ID A0A096LRL6_POEFO Unreviewed; 1289 AA.
AC A0A096LRL6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Tensin-like {ECO:0000313|Ensembl:ENSPFOP00000021807.1};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000021807.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000021807.1}
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}.
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DR EMBL; AYCK01011975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01011976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPFOT00000030901.1; ENSPFOP00000021807.1; ENSPFOG00000014114.2.
DR GeneTree; ENSGT00940000155400; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
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:UP000028760};
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 175..301
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1021..1130
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 338..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..733
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1289 AA; 141685 MW; 9E215CC26F1E0642 CRC64;
MEESYEVDLV YITERIISLS FPAAADERSY TNNLKEVATM LQSKHGEHYL VLNLSEQRND
LTKLNHKVLE FGWPDHHAPA LDKICSMCKA MDTWLSGDQR NVVLLHNKGN RGRTGVVVAA
YMHYSNISAS ADQALDRFAM RRFYEDKALP GGQPSQRRYV QYFNGLLSGH IKINNKPLFL
HHVIMHGIPN FESKGGCRPF LKIYQAMQPV YTSGIYNVQG DSNTSICITI EPGLLLKGDI
LLKCYHKRYR NPTRDVVFRV QFHTCAIHDL GVVFGKAELD ETFKDERFPE YGKVEFVFSY
GPEKIRGLDH LENGPSVSVD YNTQDPLIRW DSYESFSHPS EDAVDTENDV GHTQGPLDGS
LYARQSNHHL QKTEQSLPVA GHTSLPAVDH TLSVSSDSGN STASTAGHSN STTAHPTLSP
QEKRELDQLL SGLEILRAPS TEERETDILD DELPNSQEGN SVDSLGTLSS LEGQATPASL
YYQSQTPVGG QNDGPYLERN VLGEKLNEMP VHGVQTPTAM QERSVDSPSL QNTLSSSQIP
FSQTLARPSY QGDSAIHGYN NPGSMNSTYH QRQPGRVPAV PNQSPVTESP TYSPQRSNTG
YPYQNTTPTH TPEPYLHTRQ AAHHCPIDTS ANVNQQSPQT QHLFFSSSCA HPPTQGNVFF
SLAKRARCRG GDSELGRPGC SPYRCLYYRS TVAFCTAVLT WPHKISSAAE TKHLPHPLPP
PPAASPPSPD FPPLEQRVRS KGMTPEVTQE TGRRRTTSEG HYQSVSPRVD LRKTLDVSIY
DSESSGKNSL NSFKNRTFCC SNSGLNPRST PGLTKTPLSA LGLKPHQQDS APRSPVSPYT
NRPASPEGSQ VNIMGVHTVP GSPNTLHRTV ATNTPPSPAL QRRLGQASPS LTRHQPPSSP
LIGRNPKTAS TAIPPSPLMG RRAGSSGCST PDELGAASRQ GSAQPPPTPA FPVSPQLPEK
RHMSSGDAER TDNRNLTPAS GGSTPNLSGT HTLPDVSKSI YDGYPDIKMN VKFVQDTSRF
WYKPDISREQ AISLLKDREP GAFIIRDSHS FRGAYGLAMK VACPPPTVQQ NKKVADMTNE
LVRHFLIETS PKGVRLKGCP NEPYFGCLSA LVYQHAMTPL ALPCKLMIPT KEKDPNEEAL
ELATPTDQVV ELLKQGAACN VLFINSVDME SLTGPQAIAK AISQTLTTNP LPAATTVHFK
VSMQGITLTD SQRKIFFRRH YPLNTVTYCD LDPQDRKWVK DGGGSVKLFG FVARKQGSTT
DNVSHLFAEL DPDQPASAIV SFVSKMMKR
//
