ID A0A8C1J2K9_CYPCA Unreviewed; 1361 AA.
AC A0A8C1J2K9;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 16.
DE SubName: Full=Collagen type XVIII alpha 1 chain a {ECO:0000313|Ensembl:ENSCCRP00010026331.1};
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:ENSCCRP00010026331.1, ECO:0000313|Proteomes:UP000694427};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00010026331.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00010026331.1}
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; ENSCCRT00010028901.1; ENSCCRP00010026331.1; ENSCCRG00010011220.1.
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; 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: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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1361
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034085741"
FT DOMAIN 64..253
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 254..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1099..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..284
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..390
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..421
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..481
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..523
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..535
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..561
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..604
FT /note="Gly 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 645..661
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..723
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..750
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..870
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..935
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..977
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1001
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1025
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1145
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1361 AA; 140155 MW; 3AA28A646F7B19DB CRC64;
MSKLRFWLCL FILVCLRIHH THGWLWFNDS KENAKGAQTP AYLTTVRPTS PPRTEPPRTT
EESGVSLLQL VGDPPPDGVS KVFDDANNPS YVFDQSSNVG QSAAAHLPNP FFRDFSLIFN
IKPTSSKPGV IFSITDPTQN IMYVGVKLSA VEKGKQYIIF YYTEPDSQSS YEAARFSVPS
MVNTWTRFSI SVLNERVSLY FNCDSDPQVI RFERSPDDMD LDAGAGVFVG HASGADPDKF
LGVIGDMRVL KDPGAAERHC EEDEDDFDAN LQGSGDYGAS GDGEGQPSVQ PTPPSSRPIQ
QPPVTSRPLD EKQQTGAKGD RGEKGAKGDR GLVGPKGDAG SGSVSSGGEI LVKGDAGEKG
MKGNPGFGYP GSKGDRGPPG PPGPPGPPGP SAAVEERGDG SVVQRVAGPR GPPGPPGPPG
PAGADGEPGD PGEDGKAGQV GPPGFPGTPG SSGLKGEKGE RGEIQPGPRG PPGPPGPPGP
PSRSDRPTFV DMEGSGFDLD SVRAMPGLPG LPGPPGPPGP PGPSGTGSSG SGGIGPPGPP
GQNGAPGQPG LPGPSGADGK PGSPGPKGEK GDAGELGLPG PVGEKGAIGS PGSPGLPGEG
GLAGLPGPMG PVGPPGPPGP SYHVGFDDME GSGVHFSSVP GVRGPMGVQG PPGDPGPQGK
SGLPGFPGEK GSEGPQGKDG QPGLDGFPGP QGPRGDKGDR GDRGEPGRDG NGLPGPPGPP
GPPGQITYRY SEIYDETGGP GPQGGAGLPG QAGFPGPSGP KGDRGEPGSP GYGIKGEKGE
PGLILGPDGN PLYPGGLTGQ KGERGLPGPV GPSGPAGPSG LKGEFGMPGR PGRPGVNGYK
GEKGESGSGS GYGYPGPPGP PGPPGPPGPA VPLDRFGRYE DHSRHYPAMK GDKGDQGAPG
VPGSPGFSSN FDIYALKNEM KGERGELGLK GEKGEPGGGF YDPRFGAVQG PPGNPGLPGP
KGDSIRGPPG PQGPPGTPGV GYDGRPGNPG PPGPPGPPGS PSLPGAYRPQ LSIPGPPGPP
GPPGIPGTES GVAFLRSYDI MMATARRQTE GALIYILDRS DLYLRVRDGV RQVMLGDYKP
FYGEVDNEVA AVQPPPVVHY SQDHTANNGA EQISPQHPPI EFPRREPENR NPNPPDSRYP
DPRYPPYTDS RYTDPVQPER NPIVPARRPS PPVNQPEGHV HTSGPGLHLI ALNSPQVGNM
RGIRGADFLC FQQARAVGLK GTFRAFLSSK LQDLYSIVRK SDRETLPIVN LKDQVLFRSW
ESLFSDSESR MKDNAPIYSF DGRDVLRDSA WPEKMIWHGS SGRGHRQTDN YCETWRAGDR
AVTGLASSLQ AGQLLQQTSS SCSSSYIVLC IENSYMTQSK K
//
