ID A0A9J7XDQ7_CYPCA Unreviewed; 1238 AA.
AC A0A9J7XDQ7;
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:ENSCCRP00000104426.1};
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:ENSCCRP00000104426.1, ECO:0000313|Proteomes:UP001108240};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00000104426.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00000104426.1}
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; A0A9J7XDQ7; -.
DR Ensembl; ENSCCRT00000123320.1; ENSCCRP00000104426.1; ENSCCRG00000057698.1.
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; 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:SF1077; COLLAGEN ALPHA-3(IV) CHAIN; 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}.
FT DOMAIN 11..199
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 199..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..332
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..412
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..458
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..546
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..590
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..601
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..625
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..786
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..811
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..831
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..893
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..916
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..936
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..958
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1029
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1039
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1238 AA; 126356 MW; 4FE1F7D2B19CA60D CRC64;
MWKSERGSKG 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 PGRVIGLNRV NNNNSQQGNG RASLGVKGDK
GDVGNPGLPG TAVPLFPHGH VGAKGDNGYK GQKGEKGDPG LPGSSGLPGR TGLVGPKGDS
IVGPPGNTGP PGPPGLPGYG IPGPQGPPGP PGPPGTPSAY GSAVSLPGPA GPQGPPGAPG
HGNPVRTYKN SQTLIRETSQ AAEGTLAYVI DKSELYIRVR GGWKKVELGE LIPVPQDSSS
SALSQGLSRP SDRSVPRVHS QELKSSLPDY HVFLQNAHSM PALHLVALNA PFTGDMHGIR
GADYQCYQQA RARGLTSTYR AFLSSHLQDL SSIVKKGDRF GMPVVNLKGD VLFGSWMAMF
SGDGAVFDPL TPIYSFDGRN VMSDQAWPQK LVWHGSDTAG IRMTTSYCEA WRTGDMAVTG
QASLLQTGRL LGQHARSCSN HFIVLCIENS YIQNPGRN
//
