ID A0A2K6DWU5_MACNE Unreviewed; 1855 AA.
AC A0A2K6DWU5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Tensin 1 {ECO:0000313|Ensembl:ENSMNEP00000040362.1};
GN Name=TNS1 {ECO:0000313|Ensembl:ENSMNEP00000040362.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000040362.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000040362.1}
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 Ensembl; ENSMNET00000064854.1; ENSMNEP00000040362.1; ENSMNEG00000042642.1.
DR GeneTree; ENSGT00940000155400; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000042642; Expressed in lung and 11 other cell types or tissues.
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 CDD; cd20888; C1_TNS1_v; 1.
DR CDD; cd01213; PTB_tensin; 1.
DR CDD; cd14560; PTP_tensin-1; 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:SF3; TENSIN-1; 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:UP000233120};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 10..57
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 119..291
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 296..422
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1583..1692
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 73..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1452..1473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1482..1498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1855 AA; 198802 MW; 629F2C02A299F103 CRC64;
MPEDLEAPKT HHFKVKTFKK VKPCGICRQV ITQEGCTCKV CSFSCHRKCQ AKVAAPCVPP
SNHELVPITT ENTPKNVVDT GEGASRGGNT RKSLEDNGSA RVTPSVQPHL QPIRNMSVSR
TMEDSCELDL VYVTERIIAV SFPSTANEEN FRSNLREVAQ MLKSKHGGNY LLFNLSERRP
DITKLHAKVL EFGWPDLHTP ALEKICSICK AMDTWLNADP HNVVVLHNKG NRGRIGVVIA
AYMHYSNISA SADQALDRFA MKRFYEDKIV PIGQPSQRRY VHYFSGLLSG SIKMNNKPLF
LHHVIMHGIP NFESKGGCRP FLRIYQAMQP VYTSGIYNIP GDSQTSVCIT IEPGLLLKGD
ILLKCYHKKF RSPARDVIFR VQFHTCAIHD LGVVFGKEDL DDAFKDDRFP EYGKVEFVFS
YGPEKIQGME HLENGPSVSV DYNTSDPLIR WDSYDNFSGH RDDCMEEVVG HTQGPLDGSL
YAKVKKKDSL HGSTGAVNAT RPTLSATPNH VEHTLSVSSD SGNSTASTKT DKTDEPVPGA
SSAPAALSPQ EKRELDRLLS GFGFEREKQG AMYHTQHLRS RPAGGPAVPS SGRHVVPAQV
HVNGGALASE RETDILDDEL PNQDGHSAGS VGTLSSLDGV TNTSEGGYPE ALSPLTNGLD
KPYPMEPMVN GGGYPYESAS RAGPAHAGHT VPMRPSYSAQ EGLAGYQREG PHPAWPQPVT
TSHYAHDPSS MFRSQSFSEA EPQLPPAPVR GGSSREAVQR GLNSWQQQQQ QQQQQPQPQP
QPRPPPRQQE RVHLESLVAS RPSPQPLAET PIPSLPEFPR AASQQEIEQS IEALNMLMLD
LEPASTAAPL HKSQSVPGAW PGASPLSSQP GSSRQSHPLT QSRSGYITSG HSLGTPEPAP
RASLESVPPG RSYSPYDYQP CSAGPNQDFR SKSPASSSLP AFLPTTHSPL GPQQPPASLP
GLTAQPLLSP KEATSDPSRT PEEEPLNLEG LVAHRVAGVQ AREKQPAEPP APLRRRAASD
GQYENQSPEA TSPRSPGVRS PVQCVSPELA LTIALNPGGR PKEPHLHSYK EAFEEMEGTS
PSSPPPSGVR SPPGLAKTPL SALGLKPHNP ADILLHPTGV TRRCIQPEED EGKVVVRLSE
EPRSYVESVA RTAVAGPRAQ DSEPKSFSAP AAQAYGHEIP LRNGTLGGSF VSPSPLSTSS
PILSADSTSV GSFPSGESSD QGPRTPTQPL LESGFRSGSL GQPSPSAQRN YQSSSPLPTV
GSSYSSPDYS LQQFSSSPES QARAQFSVAG VHTVPGSPQA RHRTVGTNTP PSPGFGRRAI
NPSMAAPSSP SLSHRQVMGP PGTGFHGSTV SSPQSSAATT PGSPSLGRHP TGAYQVSGLH
NNVATTPGSP SLGRHPGTHQ GNLASGLHGN AIPSPGSPSL GRHLGGSGSV VPGSPCLDRH
VAYGGYSTPE DRRPTVSRQS SASGYQAPST PSFPVSPAYY PGLSSPATSP SPDSAAFRQG
SPTPALPEKR RMSVGDRAGS LPNYATINGK VSSPVASGMS SPSGGSTVSF SHTLPDFSKY
SMPDNSPETR AKVKFVQDTS KYWYKPEISR EQAIALLKDQ EPGAFIIRDS HSFRGAYGLA
MKVSSPPPTI MQQNKKGDMT HELVRHFLIE TGPRGVKLKG CPNEPNFGSL SALVYQHSII
PLALPCKLVI PNRDPTDESK DSSGPANSTA DLLKQGAACN VLFVNSVDME SLTGPQAISK
ATSETLAADP TPAATIVHFK VSAQGITLTD NQRKLFFRRH YPLNTVTFCD LDPQERKWMK
TEGGAPAKLF GFVARKQGST TDNACHLFAE LDPNQPASAI VNFVSKVMLN AGQKR
//
