ID A0A3Q1HWE3_ANATE Unreviewed; 1704 AA.
AC A0A3Q1HWE3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Tensin 1b {ECO:0000313|Ensembl:ENSATEP00000013312.2};
GN Name=TNS1 {ECO:0000313|Ensembl:ENSATEP00000013312.2};
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:ENSATEP00000013312.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000013312.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}.
CC -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC {ECO:0000256|ARBA:ARBA00007881}.
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DR Ensembl; ENSATET00000013529.2; ENSATEP00000013312.2; ENSATEG00000009288.2.
DR GeneTree; ENSGT00940000155400; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR CDD; cd20888; C1_TNS1_v; 1.
DR CDD; cd01213; PTB_tensin; 1.
DR CDD; cd09927; SH2_Tensin_like; 1.
DR Gene3D; 2.60.40.1110; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR013625; PTB.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR035012; Tensin-like_SH2.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR InterPro; IPR033929; Tensin_PTB.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR PANTHER; PTHR45734; TENSIN; 1.
DR PANTHER; PTHR45734:SF3; TENSIN-1; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF08416; PTB; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 22..69
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 63..235
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 240..366
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1437..1545
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 459..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1225..1385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..879
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..930
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1704 AA; 185329 MW; BA3E8B9DD3075D31 CRC64;
KSTHDLSIML WMWPEELEAL HSHTFRVKTF KKAKHCSVCK QTIIQDGLIC RVCRISCHKK
CEAKALEENY ELDLIYITER IISVSFPSNV EEQSYAANLR EVASMLRSKH GHNYLLFNLS
EKRYDISELN PKVLDFGWPD HHAPALDKIC SICKAMDTWL SADSHNVVVI HNKGNRGRTG
VVVAAYMHYS NISASADQAL DRFAMKRFYE DKVLPVGQPS QKRYVEYFSG LLSGHIKINN
KPLFLHHVIM HGIPNFESKG GCRPFLKIYQ AMQPVYTSGI YNVQGDSQTS ICITIEPGLL
LKGDILLKCY HKRYRSPCRD VIFRVQFHTC AIHDLGIVFG KDELDETFKD DRFPEYGKVE
FIFSFGPEKI HGVDHLENGP SVSVDYNTQD PLIRWDSYEN FNQNCEDTTD EVIHTQGPLD
GSLYAKVRKK ESVDGTLTAN GLPPTAVEHA LPAVDHALSV SSDSGNSTAS IKTDRTDEPT
SVHHCAPPAQ QQISPQEKQE LEQLLSGLEG PLHQQGYLST PTSAAGRMLH LVPAQVHVNG
HNSIDRETDI LDDELPTSQE GNSVDSLGTF SSTDGRATPA DLYYQSESLT NGQDHVPYLE
RNVPEKPLET IQPHVATSNK PVSLTQSDSI PSSGSYIATQ NGNLYRSQSF GSEPKSMPQA
PTRTTSSRDA VQRGLNVWQQ FGVPEEPVTE GLTFSPPPSV AVIPSHHSLP QFPHRHSASQ
QEIEKSIETL NLLMLDLEPG HSLVSKSQSA PLQEKSLVVT TQPSFSQSQT RPSYQDDAAI
HAHFSGPMSN LASHSSPAQI SPGKSSTPEP GPVQGSLSYT SDLAENSRPS EASPTVAGQI
QLKSINNYPP STLSKSVEIS EPQRSPSAAS ASPQQRDSEP DEVFNVEGLV AQRVAGVQAR
AVSLDEPATV PRRRITSEGQ YQNSPDDVSS PDVPLRSPIR CVSPEFVNAI AMNPGGRPKE
RNMHSYREAF EEMEGGPISP TPTVGRSPPG LAKTPLSALG LKPHNPAEIL LNQTGSAPRS
YVESVARSAV AGGEPPTSPR SLSPPGETAT QQRSQSPSSH TLNPPLSSSS PIQSSQGSVS
TPSQPTTDSG FRSQATESAY PTPTLSYQTA NTPTSSYLDS SSPAPSYLGT TTPTLSYLDP
NALLGSHTSL DPSLPTSQPS QTTLSHGSPH ARHRTNILGS THSPVLQHRS TTNQDGSTMV
QQTSIVNGFD VGMPGVSSSP ILSHRLSQGA QSSPVLSRQA SLGQQSERSP VLSRQTSLGQ
PIQSSPVLSR QSSITHPQGS PVFAHHPSVS QVSQRSPSLD RHPMHSGYNT PDERHGNLSR
QSSSSGYQGP PTPSFPISPA GYPDGGSMGM GGGFRQGSPA PGFQPQLPEK RRMSSGDRPN
GALSYGSLNG KIMSPMSGGS TPSYFHTLSD FSKFNIPDGS PDSRLNVKFV QDTTKFWYKP
DISRDQAISL LREREPGAFV IRDSHSFRGA YGLAMKVASP PPSVHQNKKG DITNELVRHF
LIESSPKGVK LKGCPNEPYF GCLSALVYQH AITPLALPCK LLIPATDLTE EVPEVATTNP
LAERLKQGAA CNVLYINSVE MESLTGPQAV AKAISETLAA ASPPTATIVH FKVSSQGITL
TDNQRKLFFR RHYPSNTVTF CDIDPQDRKW NKPEGGTAKL FGFVARKQGS TTDNVSHLFA
EMDPDQPASA IVNFVSKMIV SQKR
//
