PI3R5_PIG
ID PI3R5_PIG Reviewed; 877 AA.
AC O02696;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Phosphoinositide 3-kinase regulatory subunit 5;
DE Short=PI3-kinase regulatory subunit 5;
DE AltName: Full=IB PI3-kinase p101 subunit;
DE AltName: Full=PI3-kinase p101 subunit;
DE AltName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase regulatory subunit;
DE Short=PtdIns-3-kinase regulatory subunit;
DE AltName: Full=PtdIns-3-kinase p101;
DE AltName: Full=p101-PI3K;
GN Name=PIK3R5;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, INTERACTION WITH
RP PIK3CG, AND ACETYLATION AT MET-1.
RC TISSUE=Neutrophil;
RX PubMed=9094719; DOI=10.1016/s0092-8674(00)80187-7;
RA Stephens L.R., Eguinoa A., Erdjument-Bromage H., Lui M., Cooke F.,
RA Coadwell J., Smrcka A.S., Thelen M., Cadwallader K., Tempst P.,
RA Hawkins P.T.;
RT "The G beta gamma sensitivity of a PI3K is dependent upon a tightly
RT associated adaptor, p101.";
RL Cell 89:105-114(1997).
RN [2]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=12507995; DOI=10.1083/jcb.200210115;
RA Brock C., Schaefer M., Reusch H.P., Czupalla C., Michalke M., Spicher K.,
RA Schultz G., Nurnberg B.;
RT "Roles of G beta gamma in membrane recruitment and activation of p110
RT gamma/p101 phosphoinositide 3-kinase gamma.";
RL J. Cell Biol. 160:89-99(2003).
RN [3]
RP SUBCELLULAR LOCATION, AND DOMAINS.
RX PubMed=15611065; DOI=10.1074/jbc.m413104200;
RA Voigt P., Brock C., Nurnberg B., Schaefer M.;
RT "Assigning functional domains within the p101 regulatory subunit of
RT phosphoinositide 3-kinase gamma.";
RL J. Biol. Chem. 280:5121-5127(2005).
CC -!- FUNCTION: Regulatory subunit of the PI3K gamma complex. Required for
CC recruitment of the catalytic subunit to the plasma membrane via
CC interaction with beta-gamma G protein dimers. Required for G protein-
CC mediated activation of PIK3CG. {ECO:0000269|PubMed:12507995}.
CC -!- ACTIVITY REGULATION: Greatly activated by G gamma proteins.
CC -!- SUBUNIT: Heterodimer of a catalytic subunit (PIK3CG/p120) and a
CC regulatory (PIK3R5a/p101) subunit. Interacts with beta-gamma G protein
CC dimers. {ECO:0000269|PubMed:12507995, ECO:0000269|PubMed:9094719}.
CC -!- INTERACTION:
CC O02696; P48736: PIK3CG; Xeno; NbExp=6; IntAct=EBI-6172343, EBI-1030384;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12507995,
CC ECO:0000269|PubMed:15611065}. Cytoplasm {ECO:0000269|PubMed:12507995,
CC ECO:0000269|PubMed:15611065}. Cell membrane
CC {ECO:0000269|PubMed:12507995, ECO:0000269|PubMed:15611065}; Peripheral
CC membrane protein {ECO:0000305|PubMed:12507995}. Note=Predominantly
CC localized in the nucleus in absence of PIK3CG/p120 (PubMed:12507995,
CC PubMed:15611065). Colocalizes with PIK3CG/p120 in the cytoplasm
CC (PubMed:12507995, PubMed:15611065). Translocated to the plasma membrane
CC in a beta-gamma G protein-dependent manner (PubMed:12507995,
CC PubMed:15611065). {ECO:0000269|PubMed:12507995,
CC ECO:0000269|PubMed:15611065}.
CC -!- DOMAIN: The heterodimerization region allows the binding to the
CC catalytic subunit. {ECO:0000269|PubMed:15611065}.
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DR EMBL; Y10742; CAA71730.1; -; mRNA.
DR RefSeq; NP_999016.1; NM_213851.1.
DR PDB; 7MEZ; EM; 2.89 A; B=1-877.
DR PDBsum; 7MEZ; -.
DR AlphaFoldDB; O02696; -.
DR SMR; O02696; -.
DR IntAct; O02696; 2.
DR STRING; 9823.ENSSSCP00000019060; -.
DR iPTMnet; O02696; -.
DR PaxDb; O02696; -.
DR PRIDE; O02696; -.
DR GeneID; 396851; -.
DR KEGG; ssc:396851; -.
DR CTD; 23533; -.
DR eggNOG; ENOG502QV4A; Eukaryota.
DR InParanoid; O02696; -.
DR OrthoDB; 142794at2759; -.
DR BRENDA; 2.7.1.137; 6170.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central.
DR GO; GO:0005944; C:phosphatidylinositol 3-kinase complex, class IB; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; IDA:UniProtKB.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IDA:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
DR InterPro; IPR019522; PIK3R5/6.
DR PANTHER; PTHR15593; PTHR15593; 1.
