ID A0A2Y9JQB8_ENHLU Unreviewed; 1741 AA.
AC A0A2Y9JQB8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Tensin-1 isoform X1 {ECO:0000313|RefSeq:XP_022361749.1};
GN Name=LOC111149091 {ECO:0000313|RefSeq:XP_022361749.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022361749.1};
RN [1] {ECO:0000313|RefSeq:XP_022361749.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022361749.1};
RG RefSeq;
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 RefSeq; XP_022361749.1; XM_022506041.1.
DR KEGG; elk:111149091; -.
DR Proteomes; UP000248482; Unplaced.
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; 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:UP000248482};
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 1469..1578
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 398..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..850
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1410..1433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1741 AA; 185621 MW; E51457F1FAC51F66 CRC64;
MSVSRAMEDS CELDLVYVTE RIIAVSFPST ANEENFRSNL REVAQMLKSK HGGSYLLFNL
SERRPDITKL HAKVLEFGWP DLHTPALEKI CSVCKAMDTW LNADPHNVVV LHNKGNRGRI
GVVIAAYMHY SNISASADQA LDRFAMKRFY EDKIVPIGQP SQRRYVHYFS GLLSGSIKMN
NKPLFLHHVI MHGIPNFESK GGCRPFLRIY QAMQPVYTSG IYNVQGDSQT SICITIEPGL
LLKGDILLKC YHKKFRSPAR DVIFRVQFHT CAIHDLGVVF GKEDLDDAFK DDRFPEYGKV
EFVFSYGPEK IQGMEHLENG PSVSVDYNTS DPLIRWDSYD NFDGHREDGM EEVVGHTQGP
LDGSLYAKVK KKDSLHGSTG AVNAVRPALS ATPNHVEHTL SVSSDSGNST ASTKTDKTDE
PAPGPSSAPA ALSPEEKREL DRLLSGFGVE REKAAPMYHT QHLRSRPAGG LAAPAAGRHV
VPAQVHVNGG TLASERETDI LDDELPNQDG HSVGSMGTLS SLDGVTNTSE GGYPEALSSL
TNGLDKSYPG EPMVNGGGYP YESASRAAPA HVSPPAPVRP SYSAQEGLAG YQREGPHPAW
PQPVPTSHYG LDPSGMFRSQ SFPESEPQLP PAPARSGSSR EAVQRGLNSW QQQQQQQQQQ
QQQQPRPPPR QQERAHLESL GHSRPSPQPL AETPTPGLPE FPRAASQQEI EQSIEALNML
MLDLEPAAAA APLHKSQSVP GAWPGASPLS SQPLSGSPCQ PHPLTQSRSG YIPSGHSLGT
PEPAPRSSLA LESFPSGRPY SPYDYQPCPA GSSLSFRPKS PASSSSSTFL PTTQSPPGPQ
QPPVSLSGLP AQPQFPPKEA TSDPSRTPDE EPLNLEGLVA HRVAGVQARE KQPAEPPAPL
RRRAASDGQY ENQSPEPASP RSPGVRSPVQ CVSPELALTI ALNPGGRPKE PHLHSYKEAF
EEMEGTSPTS PPSSGVRSPP GLAKTPLSAL GLKPHNPADI LLHPTGVTRR LIQPEEDEGK
VVTELPKEPR SYVESVVRTA VAGPRAQDPE PKSFSAPAAQ AYGHETPLRN GTLGGSFVSP
SPLSTSSPIL SADSTSVGSF PSGESSDQGP RTPTQPLLDS GFRPGSLGQP SPSAQRNYQS
SSPLPPAGSS YGSPDYSLQQ FGSPEGQARS QFTVAGVHTV PGSPQARHRT VGTNTPPSPG
FGRRAINPSL AAPGSPSLSH RQVMGPAGTG FHGSTVSSPQ GSAATTPGSP SLGRHPGAHQ
VPGLHGGVAT TPGSPSLGRH PGAHQSSLAP GLHGNTIASP GSPSMGRHLG GSGSVVPGSP
SLDRHVAYGG HSTPEDPRPT LSRQSSASGY QAPSTPSFPV SPAYYPGLSS PAASPSPDSA
AFRQGSPTPA LPEKRRMSVG DRAGSLPNYA TVNGKVSSSP VASGMSSPSG GSTVSFSHTL
PDFSKYSMPD NSPETRAKVK FVQDTSKYWY KPEISREQAI ALLKDQEPGA FIIRDSHSFR
GAYGLAMKVS SPPPTIMQQN KKGDMTHELV RHFLIETGPR GVKLKGCPNE PNFGSLSALV
YQHSIIPLAL PCKLVIPNRD PTDESKASSG PANSTTDLLK QGAACNVLFV NSVDMESLTG
PQAISKATSE TLAADPTPAA TIVHFKVSAQ GITLTDNQRK LFFRRHYPLN TVTFCDLDPQ
ERKWMKTEGG VPAKLFGFVA RKQGSTTDNA CHLFAELDPN QPASAIVNFV SKVMLNAGQK
R
//
