ID H3DCK8_TETNG Unreviewed; 1355 AA.
AC H3DCK8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Tensin 3 {ECO:0008006|Google:ProtNLM};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000018251.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000018251.1}
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; ENSTNIT00000018476.1; ENSTNIP00000018251.1; ENSTNIG00000015194.1.
DR GeneTree; ENSGT00940000156328; -.
DR HOGENOM; CLU_002189_1_0_1; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd01213; PTB_tensin; 1.
DR CDD; cd09927; SH2_Tensin_like; 1.
DR Gene3D; 2.60.40.1110; -; 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; IPR035892; C2_domain_sf.
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 InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR45734; TENSIN; 1.
DR PANTHER; PTHR45734:SF5; TENSIN-3; 1.
DR Pfam; PF08416; PTB; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR Pfam; PF00017; SH2; 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; 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; PS50056; TYR_PHOSPHATASE_2; 1.
PE 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}.
FT DOMAIN 1..170
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 103..142
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 175..301
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1075..1184
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 340..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1027
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1355 AA; 148238 MW; E6E2B4B8F3A45844 CRC64;
MEEGYELDLT YITERIIAVS FPRGCSEEIY SHNLKDVTRM LRSKHADNYL IINLSEKRHD
LTKMNPKTLD TGWPDMHAPP LDKICTICKA MEGWLNADPL HVVVIHCRGG KGRIGVVISS
FVNFTEVSAS ADQALDRFAM RKYHDDKVSA LMTPSQKRYV WILNSLLSGS MKINASPLFL
HCLILHGIPN FDAAGVCHPY IKVYQGMQAV YSSGIYHIGP GHRDRVCITL EPAQLLKGDI
MIKCYHKGDV ASVREVVFRL QFHTGAVQGY NLMFEKEDME SANKDSRFPD YGKVELVFSE
GPERIPGADR WQNGPDVIVD YNTADPLIRW DSYQNICDGD APRSQGLTQD KVSSKQSPSG
GEGTLGRGAC TTSATSSPDH SDHALSVSSD SGLSSTSLWA DKPASVVAST ITTGTIKHNQ
GPSQQEKVEL KRLLSGFGLE GPSAEDMDDQ GPRVGIQQIV PAQVHINGEP RPRERETDIL
DDEITVAHDL RSVDSLGTLS SSCHKSSQNS LLSDGFGSPG GEEHQGQSQH CTAPPAVEEY
ERAYADARRG CLTSRSNSVA SANPSSASIG KQHVYRQGSY STQSWVRQQQ MVAAQQFIYM
PENENEAEVY RGNKQGSSVS KASQPSQPTG TTTDTTKEAL RNKVPHKDEA TQQRDEEFKS
LTLDIDNSID QLNQLIMDLD PTFVPLSGLS SSIKRNGVSG SAPKCSNGIN LKFEDKNTGA
LKNTQQTGKL VGQSWCGGGR RHLSLQRYLQ NPGNLPRHRA HWHPLYRSTS AEYRPRVPEM
DSGVEVGSDT TPPTPAFPIS PPTPYDKTKK RDAQNFPSLP PLKCQSAGRK PRGYPVVTSH
VGVDGSPETS VNCHRTLSST QSASAVGPFQ RTESSCSVSP PWPEHPSLSC QASLGTYSST
RQPLHHSLSL DYSCCSPPLN HSHVHPAPNA HSSPRSGQRS RMACYALSRS PAQSFAEQED
SNLGYSTDCP NSTTSLLGNG SMDRDLLDGQ NPSLLLPPHL PEKKRASDGE HSFRTASPSL
SGFSSPHSGS SLSIPFPNVL PDLSSQMSGT ASPLPDVLAS KQVTAKFVQD TSKFWYKPDI
SRDQAISVLK DKEPGCFIIR DSHSFRGAYG LAMKVATPPP SVLQQSKKAD LSNELVRHFL
IECTQKGVRL KGCPNEPYFG SLTALVCQHS ITPLALPCKL ILPDRGLCFP LKDPLEDVVE
ATSQSVTNSA AELLKQGAAC NVWYLSSVEM ESLTGVQAVQ KATSMTLSSN PPPMSTVVHF
KVSSQGITLT DNQRKLFFRR HYHVNTVIYC ALDPQDRKWK RDGYPSARIF GFVARKTGNS
TDNVCHLFAE HDPEQPASAI VNFVSKVMIG SQKSK
//
