ID G3QLN8_GORGO Unreviewed; 1445 AA.
AC G3QLN8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Tensin 3 {ECO:0000313|Ensembl:ENSGGOP00000003397.2};
GN Name=TNS3 {ECO:0000313|Ensembl:ENSGGOP00000003397.2};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000003397.2, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000003397.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000003397.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000003397.2}
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 EMBL; CABD030051200; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030051201; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030051202; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030051203; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_018886959.1; XM_019031414.1.
DR RefSeq; XP_018886960.1; XM_019031415.1.
DR STRING; 9593.ENSGGOP00000003397; -.
DR Ensembl; ENSGGOT00000003474.3; ENSGGOP00000003397.2; ENSGGOG00000003450.3.
DR GeneID; 101131841; -.
DR CTD; 64759; -.
DR eggNOG; KOG1930; Eukaryota.
DR eggNOG; KOG2283; Eukaryota.
DR GeneTree; ENSGT00940000156328; -.
DR HOGENOM; CLU_002189_1_0_1; -.
DR InParanoid; G3QLN8; -.
DR OMA; QGSEHLH; -.
DR OrthoDB; 3439226at2759; -.
DR TreeFam; TF315996; -.
DR Proteomes; UP000001519; Chromosome 7.
DR Bgee; ENSGGOG00000003450; Expressed in adult mammalian kidney and 6 other cell types or tissues.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
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; cd14561; PTP_tensin-3; 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:UP000001519};
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 96..159
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 1172..1282
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 358..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1076..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1445 AA; 155168 MW; 21BE5E3CB77F0042 CRC64;
MEEGHGLDLT YITERIIAVS FPAGCSEESY LHNLQEVTRM LKSKHGDNYL VLNLSEKRYD
LTKLNPKIMD VGWPELHAPP LDKMCTICKA QESWLNSNPQ HVVVIHCRGG KGRIGVVISS
YMHFTNVSAS ADQALDRFAM KKFYDDKVSA LMQPSQKRYV QFLSGLLSGS VKMNASPLFL
HFVILHGTPN FDTGGVCRPF LKLYQAMQPV YTSGIYNVGP ENPSRICIVI EPAQLLKGDV
MVKCYHKKYR SATRDVIFRL QFHTGAVQGY GLVFGKEDLD NASKDDRFPD YGKVELVFSA
TPEKIQGSEH LYNDHGVIVD YNTTDPLIRW DSYENLSADG EVLHTQGPVD GSLYAKVRKK
SSSDPGIPGG PQAIPPTNSP DHSDHTLSVS SDSGHSTASA RTDKTEERLA PGTRRGLSAQ
EKAELDQLLS GFGLEDPGSS LKEMTDARSK YSGTRHVVPA QVHVNGDAAL KDRETDILDD
EMPHHDLHSV DSLGTLSSSE GPQSAHLGPF TCHKSSQNSL LSDGFGSNVG EDPQGTLVPD
LGLGMDGPYE RERTFGSREP KQPQPLLRKP SVSAQMQAYG QSSYSTQTWV RQQQMVVAHQ
YTFAPDGEAR LVSRCPADNP GLVQAQPRVP LTPTRGTSSR VAVQRGVGSG PHPPDTQQPS
PSKAFKPRFP GDQVVNGAGP ELSTGPSPGS PTLDIDQSIE QLNRLILELD PTFEPIPTHM
NALGSQANGS VSPNSVGGGL RASSRLPDTG EGPSRATGQQ GSSAEQPLGG RLRKLSLGQY
DNDAGGQLPF SKCAWGKAGV DYAPNLPPFP SPADVKETMT PGYPQDLDII DGRILSSKES
MCSTPAFPVS PETPYVKTAL RHPPFSPPEP PLSSPASQHK GGREPRGCPE TLTHAVGMSE
SPIGPKSTML RADASSTPSF QQAFASSCTI SSNGPGQRRE SSSSAERQWV ESSPKPTVSL
PGSGRPTGSP LSAEFSGTRK DSPVLSCFPP SELQAPFHSH ELSLAEPPDS LAPPSSQAFL
GFGTAPVGSG LPPEEDLGAL LANSHGASPT PSIPLTATGA ADNGFLAHNF LTVAPGHSSH
HSPGLQGQGV TLPGQPPLPE KKRASEGDRS LGSVSPSSSG FSSPHSGSTI SIPFPNVLPD
FSKASEAASP LPDSPGDKLV IVKFVQDTSK FWYKADISRE QAIAMLKDKE PGSFIVRDSH
SFRGAYGLAM KVATPPPSVL QLNKKAGDLA NELVRHFLIE CTPKGVRLKG CSNEPYFGSL
TALVCQHSIT PLALPCKLLI PERDPLEEIA ESSPQTAANS AAELLKQGAA CNVWYLNSVE
MESLTGHQAI QKALSITLVQ EPPPVSTVVH FKVSAQGITL TDNQRKLFFR RHYPVNSVIF
CALDPQDRKW IKDGPSSKVF GFVARKQGSA TDNVCHLFAE HDPEQPASAI VNFVSKVMIG
SPKKV
//
