ID A0A3P9N3X5_POERE Unreviewed; 1653 AA.
AC A0A3P9N3X5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Tensin-2-like {ECO:0000313|Ensembl:ENSPREP00000004217.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000004217.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000004217.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000004217.1};
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 RefSeq; XP_008410996.1; XM_008412774.2.
DR Ensembl; ENSPRET00000004275.1; ENSPREP00000004217.1; ENSPREG00000002963.1.
DR GeneID; 103466881; -.
DR CTD; 799109; -.
DR GeneTree; ENSGT00940000163886; -.
DR OrthoDB; 3439226at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000002963; Expressed in caudal fin and 1 other cell type or tissue.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR CDD; cd20887; C1_TNS2; 1.
DR CDD; cd01213; PTB_tensin; 1.
DR CDD; cd14562; PTP_tensin-2; 1.
DR CDD; cd09927; SH2_Tensin_like; 1.
DR Gene3D; 2.60.40.1110; -; 1.
DR Gene3D; 3.30.60.20; -; 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; IPR046349; C1-like_sf.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR002219; PE/DAG-bd.
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:SF1; TENSIN-2; 1.
DR Pfam; PF08416; PTB; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00109; C1; 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; SSF57889; Cysteine-rich domain; 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.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 13..60
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 108..280
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 285..411
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1382..1491
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 63..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..971
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1035
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1089
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1315
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1653 AA; 182520 MW; 520AF508375428F7 CRC64;
MSGKMSKAGK GEPHVFKEKT FKKKRQCSVC RQNIDNVGSF CRVCKTGTHR KCEGKVTSAC
IPPPSNDLQR RGTAPSRHNQ HMGSTKSLTY TKQRNTLPRS FSVDRVMERV MERHYDFDLT
YITERIISVF FPPKLEEQRY RLNLKEVAAM LKSKHQDKFL LLNLSERRHD ITRLNPKVHD
FGWPDLHAPP LDKICAICKA MENWLTSDPQ HVVVLHCKGN KGKTGVIIAA YMHYSKISAG
ADQALSTLAM RKFCEDKVSS SLQPSQNRYI YYFGGLLSGA IKMNSSPLFL HQVLIPSLPN
FQGEGGYHPF LKIYQSMQLV YTSGIYDLQG TGGRRLCVSV EPALLLKGDI MVKCYHRRAH
GADRDTVFRL QFHTCTIHGS QLWFGKGELD EAFTDERFPS DATVEFVFSS GPERVKGREY
HKNDPAVIVD YNTSDPVVRW DSYENFNQRY QDSLEDIAHT RGPLDGSLYA QIKKRRGPSS
GSLTSTNGSS PAGGPAEDRP DHLIPQGSDS GLSAHSLHLN QSSVHPDHPE ELVRPPPPTR
QEREELERLL GGIEGNKDGE RETAILDDGD SWPPERIGTL RLNRSCSCRD DYRSQRCAEP
GCDRTLLMPN GYCLDRAPGT NGHHGATPST SPNPAGPPSH MDMCQHYSPH THQSLPPPDL
VWDRQSGPPH YLHRSCSEAP SSRHICPYPS PDLTPHSHNP PHHHPVPAAG RLYCREDVPF
HYPPPPLSHH HTHSHHPKPS TSPTYHDIML MDNLPPSSCP CRDCSIRRED SAAYHTLRLE
RGDSFHWDRE AELQQREAGL RRTRETELTR GPELHWERDP GLRRGRELSL HWERDREAEL
QWERDREAEY WHRRATVASY GPQGHDLPAF SFDPLPSGHP AYPEASRSHA HSHLDLKYSS
SSSGYQTPRQ ACPCSPYQPS PSESRGYASG YQSESTSPLP PPSSMVGTCS HSNGPADHIP
NHHHHHADSQ QSYSSDSHTD GLRSSGESVG WRDHITHGSF RRVHRDAHVA CSTPSDMSGP
STPVHTSSPL RTQESPSPAG RDYEIRTTDI ISSDNEGSPS QDGHFSNANV IQESSAHPKT
STKQEDPLSP TKPDSPRVDP PKATAPHQNC TIDAPSASPL DSVTPTTTSR EHCQVPSSSA
PNTHPQTLPL NPSEAAAVPS TVVQTVTPSQ TQTQANGLSS AHVNGLSPTK SHPEGPKSPT
SNPPSAPASS PSSQPGSSSM DGSPVSDVPV PGFATLGRRL MLSGSESHHP NYLQHHGPPH
HHYAILDHSA PLDASKRNGY FGPAXHLPPA SYSNYSTISI PLPHPQPPLP EKRHHPAQPG
SPCEGVRPNV GQAPPSAQHQ HHVTFSPMVG EIAPLAGHNE EVEGETTNRV SVKFVQDSSR
FWYKPGISRE QAIAALKERE PGTFLVRDSN SFQGAYGLAL KVATPPPNAS LSSKASDPLE
QLVRHFLIET GPRGVKIKGC QNEPHFGSLS ALVYQHSITP ISLPCALKIP EKDLVGEVQE
VQPVTNISTA ADLLKQGAAC NVLYLNSVET ESLTGPQAIA KATDATLGRN PRPSATVVQF
KVTSQGITLT DSQRRVFFRR HYPVNSVTFS SVDPKDRRWT NSDNAMVQVF GFVARKPGST
AENVCHLFAE LDPEQPASAI VNFINKVMLA QRR
//
