ID   PIRK5_CHICK             Reviewed;         881 AA.
AC   Q5ZIB8;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Phosphoinositide 3-kinase regulatory subunit 5;
DE            Short=PI3-kinase regulatory subunit 5;
GN   Name=PIK3R5; ORFNames=RCJMB04_28f9;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Regulatory subunit of the PI3K gamma complex. {ECO:0000250}.
CC   -!- ACTIVITY REGULATION: Greatly activated by G gamma proteins.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer. Interacts with a catalytic subunit and with G
CC       beta gamma proteins (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}.
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DR   EMBL; AJ720866; CAG32525.1; -; mRNA.
DR   RefSeq; NP_001025868.1; NM_001030697.1.
DR   AlphaFoldDB; Q5ZIB8; -.
DR   SMR; Q5ZIB8; -.
DR   STRING; 9031.ENSGALP00000001860; -.
DR   PaxDb; Q5ZIB8; -.
DR   GeneID; 417319; -.
DR   KEGG; gga:417319; -.
DR   CTD; 23533; -.
DR   VEuPathDB; HostDB:geneid_417319; -.
DR   eggNOG; ENOG502QV4A; Eukaryota.
DR   InParanoid; Q5ZIB8; -.
DR   OrthoDB; 142794at2759; -.
DR   PhylomeDB; Q5ZIB8; -.
DR   PRO; PR:Q5ZIB8; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; IBA:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0043406; P:positive regulation of MAP kinase activity; IBA:GO_Central.
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..881
FT                   /note="Phosphoinositide 3-kinase regulatory subunit 5"
FT                   /id="PRO_0000058447"
FT   REGION          23..99
FT                   /note="Heterodimerization"
FT                   /evidence="ECO:0000250"
FT   REGION          312..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          472..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          657..757
FT                   /note="Interaction with G beta gamma proteins"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        313..332
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   881 AA;  98374 MW;  6AB0E56843A5A67C CRC64;
     MQHTTCTEDR IYHALERCLH GLSRDAVSSR WAAGLCLNCW SLQELVSRDA GNYLILVEKI
     LGKAREVQEK CDYDLVMPLA LLFYYAVLYA PHIPPDSELL LKAASIYHSF LTWPVPYCDV
     FRELLTFISD ELKAPGISFQ RLVRTEQGLP VKNYQSSTVT VLLLNRSEVQ SEFLSIAEKL
     SSTEPPRHAT LVLLLEHLYQ VTFGTRCDLG SLHHLLKAKT LEELSEIYTS AAEAQEIAAA
     SSDPVLARER LQSALRDIAG AAALPTIAGD AQPRRLQPIP IPTSRCYTYS WDQDNFDVLN
     DVLSKECSVV EPVASENEED EEEEEEDVET DGCSPERDSL LSPISSISKD SVYSALSEDG
     PKHSCVSLFS SSKDSISELT VVSKKSLRSF VSSLKDCMDS GYAEDSDESS LDTLGRPELK
     VEKTHHKYRH TLTNKIYKLF KSKSQLVLRR DLKDCVDTGS LPLRRAESLC HPQAKPRIPA
     RSRRAHSLPQ HGLGQKLQTP QTPQLLSLPR RPFLSYDEDA KVATMRVVVF GSDRISGKVA
     RAYSNLRLKE STCPTLTRYF KLQFFYVPVK RSCLLPAALL MHPPPSPSDL QLRALAQAEP
     TLAGAESSTN DISHYIGMLD PWYERNVLGL MNLPMDVLCQ SAKPEAEPQE DSREQLPILA
     DMILYYCRFA TRPVLLQLYQ TELTFIGGEK MTEVFIHSLE LGHSAATRAI KASGPGSKRL
     GIDGDREAIP LTLQIAYSKT AISGRSQWND VEKVCTSVNL SKACKKYEEL ASKTECLNLT
     MTEVVKRQNS KSKKSFNQLS VSQIKVDKVQ IIGVQSSFAV CLDQDEQKIL QSVTRCEISV
     CYRPRDSDPL ALRRSSLTPQ DPSEFHSLLC LPISTFSGAL P