ID A0A668U6K0_OREAU Unreviewed; 1356 AA.
AC A0A668U6K0;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2025, sequence version 2.
DT 28-JAN-2026, entry version 23.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN Name=col18a1a {ECO:0000313|Ensembl:ENSOABP00000035504.2};
OS Oreochromis aureus (Israeli tilapia) (Chromis aureus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=47969 {ECO:0000313|Ensembl:ENSOABP00000035504.2, ECO:0000313|Proteomes:UP000472276};
RN [1] {ECO:0000313|Ensembl:ENSOABP00000035504.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSOABP00000035504.2}
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 RefSeq; XP_031613233.1; XM_031757373.2.
DR AlphaFoldDB; A0A668U6K0; -.
DR Ensembl; ENSOABT00000036483.2; ENSOABP00000035504.2; ENSOABG00000016243.2.
DR GeneID; 116334061; -.
DR CTD; 564123; -.
DR Proteomes; UP000472276; Unassembled WGS sequence.
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; 4.
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:UP000472276};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1356
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044315285"
FT DOMAIN 30..219
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 225..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..337
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..380
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..409
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..468
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..507
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..532
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..607
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..634
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..710
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..738
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..806
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..825
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..844
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..861
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..887
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..924
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..966
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..987
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1014
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1356 AA; 139482 MW; D2473A3F4AD0C726 CRC64;
MRCSSWLERL VCCALILAGP MASQWSEDSG VSLLQLIGDP PPSEITQIYG PDNTPSFVFG
PDANTGQLAR AHLPNPFYRD FSLIFNLKPT TNQGGVIFSI TDARQSIMHV GVKLSAVQNN
NQNVILYYTK PKSARSFEAA RFLVTSMTDT WTRFSLAVMD NKVLFYFNCD TDPQVVHIER
STEDMELESG AGVFVGQAGG ADPDKFLGVI GELRVVGDPF AANRHCEEDE DDSDMASGEG
SGYVETRPPR PGTEKHTWTT ARPTLRPIPH PPMTRNDETA RDSQYVSLSV ESSPALRGPQ
VEAKGQKGDK GDRGEKGERG PAGPKGEAGS GSSSRSGSRG EKGESGTKGE KGSAGFGNKG
VKGEPGPPGP PGPPGPPGPA PEHTVGSDGS VSRVPGPRGP PGAPGPQGPP GADGEPGDPG
EDGKTGAQGP PGFPGTPGDS GAKGEKGDRG EGHPGPRGPP GPPGPPGPGF RSTFEDMEAS
GFPDLESIRG LPGLPGPPGP PGPPGLPGPS TAETASSSAA FGPPGKDGAP GKPGLPGIPG
TDGKPGAPGP NGEKGDAGEL GLPGAIGEKG AQGERGLPGT QGEPGLAGLP GPRGPVGPPG
PPGPPGPSYR VGFDDMEGSA GGFNGRPGIG GPDGIQGPPG LPGLPGNPGL PGRPGEKGDE
GPAGRDGQPG LDGFPGPPGS KGDRGDKGER GEPGRDGTGL PGPPGPPGPP GQIVYQTSGN
FDEVVGRAGP QGGPGLPGRA GFPGPMGPKG DRGDPGPPGY GEKGEKGEPG LVIGPDGNFL
NLAQLAGPKG DRGLPGPVGP PGPYGPPGLK GEIGMPGRPG RPGINGYKGE KGEPGVGSGL
GYPGVPGPPG PPGPPGPPGP ASPLDRFNRY DERNYPAIKG EKGERGEPGL PGIPGASSNV
DIYTFRNELK GERGEPGVKG EKGEPGGGYY DPRFGGVQGP PGPPGLPGPK GDSIIGPPGP
SGPTGPPGIG YDGRPGPPGP PGPPGPPGSL SGSYRPNYSV SIPGPAGPPG PPGAPGLSSG
VTVLRSYDTM IATARRQEEG SLIYIIDRAD LYLRVRDGVR QVMLGEYNPF FRELENEVAE
VQPPPVILYP ESQDQSQNNG AGHYSEGFTL IKPIEPPAPT PADPRYFPKY EPRFPDQTHT
GHTDGRFATQ QTESRFPVTP QRQPVPPVLE PAGRFDVHGS GLHLIALNSP HTGNMRGIRG
ADFLCFQQAR AIGLKGTFRA FLSSKLQDLY TIVRRSDRDS IPIVNLKNQV LFSSWDSLFG
DNVSTMRENV PIYSFDGRDI LRDSAWPEKM VWHGSSKKGH RQTDQYCETW RIGDHAVTGL
ASSLHSGHLL QQTPSSCSSS YIVLCIENAF TSPSKK
//
