ID A0A8C8FZN6_ONCTS Unreviewed; 1426 AA.
AC A0A8C8FZN6;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2025, sequence version 2.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN Name=LOC112234908 {ECO:0000313|Ensembl:ENSOTSP00005040804.2};
OS Oncorhynchus tshawytscha (Chinook salmon) (Salmo tshawytscha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=74940 {ECO:0000313|Ensembl:ENSOTSP00005040804.2, ECO:0000313|Proteomes:UP000694402};
RN [1] {ECO:0000313|Ensembl:ENSOTSP00005040804.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSOTSP00005040804.2}
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 Ensembl; ENSOTST00005044415.2; ENSOTSP00005040804.2; ENSOTSG00005019501.2.
DR GeneTree; ENSGT00940000158212; -.
DR Proteomes; UP000694402; 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:UP000694402};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 70..259
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 35..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..421
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..461
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..514
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..594
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..637
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..656
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..698
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..760
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..902
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..966
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1031
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1061
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1177
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1426 AA; 146623 MW; 731B5D7A538CA688 CRC64;
MVGDASFLCP GSSDSRSIAM ASEALWFSWS STDGTTEAPT LDNEGSGNPD NVGEDGAEII
DVASGKHESS VSLLQLIGDP PPAEITKVYG PDNSPGYVFG PDANTGQLAR AHLPSPFYRD
FSLLFNLKPQ STNGGVIFSV TDPLQQIMYV GVKLSPVKAN RQNVIFYYTE PDSQESYVAA
TFPVHNLADQ WNRFSISVLD DKVTFYINCD DQPQVVRFER SPDEMELESG AGVFVGQAGG
ADPNKFLGVI GELRVVGDPR AAERQCEEEG DDSDAASGDG GSGDERIPDG EKKGSGTSIW
DAKIRKYVLV EDVRLTVTTT PTSSRPIQQP PVTRKQPEVS PKKERDQGGS RGEKGDRGEK
GDRGPIGLKG DSGSESGTRG GARGEKGVLG EKGMKGKAGF GYPGSKGDPG PAGPPGPPGL
PGPAAEVVSR GDGSVVQTVA GPRGPAGPPG ASGPEGPAGA DGEPGDPGED GSQGPVGPPG
FPGIPGDPGL KGEKGDRGEG QPGPRGPPGP PGQPAPTRHD RPTFADMEGS GFPDLETLRG
LPGLPGPPGL PGAPGTSVVG TGVSGLFGPK GPPGQDGAPG QPGLHGLPGA DGRPGAAGAG
GEKGDPGELG LPGAVGVKGA QGLNGIPGQP GQGGLAGLPG PMGPLGQPGP PGPPGPSYRV
GFDDMEGSGV GVANGVPGAR GPEGQQGPPG IPGLPGRSGF PGIPGEKGSE GPQGSDGRPG
LDGFPGPNGQ KGDSGDRGER GESGRDGNGQ PGPPGPPGPP GQIIYQTSSS YDGVVGGAGP
QGQAGFPGPI GPKGNMGDPG QPSYGVKGEK GEPGSIIGPD GNTLYLGRLS GEKGDRGPAG
PVGPPGQYGS PGIKGEFGMP GRPGRPGVNG YKGEKGEPST GAGFSYPGVP GPPGPPGPPG
PAVPVDRFNG YDASRNYPVT KGEKGDFGAQ GLPGTPGVAS NFDIFTFKND LKGERGDTGV
KGEKGEPSGG YYDPRFGRQQ GPPGPPGNPG LMGPKGDSIT GPPGPQGPPG SSGIGYDGRP
GNPGPPGPPG PTGSHSLPGA YRPTHPISIP GPPGPAGPPG IPGHTSGVTV LRSYDTMIAT
ARRQSEGTLI YIVDKTDLYI RVRNGFRQIM LSDYSPFYRD LDNEVAAVQP PPVVNYPQSQ
DHSANNGAEQ FSQGGAATHP IVPPPRQPIE IPRPAQPNNR DPRDPPQYDH RYPSQTDPRY
PPQTDGRYSP VQPENRYPTQ PERRYHITPQ RQPVPPPVPQ PAGHVHTSGP GLHLIALNTP
QVGNIRGIRG ADFLCFQQAR AVGLKGTFRA FLSSKLQDLY SIVRKSDRGS LPILNLKDHV
LFNSWESLFS KTEGRMEENA PIYSFDGRDI LRDSAWPEKM VWHGSSSEGH RQTDNYCETW
RAGDRAVTGL ASSLQTGQLL QQLPSSCSSS YIVLCIENSY LSHSKK
//
