ID M3WS71_FELCA Unreviewed; 1884 AA.
AC M3WS71;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 4.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Tensin 1 {ECO:0000313|Ensembl:ENSFCAP00000017207.4};
GN Name=TNS1 {ECO:0000313|Ensembl:ENSFCAP00000017207.4,
GN ECO:0000313|VGNC:VGNC:66435};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000017207.4, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000017207.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000017207.4,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000017207.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000017207.4,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000017207.4}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000017207.4};
RG Ensembl;
RL Submitted (SEP-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 EMBL; AANG04002752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSFCAT00000031289.4; ENSFCAP00000017207.4; ENSFCAG00000001073.6.
DR VGNC; VGNC:66435; TNS1.
DR GeneTree; ENSGT00940000155400; -.
DR Proteomes; UP000011712; Chromosome C1.
DR Bgee; ENSFCAG00000001073; Expressed in adult mammalian kidney and 9 other cell types or tissues.
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 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:UP000011712};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 24..71
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 133..305
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 310..436
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1612..1721
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 85..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1221..1576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..962
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..978
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1376..1393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1480..1501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1510..1524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1553..1576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1884 AA; 201572 MW; 4591895679754A12 CRC64;
MIWAAGPSPL HSLFLPEDLE APKTHHFKVK TFKKVKPCGI CRQAITREGC TCKVCSFSCH
RKCQAKVAAP CIPPSNHELV PINPENAPKN VADTGEGAFR GGNTRKSLEE DGSSRVTPSV
QPHPQPIRNM SLSRTTEDSC ELDLVYVTER IIAVSFPSTA NEENFRSNLR EVAQMLKSKH
GGSYLLFNLS ERRPDIAKLH AKVLEFGWPD LHTPALEKIC SVCKAMDTWL NADPHNVVVL
HNKGNRGRIG VVIAAYMHYS NISASADQAL DRFAMKRFYE DKIVPIGQPS QRRYVHYFSG
LLSGSIKMNN KPLFLHHVIM HGIPNFESKG GCRPFLRIYQ AMQPVYTSGI YNVQGDSQTS
ICITIEPGLL LKGDILLKCY HKKFRSPARD VIFRVQFHTC AIHDLGVVFG KEDLDDAFKD
DRFPEYGKVE FVFSYGPEKI QGMEHLENGP SVSVDYNTSD PLIRWDSYDN FNGHREDGME
EVVGHTQGPL DGSLYAKVKK KDSLHGSTGA VNATRPVLSA TPNHVEHTLS VSSDSGNSTA
STKTDKTDEP APGPSSAPAA LSPEEKRELD RLLSGFGVER EKQGAMYHTQ HLRSRPAGGP
AVPSPGRHVV PAQVHVNGGA LASERETDIL DDELPNQDGH SVGSMGTLSS LDGVTNTSEG
GYPEALSSLT NGLDKPYPAE PMVNGGGYAY ESASRSVPAH AGHTAPMRPS YSAQEGLAGY
QREGPHPAWP QPITTSHYGH DPSGMFRSQS FPETEPQLPP APARGGSSRE AVQRGLNSWQ
QQQQQQQQPQ QQQQQPRPPP RQQDRAYLES LGPSRPSPQP LAETPIPGLP EFPRAASQQE
IEQSIETLNM LMLDLEPTAA APLHKSQSVP GAWPGASPLS SQPLSGSSCQ PHPLTQSRSG
YIPSGHSLGA PEPAPRASLE SFPPGRAYSP YDYQPCPGGP NQSFRPKSPA SSSSSAFLPT
THSPPGPQQP PASLPGLTAQ PQLPPKEVTS DPSRTPEEEP LNLEGLVAHR VAAYNAKLQS
IGHTSFQLPP LHRLRSSSLS GVQAREKQPA EPPAPLRRRA ASDGQYENQS PEPASPRSPG
VRSPVQCVSP ELALTIALNP GGRPKEPHLH SYKEAFEEME GASPTSPPPG GVRSPPGLAK
TPLSALGLKP HNPADILLHP AGVTRRLIQP EPRSYVESVV RTAVAGPRTQ DPEPKSFSAP
PVQAYSHEMP LRNGTLGSSF VSPSPLSTSS PILSADSTSV GSFPSGESSD QGPRTPTQPL
LGSGFRSGSL GQPSPSAQRS SQSSSPLPTV GSSYSSPDYS LQQFSSPESQ ARAQFTVAGV
HTVPGSPQAR HRTVGTNTPP SPGFGRRAIN PSMAAPSSPS LSHRQVMGPA GTGYHGSAVS
SPQSSTATTP GSPSLGRHPG AHQVSGLHGS VATTPGSPSL GRHPGAHQGN LASGLHGNAV
ASPGSPSPGR HLGGPGSVIP SSPSLDRHAA YGGYSTPEDR RPTLSRQSSA SGYQAPSTPS
FPVSPAYYPG LSSPVTSPSP DPAAFRQGSP TPALPEKRRM SVGDRAGSLP NYATVNGKVS
SSPVASGMSS PSGGSTVSFS HTLPDFSKYS MPDNSPETRA KVKFVQDTSK YWYKPEISRE
QAIALLKDQE PGAFIIRDSH SFRGAYGLAM KVSSPPPTVV QQNKKGDMTH ELVRHFLIET
GPRGVKLKGC PNEPNFGSLS ALVYQHSIIP LALPCKLVIP NRDPTDESKD SSGPANSTTD
LLKQGAACNV LFVNSVDMES LTGPQAISKA TSETLAADPT PAATIVHFKV SAQGITLTDN
QRKLFFRRHY PLNTVTFCDL DPQERKWMKT EGGAPAKLFG FVARKQGSTT DNACHLFAEL
DPNQPASAIV NFVSKVMLSA GQKR
//
