ID A0A3Q3M241_9TELE Unreviewed; 1250 AA.
AC A0A3Q3M241;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Tensin 3 {ECO:0000313|Ensembl:ENSMAMP00000020993.2};
GN Name=TNS3 {ECO:0000313|Ensembl:ENSMAMP00000020993.2};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000020993.2, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000020993.2}
RP IDENTIFICATION.
RG Ensembl;
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 AlphaFoldDB; A0A3Q3M241; -.
DR Ensembl; ENSMAMT00000021534.2; ENSMAMP00000020993.2; ENSMAMG00000014107.2.
DR GeneTree; ENSGT00940000156328; -.
DR Proteomes; UP000261640; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
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; IPR003595; Tyr_Pase_cat.
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; 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; 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 Cell projection {ECO:0000256|ARBA:ARBA00023273};
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:UP000261640};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}.
FT DOMAIN 1..158
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 103..146
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 163..289
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 976..1086
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 1117..1242
FT /note="PID"
FT /evidence="ECO:0000259|PROSITE:PS01179"
FT REGION 332..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1250 AA; 137876 MW; 6018B9640C2A48AC CRC64;
MEEEYELDLT YITERVIAMS FPRGCSEEIY SHNLKDVTRM LKSKHADNYL IINLSERRQE
LSKMNPKTLD TGWPDLHAPP LDKICTICKA MENWLNADPL HVVVIHCRGG KGRIGVVISS
FVHFTDNIAT SFAQILTTFS VISHVRYVWI LNSLLSGSMK INASPLFLHC VIIHGIPNFD
ANGVCHPYIK VYQGMQAVYS SGIYHIGPGH REHVCITLEP AQLLKGDIMI KCYHKNDLTS
EREVIFRLQF HTGAVQGYNL MYEKEDMENA NKDPRFPDYG KVELVFSEGP EKIPGRLWQN
GADVTVDYNT ADPLTRWDSY QNICDGEAPR SQGLIQDKAA NKKNPSGGEA TLGRGARTTT
SSPDHSDHAL SVSSDSGLSS TSLWADRPTP ITTATTTTVK ANQGPSQQEK VQLKRLLSGF
GLEDPSPEEM NDQGPRVGIQ QMVPAQVHIN GDTRPRERET DILDDEVITG HDLHSVDSLG
TLSSSCHKSS QNSLLSDGFG SPGGEEQQNQ SQHHLHHPAP PSMEEYERAY AEARSGFLSS
RSNSVASSNP SSAPMPKQHV YRQGSYSTQS WVRQQQMVAA QQFSYITENG NDTERYPGNK
QASCSPKAGL TADPQGPTRD TTVNVLRNTV PHREQATINN NNKRDEEFKS LTMDIDNSID
QLNQLIMDLD PTFVPVSSHS SSTKKNVTHV NGSVSKCSNG INLRFNDNNA ANTQQTGKIV
SGGGDDVVLD MDSAIESRSD MTPPTPSFPI SPPTPYGKCN FFCWCNYFWM HFEPSIIATS
NPMPLPLFSF CFHYTSVRQP PPHSMSLDYG HHSPPLHHTH IHPAPNAHSS PRSSQRSRMV
HYALSRSPAQ SFDEQEDSGL GYSTDCPNST SSVLGNGGMD RDLLNGIDGQ NQSRMQPPLL
PEKKRASDGE REHSLGTASP ALSGFSSPHS GSSLSIPFPN VLPDLSVQMP GMASPLPGML
SKQVTVKFVQ DTSKFWYKPD ISRDQAISIL KDKEPGCFIV RDSHSFKGAY GLAMKVATPP
PSVLQQTKKG GDLSNELVRH FLIECTQKGV RLKGCPNEPY FGSLTALVCQ HSITPLALPC
KLIIPDRDPL EDVVENTSQS VSNSAAELLK QGAACNVWYL GSVEMESLTG VQAVQKATSM
TLSANPPPTS TVVHFKVSSQ GITLTDNQRK LFFRRHYNVN TVIFCALDPQ DRKWRKDGYP
SAKIFGFVAR KTGTSMDNIC HLFAEHDPEQ PASAIVNFVS KVMIGSQKNK
//
