ID A0A099ZI96_TINGU Unreviewed; 1177 AA.
AC A0A099ZI96;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase {ECO:0000256|ARBA:ARBA00012981};
DE EC=3.1.3.86 {ECO:0000256|ARBA:ARBA00012981};
DE Flags: Fragment;
GN ORFNames=N309_06070 {ECO:0000313|EMBL:KGL81527.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL81527.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL81527.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL81527.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC family. {ECO:0000256|ARBA:ARBA00008734}.
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DR EMBL; KL894160; KGL81527.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099ZI96; -.
DR STRING; 94827.A0A099ZI96; -.
DR Proteomes; UP000053641; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR CDD; cd09100; INPP5c_SHIP1-INPP5D; 1.
DR CDD; cd10343; SH2_SHIP; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR PANTHER; PTHR46051:SF3; PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE 5-PHOSPHATASE 1; 1.
DR PANTHER; PTHR46051; SH2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00017; SH2; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00128; IPPc; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS50001; SH2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000053641};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191}.
FT DOMAIN 4..100
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 869..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1044
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL81527.1"
FT NON_TER 1177
FT /evidence="ECO:0000313|EMBL:KGL81527.1"
SQ SEQUENCE 1177 AA; 132647 MW; 16962EF80A07A3E6 CRC64;
DQCWYHGNIT RSRAEDLLSK VGKDGSFLVR ASESIPSAYA LCVLFRNCVY TYRILPDKEN
KLIVQASEGV PVKYFENLEE LIDFYKQENM GLVWHLKYAV PREEEEAADE PEEDADLVPT
PPILPPRNIL MALPSSDVKE VPSLPETSRV ADASKLSLPE TLLQRLQHQD TSGVSDEHLK
LIQDYLRVHI TSDLEMVQTG SSNLPQLKKL LTLLCKGLFS EASRTLPSLE SIQKVFEQQL
HPGLHQRSQM LGEATPVNIV LKLNQLISLL SSIEEKVKTL LIEGPDSTHR RSLIPPVTFE
VKADSLGIFS KIHLKVDVEM GKLIIKRAKD GPEDKFYTHK KILQLIKSQK VPNKLVIVLE
TEKEKTQRKE YVFSDSKKRE GFCQLLQQMK NKHSEQPEPD MITIFIGTWN MGAAPPPKKI
TSWFLSKGQG KTRDDTADYI PHDIYVIGTQ EDPQGEKEWL ETLRQSLQEI TSISFKVIAI
HTLWNIRIVV LAKPEHENRI SHICTDNVKT GIANTLGNKG AVGVSFMFNG TSLGFVNSHL
TSGSEKKHRR NQNYTNILRF LTLGDKKLSP FNITHRFTHL FWLGDLNYRV EQPPTEAENI
IQKIRQQQYP ELLAFDQLLL ERKDHKVFLQ FEEEEITFAP TYRFERGTRE KYAYTKQKAT
GMKYNLPSWC DRVLWKSYPM VHVVCQSYGC TTDIMTSDHS PVFATFEVGV TSQFVSKNDL
KYTDSQGEIE FLHCYATLKT KSQTKFYIEF HSSCLETFVK SQEGENEDGN EGELVVKFID
ALPKLTPIIS DPEYLLDQHI LISIKSSDSD ESYGEGCIAL RIEATESLVP IHAVLTHHGE
KTGVFQGEIK LQTSQGKQRE KLYDFVKIER DENAGQKPKN VSNLDPNKDW DQTNSSTPTD
ISNANYMGMV AVPQPPSAMS QLKQIPSPEQ PSSLWSYEQQ PKENVSGMGQ REASTTSPSL
APLSPKTSLQ PTGNRSICSR SQEHLPPELG RNAAEPLLQE EGQQKPEMFE NPLYGSMGSK
GKAALKKEPD YAKASRKEQP LPHDQSFHLA KLQELESAKG PGKQPAPPFL VPTPRFRSYT
CSGQTEEKTT AEKTQGKPKV AAFTENASPL KKMVKPSRCE ASSSGQGQSS KPPLPSKSRA
VLDMQSSKGR DYRDSSELPH SGKHRTEEGP LGRTTTP
//
