ID G3WGK6_SARHA Unreviewed; 1547 AA.
AC G3WGK6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Tensin 3 {ECO:0000313|Ensembl:ENSSHAP00000014561.2};
GN Name=TNS3 {ECO:0000313|Ensembl:ENSSHAP00000014561.2};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000014561.2, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000014561.2, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000014561.2}
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 STRING; 9305.ENSSHAP00000014561; -.
DR Ensembl; ENSSHAT00000014683.2; ENSSHAP00000014561.2; ENSSHAG00000012430.2.
DR eggNOG; KOG1930; Eukaryota.
DR eggNOG; KOG2283; Eukaryota.
DR GeneTree; ENSGT00940000156328; -.
DR HOGENOM; CLU_002189_1_0_1; -.
DR TreeFam; TF315996; -.
DR Proteomes; UP000007648; Unassembled WGS sequence.
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:UP000007648};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 15..62
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 106..278
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 211..267
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 283..409
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1274..1384
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 470..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1193..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1212..1230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1547 AA; 168787 MW; D7523BC04C431B2A CRC64;
MSTGGKKPEE SASGAHSFKN KSFKKAKVCS VCKQVIDSQG VSCRVCKYSC HKKCETKVVI
PCHVPINDPL PNNSDVSGHV TRTASDSFLK SSSFCCDKFS QSAILGHIME EGYELDLTYI
TERIIAVSFP ASCSEETYLH NLQDVTRMLK SKHGDNYLVI NLSEKRYDLT KLNPKIMDVG
WPDLHAPPLD KMCTICKAQE NWLNSDPQHV VVIHCRGGKG RIGVVISSYM HFTNVSASAD
QALDRFAMKK FFDDKVSALM QPSQKRYVHF LSGLLSGSVK MNTTPLFLHF VILHGIPNFD
TGGVCRPFLK LYQAMQPVYT SGIYNVGPEN QSRVCIAIEP AQLLKGDIML KCYHKKYRSA
TRDVIFRLQF HTGAIQGYGL MFRKEDLDNA NKDDRFPDYG KIELVFSATP EKIQGSEHLQ
NDHGVVVDYN TADPLIRWDS YENMSPDGEV LHTQGPIDGS LYAKVRKKSL SDNNIPGGSQ
VVPVTRSPDH SDHTLSVSSD SGHSTASVRT DKTEERLAPG AKRGLSPQEK AELDQLLSGF
GLEDSVSSPK DMTDARNKYS GTRHIVPAQV HVNGDSKLKD RETDILDDEM PNHDLHSVDS
IGTLSSSEGQ HSSHLGNFTC HKSSQNSLLS DGFGSNTGED HHIALAPDLG IGVDPLYERS
FGNGEPKQGQ QLLRNPAAQA PAYGQGTYST QTWVRQQQLV AAHQYSYATE SEGRFAIHSS
SENSNYVPAQ SRVPLTPTRG SSSRDAVQRG LGGISNPSEV PQHSYPEGFK PRLTPEKEIN
GVDVGLNAGI LPGSPTLDID QSIEQLNRLI LELDPTFEPI PTHMNTMTSQ TNGSACPDSK
AGGALRANHR FLEKGDNNII RNSSQHGDDP SGGRIRKLSL GQYDNDSPGQ SSFGGCGWVK
ATNMDPVSTL GSFITSGETK ETMITSYPQE LDVIDGGIFS PTKNGNESVV PTPAFPLSSE
TSYVKTPHYP QISPSEQLMS SPANLYKTGH EPRSYTEGLN HSVVMSDSPI GTNPALFRSE
RPTTPCQRTF PSACTASSNS PLQRGESSST AEHQWLESSP KSTLSPQLSM MGSSRPTGFL
LGSEFSSPVP DSSLLSHFPP SELQVSNLNH HENSPAEQSQ EILANPSGRT FLNFSIQPDE
KPGTLLTNSN GASKPPIAPL AGVVDNGFLP HTFLTVAPGH SSQHSPVLQH ASLSLHSQPP
LPEKKRTSEG DRSFGSISPS SSGFSSPHSG STISIPFPNV LPDFSKVLST SPLPENPTDK
HVTVKFVQDT SKFWYKADIS REQAIAMLKD KEPGSFIVRD SHSFRGAYGL AMKVATPPPS
VLQLNKKAGD LANELVRHFL IECTSKGVRL KGCPNEPYFG SLTALVYQHS ITPLALPCKL
LIPDRDPLEE MAENSPQTAA NSAAELLKQG AACNVWYLNS VEMESLTGYQ AVQKALSMTL
VQDPPPISTV VHFKVSAQGI TLTDNQRKLF FRRHYPVNTV IFCALDPQDR KWIKDGPSAK
VFGFVARKQG SATDNVCHLF AEHDPEQPAS AIVNFVSKVM IGSPKKI
//
