ID A0A9J7YTH3_CYPCA Unreviewed; 1282 AA.
AC A0A9J7YTH3;
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:ENSCCRP00000122426.1};
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:ENSCCRP00000122426.1, ECO:0000313|Proteomes:UP001108240};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00000122426.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00000122426.1}
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; ENSCCRT00000106992.1; ENSCCRP00000122426.1; ENSCCRG00000057698.1.
DR GeneTree; ENSGT00940000164061; -.
DR OMA; WWKVSAS; -.
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: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; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 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; 5.
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1282
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039917241"
FT DOMAIN 41..229
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 229..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..362
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..442
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..488
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..576
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..620
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..631
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..655
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..816
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..841
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..937
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..960
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..980
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1002
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1073
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1084
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1282 AA; 131372 MW; 6D6D78B378A1B0FD CRC64;
MLKLLRKMKL WVLSWLLGAH LALSYRSSAL HVMEERGSKG HLVLTELVGV PLPPSVSFVT
GYEGFPAYSF GPNANVGRLT QSFVLEPFFM DFAIIVTVKP SNSRGGVLFA ITDPSQTIVQ
LGLALTPVED KTQRIVLYYS EPGLADTMEV ASFKVPDMTQ QWNRFTLTVE HEEVRLYMDC
EEYHSAPLKR SQQPLSFKQG SGIFVANAGS TGLERFVGSI QQLVIKPDPR AAEEQCEEDD
PSASGDRSGD GSGGGGDYDD EEEHGRHEVI SGQTNVREDK EKTHRPTYPV QAPPTVSPDM
DEGEFSGHVT PIDERLLRGT YKTDETGEST GDGSGQRQKG ERGEPGPAGP PGPPGPPGPS
LPPTHSGQPG QRGPQGPMGP PGRQGRPGKD GQPGSKGEEG KPGQKGPPGL PGLPGESGVK
GEKGDPGVGM PGPPGPPGPP GSSKPIKVPY GFDALGSGFE DVDIDTERLR GPPGPPGPPG
KPGPPGPNGP SGALLPGPPG APGKDGRDGQ PGLRGLPGSN GLTGQQGPKG AKGEQGMRGP
SGPKGENGDP GLIGPMGPRG VPGPPGIPGP PGPPGPSISN LMTNTLKDLE GSGESGLFLG
AGISKGYHGP PGLPGPPGPQ GLPGADGAPG LSVKGEAGSP GQDGMPGLAG LPGARGPKGD
KGSPGEKGER GRDGLSITGP RGPPGPPGPT INFQDLLLND TAAKLNLTKI RGPPGPMGSE
GLPGRAGFPG PRGQKGEIGF PGIQGPPGLK GEKGESGVSI AADGSVIPGL RGPRGPNGMK
GDIGPSGQPG IMGPIGPPGQ KGEYGLPGRP GRAGIAGRKG DKGDTSGPPG PPGPPGPPGP
PGRVIGLNRT VFPVPPRPHC KIPVNNNNSQ QGNGRASLGV KGDKGDVGNP GLPGTAVPLF
PHGHVGAKGD NGYKGQKGEK GDPGLPGSSG LPGRTGLVGP KGDSIVGPPG NTGPPGPPGL
PGYGIPGPQG PPGPPGPPGT PSAYGSAVSL PGPAGPQGPP GAPGHGNPVR TYKNSQTLIR
ETSQAAEGTL AYVIDKSELY IRVRGGWKKV ELGELIPVPQ DSSSSALSQG LSRPSDRSVP
RVHSQELKSS LPDYHVFLQN AHSMPALHLV ALNAPFTGDM HGIRGADYQC YQQARARGLT
STYRAFLSSH LQDLSSIVKK GDRFGMPVVN LKGDVLFGSW MAMFSGDGAV FDPLTPIYSF
DGRNVMSDQA WPQKLVWHGS DTAGIRMTTS YCEAWRTGDM AVTGQASLLQ TGRLLGQHAR
SCSNHFIVLC IENSYIQNPG RN
//
