ADGSLITGLR GPRGPKGMKG DIGPSGQPGI VGPIGPPGQK GEYGLPGRPG RPGIAGRKGD
KGHSSGPPVL WVSKGTKGDN GYKGQKGEKG DPGLPGPPGL PGRRGLVGPK GDSIIGPPGD
TGYPGHPGPP GFGRPGPQGP PGPPGPPGTP SVRTYKNTQT LIRETSQCAE GTLAYVIDKS
ELYFRELKSF LPGNHVFPQH AHSVPALHLV ALNAPFSGDM HGIRGADYQC YQQARARGLT
STYRAFLSSH LQDLSSIVKK GDHFSLPVVN LKGDVLFSSW ISMFSGNGAV FDPLTPIYSF
DGRNVMTDQA WPQKLVWHGS NTAGIRMTTN YCEAWRTHDM AVTGQASLLQ TGRLLGQHTR
SCSNHFIVLC IENSYIQSPK RN
//
