ID A0A8C8IFH2_ONCTS Unreviewed; 1136 AA.
AC A0A8C8IFH2;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2025, sequence version 2.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN Name=LOC112216467 {ECO:0000313|Ensembl:ENSOTSP00005078581.2};
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:ENSOTSP00005078581.2, ECO:0000313|Proteomes:UP000694402};
RN [1] {ECO:0000313|Ensembl:ENSOTSP00005078581.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSOTSP00005078581.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR AlphaFoldDB; A0A8C8IFH2; -.
DR Ensembl; ENSOTST00005085145.2; ENSOTSP00005078581.2; ENSOTSG00005059263.1.
DR GeneTree; ENSGT00940000164061; -.
DR Proteomes; UP000694402; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR050938; Collagen_Structural_Proteins.
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; PTHR37456:SF6; COLLAGEN ALPHA-1(XXIII) CHAIN-LIKE ISOFORM X2; 1.
DR PANTHER; PTHR37456; SI:CH211-266K2.1; 1.
DR Pfam; PF01391; Collagen; 2.
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 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Reference proteome {ECO:0000313|Proteomes:UP000694402};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1136
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044300383"
FT DOMAIN 36..224
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 231..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..296
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..346
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..371
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..390
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..432
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..470
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..483
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..614
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..927
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..945
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1136 AA; 115921 MW; 214AECE5728B9B47 CRC64;
MTSRISLWSV GIHLTLWYCQ LSTPYRLLDE GGSQGQMDLT ELIGVPLPPS VSFVTGFEGY
PAYRFGPDAN VGRLTKSFIP DPFYHDFTVI VTAKPTTRHG GVLFAITDAY QRVVQLGVAL
SPVEDGSQEV LLYYTDPGVG STQEAASFKL ADLTGRWARF TLTVQGTEVR LYMDCEEYHR
VAFQRSPEPL TFEASSGIFV GNAGGTGLDR FVGCIQQLVL KGYPTAQDDL CEEDDPYASG
YGSGDDSFDD TETLDEVKKV VEEREYTVPE EPWGTPVRAP PTEASPSDDE DADEISGQDV
ELKVERGPSR TADADYRPSS GTSSQKGEQG DPGPAGPPGS PGPPGPHSLF SKGLSQGLPG
PRGPQGPPGP AGTPGTPGND GQPGSGGIDG NPGETGVQGF PGLPGDPGPK GDKGDSGVGK
PGPPGPPGPP GRPNSSRSPD GVDGSGLEYF DGDTEIMTGP PGSPGLPGPP GSSEGLSASP
GAPGENGKDG EMGKPGLPGV DGNDGFPGPA GERGEKGEPG LSGTHGPKGE PGAAGFPGLP
GSEGPEGKTG LRGPPGLPGP PGQGFSLDLE GPIDKPGRPG PKGKDGQDGL PGVALKGEPG
APGAAGASGL DGLPGHTGAK GDQGDMGPKG ERGQDGFSFP SPPGPPGSSG PVINLQDVLL
RDTEGVFNFS GLLESQGLRG PQGPKGDLGN PGTIGPPGLK GEKGEPGAMV AADRSMMSEL
TGPQGPKGIK GDCGVPGPAG VTGPIGPEGP KGEYGYPGRP GRPGIMGHKG DRGDAVGVSG
SPGPPGPPGR PGMFNCPKGT VFPIPPRPHC KKAINGSENS TNGGPDCPLS GTKGDKGERG
FPGMPAPPLT MLPKGTMGNK GDKGEKGEAG LPGPPGMRGT SGMVGPQGET VMGPPGHPGV
PGSPGTPGYG RPGPEGPQGP PGHPGAPSPA VTIPGPQGPP GPAGPPGASA MMETFPSSEV
MMQRTMNSRE GTLSFITTGT GKLYIRVQEG WKEVLLGNLI YRPVNIPLPD TAQPGTARRY
GLNLVALNQP YTGNFGGDDM IDKRCYDQAM AMGLPANYRG FVSSKIQTIN KDLVPQRFRQ
SYPITNLRGD ILFSNYKSIF TGGGGKFPSN IPIYSFDGRD VMADPSQFWC VCVCVC
//