ID A0A3Q1F1V8_9TELE Unreviewed; 1816 AA.
AC A0A3Q1F1V8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Tensin 1 {ECO:0000313|Ensembl:ENSAPOP00000010768.1};
GN Name=TNS1 {ECO:0000313|Ensembl:ENSAPOP00000010768.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000010768.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000010768.1}
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; ENSAPOT00000031342.1; ENSAPOP00000010768.1; ENSAPOG00000013264.1.
DR GeneTree; ENSGT00940000155400; -.
DR Proteomes; UP000257200; 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; PS00479; ZF_DAG_PE_1; 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:UP000257200};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 14..61
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 105..277
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 282..408
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1540..1648
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 78..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1101..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1248..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1345..1498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1415..1434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1816 AA; 196937 MW; E09BCE995EA785EC CRC64;
MSLWLPEEVE ALHSHTFRVK TFKKTKHCSV CKQTIIQDGL ICRVCRIACH KKCEVKVSSS
CVPATNYELA PSSDLPLKHV DTMGSTKSSK SMESRRRPSR SVSLLQALEE NYELDLIYIT
ERIISVSFPS SVEEQSYAAN LREVASMLRS KHGHNYLLFN LSEKRYDISQ LNPKVLDFGW
PDHHAPALDK ICSICKAMDT WLSADSHNVV VIHNKGNRGR TGVVVAAYMH YSNISASADQ
ALDRFAMKRF YEDKVLPVGQ PSQKRYVEYF SGLLSGHIKI NNKPLFLHHV IMHGIPNFES
KGGCRPFLKI YQAMQPVYTS GIYNVQGDSQ TSICITIEPG LLLKGDILLK CYHKRYRSPC
RDVIFRVQFH TCAVHDLGIV FGKDELDETF KDDRFPEYGK VEFIFSFGPE KIHGQGMDHL
ENGPSVSVDY NTQDPLIRWD SYENFNQNCE DATDGENEVI HTQGPLDGSL YAKVRKKDSV
DGTVTSNGLP PTAVEHALPA VDHALSVSSD SGNSTASIKT DRTDEATTAP QASTVSQTHI
PVGEELPSVH HHAPPAQQPI SPQEKKELEQ LLSGLEGPMH RQAYLSTPTS AVGGMLHLVP
AQVHVNGHSA IDRETDILDD ELPTSQEGNS VDSLGTFSST DGRATPADLY YQSESHINGQ
DHVPYLERSV PEKPLETIQP HFGISDKPVT LIQSDLIPSS GNCMATQNGS LYRSQSFGAE
PKSMPPAPTR TTSSRDAVQR GLNVWQRFGV PEEPVTEGLT FSPPPAVAVL PSHHSLPQFP
HRHSASQQEI EQSIETLNLL MLDLEPGRSV VTKSQSAPLQ DNSVVVTTQP SFSQSQTRPS
YQADAAIHTH FSGPVSNLSS HLTPSQMSPG KPSTPEPVPV HGSLNYSSET AGTSTPLQAS
PAVSGHLQLK SINNYPPATQ PAEASEYQRS PTAASASQQP RDSEPDEVFN VEGLVAQRVA
GVQARAMSLD EPATLPRRRI TSEGQQQNGP EDNLSSEVPV RSPIRCVSPE FVNAIALNPG
GRPKERNMHS YREAFEEMEG GLIGPTPTVG GEAFPQTPAF PISPQTPYFN LCRSPPGLAK
TPLSALGLKP HNPAEILLNQ TGTDDESSEG EEAPRSYVES VARSAQTGGE LPASPRSLSP
PVETTSQQGS TSPTTHTLNP PLSSSSPIQS SQGDHPLPES SVSTPSQPTT DSGFRSQATE
SAYPTPTPSY QGLNTPTSSY LDSSSPASSY LGATTPTLSY LGPNTVLGSY VTSDPSPPNS
EPPQTTLSHG SPHAQRQTNI LGSTQSPVSQ QLRSASPDRP VMGQQMSPAN GFEVGMPGVA
GSPILGRRLS QGGQSSPVLS RQAFLGQGSQ QSPVLSRQPS LGQPIQSSPV LSRQPSLTHP
QGSPVLGRHP SVSQMSQRSP SLDRHPMHSG YTTPDERHGN LSRQSSSSGY QGPPTPSFPI
SPAGYQDGGM MGTGMGVRQG SPAPGFQPQL PEKRRMSSGD RPNGAPSYGT LNGKIMSPMS
GGSTPSYFHT LSDFSRFNMP DGSPESRLNV KFVQDTSKFW YKPDISREQA INLLREREPG
AFVIRDSHSF RGAYGLAMKV ASPPPSAHQS KKGDITNELV RHFLIESSPK GVKLKGCPNE
PYFGCLSALV YQHAITPLAL PCKLLIPTTD LIEEAPEVVP TNPLTERLKQ GAVQRAPADS
HACNVLYINS VEMESLTGPQ AVAKAISETL AAASPPTATV VHFKVSSQGI TLTDNQRKLF
FRRHYPTNTV TFCDIDPQDR KWSKPEGVSA KMFGFVARKQ GSTTDNVSHL FAELDPDQPA
SAIVNFVSKM IAAQKR
//