DR Pfam; PF10486; PI3K_1B_p101; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..877
FT /note="Phosphoinositide 3-kinase regulatory subunit 5"
FT /id="PRO_0000058423"
FT REGION 25..101
FT /note="Heterodimerization"
FT REGION 318..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..750
FT /note="Interaction with beta-gamma G protein dimers"
FT COMPBIAS 318..335
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..420
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..586
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:9094719"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYR1"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYR1"
FT VARIANT 483
FT /note="S -> G"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:7MEZ"
FT HELIX 43..48
FT /evidence="ECO:0007829|PDB:7MEZ"
FT HELIX 52..72
FT /evidence="ECO:0007829|PDB:7MEZ"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:7MEZ"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:7MEZ"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:7MEZ"
FT HELIX 117..135
FT /evidence="ECO:0007829|PDB:7MEZ"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:7MEZ"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:7MEZ"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:7MEZ"
FT HELIX 173..183
FT /evidence="ECO:0007829|PDB:7MEZ"
FT HELIX 189..204
FT /evidence="ECO:0007829|PDB:7MEZ"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:7MEZ"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:7MEZ"
FT HELIX 223..240
FT /evidence="ECO:0007829|PDB:7MEZ"
FT HELIX 246..264
FT /evidence="ECO:0007829|PDB:7MEZ"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:7MEZ"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:7MEZ"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:7MEZ"
FT STRAND 514..520
FT /evidence="ECO:0007829|PDB:7MEZ"
FT HELIX 523..525
FT /evidence="ECO:0007829|PDB:7MEZ"
FT HELIX 526..539
FT /evidence="ECO:0007829|PDB:7MEZ"
FT HELIX 540..542
FT /evidence="ECO:0007829|PDB:7MEZ"
FT HELIX 544..547
FT /evidence="ECO:0007829|PDB:7MEZ"
FT STRAND 552..557
FT /evidence="ECO:0007829|PDB:7MEZ"
FT HELIX 605..612
FT /evidence="ECO:0007829|PDB:7MEZ"
FT HELIX 614..619
FT /evidence="ECO:0007829|PDB:7MEZ"
FT HELIX 652..662
FT /evidence="ECO:0007829|PDB:7MEZ"
FT STRAND 665..668
FT /evidence="ECO:0007829|PDB:7MEZ"
FT STRAND 672..681
FT /evidence="ECO:0007829|PDB:7MEZ"
FT STRAND 683..690
FT /evidence="ECO:0007829|PDB:7MEZ"
FT STRAND 692..694
FT /evidence="ECO:0007829|PDB:7MEZ"
FT HELIX 697..706
FT /evidence="ECO:0007829|PDB:7MEZ"
FT TURN 713..716
FT /evidence="ECO:0007829|PDB:7MEZ"
FT STRAND 724..732
FT /evidence="ECO:0007829|PDB:7MEZ"
FT TURN 734..737
FT /evidence="ECO:0007829|PDB:7MEZ"
FT STRAND 740..749
FT /evidence="ECO:0007829|PDB:7MEZ"
FT STRAND 751..755
FT /evidence="ECO:0007829|PDB:7MEZ"
FT HELIX 756..758
FT /evidence="ECO:0007829|PDB:7MEZ"
FT HELIX 760..762
FT /evidence="ECO:0007829|PDB:7MEZ"
FT STRAND 770..774
FT /evidence="ECO:0007829|PDB:7MEZ"
FT STRAND 776..778
FT /evidence="ECO:0007829|PDB:7MEZ"
FT TURN 779..781
FT /evidence="ECO:0007829|PDB:7MEZ"
FT STRAND 795..805
FT /evidence="ECO:0007829|PDB:7MEZ"
FT STRAND 808..810
FT /evidence="ECO:0007829|PDB:7MEZ"
FT STRAND 814..818
FT /evidence="ECO:0007829|PDB:7MEZ"
FT STRAND 825..833
FT /evidence="ECO:0007829|PDB:7MEZ"
FT STRAND 868..873
FT /evidence="ECO:0007829|PDB:7MEZ"
SQ SEQUENCE 877 AA; 96994 MW; 4903F957EFE64817 CRC64;
MQPGATTCTE DRIQHALERC LHGLSLSRRS TSWSAGLCLN CWSLQELVSR DPGHFLILLE
QILQKTREVQ EKGTYDLLAP LALLFYSTVL CTPHFPPDSD LLLKAARTYH RFLTWPVPYC
SICQELLTFI DAELKAPGIS YQRLVRAEQG LSTRSHRSST VTVLLLNPVE VQAEFLDVAD
KLSTPGPSPH SAYITLLLHA FQATFGAHCD LSGLHRRLQS KTLAELEAIF TETAEAQELA
SGIGDAAEAR QWLRTKLQAV GEKAGFPGVL DTAKPGKLRT IPIPVARCYT YSWNQDSFDI
LQEILLKEQE LLQPEILDDE EDEDEEDEEE DLDADGHCAE RDSVLSTGSA ASHASTLSLA
SSQASGPTLS RQLLTSFVSG LSDGVDSGYM EDIEESAYER PRRPGGHERR GHRRPGQKFN
RIYKLFKSTS QMVLRRDSRS LEGSPDSGPP LRRAGSLCSP LDSPTLPPSR AQGSRSLPQP
KLSPQLPGWL LAPASRHQRR RPFLSGDEDP KASTLRVVVF GSDRISGKVV RAYSNLRRLE
NNRPLLTRFF KLQFFYVPVK RSRGTGTPTS PAPRSQTPPL PTDAPRHPGP AELGAAPWEE
STNDISHYLG MLDPWYERNV LGLMHLPPEV LCQSLKAEPR PLEGSPAQLP ILADMLLYYC
RFAARPVLLQ VYQTELTFIT GEKTTEIFIH SLELGHSAAT RAIKASGPGS KRLGIDGDRE
AVPLTLQIIY SKGAISGRSR WSNMEKLCTS VNLSKACRQQ EELDSSTEAL TLNLTEVVKR
QTPKSKKGFN QISTSQIKVD KVQIIGSNSC PFAVCLDQDE RKILQSVIRC EVSPCYKPEK
SSLCPPPQRP SYPPAPATPD LCSLLCLPIM TFSGALP
