ID   PI3R5_XENLA             Reviewed;         879 AA.
AC   Q6INI0;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Phosphoinositide 3-kinase regulatory subunit 5;
DE            Short=PI3-kinase regulatory subunit 5;
GN   Name=pik3r5;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC   -!- ACTIVITY REGULATION: Greatly activated by G gamma proteins.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer. Interacts with a catalytic subunit and with beta-
CC       gamma G protein dimers (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O02696}. Cytoplasm
CC       {ECO:0000250|UniProtKB:O02696}. Cell membrane
CC       {ECO:0000250|UniProtKB:O02696}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:O02696}.
CC   -!- DOMAIN: The heterodimerization region allows the binding to the
CC       catalytic subunit. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH72301.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC072301; AAH72301.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q6INI0; -.
DR   SMR; Q6INI0; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005944; C:phosphatidylinositol 3-kinase complex, class IB; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; IEA:InterPro.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; ISS:UniProtKB.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR   GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
DR   InterPro; IPR019522; PIK3R5/6.
DR   PANTHER; PTHR15593; PTHR15593; 1.
DR   Pfam; PF10486; PI3K_1B_p101; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasm; Membrane; Nucleus; Reference proteome.
FT   CHAIN           1..879
FT                   /note="Phosphoinositide 3-kinase regulatory subunit 5"
FT                   /id="PRO_0000058424"
FT   REGION          23..100
FT                   /note="Heterodimerization"
FT                   /evidence="ECO:0000250"
FT   REGION          314..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          570..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          651..751
FT                   /note="Interaction with beta-gamma G protein dimers"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        315..334
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        570..586
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   879 AA;  98929 MW;  4319FD704D136164 CRC64;
     MQNTSCTEDR IQHALERCLH GLSGSTDISS NWTAGLCLNY WSLEELVNRD ATNYIILAEK
     TLARTREAQK NGEYELLTPL ALMFYFAVLR APYIPETSDL LPKAFEVFHT FLTWPAPYCH
     VYQEMLSFIS EEQKAPGITY QRLVRTEQGI PTRSSCSSTA TVLLVNPAEL PSEFLSVAEQ
     LSNAEQPIQQ TLVSLIQHLF QASLGTHAHT EELGASLKSR PIEKLQEIYS DLTEAMEHAT
     MADIKPGKKR ESLKAKLLEV AEKAGLMQGN TGSSLTSRIQ PIFMPVAKCY TYSWDQDDFD
     ILNQILLSES HLESLEDDVT EEDEEVDFEE VDDKDEDGGK SPKQDSVFSN SYVYWNFPSD
     SKEDPSMSMS NLASHSMTFV SSLSSCVDSG YVEDSDEGSQ EISEIGEYQE ERANNKLKQK
     ICQLFKTKGH QAKDKLKAEL SPCISHPLLS PFPDISKTIP LRRAGSMYTP QLSRIPVRSK
     RSKSLPQPAF GTQFLDLQLS QKVAFKRRPF LSCDDDTKVS TLRIVVFGSD RISGKVARAY
     SNLRLKESSC PLLTRFFKLQ FYYIPVKRSS SSTNAPMTNA ESPLKSPSPS GRFPLQDVFG
     DEASTNDISH YIGILDPWYK RNIMGLMDLS TSMLCQSSKE ENETTETTTM PILADMVLYY
     CRFATRSLLL QLYRAEITFD SGGKQTEVFI QCLELGHSAD LRAIRASGPG CKRLGIDGDQ
     DVIPFTLQIV YSKSTVSGRS RWSNGEKVCT SVSLRKACNT YEELDSKMEC LNLTVREVVK
     RQNSKTKKSF NQICTSHIKI DKAQIIAQHG GTFPLCLDQD ERKILQRVIK CEVSPCYKPE
     DRDFCRRNRR PSWSQASQNQ SEFCSLLCLP IATFCGAQP