ID A0A3Q1LJV3_BOVIN Unreviewed; 1551 AA.
AC A0A3Q1LJV3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Tensin 3 {ECO:0000313|Ensembl:ENSBTAP00000059766.1};
GN Name=TNS3 {ECO:0000313|Ensembl:ENSBTAP00000059766.1,
GN ECO:0000313|VGNC:VGNC:36209};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000059766.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000059766.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000059766.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000059766.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000059766.1};
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; ENSBTAT00000074133.1; ENSBTAP00000059766.1; ENSBTAG00000009655.6.
DR VEuPathDB; HostDB:ENSBTAG00000009655; -.
DR VGNC; VGNC:36209; TNS3.
DR GeneTree; ENSGT00940000156328; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000009655; Expressed in saliva-secreting gland and 105 other cell types or tissues.
DR ExpressionAtlas; A0A3Q1LJV3; baseline and differential.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
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:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd20889; C1_TNS3_v; 1.
DR CDD; cd01213; PTB_tensin; 1.
DR CDD; cd14561; PTP_tensin-3; 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 InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR45734; TENSIN; 1.
DR PANTHER; PTHR45734:SF5; TENSIN-3; 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; PS50056; TYR_PHOSPHATASE_2; 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 Cell projection {ECO:0000256|ARBA:ARBA00023273};
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:UP000009136};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 34..82
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 112..284
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 217..273
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 289..415
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1278..1388
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 472..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1077
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1551 AA; 166825 MW; 4B8245CCA9AFB93A CRC64;
MRLRALTPGP PGGCARGARA LRHRRQPEEV TASLHSFKNK AFKKARVCGV CKQIIEGRGI
SCRACKYSCH KKCEAKVVSP HCVQVHLEQA PGASSTPASL CCDKPFRPAG LSPAMEDGRE
LDLTYITERI IAVSFPAGCS EESYLHNLQE VTRMLRSKHG DNYLVLNLSE KRYDLTKLNP
KILDVGWPEL HAPPLDKVCT ICKAQEAWLN SDPQHVVVIH CRGGKGRIGV VISSYMHFTN
VSASADQALD RFAMKKFYDD KLAALMQPSQ KRYVQFLSGL LSGTVKMNAS PLFLHFVILH
GTPNFDSGGV CRPFLKLYQA MQPVYTSGIY NVGPENQSRI YIAIEPAQLL KGDIMVKCYH
KKYRSATRDV IFRLQFHTGA VQGYRLVFAK EDLDNASKDD RFPDNGKIEL VFSATPEKIQ
GCEHLQNDHR VIVDFNTADP LIRWDSYENL SADGEVLHTQ GPVDGSLYAK VRKKSTSDPS
VPGGSPAVPA ASSPDHSDHT LSVSSDSGHS TASVRTDRTE EHLTPGSKRG LSPQEKAELD
QLLSGFGLED SGSPLKDMSD ARSKYSGTRH VVPAQVHVNG DTTPKDRETD ILDDEMPSHD
LHSVDSIGTL SSSEGHPSAH LSPFTCHQSS QNSLLSDGFG STAGEDQHGA LAPDLGLAAE
PLFERERAFG SCEPKQPQPV LRKPSVPAQT QAYGPSSYST QTWVRQQQMV AAHQYSFAPD
GEARLSGRGA ADSSGLLQTQ PRVPLTPTRG ASSRVAVQRG IGPGPHPPDI QRPPPGKAAF
KPRIPDVKVV NGAGPELGTD LSPGSPTLDI DQSIEQLNRL ILELDPTFEP IPTHMNMSSS
QANGPMPPDG MAGGLWASGR LQDTGDGPGR APVRQGDEPL GGRFQKLSLE QYDNEAGEQP
TFSKCSWGKT TSSEQTPGLA PFLSPDNTKE AVITTYPPDL DVIDGRIFSP TNSGSESISP
TPAFPVSPET PYGTTSPRYS PFSPSVPQMG SPSALYKGAH EPRGCPEILS HSVGMSESPV
GPKPTMLRAD MPTAPSFQRA FTSSCTISGN SPSQRRGSPS SAEHQWVETS PKSTLTLLGG
SRPGKDSPAR PHFPPADLQT SFHGPELSLA EPPEALGPPS NQAFLSFSTA PMAGGGLPAG
EDPGALLANS HGAAQAPGNP LTAAEAADNS FLSHSFLTVA PGHSGHHSPV LQGPGLALPG
QPPLPEKKRT SEGDRSFGSV SPSSSGFSSP HSGSTMSIPF PNIIPDFSKA AEGAAPSPDN
PGDKHVSVNF VQDTSKFWYK ADISREQAIA MLKDKEPGSF IVRDSHSFRG AYGLAMKVAT
PPPSVLQMNK KAGDLANELV RHFLIECTPK GVRLKGCSNE PYFGSLTALV CQHSITPLAL
PCKLLIPDRD PLEEIAENPQ QTAANSAAEL LKQGAACNVW YLNSVEMESL TGHQAIQKAL
SMTLVQEPPP LSTVVHFKVS AQGITLTDNQ RKLFFRRHYP VSSVIFCALD PQDRKWVTDG
PCSRVFGFVA RKQGSATDNV CHLFAEHDPE QPASAIVNFV SKVMIGSPKK I
//
