ID A0A1V4K7L4_PATFA Unreviewed; 1655 AA.
AC A0A1V4K7L4;
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-1 isoform F {ECO:0000313|EMBL:OPJ79887.1};
GN Name=TNS1 {ECO:0000313|EMBL:OPJ79887.1};
GN ORFNames=AV530_002330 {ECO:0000313|EMBL:OPJ79887.1};
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:OPJ79887.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ79887.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ79887.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ79887.1};
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:OPJ79887.1}.
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DR EMBL; LSYS01004331; OPJ79887.1; -; 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}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1655
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011985431"
FT DOMAIN 41..88
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 145..317
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 322..448
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1383..1492
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 669..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1238..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..972
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..987
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1655 AA; 179708 MW; 7BCC1AA0CB5BD80F CRC64;
MTRLSWCFAT LVRWGKSLVS CLLPLRACRH RKPQDLEAPS AHSFKMTSFK KVKACGICRQ
AITRQGSTCR GCKLSCHTKC QAKARPRMDF GSVMNQAVTP CSPAVNYELP SPGESIMKQV
DALDATKSPR SGQSRHKTSR SMSLTMAMES SCELDLVYIT ERIIAVSYPS TAEEQSFCSN
LREVAHMLKS KHGDNYVLFN LSERRHDINK LHPKVLDFGW PDMHTPALEK ICSICKAMDT
WLNATPHNVV VLHNKGNRGR LGVVVAAYMH YSNISASADQ ALDRFAMKRF YEDKVVPVGQ
PSQKRYIHYF SGLLSGSIKM NNKPLFLHHV IMHGIPNFES KGGCRPFLKI YQAMQPVYTS
GIYNVQGDSQ TGICITIEPG LLLKGDILLK CYHKKFRSPT RDVIFRVQFH TCAVHDLDVV
FGKEDLDEAF RDDRFPEYGK VEFVFSYGPE KIQGMEHLEN GPSVSVDYNT SDPLIRWDSY
ENFNIQREDS AEGAWAEPPQ PRKHLEKEVG HTQGPLDGSL YAKVKKKDSL HGSTGAINAT
RLPLSATPNH VEHTLSAVLS PEEKRELDRL LVHVNGNAAV LVAERETDIL DDELPNQDGH
SVGSLGTLSS LDGTTTTSEA GYQEARRVGS LCSLPNGPSS CNGAEKLLKE GLYDSELLSN
GGYPYNNQNT MMGHHLRDPL PPLRPSASAQ DHLAGYPQRP PGSHAPGWLQ PQPMPSSQPY
LYSYDPPGAY RSRSFPVVDM ANHSMPEFPR APSRREIEQS IEALDVLMLD LTPAVHKSQS
VPATSRQDKP AGPLLSSVSA HPIAGLYAQP TPQVAQPRSF GTSVSPAASE PRGKAYSPGE
SDYGVHEYRE TYSPYSYQPA PVPEPRNYSQ APAGAAMGIL PLSTSYSPVG SQQLHVSSPP
SPTVTPQTQM PPKGLESYED LSRSAEEPLN LEGLVAHRVA GVQSREKPLE ESTVPARKRT
PTDSHHEKSS PEPSSPRSPT ILSPEVVSTI AANPGGRPKE PHLHSYKEAF EEMESASPTS
PPSSGVRSPP GLAKTPLSAL GLKPHNPAEI LLHPVGEPRS YVESVARTAT TGRGGTLPAA
QPGGPEMPTR NGTFANSFTA PSPVSTSSPI HSMDGASLHS YPSEGSPHGT LTPPHALAEP
VYRSPVGSQM PSAHSSYQNS SPSSLTMIQG SPRTLHRTVA TNTPPSPGFG RRAVNPSMSG
APGSPGLGRH AVAAHGNLVA PPGSPSLVRH QVATAVPPGS PLYGYPSPEE RHPTLSRQSS
SSGYQPPSTP SFPVSPAYYP GTSTPHSSSP DSAAYHQGSP TPQPALPEKR RISTGDRSNS
LPNYATINGK ASSPLSSGMS SPSGGSTVTF SHTLPDFSKF SMPDISPETR ANVKFVQDTS
KYWYKPEISR EQAIALLKDR EPGAFIIRDS HSFRGAYGLA MKVASPPPTV MQQNKKGDIT
NELVRHFLIE TSPRGVKLKG CANEPYFGCL SALVYQHSIM PLALPCKLVI PDRDPMEEKK
DNTSATNSAT DLLKQGAACN VLFINSVEME SLTGPQAIAK AVAETLVADP TPTATIVHFK
VSAQGITLTD NQRKLFFRRH YPLNTVTFCD LDPQERKWTK TDGSGPAKLF GFVARKQGST
TDNVCHLFAE LDPDQPAAAI VNFVSRVMLG SGQKR
//
