ID A0A3Q7SCL9_VULVU Unreviewed; 1857 AA.
AC A0A3Q7SCL9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Tensin-1 isoform X4 {ECO:0000313|RefSeq:XP_025857969.1};
GN Name=TNS1 {ECO:0000313|RefSeq:XP_025857969.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025857969.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025857969.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025857969.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025857969.1};
RG RefSeq;
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 RefSeq; XP_025857969.1; XM_026002184.1.
DR Proteomes; UP000286640; Unplaced.
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; cd01213; PTB_tensin; 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:UP000286640};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 20..67
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 129..301
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 306..432
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1585..1694
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 86..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..545
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 767..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..819
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..982
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1454..1474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1483..1499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1526..1549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1857 AA; 198640 MW; FC52E621E937501C CRC64;
MTWICLSCML WPEDLEAPKT HHFKVKTFKK VKPCGICRQV ITREGCTCKV CSFSCHRKCQ
AKVAAPCIPP SSHELVPINA ESAPKNVANT GEGAFRSGNT RKSLEEDGTT RVTPSVQPHP
QPIRNMSVSR TMEDSCELDL VYVTERIIAV SFPSTANEEN FRSNLREVAQ MLKSKHGGSY
LLFNLSERRP DITKLHAKVL EFGWPDLHTP ALEKICSVCK AMDTWLNADP HNVVVLHNKG
NRGRIGVVIA AYMHYSNISA SADQALDRFA MKRFYEDKIV PIGQPSQRRY VHYFSGLLSG
SIKMNNKPLF LHHVIMHGIP NFESKGGCRP FLRIYQAMQP VYTSGIYNVQ GDSQTSICIT
IEPGLLLKGD ILLKCYHKKF RSPARDVIFR VQFHTCAIHD LGVVFGKEDL DDAFKDDRFP
EYGKVEFVFS YGPEKIQGME HLENGPSVSV DYNTSDPLIR WDSYDNFDGH REDGMEEVVG
HTQGPLDGSL YAKVKKKDSL HGSTGAVNAT RPALSATPNH VEHTLSVSSD SGNSTASTKT
DKTDEPAPGP SSAPAALSPE EKRELDRLLS GFGVEREKQG AMYHPQHLRS RPAGGPAVPS
SGRHVVPAQV HVNGGALASE RETDILDDEL PNQDGHSVGS MGTLSSLDGV TNTSEGGYPE
ALSSLTNGLD KPYPVEPMVN GGAYPYESAS RTAPAHAAHV APMRPSYSAQ EGLAGYQREG
PHPAWPQPVT TSHYGHDPSS MFRSQSFPES EPQLPLAPAR GGSSREAVQR GLNSWQQQQQ
QQQQQQPRPP PRQQERAHLE SLGPSRPSPQ PPAETPTPGL PEFPRAASQQ EIEQSIEALN
MLMLDLEPAT ASAPLHKSQS VPGAWPGASP LSSQPLSGSS CQPHPLTQSR SGYIPSGHSL
GTPELAPRAS LAVESFPPGR PYSPYDYQPC PAGSSQSFRP KSPVSSSSAF LSTTQSPPGH
QQPPASLPGL TAQPPLPPKE ATSDPSRTPE EEPLNLEGLV AHRVAAYNAK LQGLGHPGSR
LPPLHRLRSS SLSGVQAREK QPAEPPAPLR RRAASDGQYE NQSPEPGSPR SPGVRSPVQC
VSPELALTIA LNPGGRPKEP HLHSYKEAFE EMEGTSPTSP PPSGVRSPPG LAKTPLSALG
LKPHNPADIL LHPTGEEDEG KVMTELPKEP RSYVESVVRT AVAGPRAQDP EPKSFSAPAA
QAYGHDTPLR NGTLGGSFVS PSPLSTSSPI LSADSTSVGS FPSGESSDQG PRTPTQPLLD
SGFRSGSLGQ PSPSAQRSYQ SSSPLPTVGS SYGSPDYPLQ QFSSPESQAR AQFTVAGVHP
VPGSPQARHR TVGTNTPPSP GFGRRAFNPS VAAPGSPSLS HRQAMGPAGT GFHGSTVSSP
QSSAATTPGS PSLARHPGAH PGGLASGVHG SALGSPGSPS LGRHLGAPGP GLPGSPGLER
HAAYGGYSTP EDPRPALSRQ SSASGYQAPS TPSFPVSPAY YPGLSSPATS PSPDSAAFRQ
GSPTPALPEK RRMSVGDRAG SLPNYATVNG KVSSSPVASG MSSPSGGSTV SFSHTLPDFS
KYSLPDNSPE TRAKVKFVQD TSKYWYKPEI SREQAIALLK DQEPGAFIIR DSHSFRGAYG
LAMKVSSPPP TIMQQNKKGD MTHELVRHFL IETGPRGVKL KGCPNEPNFG SLSALVYQHS
IIPLALPCKL VIPNRDPTDE SKDSSGPANS TTDLLKQGAA CNVLFVNSVD MESLTGPQAI
SKAASETLAA DPTPAATIVH FKVSAQGITL TDNQRKLFFR RHYPLNTVTF CDLDPQERKW
MKTEGGVPAK LFGFVARKQG STTDNACHLF AELDPNQPAS AIVNFVSKVM LSAGQKR
//
