ID A0A096NRW1_PAPAN Unreviewed; 1744 AA.
AC A0A096NRW1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Tensin 1 {ECO:0000313|Ensembl:ENSPANP00000015781.3};
GN Name=TNS1 {ECO:0000313|Ensembl:ENSPANP00000015781.3};
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000015781.3, ECO:0000313|Proteomes:UP000028761};
RN [1] {ECO:0000313|Ensembl:ENSPANP00000015781.3, ECO:0000313|Proteomes:UP000028761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT "Whole Genome Assembly of Papio anubis.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPANP00000015781.3}
RP IDENTIFICATION.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSPANT00000017510.3; ENSPANP00000015781.3; ENSPANG00000009910.3.
DR eggNOG; KOG1930; Eukaryota.
DR eggNOG; KOG2283; Eukaryota.
DR GeneTree; ENSGT00940000155400; -.
DR HOGENOM; CLU_002189_1_0_1; -.
DR Proteomes; UP000028761; Chromosome 10.
DR Bgee; ENSPANG00000009910; Expressed in aorta and 65 other cell types or tissues.
DR ExpressionAtlas; A0A096NRW1; baseline.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR CDD; cd01213; PTB_tensin; 1.
DR CDD; cd14560; PTP_tensin-1; 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 PANTHER; PTHR45734; TENSIN; 1.
DR PANTHER; PTHR45734:SF3; TENSIN-1; 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.
PE 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
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:UP000028761};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}.
FT DOMAIN 34..206
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 211..337
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1472..1581
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 407..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..1415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1234..1255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1371..1387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1744 AA; 186298 MW; 1E389C635A4AC0C8 CRC64;
MPLKLVGEAL LKGSARVTPS VQPHLQPIRN MSVSRTMEDS CELDLVYVTE RIIAVSFPST
ANEENFRSNL REVAQMLKSK HGGNYLLFNL SERRPDITKL HAKVLEFGWP DLHTPALEKI
CSICKAMDTW LNADPHNVVV LHNKGNRGRI GVVIAAYMHY SNISASADQA LDRFAMKRFY
EDKIVPIGQP SQRRYVHYFS GLLSGSIKMN NKPLFLHHVI MHGIPNFESK GGCRPFLRIY
QAMQPVYTSG IYNIPGDSQT SVCITIEPGL LLKGDILLKC YHKKFRSPAR DVIFRVQFHT
CAIHDLGVVF GKEDLDDAFK DDRFPEYGKV EFVFSYGPEK IQGMEHLENG PSVSVDYNTS
DPLIRWDSYD NFSGHRDDGM EEVVGHTQGP LDGSLYAKVK KKDSLHGSTG AVNATRPTLS
ATPNHVEHTL SVSSDSGNST ASTKTDKTDE PVPGASSAPA ALSPQEKREL DRLLSGFGLE
REKQGAMYHT QHLRSRPAGV PAVPSSGRHV VPAQVHVNGG ALASERETDI LDDELPNQDG
HSAGSVGTLS SLDGVTNTSE GGYPEALSPL TNGLDKPYPM EPMVNGGGYP YESASRAGAA
HAGHTVPMRP SYSAQEGLAG YQREGPHPAW PQPVTTSHYA HDPSSMFRSQ SFSEAEPQLP
PAPVRGGSSR EAVQRGLNSW QQQQQQQPQP RPPPRQQERV HLESLVASRP SPQPLAETPI
PSLPEFPRAA SQQEIEQSIE ALNMLMLDLE PASAAAPLHK SQSVPGAWPG ASPLSSQPLS
GSSRQSHPLT QSRSGYITSG HSLGTPEPAP RASLESVPPG RSYSPYDYQP CSAGPNQDFR
SKSPASSSLP AFLPTTHSPL GPQQPPASLP GLTAQPLLSP KEATSDPSRT PEEEPLNLEG
LVAHRVAGVQ AREKQPAEPP APLRRRAASD GQYENQSPEA TSPRSPGVRS PVQCVSPELA
LTIALNPGGR PKEPHLHSYK EAFEEMEGTS PSSPPPSGVR SPPGLAKTPL SALGLKPHNP
ADILLHPTGE PRSYVESVAR TAVAGPRAQD SEPKSFSAPA AQAYGHETPL RNGTLGGSFV
SPSPLSTSSP ILSADSTSVG SFPSGESSDQ GPRTPTQPLL ESGFRSGSLG QPSPSAQRNY
QSSSPLPTVG SSYSSPDYSL QQFSSSPESQ ARAQFSVAGV HTVPGSPQAR HRTVGTNTPP
SPGFGRRAIN PSMAAPSSPS LSHRQVMGPP GTGFHGSTVS SPQSSAATTP GSPSLGRHPT
GAYQVSGLHN NVATTPGSPS LGRHPGAHQG NLASGLHGNA IASPGSPSLG RHLGGSGSVV
PGSPCLDRHV AYGGYSTPED RRPTVSRQSS ASGYQAPSTP SFPVSPAYYP GLSSPATSPS
PDSAAFRQGS PTPALPEKRR MSVGDRAGSL PNYATINGKV SSPVASGMSS PSGGSTVSFS
HTLPDFSKYS MPDNSPETRA KVKFVQDTSK YWYKPEISRE QAIALLKDQE PGAFIIRDSH
SFRGAYGLAM KVSSPPPTIM QQNKKGDMTH ELVRHFLIET GPRGVKLKGC PNEPNFGSLS
ALVYQHSIIP LALPCKLVIP NRDPTDESKD SSGPANSTAD LLKQGAACNV LFVNSVDMES
LTGPQAISKA TSETLAADPT PAATIVHFKV SAQGITLTDN QRKLFFRRHY PLNTVTFCDL
DPQERKWMKT EGGAPAKLFG FVARKQGSTT DNACHLFAEL DPNQPASAIV NFVSKVMLNA
GQKR
//
