ID A0A3P8X7J1_ESOLU Unreviewed; 1098 AA.
AC A0A3P8X7J1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Tensin 3 {ECO:0008006|Google:ProtNLM};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000000291.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000000291.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000000291.2}
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 AlphaFoldDB; A0A3P8X7J1; -.
DR Ensembl; ENSELUT00000019313.2; ENSELUP00000000291.2; ENSELUG00000001917.2.
DR GeneTree; ENSGT00940000156328; -.
DR OrthoDB; 3439226at2759; -.
DR Proteomes; UP000265140; LG08.
DR Bgee; ENSELUG00000001917; Expressed in liver and 14 other cell types or tissues.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR GO; GO:0070887; P:cellular response to chemical stimulus; IEA:UniProt.
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; IPR000242; PTP_cat.
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 Pfam; PF00102; Y_phosphatase; 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:UP000265140};
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 82..159
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 175..306
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 824..935
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 966..1091
FT /note="PID"
FT /evidence="ECO:0000259|PROSITE:PS01179"
FT REGION 364..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1098 AA; 120675 MW; C512B86206CB6CD9 CRC64;
MEAEYRIDLD YITERIITVS FSKAVPDQIY IKNLQDITQM IKSKHGHNYM VINLSEKNAS
LTQMNPEVLD TGWLDGLAPS LEQMCDVCKT MENWLQSHTK HVLVIHCQGG QGRVGVLVAT
YIHFSCLSDS ADLALDHFAM RKFYNDKVSS LMSPSQKRYV WMFSSLLKGV MKMNPSPLFL
PCVLLHGVPV LTPEGGRISE RNPLVQYKIS FQTHTQHTVY RYTTLSVALP TDLSVFPFVS
LSALVQVVCY NKNPEAASRE VIFRLQFHTG VIHGHPMLFP KQELDIANKD PRFPVDGKVE
LMFYDSPEKM PGIGCWKNGP SVMIDYDTLD PLIRRDSYEN ISPDGKDLPL SPVDARLYVR
KRSTDEGGAL FPPASSGPNP VDLNMSTSSD SGLSIASQWN GANPRRGPSQ DKCTQPRRVL
SEVNPEPAQC LPKDMAELPG SSNGGEGLVG EGQRIKGEPL PSERETDILD DYEASHKATL
ALDRPSKASI GLLSSGTQRL VQSGRTYSTQ TTHTTQSWIQ QQQMVDAHPQ TYPHTDEEEL
TDRRRLISPP ISQEAMSFPA TPSRGSSSRE AVLRVVVGGV GGGELLVPND TDTKAEHTKH
TLHTTRPTHT PHDTHAKETL PVSGEPCGQE ELALLATDMD ESIEQLNQLI LDLDPTFIPV
PTRHHPLHLS RSASLYANGT SQMTTHPNGS QSGENRLISP QWPSRSPEVP GGQSQGERSE
GDQRQENSLL LGNWGLERSL LEAMEGLDLG LDLGLAEDRL GGLPPLLPEK RVLGLGQAGS
RSPSLSGFSS PLSGSCLSIP FPSANTFASK QDTVKFVQDT SKFWYKPDIS RDQAIVVLKD
REPGSFIVRD SHSFRGAYGL AMKVSSPPPS VLTQSKKVSG DLSNELVRHF LIECTQKGVR
LKGCPNEPYF GSLTALVCQH AITPLALPCK LIIPGRDPLE ETSESSTQTA TNSAADLLKQ
GAACNVWFLG SVELESLTGY QAVQKAASQM LAMDPPPTST VVHFKVSTQG ITLTDNQRKL
FFRRHYNVNT VIFCALDPQD RKWTKDGCTS AKIFGFVARK SMSGAENVCH VFAEHDPEQP
ASAIVNFVSK VMIGSTKK
//
