ID A0A9J7WZP0_CYPCA Unreviewed; 1312 AA.
AC A0A9J7WZP0;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 28-JAN-2026, entry version 13.
DE SubName: Full=Collagen, type XV, alpha 1b {ECO:0000313|Ensembl:ENSCCRP00000100682.1};
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:ENSCCRP00000100682.1, ECO:0000313|Proteomes:UP001108240};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00000100682.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00000100682.1}
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 Ensembl; ENSCCRT00000171710.1; ENSCCRP00000100682.1; 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: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; 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:SF1070; COLLAGEN ALPHA-3(IV) CHAIN; 1.
DR Pfam; PF01391; Collagen; 6.
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1312
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039896366"
FT DOMAIN 91..279
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 39..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..58
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..409
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..433
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..489
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..535
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..620
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..664
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..860
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..885
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..904
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..985
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1010
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1312 AA; 135369 MW; 217D9EBB1388C41B CRC64;
MAALVLPLTC LVLLSLVSVS SQIQWFRFLW VPEMTSPPPA VTTPAPTATA PEESTAPVFP
ASPPQPTAGF SKAQAKRPLR MWKSERGSKG HLVLTELVGV PLPPSVSFIT GYEGFPAYNF
GPHANVGRLT QSFVPEPFFK DFAIIVTVKP SNSRGGVLFA ITDPSQKIVH LGLALTPVED
KTQRIELYYS QPGLADTMEV ASFKVPDMTQ QWNRFTLMVE QEEVRLYMDC EEYHSTPLKR
SQQPLSFKPG SGIFVANAGS TGLERFVGSI QQLVIKQDPR AAEEQCEEDE PSLQSSSDGS
GEADYDYEEE HGRREVIFGR TNEREDKETT HRPTFPVQAP PTVLPDMDEG EVSGHVTPID
ERLLRGTYKT EEIEESTGNG SGQGQKGERG EPGPEGPPGP PGPPGPSLPP IHSAQPGQRG
PQGPVGPPGS QGRPGKDGQP GSKGEEGKPG QRGPPGLPGL PGESGVKGEK GDPGVGQPGP
PGLPGPPGAS KPIKVPYGFD SLGSGFGDVN IDTELLRGPP GPPGPPGKPG PPGPNGPLRS
LLPGPPGAPG KDGRDGQPGL PGVPGQDGLI GQQGPKGAKG EQGIRGPPGL KGENGDPGPI
GPIGPRGVPG PPGPPGPPGP LSNNFMTDTL KDLEGSGESG LFLGARISKG YQGPPGLPGP
PGPQGLPGAD GAPGLSIKGE PGSPGKDGIQ GSAGFPGARG PKGDKGSLGE KGEQGRDGLS
IIGLPGPPGP PGPIINFQDL LLNDTAAKLN LTKIRGPPGP MGPEGLPGRA GFPGPRGPKG
EVGFPGIQGP PGLKGEKGEP GVSIAADGSL ITGLRGPRGP KGMKGDIGPS GQPGIVGPIG
PPGQKGEYGL PGRPGRPGIA GRKGDKGHSS GPPGPPGPPG PPGPPGRVIG LNGVNNNNSQ
PGNGRVSLGV KGDKGDVGNP GLPGTAVPMF PHGYVGTKGD NGYKGQKGEK GDPGLPGPPG
LPGRRGLVGP KGDSIIGPPG DTGYPGHPGP PGFGRPGPQG PPGPPGPPGT PSAYGSAASL
PGHPGPPGTP GAPGHGNPVR TYKNTQTLIR ETSQCAEGTL AYVIDKSELY FRVRGGWKKV
ELGELIPVPQ DSSTSDLSQG LSRPSDHSVP KVHSQELKSF LPGNHVFPQH AHSVPALHLV
ALNAPFSGDM HGIRGADYQC YQQARARGLT STYRAFLSSH LQDLSSIVKK GDHFSLPVVN
LKGDVLFSSW ISMFSGNGAV FDPLTPIYSF DGRNVMTDQA WPQKLVWHGS NTAGIRMTTN
YCEAWRTHDM AVTGQASLLQ TGRLLGQHTR SCSNHFIVLC IENSYIQSPK RN
//
