ID A0AAZ1XI18_OREAU Unreviewed; 1259 AA.
AC A0AAZ1XI18;
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=LOC116324436 {ECO:0000313|Ensembl:ENSOABP00000067294.1};
OS Oreochromis aureus (Israeli tilapia) (Chromis aureus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=47969 {ECO:0000313|Ensembl:ENSOABP00000067294.1, ECO:0000313|Proteomes:UP000472276};
RN [1] {ECO:0000313|Proteomes:UP000472276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Israel {ECO:0000313|Proteomes:UP000472276};
RA Xu L., Tao W., Wang D., Zhou Q.;
RT "Evolution of repeat sequences and sex chromosomes of tilapia species
RT revealed by chromosome-level genomes.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOABP00000067294.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSOABP00000067294.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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DR AlphaFoldDB; A0AAZ1XI18; -.
DR Ensembl; ENSOABT00000065433.1; ENSOABP00000067294.1; ENSOABG00000017832.2.
DR Proteomes; UP000472276; 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:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
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 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Reference proteome {ECO:0000313|Proteomes:UP000472276};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1259
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044326210"
FT DOMAIN 38..227
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 228..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..300
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..351
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..376
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 457..472
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..516
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..554
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..585
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..623
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..694
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..792
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..810
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..835
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..938
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..951
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..971
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..981
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1000
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1259 AA; 129061 MW; 2BCB96EA13BB46AE CRC64;
MAPRIPPWLF GLFLLALRFC CHCSSAYQLL DDRGPRGALD LTELIGIPLP PSVSFVTGFE
GYPAYSFGPE ANVGRLTKSF IPDPFYHDFA ITVTAKPTTR QGGVLFAITD AYQKIVQLGV
ALSEVEDGSQ RVILYYTDAE TRGRTQEAAS FKMGDLTGRW ARFTLTVQGS EVRLYMDCEE
YHRVAFIRSA QPLTFESSSG IFVGNAGGTG LQRFVGSIQQ LLLKADPTAP DDQCEEDDPY
ASGYGSGDDE DLKGNDEVKK IVEEREFTMP ELAPTYIVIP PPPTEMPTSD DEDDDFEEAS
GQEMEATTVQ AKSFQTGAAV STPDTSLQVY PGQKGEPGPA GPPGAPGPPG PASAEGQGGE
PGPRGPQGPQ GPPGTPGLPG KDGQPGSKGE TGSPGANGFP GLPGESGPKG EKGDPGVGLP
GPPGPPGPPG QPSKSSVFLE GSGFEDFDSD TEIIRGPPGP PGPPGLPGPP GSPSEDIFSG
LPGTPGKDGR DGAKGEPGLP VTEEWFSGSG SDSESGSGQG VSGIDGIPGP AGEKGDKGEP
GVSGQPGPKG DQGPPGFPGL PGADGPEGHP GPRGLPGPPG PPGPPGRNFI PDFEDLEGSG
LETAAGATLP RGPQGPPGLP GLPGPKGKDG FEGVPGKPGQ KGEQGVPGHP GIPGTDGLTG
TEGPKGDKGD QGQKGEPGQD GRSLPGPPGP PGPPGTIINL QDLLLNDTDG SFNFSGIFEA
QGPAGPKGPK GDIGLPGFQG PPGLKGEKGE PGFVISADGS MMSGLSGPVG PKGVKGDNGV
PGPPGIQGPI GPPGHKGEFG LPGRPGRPGL MGHKGEKGDS RGLPGPPGPP GPPGRPGMFN
CPKGTVFPIP PRPHCKMPLN SNGTIATGNC QTGIKGEKGE RGLPGIPAPP MSYNQRGGWV
MNGDQGIKGE KGEAGFPGIS GISGRPGPVG PKGESVVGPP GPPGPPGPPG IPGYGKPGLV
GPPGPPGPPG PSGSSLRYGS GLTIAGPPGP PGPPGPPGPA SPSSNTASLK TFSTRESMMQ
QTVKDAEGTL AFVTTTGSLF LKVSQGWKEI QLGSLIYLSN NIIPQDEPRA SHHVRGDTMQ
RIHSVKGRLN LVALNQPHSG DMMGLDMADR MCFEQAKAMG LAPNYRAFIS SHRQDLVHVV
YPGFRQTLPV TNLRGDMMFR NWRSIFTGNG GPINTRIPIY SFDGRDVLAD PFWPQKSVWH
GSTSQGLRAT DKHCETWRAD HVSVMGQSSS LTSGLLLGQE TRSCSNEYIV LCIETHKNP
//
