ID A0A9J7WVD4_CYPCA Unreviewed; 1338 AA.
AC A0A9J7WVD4;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 28-JAN-2026, entry version 14.
DE SubName: Full=Collagen type XVIII alpha 1 chain b {ECO:0000313|Ensembl:ENSCCRP00000098819.1};
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:ENSCCRP00000098819.1, ECO:0000313|Proteomes:UP001108240};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00000098819.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00000098819.1}
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; ENSCCRT00000128720.1; ENSCCRP00000098819.1; ENSCCRG00000065024.1.
DR GeneTree; ENSGT00940000158212; -.
DR Proteomes; UP001108240; Unplaced.
DR GO; GO:0005587; C:collagen type IV trimer; 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: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: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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1338
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039886815"
FT DOMAIN 33..222
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 232..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..249
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..333
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..375
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..394
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..419
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..461
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..503
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..560
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..577
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..678
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..776
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..794
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..825
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..898
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..933
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..956
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..983
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1338 AA; 139815 MW; 3B09FB287B6FAB5D CRC64;
MIKMPSLWFI LGLSFYLVLT VKISEAQQAA ESGISLLQLI GNPPPEDITR VTGPNGRTAY
LFTNDTNTEQ MARAHLPTPF FREFSLVFHL KPNSENAGVL FSITDSNQKI MYIGVKLSAV
EDGKRKLFFY YTEPDSDTSQ EVASFDVEHK PQEWSRFSLA VSLDQVSFYS DCVSEPKVEK
FERSPDDLEL ETNSKIFVGQ SGTDDPDKYQ GMISELRVVG NPLAAERHCN DAAAADDDDD
DDDDDDYESS GENGSGIDNR MDMEPNLDSQ PVPTGDKPKL GKDDQQKATE AKTDPTTFSS
TGEEKGSIGS GYPGPEGDRG SPGPTGPPGP AGPQSPVTEV ITAEDIKVER VQGLMGPPGP
KGPQGEPGEP GQDGKPGPEG PRGFQGPPGT TGPKGQKGEK GEGHSGPRGP PGPPGPPGPS
ISDRTTFMDM EGSGSLPHLC CHPGLPGPPG LPGLPGPPGP DWPAESGLEP FEAGPTGQPG
QNGLPGRSGP PGRPGKPGPP GPPGQKGDCG DLGLPGVAGE KQSSDFSFFS NWFPSWETSG
AQGPQGTVGI PGPEGMAGLP GPMGPQGPPG PPGPPGPGFR ITTDGKEKEV DLQYIPGVMG
PPGPQGPQGI PGLPGKSGLP GISGQKGEEG QKGQEGMPGL DGFPGKIGLK GERGWKGEKG
DPGHALGPAG PPGPPGPPGQ VIYINGSTNG EYGIPGPQGT PGIAGQAGFP GPVGPKGDQG
EPGLPGDSVK GQKGEPGLIV DSSGKPIYIG GLAGQLGEPG PPGPEGPLGP VGPPGPKGEI
GLPGRPGRPG LNGKKGQKGD SGGGYGYEYQ GPPGPPGPPG PPGPPVSVGR YDGYDEGSSK
FPYAIKGEKG ERGAAGIPGL PGLTSTFDIY AFKHELKGEL GPKGQKGEPG EGYYDPHHSG
AQGPPGRPGP PGPRGESING PPGRPGPPGP PGTPGIGYDG RPGIPGPPGP PGPPGSLLPG
AHQPSQTFSI PGPPGPPGPP GPPGHLTGVM VLRSVDTMAA TTIRYPEGTL IYVKDNRELY
MRVHDGIREV MLGEYTPFPK GLDKQMEAVE PPQLVQYSQD YPTISPQQGP PQPGAQYPVP
LDPRLQPSYD PQHGYTFPHY SSPTDPRHSP SIDSIYQHHP DSRKHIPSSH PDHSGYPDSR
YGRTHHHRPV IQESKLPAHT HTSGRALHLI ALNSPQPGNM QGIKGVDHQC FLQAQAIGLK
GTFRAFLSSR LQDLYSIVRQ NNRELLPIVN LQDEELFSNW KSIFSGSEGK MNDNVRIYSF
DGRDVLDDDA WPEKMVWHGS SPEGSRQTDS YCETWRTGGH AVTGMASSVQ EGYLLQQLPR
GCSSSFIVLC IENSYTAE
//
