ID A0A1V4JVD0_PATFA Unreviewed; 1576 AA.
AC A0A1V4JVD0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Tensin-3 isoform B {ECO:0000313|EMBL:OPJ76104.1};
GN Name=TNS3 {ECO:0000313|EMBL:OPJ76104.1};
GN ORFNames=AV530_015409 {ECO:0000313|EMBL:OPJ76104.1};
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:OPJ76104.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ76104.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ76104.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ76104.1};
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:OPJ76104.1}.
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DR EMBL; LSYS01006073; OPJ76104.1; -; Genomic_DNA.
DR Proteomes; UP000190648; Unassembled WGS sequence.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
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 GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd20889; C1_TNS3_v; 1.
DR CDD; cd01213; PTB_tensin; 1.
DR CDD; cd14561; PTP_tensin-3; 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 InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR45734; TENSIN; 1.
DR PANTHER; PTHR45734:SF5; TENSIN-3; 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; PS50056; TYR_PHOSPHATASE_2; 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 Cell projection {ECO:0000256|ARBA:ARBA00023273};
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 25..72
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 117..289
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 201..278
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 294..420
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1293..1403
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 479..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1202..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1576 AA; 172445 MW; 3CAF6D756C112F1E CRC64;
MFCTTGLPCV AAESGSEPQE TASRSHTFKN KSFKKSKICG ICKQVIDSQG ISCRVCKYAC
HRKCEEKVVT PCLLPSNYEL ANNSEALKNH VTRTGSSSTS KNLSFSCDKG SRSAEFDHIM
EEGYELDLTY ITERIIAVSF PASCSEETYL RNLQDVTRML KSKHGDNYLV LNLSEKRYDL
AKLNPKIMDV GWPDLHAPPL DKVCTICKAM ESWLNNDPQH VVVIHCRGGK GRIGVVISSY
MHFTNVSASA DQALDRFAMK KFFDDKVSAL MQPSQRRYVQ FLSGLLSGSV KMNAAPLFLH
YVILHGIPSF DAGAAFRPFL KLYQAMQPVY TSGIYSVGPE NQTRICIAID PAQLLKGDIM
LKCYHKKYRS ATRDVVFRLQ FHTGAIQGHG LVFSKEDLDN ANKDDRFPDY GKVELVFSGT
PEKIQGCEYL QNDHGVMVDY NTSDPLIRWD SYENMSPDGE VLHTQGPIDG SLYAKVRKKS
SSDSSIPGVA QGVPVTGSPD HSDHTLSVSS DSGHSTASIR TDKTEEHLGP GVKRGLSLQE
KAELNQLLSG FGLEDPVSTT KDMTDVRSKY SGTHHIVPAQ VHVNGDTKLK DRETDILDDE
MPNHDLHSVD SIGTLSSSEG QHSTHLGNFS CHKSSQNSLL SDGFGSNTGE EHHNAFAPDL
GIGVDPLYER SFGSTEPKST RQLQRNPCTS PQPQAYGPNN YSTQTWVRQQ QMVTHQYGFA
PENEIRVGIH NTVGSVQSQA QVPDTPTRGS SSRDAVQRGL GSMPCAAEAA EHASAETVKS
RPVPQRETNA LDRGQNSDDL PASPTLDIDQ SIEQLNRLIL ELDPTFEPIP TRINTVPRDR
NQVNGFTSLD VDVEGLGRSP GFHDKLEVTN RNPSQHATVM QDDATGGRIR KLSVGQYDND
VAGQPSYNRC GWMKSPATDQ AVNPGSPVPV GETKEMVVEH YQDEIDGGMF SPTNGNKAAP
STPAFPLSPD TPYMKTPPLY NQRTTSSQKI SSPSELYRAS PESRSYTEAV SHSLVMSDST
VSTNPPLLRA SMQTDPSFQH CFTSSCTVSS NSPIPGGESS SATESPWLES SPKATPSLQL
SMGNSRPPGG YLVPSEFSNA MQDVSLLSHF QTPGLQVITL SSLENSPAEP QQERAVSSST
QAYLSYSGGN MGSNSPREQK QANFIANASI SPKTVSSSVA NAEDNGFLTQ NFVTVASGHD
SQNSMVQQHR GGNIHAQPPL PEKKRSSEGD RSFTSVSPSS SGFSSPHSGS TISIPFPNVL
PDFSKMLSTS PVPENTTDKH VTVKFVQDTS KFWYKPDISR EQAIAVLKDK EPGSFIVRDS
HSFRGAYGLA MKVATPPPSV LQLNKKVGDL SNELVRHFLI ECTHKGVRLK GCPNEPYFGS
LTALVYQHSI TPLALPCKLL IPDRDPLEEI AETSPQTAAN SAVELLKQGA ACNVWYLNSV
EMESLTGYQA VQKALSLTLV QDPSPISTVV HFKVSAQGIT LTDNQRKLFF RRHYPVNSVI
FCALDPQDRK WTKDGLSAKV FGFVARKQGS TTDNLCHLFA EHDPEQPASA IVNFVSKKTE
EAESHPDLYS PYMNEA
//
