ID A0A3Q3KUK9_9TELE Unreviewed; 1728 AA.
AC A0A3Q3KUK9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Tensin 2a {ECO:0000313|Ensembl:ENSMAMP00000001059.2};
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:ENSMAMP00000001059.2, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000001059.2}
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 Ensembl; ENSMAMT00000001078.2; ENSMAMP00000001059.2; ENSMAMG00000000750.2.
DR GeneTree; ENSGT00940000163886; -.
DR OrthoDB; 3439226at2759; -.
DR Proteomes; UP000261640; Unplaced.
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; PF00130; C1_1; 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:UP000261640};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 49..96
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 143..315
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 320..446
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1456..1566
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 509..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1110..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1363..1385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1046
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1071
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1224..1256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1728 AA; 190405 MW; AC7B4C9652B30205 CRC64;
MGCVLSSDWC GEEEVQPVPV VRSSSLKRRS LERTDSGRMR LTKAGKVEPH VFKEKTFKKK
RQCSVCRQNI DSVGSFCRVC KTATHRKCEA KVTSACIPAP SNDLRRGTTP SRHIQHLGST
KSLTYTKQRN TLPRSFSVDR VMERVMERHY DFDLTYITER IISVFFPPKL EEQRYRLNLK
EVAAMLKSKH QDKFLLLNLS ERRHDISRLN PKVHDFGWPD LHAPPLDKIC AICKAMETWL
TSDPQHVVVL HCKGNKGKTG VIIAAYMHYS KISAGADQAL STLAMRKFCE DKVSSSLQPS
QNRYIYYFGG LLSGTIKMNS SPLFLHQVLI PSLPNFQGEG GYYPFLKIYQ AMQLVYTSGI
YDLQGTGGRR LCVTIEPALL LKGDIMVKCY HRRAHSADRD TVFRLQFHTC TIHGSQLWFG
KGELDEACTD ERFPSDATVE FVFSSGPEKI KGREYQKNDP AVTVDYNTAD PVVRWDSYEN
FNQRYQDSLE DIAHTRGPLD GSLYAQIKKR RGPSSGSLPS TNGSSPGAGL GEDRPDHLLA
QGSDSALSGH SINLNQSSLH PDHQEESIRP PPPTRQEREE LERLLGGIEG NRDGERETAI
LDDGDSLPSE QTGTLRLSRS CSCRDGYRSQ RCAEPGCDRT LLMPNGYCLD RAPGTNGHHG
APPSTSPGPP VPPAHMDLCQ HYNPHPHQSL PPPDLVWDRQ NGPPHYLHRS CSDAPPSRHI
CPYPSPSLSP HSHNHQHHHP LSAQGHICCR EDDYGPYHHP NTPHSHHHPH THHPKPSTSP
TYHDIMLMDS LPGPGCPCRD CSIRRDDSAA YHSLRLDRGD SFHWDREAEL QQRDVGLRRA
REAELPHGSE LHWERDPGLR RGRELSLHWE RDREAELQWE RDREAEYWHR RATVASYGPQ
GHDLPAFTFD PLPSGHPAYP EASRSHAHSH LDLKYSSSSS GYQTPRQVCP CSPYQPSPSE
SRGYASGYQS ESTSPLPPAS SMTGPSSHSN GQSQHNHNHH HHHPESQQSY GSDSHTDGLR
SSGESVGWRD HITHGSFKRV HRDGHATCST PSDMSGPSTP VHTSSPLRAQ ESPSPGGREY
EIRTTDIISS DYNISKPQDG HFNAGNIVQE SQSSSAEPSS LPQATKETQS HTATPVPTEP
RNHCTAQADL SPTPPQQQHC SADMSSASPF DSVTAKSSNQ EHYQAPSSLL HASPAPDTQP
QPGPHPAQTP HSSEAAALPS AVAEAISQPQ SQTQVPGSAG PIPTQINGSS PTRDSHPEVP
KPTGPQAPAS PTPVSSSPQG ATSSMEGSPV SDAPVPGFAT LGRRLMLSGS DSHHSNHIQQ
QGPPHHHSTA MEQTAVLDSN RRQCYSAHTP QLYPSSYSNY STISIPLPHP QPPLPEKRHP
PAQAAASDGV GTLRLAVGQV PASTSSTTQH QHHVTFSPTV GEIAPPAGQI EEVASVDPEN
TNRVSVKFVQ DSSRFWYKPS ISREQAIAAL KEREPGTFLI RDSNSFQGAY GLALKVATPP
ANVNNHSSKV SDPLEQLVRH FLIETGPRGV KIKGCQNEPY FGSLSALVYQ HSITPISLPC
TLKISEKDLI GDMQEVQAVT NISTAADLLK QGAACNVLYL NSVETESLTG PQAIAKATDA
TLGCNPRPAA TVVQFKVTSQ GITLTDSQRR VFFRRHYPVN SVTFSSIDPK DRRWTNSDTT
TVKVFGFVAK KPGSLAENVC HLFAELDPEQ PASAIVNFIN KVMLSQRR
//
