ID A0A6P7JXG9_9TELE Unreviewed; 1440 AA.
AC A0A6P7JXG9;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE SubName: Full=Collagen alpha-1(XVIII) chain-like isoform X3 {ECO:0000313|RefSeq:XP_028280211.1};
GN Name=LOC114447874 {ECO:0000313|RefSeq:XP_028280211.1};
OS Parambassis ranga (Indian glassy fish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Ambassidae; Parambassis.
OX NCBI_TaxID=210632 {ECO:0000313|Proteomes:UP000515145, ECO:0000313|RefSeq:XP_028280211.1};
RN [1] {ECO:0000313|RefSeq:XP_028280211.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-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 RefSeq; XP_028280211.1; XM_028424410.1.
DR GeneID; 114447874; -.
DR Proteomes; UP000515145; Chromosome 2.
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; 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:UP000515145};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1440
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027813397"
FT DOMAIN 124..313
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 94..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..106
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..412
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..455
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..516
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..548
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..588
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..630
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..711
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..794
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..808
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..957
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1059
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1080
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1103
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1440 AA; 147928 MW; C32758C2BEE1D6DD CRC64;
MVRAQTMWLV LLVLCAGRLE AWWWAPGPKT ELTTEPTTEA PTTERTWTTG ATTTAGGVKK
KEGEDKDNLS GVGEEIINVA TGIRKFVEAW DATTTTTPGT TNGGLTEKVE NANPNMTDNT
EDSGVSLLQL IGDPPPDQIT RVYGPTGDSA YVFTRAAVSG QLALAHVPNP FYRHFSLIFH
VKPTSHAAAV LFSITDGPQK FMYIGVKLSA EDSGRQKVQF FYTEPDSEAS YEAAVFNVPS
IVNSWTRFSL SIFEDQVMFY LGCDSEPQVV KFERSPDPME LDTAAGIFVG QAGGADPNKF
QGEIADLKVV GNHRAAERLC DDEDDYDTAS GDFGSGEVDS RQTGRTVKTT PASFRPVPEP
PLTSSHGSRL QETGPTGSKG EKGDGGEKGS KGDQGPSGPK GDSGSSSGSG FSSQGGGREQ
KGEKGEKGNS GFGYPGSKGE RGNPGSPGPP GPPGPAAEVV RLGDGSVVQQ VAGPPGPPGP
PGVDGAVGPR GTDGEAGDPG EDGKAGPPGP KGPPGNPGLA GTKGQKGERG EGQPGPRGPP
GPPGPPGPGT GDRPTFVDME GSGFPDLDRF RGGQGLPGPP GPPGPPGIPG TSVALGPNGP
VAFGPPGPPG QDGAPGRPGP PGPPGPPGPP GTRGVKGDGG DLGLPGTAGE KHDAQDSNFF
NDLFSYFAPP SSGARGDRGQ TGTTGESGLA GLPGPMGPVG PPGPPGPPGP PFRIGYDGYN
LINDLPGVRG PPGPQGPPGI AGLPGKPGLP GNHGNKGAEG PRGPPGISGL DGYPGLGGEK
GDRGEKGEMG RPGRDGGPPG PPGPPGPPGQ GFYQPTGDYT EANWNEASEG RSGVPGRPGF
PGPMGPKGDK GDTGRPGYAP KGEKGEPGII LGPDGRPMYL GGLAGKPGDR GIQGPEGPPG
PYGPPGQKGE IGFPGRPGRP GLNGVKGEKG DSGGGSGYGY YPGPPGPPGP PGPPGPPSHL
VSGAGYDDSS RGYPVKGEKG DRGPPGITLE LPGDRSKVDL YTLWDELKGS PGQKGEKGEP
SYDPRYGGSG VGAPGAPGPP GPQGDSITGP PGPQGPPGSP GRGYDGRPGP PGPPGPPGPS
LPGAYRGTQT ISIPGPPGPP GAPGLPGQSS GVTVLRSYDT MRATARRQPE GSLVYIIDQT
DLYLRVRDGV RQVQLGSYIP LPPADGNEVA AVQPPPVIPY PDHHSTHDSQ SPPENQPQPH
NPTHTDPRYQ PDPRYPPPTD PRFPSYSDRL NQPDGRYSAP ESRYPVTPQR RPPPPVPQTP
VHHHTSGPGL HLIALNSPQT GAMRGIRGAD FMCFTQAQAI GMKGTFRAFL SSRLQDLQSI
VRRADRDSIP IVNLKDEVLF DNWDAIFSNS RMKDNVPIYS FDGKDVLTDS TWPEKMMWHG
STAVGQHHDN GLCEAWRVGD RALSGMASSL RDGSLLQQSA SSCSSSYTVL CIENSYIAKR
//
