ID A0A6P7JTE9_9TELE Unreviewed; 1439 AA.
AC A0A6P7JTE9;
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 X4 {ECO:0000313|RefSeq:XP_028280220.1};
GN Name=LOC114447874 {ECO:0000313|RefSeq:XP_028280220.1};
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_028280220.1};
RN [1] {ECO:0000313|RefSeq:XP_028280220.1}
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_028280220.1; XM_028424419.1.
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: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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1109; COLLAGEN ALPHA-4(IV) CHAIN-LIKE; 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..1439
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028114938"
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..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..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 385..398
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..432
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..475
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..536
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..568
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..608
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..650
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..710
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..793
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..807
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..956
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1058
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1079
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1102
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1439 AA; 147829 MW; A874355CDA5BD823 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 QETDIRYRQP SVEYSRSGSP GPRGPTGSKG 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 KGARGDRGQT GTTGESGLAG LPGPMGPVGP PGPPGPPGPP FRIGYDGYNL
INDLPGVRGP PGPQGPPGIA GLPGKPGLPG NHGNKGAEGP RGPPGISGLD GYPGLGGEKG
DRGEKGEMGR PGRDGGPPGP PGPPGPPGQG FYQPTGDYTE ANWNEASEGR SGVPGRPGFP
GPMGPKGDKG DTGRPGYAPK GEKGEPGIIL GPDGRPMYLG GLAGKPGDRG IQGPEGPPGP
YGPPGQKGEI GFPGRPGRPG LNGVKGEKGD SGGGSGYGYY PGPPGPPGPP GPPGPPSHLV
SGAGYDDSSR GYPVKGEKGD RGPPGITLEL PGDRSKVDLY TLWDELKGSP GQKGEKGEPS
YDPRYGGSGV GAPGAPGPPG PQGDSITGPP GPQGPPGSPG RGYDGRPGPP GPPGPPGPSL
PGAYRGTQTI SIPGPPGPPG APGLPGQSSG VTVLRSYDTM RATARRQPEG SLVYIIDQTD
LYLRVRDGVR QVQLGSYIPL PPADGNEVAA VQPPPVIPYP DHHSTHDSQS PPENQPQPHN
PTHTDPRYQP DPRYPPPTDP RFPSYSDRLN QPDGRYSAPE SRYPVTPQRR PPPPVPQTPV
HHHTSGPGLH LIALNSPQTG AMRGIRGADF MCFTQAQAIG MKGTFRAFLS SRLQDLQSIV
RRADRDSIPI VNLKDEVLFD NWDAIFSNSR MKDNVPIYSF DGKDVLTDST WPEKMMWHGS
TAVGQHHDNG LCEAWRVGDR ALSGMASSLR DGSLLQQSAS SCSSSYTVLC IENSYIAKR
//
