ID A0AAZ3QTS8_ONCTS Unreviewed; 1280 AA.
AC A0AAZ3QTS8;
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=COL18A1 {ECO:0000313|Ensembl:ENSOTSP00005132727.1};
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:ENSOTSP00005132727.1, 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:ENSOTSP00005132727.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSOTSP00005132727.1}
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 AlphaFoldDB; A0AAZ3QTS8; -.
DR Ensembl; ENSOTST00005129444.1; ENSOTSP00005132727.1; ENSOTSG00005063588.1.
DR GeneTree; ENSGT00940000164061; -.
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:SF1090; ALPHA2(IV)-LIKE COLLAGEN; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 5.
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1280
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044321084"
FT DOMAIN 35..226
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 225..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..345
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..431
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..473
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..538
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..857
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..875
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..923
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..984
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1001
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1072
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1280 AA; 131556 MW; 624B6158257013C8 CRC64;
MIIRLPRWSS VLLLSLLYHF EPAVQVIEEL GSTGHLDLTE LIGVPLPPSV SYITGYEGFR
TAYNFGPGAN IGRLTKTFMP DPFFRDFAII VTIRPSSNQG GVLFAITDAQ QRVVQLGLAL
TAVEDQTQRI QLYYTEGGQE SSQSQQVVSF KVPDMTKKWT IFTLSVQDQE VCLYMNCDDF
QAETFHRSSR QLSFEPSSGI FVGNAGGTGL ERFVGSIQQL VIKSDPRAAE EQCEEDDPYA
SGDGSGAETM NDMKRRKETA RPEDMLSGPV RAPPTESPEV ELDEYSGHLT PTEEAHQEMH
LRGPHQTEEP EMSGDGGPLS HRLKGERGEP GPIGPAGPRG PPGPPTLSEG RRSGHRQPGP
RGPLGPSGPT GAPGVPGKDG QQGSKGEDGD PGQRGPQGFP GLAGEVGVKG DKGDPGAGLP
GPPGPPGPPG PLRSHSVPYG EDALGSGFGD LDNTELIRGP PGPPGQPGPP GPTSPFNASE
GLFTGQPGPP GRYGLVGKPG PPVNEDWFSG SGLGSGFDTE FGSGLFGSGL GSGEGQPGLD
GDVGPTGPKG LKGEQGRVGP KGEPGDQGLA GATGLRGPEG KRGDTGPRGL PGPPGPPGAG
LFVEDMEGSG KNDMLLGVGL KGPQGPPGLP GSAGPKGEDG KDGAPGLSVK GEPGAPGPEG
LQGLAGLPGA RGLKGDKGDP GPKGECGPDG HSVPGSPGPP GSPGPIINLQ DLLLNDTEGM
FNQIRGPPGP MGPEGEPGRA GFPGPRGPKG DIGLPGLHGP PGMKGAKGDS GVTIAADGTV
LTGVRGPQGP KGIKGERGFP GVAGIMGPIG PTGQKGEYGF PGRPGRTGMA GKKGDKGDAI
GQPGLPGPPG PPGPPGPVIG LNGVNGSRGS SQGSRRGNRG SKGEKGEVGL PGTPGEPDGV
LPEGFVGEKG DVGYEGMKGE KGDAGLPGPP GLPGRSGLVG PKGESIIGAP GHPGAPGEPG
VPGTGRPGTR GPPGPAGPPG PPPVYASAVS IPGPPGPPGP PGITGYENLV TTYRNTITLM
RESHRAAEGS MAYVSDKGEL YVRARDGWRK VQLGELIPVP AETPSSALSQ ALSRPDRSRP
HRQELVGTSY MPNYNVLPHT VHSVLGLHLV ALNAPFSGDM RGIRGADFQC YQQARTIGLT
ATYRAFMSSH LQDLATIVKK GDRYSMPVIN LKGEVLYGSW MNIFSGNVLD PSIPIYSFDG
RNVMTDPTWP QKLVWHGSST VGIRMTTNYC EAWRAGDMAV TGQASLLQTG RLLGQHTRSC
SNRFVVLCIE NSYTDHRRSN
//
