ID A0A1V4K686_PATFA Unreviewed; 1634 AA.
AC A0A1V4K686;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Tensin-1 isoform B {ECO:0000313|EMBL:OPJ79883.1};
GN Name=TNS1 {ECO:0000313|EMBL:OPJ79883.1};
GN ORFNames=AV530_002330 {ECO:0000313|EMBL:OPJ79883.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ79883.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ79883.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ79883.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ79883.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ79883.1}.
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DR EMBL; LSYS01004331; OPJ79883.1; -; Genomic_DNA.
DR Proteomes; UP000190648; Unassembled WGS sequence.
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; 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; 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:UP000190648};
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 124..296
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 301..427
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1362..1471
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 648..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1217..1326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..951
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1634 AA; 177158 MW; 44F19B0DE29203F1 CRC64;
MTGLCLSCLL WPQDLEAPSA HSFKMTSFKK VKACGICRQA ITRQGSTCRG CKLSCHTKCQ
AKARPRMDFG SVMNQAVTPC SPAVNYELPS PGESIMKQVD ALDATKSPRS GQSRHKTSRS
MSLTMAMESS CELDLVYITE RIIAVSYPST AEEQSFCSNL REVAHMLKSK HGDNYVLFNL
SERRHDINKL HPKVLDFGWP DMHTPALEKI CSICKAMDTW LNATPHNVVV LHNKGNRGRL
GVVVAAYMHY SNISASADQA LDRFAMKRFY EDKVVPVGQP SQKRYIHYFS GLLSGSIKMN
NKPLFLHHVI MHGIPNFESK GGCRPFLKIY QAMQPVYTSG IYNVQGDSQT GICITIEPGL
LLKGDILLKC YHKKFRSPTR DVIFRVQFHT CAVHDLDVVF GKEDLDEAFR DDRFPEYGKV
EFVFSYGPEK IQGMEHLENG PSVSVDYNTS DPLIRWDSYE NFNIQREDSA EGAWAEPPQP
RKHLEKEVGH TQGPLDGSLY AKVKKKDSLH GSTGAINATR LPLSATPNHV EHTLSAVLSP
EEKRELDRLL VHVNGNAAVL VAERETDILD DELPNQDGHS VGSLGTLSSL DGTTTTSEAG
YQEARRVGSL CSLPNGPSSC NGAEKLLKEG LYDSELLSNG GYPYNNQNTM MGHHLRDPLP
PLRPSASAQD HLAGYPQRPP GSHAPGWLQP QPMPSSQPYL YSYDPPGAYR SRSFPVVDMA
NHSMPEFPRA PSRREIEQSI EALDVLMLDL TPAVHKSQSV PATSRQDKPA GPLLSSVSAH
PIAGLYAQPT PQVAQPRSFG TSVSPAASEP RGKAYSPGES DYGVHEYRET YSPYSYQPAP
VPEPRNYSQA PAGAAMGILP LSTSYSPVGS QQLHVSSPPS PTVTPQTQMP PKGLESYEDL
SRSAEEPLNL EGLVAHRVAG VQSREKPLEE STVPARKRTP TDSHHEKSSP EPSSPRSPTI
LSPEVVSTIA ANPGGRPKEP HLHSYKEAFE EMESASPTSP PSSGVRSPPG LAKTPLSALG
LKPHNPAEIL LHPVGEPRSY VESVARTATT GRGGTLPAAQ PGGPEMPTRN GTFANSFTAP
SPVSTSSPIH SMDGASLHSY PSEGSPHGTL TPPHALAEPV YRSPVGSQMP SAHSSYQNSS
PSSLTMIQGS PRTLHRTVAT NTPPSPGFGR RAVNPSMSGA PGSPGLGRHA VAAHGNLVAP
PGSPSLVRHQ VATAVPPGSP LYGYPSPEER HPTLSRQSSS SGYQPPSTPS FPVSPAYYPG
TSTPHSSSPD SAAYHQGSPT PQPALPEKRR ISTGDRSNSL PNYATINGKA SSPLSSGMSS
PSGGSTVTFS HTLPDFSKFS MPDISPETRA NVKFVQDTSK YWYKPEISRE QAIALLKDRE
PGAFIIRDSH SFRGAYGLAM KVASPPPTVM QQNKKGDITN ELVRHFLIET SPRGVKLKGC
ANEPYFGCLS ALVYQHSIMP LALPCKLVIP DRDPMEEKKD NTSATNSATD LLKQGAACNV
LFINSVEMES LTGPQAIAKA VAETLVADPT PTATIVHFKV SAQGITLTDN QRKLFFRRHY
PLNTVTFCDL DPQERKWTKT DGSGPAKLFG FVARKQGSTT DNVCHLFAEL DPDQPAAAIV
NFVSRVMLGS GQKR
//
