ID A0A2R9C5B6_PANPA Unreviewed; 1734 AA.
AC A0A2R9C5B6;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Tensin 1 {ECO:0000313|Ensembl:ENSPPAP00000036083.1};
GN Name=TNS1 {ECO:0000313|Ensembl:ENSPPAP00000036083.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000036083.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000036083.1}
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 EMBL; AJFE02063676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_008970175.1; XM_008971927.2.
DR RefSeq; XP_014199570.1; XM_014344084.1.
DR RefSeq; XP_014199571.1; XM_014344085.1.
DR Ensembl; ENSPPAT00000058973.1; ENSPPAP00000036083.1; ENSPPAG00000040585.1.
DR GeneID; 100976798; -.
DR CTD; 7145; -.
DR GeneTree; ENSGT00940000155400; -.
DR OMA; RYKQADN; -.
DR OrthoDB; 3439226at2759; -.
DR Proteomes; UP000240080; Unplaced.
DR Bgee; ENSPPAG00000040585; Expressed in heart and 6 other cell types or tissues.
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:UP000240080};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}.
FT DOMAIN 4..176
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 181..307
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1462..1571
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 377..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..838
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1019
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1224..1242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1734 AA; 185595 MW; 2C556699A9E3418B CRC64;
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 YHKKFRSPSR DVIFRVQFHT CAIHDLGVVF GKEDLDDAFK DDRFPEYGKV
EFVFSYGPEK IQGMEHLENG PSVSVDYNTS DPLIRWDSYD NFSGHRDDGM EEVVGHTQGP
LDGSLYAKVK KKDSLHGSTG AVNATRPTLS ATPNHVEHTL SVSSDSGNST ASTKTDKTDE
PVPGASSATA ALSPQEKREL DRLLSGFGLE REKQGAMYHT QHLRSRPAGG SAVPSSGRHV
VPAQVHVNGG ALASERETDI LDDELPNQDG HSAGSMGTLS SLDGVTNTSE GGYPEALSPL
TNGLDKSYPM EPMVNGGGYP YESASRAGPA HAGHTAPMRP SYSAQEGLAG YQREGPHPAW
PQPVTTSHYA HDPSGMFRSQ SFSEAEPQLP PAPVRGGSSR EAVQRGLNSW QQQQQQQQPR
PPPRQQERAH LESLVASRPS PQPLAETPIP SLPEFPRAAS QQEIEQSIET LNMLMLDLEP
VSAAAPLHKS QSVPGAWPGA SPLSSQPLSG SSRQSHPLTQ SRSGYIPSGH SLGTPEPAPR
ASLESVPPGR SYSPYDYQPC LAGPNQDFHS KSPASSSLPA FLPTTHSPPG PQQPPASLPG
LTAQPLLSPK EATSDPSRTP EEEPLNLEGL VAHRVAGVQA REKQPAEHPA PLRRRAASDG
QYENQSPEAT SPRSPGVRSP VQCVSPELAL TIALNPGGRP KEPHLHSYKE AFEEMEGTSP
SSPPPSGVRS PPGLAKTPLS ALGLKPHNPA DILLHPTGVT RRRIQPEEDE GKVVVRLSEE
PRSYVESVAR TAVAGPRAQD SEPKSFSAPA TQAYGHEIPL RNGTLGGSFV SPSPLSTSSP
ILSADSTSVG SFPSGESSDH GPRTPTQPLL ESGFRSGSLG QPSPSAQRNY QSSSPLPTVG
SSYSSPDYSL QHFSSSPESQ ARAQFSVAGV HTVPGSPQAR HRTVGTNTPP SPGFGRRAIN
PSMAAPSSPS LSHRQMMGPP GTGFHGSTVS SPQSSAATTP GSPSLGRHPA GAYQVSGLHN
NVATTPGSPS LGRHPGAHQG NLASGLHSNA IASPGSPSLG RHLGGSGSVV PGSPCLDRHV
AYGGYSTPED RRPTLSRQSS ASGYQAPSTP SFPVSPAYYP ALSSPATSPS PDSAAFRQGS
PTPALPEKRR MSVGDRAGSL PNYATINGKV SSPVASGMSS PSGGSTISFS 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
//
