ID A0A493TLJ3_ANAPP Unreviewed; 1872 AA.
AC A0A493TLJ3;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Tensin 1 {ECO:0000313|Ensembl:ENSAPLP00000026762.1};
GN Name=TNS1 {ECO:0000313|Ensembl:ENSAPLP00000026762.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000026762.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000026762.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000026762.1}
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; ENSAPLT00000039903.1; ENSAPLP00000026762.1; ENSAPLG00000025012.1.
DR GeneTree; ENSGT00940000155400; -.
DR Proteomes; UP000016666; Chromosome 7.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
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; 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 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; 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.
PE 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
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:UP000016666};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}.
FT DOMAIN 149..321
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 326..452
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1600..1709
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 91..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1455..1565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..880
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1364..1380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1468..1485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1492..1516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1536..1565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1872 AA; 200360 MW; 69BE86C9FAF40749 CRC64;
MAPGEAMCLP SECLHRARER TGCALAPAAA PGTARVSTGP DIRRLGLVYQ SSWGREKQKP
PPKGRDMRQR WACVTHRQLG GLCHGPRASA CPAPGATAQH PRVPQPSQGT PGVTAATPCA
PAVNYELDTT KSPRSGQSRR KASRSMSVTA AMESSCELDL VYITERIIAV SYPSAAEEQS
FRSNLREVAH MLKSKHGDNY VLFNLSERRH DISKLHPKVL DFGWPDLHTP ALEKICSICK
AMDTWLNAGA HNVVVLHNKG NRGRLGVVVA AYMHYSNISA SADQALDRFA MKRFYEDKVV
PVGQPSQRRY IHYFSGLLSG SIKMNNKPLF LHHVIMHGIP NFESKGGCRP FLKIYQAMQP
VYTSGIYNVQ GDSQTGICIT IEPGLLLKGD ILLKCYHKKF RSPTRDVIFR VQFHTCAVHD
LDIVFGKEDL DEAFRDDRFP EYGKVEFVFS YGPEKIQGME HLENGPSVSV DYNTSDPLIR
WDSYENFNIQ REDSAEGTWA EPPLPAKHLE KEVGHTQGPL DGSLYAKVKK KDSLHGSTGA
VNAARLPLSA TPNHVEHTLS VSSDSGNSTA STKTDRTDEP GAPGAPGGHA VLSPEEKREL
DRLLVGFGLE SAAPMHNHAP GPVPARAPAV PGRHVVPAQV HVNGGAAPLV AERETDILDD
ELPNQDGHSV GSLGTLSSLD GTTTASEAGY HEAPRVGSLS SLPNGPASYN GAEKMLKEGL
YEAEPLSNGT YPYGNQNALV GHHLRDPLAH LRPSASAQEH LAAYPQRPPA TASPGWLQPP
APQSYVYGYE LPGAHRSQSF PAVGTAKYEA NPALPQAPAR STSSREAVQR GLNSWQQQGG
SRPPSRLQDG GLESHSPSLS SCSPQPSPLQ PVPPHSHSMP EFPRAPSRRE IEQSIEALDV
LMLDLAPSVH KSQSVPTATR QDKPAALLSS LSAQPLASHY AQPAPQVAQP RSFGTPVGSD
PLAKAYSPGP LAPVGRGAME PDYTVHEYRE TYTPYSYQPV PEPRSYSHAV APASVLPLST
SYSPVGSQQL LVSSPPSPTI PAQSQMPPKG LESYEDLSRS AEEPLNLEGL VAHRVAEYNA
KLRDLNKSTK APRPPPKQQR SFSSSGVQSR EKPPEESSIP ARRRTPSDSH YEKSSPEPSS
PRSPTVLSPE VVSTIAANPG GRPKEPHLHS YKEAFEELDG ASPSSPTSGG VRSPPGLAKT
PLSALGLKPH NPAEILLHPV GEGEAGAASA EEPRSYVESV ARTATTGGGG TLPAAQPGGL
EVPTRNGAFG NSFTAPSPVS TSSPIHSVDG ASLHSYPSEG SPHGTVTPPH AAAEPAYRSP
VASQMPSAHS SYQTSSPSSF QAATPGSLYA SPDYPDSRAG FQPDPQMRPQ QQQQQVNVVG
VHALPGSPRT LHRTVATNTP PSPGFGRRAV NPAVGGAPGS PGLGRHAVAP HGNLAVPPGS
PNLARHQAAV AAVPPGSPVY GYSSPEERRP TLSRQSSSSG YQPPSTPSFP VSPAYYPGTS
TPHSSSPDSA AYRQGSPTPQ PALPEKRRMS AGERANSLPN YATVNGKASS PLSSGMSSPS
SGSAVAFSHT LPDFSKFSMP DISPETRANV KFVQDTSKYW YKPEISREQA IALLKDREPG
AFIIRDSHSF RGAYGLAMKV ASPPPTVMQQ NKKGDITNEL VRHFLIETSP RGVKLKGCPN
EPNFGCLSAL VYQHSIMPLA LPCKLVIPDR DPMEEKKDAA SASNSATDLL KQGAACNVLF
INSVEMESLT GPQAISKAVA ETLVADPTPT ATIVHFKVSA QGITLTDNQR KLFFRRHYPL
NTVTFCDLDP QERKWTKTDG SGPAKLFGFV ARKQGSTTDN VCHLFAELDP EQPAAAIVNF
VSRVMLGSGQ KR
//
