ID A0AAQ6ICR5_ANATE Unreviewed; 1798 AA.
AC A0AAQ6ICR5;
DT 27-NOV-2024, integrated into UniProtKB/TrEMBL.
DT 27-NOV-2024, sequence version 1.
DT 28-JAN-2026, entry version 6.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000072914.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000072914.1, ECO:0000313|Proteomes:UP000265040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Wellcome Sanger Institute Data Sharing;
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSATEP00000072914.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSATEP00000072914.1}
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; ENSATET00000077929.1; ENSATEP00000072914.1; ENSATEG00000013793.3.
DR GeneTree; ENSGT00940000165423; -.
DR Proteomes; UP000265040; Chromosome 2.
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; 3.
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:UP000265040};
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..1798
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5043714502"
FT DOMAIN 478..667
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 30..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..1450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1523..1583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..69
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..157
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..262
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..418
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..757
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..773
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..792
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..834
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..869
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..927
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..965
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1004
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1042
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1067
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1109
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1249
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1301
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1364..1380
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1413..1424
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1448
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1526..1536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1554..1568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1798 AA; 185098 MW; 678775E6E583791E CRC64;
MLKIQMWLFL LFLCCGSLEA WFWSSNSQPI TETPEGTTAA ETTPAWKTTN TTTTASNTTN
STLTTPAETM ENETSPIRLI PSDTSSETTT PSNTTNPTLT TPTETMPTGR TSETITPSNT
TNPTLTTPTE TMPTGRTTET TTESNTTNST LTTPAETMEN ETSPIRVIPS DTSSETTTES
NTTNPTLTTP TETMPTGRTS ETTTESNTTN PTLTTPTETM PTGRTSETTT ESNTTNPTLT
TPTKTRVETT ATETMPTKTR ATGTTPIETT AKQTTPVETT AIETTPIETT PTKTTATETT
PIETTATETT PIETTPIETT PTKTTATETT PTETTPTETT PTKTTATETT PIETTATETT
PTETTPTETT PTKTTATETT PTETTPTETT PTKTTATETT PVETVTTITT SGPATATVTR
KDEVGEEDSL SGLGEEIINL DIGFRRLYET WDATPTNGTA STGLTEKVEI ANTADESGTS
LLQLIGDPPP NGITKDYGPR GEAVYVFTSD TVTGQPALSH VPNPFYRHFS LFFNIKPSTP
AASVLFSITD GAHKLMHISV KLSAVQSGRQ TVQFFYTEPD AEASYEAASF DVPSLVDTWS
RFSLAVSEDE VMFYHGCDSE PQIVKFERSP DPMELDPAAG IFVGQAGGAD PDKFQGEIAE
LKVVGNSRAA ERLCDDEDDI EAASGDFGSG EGDRRQTGHT VIKQPVKTTA APSRPVPEPP
LISSQGTTLK ESDVKYKQQS ADYSQSGSTG PRGPSGPKGD KGDRGEKGSK GDEGPAGPKG
DSGSRSDSGV SSQAGERGQK GEKGVKGSSG FGYPGNKGER GAQGPPGPPG PPGPAAEVVR
LGDGSVVQQV AGPPGPSGPP GLDGAAGRPG ADGEPGDPGE DGKSGPAGPQ GSPGKPGTPG
AKGQKGELGE GQPGPRGPPG PPGPPGPGTG STFVDMEGSG FPDLDKYRGS RGLPGPPGPP
GPPGIPGTSV ALGPNGPVAF GPPGPPGQDG VPGLPGPPGP PGAPGPSGAR GEKGDCGELG
LPGPAGEKGS QGEPGQTGTS GQIGLAGLPG PIGPVGPPGP PGPPGPPYRA GFSDQDGYEV
INGLPGLTGP PGPQGPPGVA GLPGQPGLPG NHGDKGAEGP RGPPGIPGID GVPGQAGEKG
ERGEKGEMGR PGRDGGPPGP PGPPGPPGEI ISRSTGEDGP GTPGRAGFPG PMGPKGDKGD
SGPPGYAPKG QKGEPGIILG PDGTPMYLGG LAGQPGDAGP PGPVGPPGPS GLKGEIGFPG
RPGRPGLNGI KGEKGDSGSG SGYGYPGPPG PPGPPGPPGP SVPVDRLGGY EDYSRYYPTL
KGEKGDRGPP GIPGVGSNSD FYTFKNELKG ETGSPGVKGD KGEPGGGYYD PRYGGVGAPG
VPGPPGPKGD SIIGPSGPPG PIGPPGIGYD GRPGPPGPPG PPGPSLSDIY RGTQTITIPG
PPGPPGVPGL PGHAGVTVLR SYDTMTATAR RQPEGSLVYI IDQTDLYLRV RDGVRQVQLG
TFIALPSDDG NEVAAVEPRQ DISYYPDHHS NTDTHYPHVT QTNPQNPDPR NHPDSQYQPD
PRYPSSTDPR FPSYAERLNH PDGRYSVHTV QEQPVYPDAR YAVTPQRRPP PPVQTPVHHH
NSGPGLHLIA LNSPQTGSMR GIRGADFLCF TQAQAIGMKG TFRAFLSARL QDLYSIVRKT
DRDHLPIVNM KDETLFDNWE AIFSGSRMKD NVPIYSFDGK DVLTDSAWPE KMVWHGSTSA
GQRHIDSYCE TWRVGDRALS GMASSLQSGS LVQQSSSSCS SSYVVLCIEN SYMGQSKR
//
