ID A0A1S3KJI3_SALSA Unreviewed; 1091 AA.
AC A0A1S3KJI3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Tensin-3-like {ECO:0000313|RefSeq:XP_013978750.1};
GN Name=LOC106560396 {ECO:0000313|RefSeq:XP_013978750.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013978750.1};
RN [1] {ECO:0000313|RefSeq:XP_013978750.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013978750.1};
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}.
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 RefSeq; XP_013978750.1; XM_014123275.1.
DR AlphaFoldDB; A0A1S3KJI3; -.
DR STRING; 8030.ENSSSAP00000022705; -.
DR KEGG; sasa:106560396; -.
DR OrthoDB; 3439226at2759; -.
DR Proteomes; UP000087266; Chromosome ssa10.
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; 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; 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; PS01179; PID; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
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..159
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 827..938
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 969..1084
FT /note="PID"
FT /evidence="ECO:0000259|PROSITE:PS01179"
FT REGION 450..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1091 AA; 119965 MW; 3E061EDC85D11ACD CRC64;
MEEGYRIDLD YITERIITVS FPQACPDQTY LQNLRDITQM LKSKHGHNYM VINLSEKNDS
LTQMNPKVLD TGWLDLLAPS MEQMCGVCKT MENWLHSHTQ HVLVMHCRGG QGRVGVMVAS
YIHFSSISTS ADLGLDHFAM RRFYNDKVSS LMTPSQKRYV WMFSSLLRGV MNMDHSPLFL
LCVVLHGVPN INSVGECGLF LRVYQSLQVI CTSAVYHVRA VQTDRVYFVL QPAQLLKGDI
MVVCYNKNHQ TASREVIFRL QFHTGIIHGR PLLFPKEDLD TAYIDPRFPD DGKVELVFSE
SPEKMPGSGH WQNGPSVIVD YDTWDPLVRR DSYEYISPEG LALPRSPGPV DGNLYARVRK
GSSDEGAPFH LATSCPIPSD LKLSASKDSG LSIASQRTGG ITALSRRRGP SQDELIQLRR
LLSGVGLEPA QPHLEDMTDL PASCNAAREM EGDEAGLGQP VKASPSERES DILYDDEVSP
EASIGSFSSE SIPEAQGLVQ SGSGYSTPST QSWVQQQQIV VRGQDSPVDT LSLIGPNTLS
LSDTPNRGSS SRESVQRGVE GGVGSAVQTD SHTHASHTTH TPLPSGEPCG QEELASLATD
IDESIEQLNQ LILDLDPTFI PVPTRHTPLP LALSTSLYTN GNSHTTTHAN ASQSGWKHRQ
ASDVTDYPGF YSPGWGGAQT FQNAPIYRPN LPPSQCGRLS RMDSVDYEGP TPVMDSYDIV
PSTPAFPISP PTPYVKSFPV FSYLRPGEGH WEKSGISQDS QSFLDSSMNQ TPVSSEGQEF
RSEVSVTTAS CQRMFGSMRS VSSGISFPHT DSKQHTVKFV QDTSKFWYKP DISRDQAITI
LKDSEPGSFV VRDSHSFRGA YGLAMKVATP PPSVLTQSKK VGGDLSNELV RHFLIECTQK
GVRLKGCPNE PYFGSLTALV FQHSITPLAL PCKLIIPDRD PMEETSEPST QSATNSAAEL
LKQGAACNVW FLGSVELESL TGYQAVQKAA SLILAMDPPS TSTVVHFKVS AQGITLTDNQ
RKLFFRRHYT VNTVIFCALD PQERKIFGFV ARKSMNGTEN VCHLFAEHDP EQPASAIVNF
VSKVMIGSPK K
//
