ID A0AAZ3RNN8_ONCTS Unreviewed; 1366 AA.
AC A0AAZ3RNN8;
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:ENSOTSP00005142673.1};
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:ENSOTSP00005142673.1, 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:ENSOTSP00005142673.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSOTSP00005142673.1}
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; ENSOTST00005162061.1; ENSOTSP00005142673.1; ENSOTSG00005063588.1.
DR GeneTree; ENSGT00940000164061; -.
DR Proteomes; UP000694402; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; 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; 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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1366
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044331239"
FT DOMAIN 107..298
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 297..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..417
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..503
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..545
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..610
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..929
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..961
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1009
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1070
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1087
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1366 AA; 140966 MW; 7DE4B250F003440B CRC64;
MAVLRLCSLL LLLLMAPVHG QWWSVLWGNA QEMTTQPPTT KVFWTMEGTE VGQEGTQTEV
YTTAPVQSTP LQSTHEPAGA GTTEIKPKAK KIPLKMWKSR ELGSTGHLDL TELIGVPLPP
SVSYITGYEG FRTAYNFGPG ANIGRLTKTF MPDPFFRDFA IIVTIRPSSN QGGVLFAITD
AQQRVVQLGL ALTAVEDQTQ RIQLYYTEGG QESSQSQQVV SFKVPDMTKK WTIFTLSVQD
QEVCLYMNCD DFQAETFHRS SRQLSFEPSS GIFVGNAGGT GLERFVGSIQ QLVIKSDPRA
AEEQCEEDDP YASGDGSGAE TMNDMKRRKE TARPEDMLSG PVRAPPTESP EVELDEYSGH
LTPTEEAHQE MHLRGPHQTE EPEMSGDGGP LSHRLKGERG EPGPIGPAGP RGPPGPPTLS
EGRRSGHRQP GPRGPLGPSG PTGAPGVPGK DGQQGSKGED GDPGQRGPQG FPGLAGEVGV
KGDKGDPGAG LPGPPGPPGP PGPLRSHSVP YGEDALGSGF GDLDNTELIR GPPGPPGQPG
PPGPTSPFNA SEGLFTGQPG PPGRYGLVGK PGPPVNEDWF SGSGLGSGFD TEFGSGLFGS
GLGSGEGQPG LDGDVGPTGP KGLKGEQGRV GPKGEPGDQG LAGATGLRGP EGKRGDTGPR
GLPGPPGPPG AGLFVEDMEG SGKNDMLLGV GLKGPQGPPG LPGSAGPKGE DGKDGAPGLS
VKGEPGAPGP EGLQGLAGLP GARGLKGDKG DPGPKGECGP DGHSVPGSPG PPGSPGPIIN
LQDLLLNDTE GMFNQIRGPP GPMGPEGEPG RAGFPGPRGP KGDIGLPGLH GPPGMKGAKG
DSGVTIAADG TVLTGVRGPQ GPKGIKGERG FPGVAGIMGP IGPTGQKGEY GFPGRPGRTG
MAGKKGDKGD AIGQPGLPGP PGPPGPPGPV IGLNGTVFPV RPRPFCKTPV NGSRGSSQGS
RRGNRGSKGE KGEVGLPGTP GEPDGVLPEG FVGEKGDVGY EGMKGEKGDA GLPGPPGLPG
RSGLVGPKGE SIIGAPGHPG APGEPGVPGT GRPGTRGPPG PAGPPGPPPV YASAVSIPGP
PGPPGPPGIT GYENLVTTYR NTITLMRESH RAAEGSMAYV SDKGELYVRA RDGWRKVQLG
ELIPVPAETP SSALSQALSR PDRSRPHRQE LVGTSYMPNY NVLPHTVHSV LGLHLVALNA
PFSGDMRGIR GADFQCYQQA RTIGLTATYR AFMSSHLQDL ATIVKKGDRY SMPVINLKGE
VLYGSWMNIF SGNVLDPSIP IYSFDGRNVM TDPTWPQKLV WHGSSTVGIR MTTNYCEAWR
AGDMAVTGQA SLLQTGRLLG QHTRSCSNRF VVLCIENSYT DHRRSN
//
