ID A0A2U9BJ45_SCOMX Unreviewed; 1379 AA.
AC A0A2U9BJ45;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative tensin-3 {ECO:0000313|EMBL:AWP04013.1};
DE SubName: Full=Tensin 3 {ECO:0000313|Ensembl:ENSSMAP00000033095.1};
GN Name=TNS3 {ECO:0000313|Ensembl:ENSSMAP00000033095.1};
GN ORFNames=SMAX5B_006591 {ECO:0000313|EMBL:AWP04013.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP04013.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP04013.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSMAP00000033095.1}
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; CP026249; AWP04013.1; -; Genomic_DNA.
DR STRING; 52904.ENSSMAP00000033095; -.
DR Ensembl; ENSSMAT00000033507.2; ENSSMAP00000033095.1; ENSSMAG00000020276.2.
DR GeneTree; ENSGT00940000156328; -.
DR OrthoDB; 3439226at2759; -.
DR Proteomes; UP000246464; Chromosome 7.
DR Proteomes; UP000694558; Chromosome 7.
DR Bgee; ENSSMAG00000020276; Expressed in liver and 6 other cell types or tissues.
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; 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:UP000246464};
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 103..142
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 175..301
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1106..1216
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 340..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..1004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1379 AA; 150980 MW; 6CBDA32BBAD6FC85 CRC64;
MEEGYELDLT YITERIIAVS FPRGCSEEVY SHNLKDVTRM LKSKHADNYL IINLSERRHD
LSKMNPKTLD TGWPDMHAPP LDKICTICKA MESWLNADPL HVVVIHCRGG KGRIGVVISS
FVHFTDVSAS ADQALDRFAM RKYYDDKVSA LMTPSQKRYV WILNSLLSGS MKINASPLFL
HCVILHGIPN FDATGVCRPY IKVYQGMQAV YSSGIYHIGP GHRDRVCITL EPAQLLKGDI
MIKCYHKSDL TSERGVIFRL QFHTGAVQGY SMMFEKEDME TASKDPRFPD YGKVELMFSE
GPERIPGADR WQNGADVSVD YNTADPLIRW DSYQNICDGE APRSQGLTQD KAANKRSPSG
GEATLGRGAR TTSTTSSPDH SDHALSVSSD SGLSSTSLWA DRPTPTTAAT VRANLGPSQH
EKVQLKRLLS GFGLEDPSLE EMDDQGPRVG IQQIVPAQVH INGDPRPKER ETDILDDEVI
TGHDLHSVDS LGTLSSSCHK SSQNSLLSDG FGSPGGDEQQ SQSQHSLHHP APPPMEEYER
AYAEAGRGCL SSRSNSVASS NPSSAPVPKQ HVYRQGSYST QSWVRQQQMV AAQQFIYMPE
EGNDAERYPG NKQGSSLPKA GLPAEPQGPA RDTTADALRN AAPHKEQTTM NNNNNNKQDE
EFKSLTMDID NSIDQLNQLI MDLDPTFVPV SSHGSSMKRN GSAHVSSSVG KCSNGIDDSN
AATLTNTQQT AVQSSEGRTG VTRSLSRQGS DVTDQPGFCS SGWRGPEEYR GQRTYSPCVP
QSQLRMLFRS DSADFRAQGP DMDGRVEAGS DMAPPTPAFP ISPPTPYVKN MSELNHLRQT
PSPSMQSYGG YRPDHEPREY SEMIGHVGVE SLPDSSINCH RTLSATQSAS IVGTLQRTDS
SSMNQSWPEH PVLSRHSSLS SYTSARQPPQ HSMSLDYDHH SAPLHHPHIH PAPNAHSSPR
SSQRSCMARY ALGHSSGQSF DEQDDSRVGY ASDCPNSSSS LLGNGGMDRD LMMSIDRQIQ
SHTPQVQPPL LPEKKRASDG EHSLGTASPA PSGFSSPHSG SSVSIPFPNV LPDLSSQTSG
TASPLPDVLA SKQVTVKFVQ DTSKFWYKPD ISRDQAISVL KDKEPGCFIV RDSHSFRGAY
GLAMKVATPP PSVLQQTKKG GDLSNELVRH FLIECTQKGV RLKGCPNEPY FGSLTALVCQ
HSITPLALPC KLIIPDRDPL EDVVENTSQT VTNSAAELLK QGAACNVWYL GSVEMESLTG
IQAVQKATSM TLSTNPPPTS TVVHFKVSSQ GITLTDNQRK LFFRRHYNVN TVIYCALDPQ
DRKWKKDGCP AKIFGFVARK SGTSMDNICH LFAEHDPEQP ASAIVNFVSK VMIGSQKSK
//
