ID A0AAZ3SI04_ONCTS Unreviewed; 1468 AA.
AC A0AAZ3SI04;
DT 05-FEB-2025, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2025, sequence version 1.
DT 28-JAN-2026, entry version 5.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN Name=LOC112234908 {ECO:0000313|Ensembl:ENSOTSP00005152656.1};
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:ENSOTSP00005152656.1, ECO:0000313|Proteomes:UP000694402};
RN [1] {ECO:0000313|Proteomes:UP000694402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=29621340;
RA Christensen K.A., Leong J.S., Sakhrani D., Biagi C.A., Minkley D.R.,
RA Withler R.E., Rondeau E.B., Koop B.F., Devlin R.H.;
RT "Chinook salmon (Oncorhynchus tshawytscha) genome and transcriptome.";
RL PLoS ONE 13:e0195461-e0195461(2018).
RN [2] {ECO:0000313|Ensembl:ENSOTSP00005152656.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSOTSP00005152656.1}
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; ENSOTST00005190160.1; ENSOTSP00005152656.1; 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, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1468
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044283913"
FT DOMAIN 112..301
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 87..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..463
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..503
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..556
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..636
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..679
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..698
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..740
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..802
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..944
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1008
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1073
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1103
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1219
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1222..1234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1468 AA; 151680 MW; DD576C600612B301 CRC64;
MDCKIGVSFL LVLLLGRSEA LWFSWSSTDG TTEAPTLDNE GSGNPDNVGE DGAEIIDVAS
GKRKFVQTWD QNLKATETHK LTTVWSQARN ERPIEKDAHG STSRGSKPDE SSVSLLQLIG
DPPPAEITKV YGPDNSPGYV FGPDANTGQL ARAHLPSPFY RDFSLLFNLK PQSTNGGVIF
SVTDPLQQIM YVGVKLSPVK ANRQNVIFYY TEPDSQESYV AATFPVHNLA DQWNRFSISV
LDDKVTFYIN CDDQPQVVRF ERSPDEMELE SGAGVFVGQA GGADPNKFLG VIGELRVVGD
PRAAERQCEE EGDDSDAASG DGGSGDERIP DGEKKGSGTS IWDAKIRKYV LVEDVRLTVT
TTPTSSRPIQ QPPVTRKQPE VSPKKERDQG GSRGEKGDRG EKGDRGPIGL KGDSGSESGT
RGGARGEKGV LGEKGMKGKA GFGYPGSKGD PGPAGPPGPP GLPGPAAEVV SRGDGSVVQT
VAGPRGPAGP PGASGPEGPA GADGEPGDPG EDGSQGPVGP PGFPGIPGDP GLKGEKGDRG
EGQPGPRGPP GPPGQPAPTR HDRPTFADME GSGFPDLETL RGLPGLPGPP GLPGAPGTSV
VGTGVSGLFG PKGPPGQDGA PGQPGLHGLP GADGRPGAAG AGGEKGDPGE LGLPGAVGVK
GAQGLNGIPG QPGQGGLAGL PGPMGPLGQP GPPGPPGPSY RVGFDDMEGS GVGVANGVPG
ARGPEGQQGP PGIPGLPGRS GFPGIPGEKG SEGPQGSDGR PGLDGFPGPN GQKGDSGDRG
ERGESGRDGN GQPGPPGPPG PPGQIIYQTS SSYDGVVGGA GPQGQAGFPG PIGPKGNMGD
PGQPSYGVKG EKGEPGSIIG PDGNTLYLGR LSGEKGDRGP AGPVGPPGQY GSPGIKGEFG
MPGRPGRPGV NGYKGEKGEP STGAGFSYPG VPGPPGPPGP PGPAVPVDRF NGYDASRNYP
VTKGEKGDFG AQGLPGTPGV ASNFDIFTFK NDLKGERGDT GVKGEKGEPS GGYYDPRFGR
QQGPPGPPGN PGLMGPKGDS ITGPPGPQGP PGSSGIGYDG RPGNPGPPGP PGPTGSHSLP
GAYRPTHPIS IPGPPGPAGP PGIPGHTSGV TVLRSYDTMI ATARRQSEGT LIYIVDKTDL
YIRVRNGFRQ IMLSDYSPFY RDLDNEVAAV QPPPVVNYPQ SQDHSANNGA EQFSQGGAAT
HPIVPPPRQP IEIPRPAQPN NRDPRDPPQY DHRYPSQTDP RYPPQTDGRY SPVQPENRYP
TQPERRYHIT PQRQPVPPPV PQPAGHVHTS GPGLHLIALN TPQVGNIRGI RGADFLCFQQ
ARAVGLKGTF RAFLSSKLQD LYSIVRKSDR GSLPILNLKD HVLFNSWESL FSKTEGRMEE
NAPIYSFDGR DILRDSAWPE KMVWHGSSSE GHRQTDNYCE TWRAGDRAVT GLASSLQTGQ
LLQQLPSSCS SSYIVLCIEN SYLSHSKK
//
