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Database: UniProt
Entry: A0A1S3W7W3_ERIEU
LinkDB: A0A1S3W7W3_ERIEU
Original site: A0A1S3W7W3_ERIEU 
ID   A0A1S3W7W3_ERIEU        Unreviewed;      1341 AA.
AC   A0A1S3W7W3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Tensin-1 isoform X4 {ECO:0000313|RefSeq:XP_016042578.1};
GN   Name=TNS1 {ECO:0000313|RefSeq:XP_016042578.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016042578.1};
RN   [1] {ECO:0000313|RefSeq:XP_016042578.1}
RP   IDENTIFICATION.
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_016042578.1; XM_016187092.1.
DR   CTD; 7145; -.
DR   OrthoDB; 3439226at2759; -.
DR   Proteomes; UP000079721; Unplaced.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   CDD; cd01213; PTB_tensin; 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; 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; PF08416; PTB; 1.
DR   Pfam; PF10409; PTEN_C2; 1.
DR   Pfam; PF00017; SH2; 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.
PE   3: Inferred from homology;
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191}.
FT   DOMAIN          4..176
FT                   /note="Phosphatase tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51181"
FT   DOMAIN          181..307
FT                   /note="C2 tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51182"
FT   DOMAIN          1116..1225
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   REGION          397..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          607..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          687..1058
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..447
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        691..705
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        719..807
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        834..848
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        880..895
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        936..950
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        986..1005
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1014..1030
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1341 AA;  143857 MW;  01CDBCA8D091517D CRC64;
     MSVSPPVEDS CELDLVYVTE RIIAVSFSSS ANEDTFRSNL RQVAQMLSSK HGGSYLLFNL
     SERRPDITKL HAKVLEFGWP DLHTPALEKI CSVCKAMDTW LNADPHNVVV LHNKGNRGRI
     GVVIAAYMHY SNISASADQA LDRFAMKRFY EDKIVPIGQP SQRRYVHYFS GLLSGSIKMN
     NKPLFLHHVI MHGIPNFESK GGCRPFLRIY QAMQPVYTSG IYNVQGDSQT SICITIEPGL
     LLKGDILLKC YHKKFRSPAR DVIFRVQFHT CAIHDLGVVF GKEDLDDAFR DDRFPEYGKV
     EFVFSYGPEK IQGMEHLVNG PSVSVDYNTA DPLIRWDSYD NFNGYREDGM EEVVGHTQGP
     LDGSLYAKVK KKDSLQGSPG GVHIQRPVLS ATPNHVEHTL SHCPAGPTQS LHPKSPATAS
     STSPAFLPAT HSPPGPQQPP ASIPGLTAQP QLPPKEGTPD PSRTPEEEPL NLEGLVAHRV
     AAYNARLQGL GHSVGSRRPP LHRLQDSSLS GGPPDPLVSR APGMPMDTQC HQLERSRPGF
     WKSEGWREEL GVQARERQPA EPPAPLRKRA ASDGQYEYHS PEPSSPRSPG VRSPVQCVSP
     ELALTIALNP GGRPKEPHLH SYKEAFEEME GTSPASPPPS GVRSPPGLAK TPLSALGLKP
     HNPADIVLYS MGEPRSYVES VVRTAVTGPR AQDPESKSFT APTVQAYSHE PPLRNGTLGS
     SFVPPSPLST SSPILSAEST SMGSFPSGES SSQGHWTPTQ PYMDPSFRSG SLGQPSPSAQ
     RNYQSSSPLP ATGSSGAYSS PDYAFQPFST PDGQARPPFS SAGVHPVPGS PQARHRTVGT
     NTPPSPGFGR RALNSGMATP GSPGLSHRQV MGPGAGFHGN VVSSPQSSTV TTPGSPGLAR
     HPGVHQSSGL HGSNLVATPG SPNLGRHPGV HQGSLASGLH GSTTPSPGSP SLGRHLGASG
     TVVPGSPSLD RHTAYGGHST PEERRPALSR QSSASGYQAP STPSFPVSPA YYPGLSSPAT
     SPSPDSAAFR QGSPTPALPE KRRMSMGDRA GSLPNYATIN GKVSSSPVAS GMSSPSGGST
     VSFSHTLPDF SKYSMPDNSP ETRAKVKFVQ DTSKYWYKPE ISREQAIALL KDQEPGAFII
     RDSHSFRGAY GLAMKVSSPP TTIMQQNKKG DMTHELVRHF LIETGPRGVK LKGCPNEPNF
     GSLSALVYQH SIIPLALPCK LVIPNRDPTD DAKDSSGPAN STTDLLKQGA ACNVLFVNSV
     DMESLTGPQA ISKATSETLA ADPTPAATIV HFKVSAQGIT LTDNQRKLFF RRHYPLNTVT
     FCDLDPQERK WMKTEGGAPA K
//
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