ID PI3R5_MOUSE Reviewed; 871 AA.
AC Q5SW28; Q3TU01; Q3UDZ2; Q8C215; Q8CGQ7;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 24-JAN-2024, entry version 124.
DE RecName: Full=Phosphoinositide 3-kinase regulatory subunit 5;
DE Short=PI3-kinase regulatory subunit 5;
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Procko E., McColl S.R.;
RT "Cloning of a murine ortholog of a PI3-kinase gamma regulatory protein.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 of a catalytic subunit (PIK3CG/p120) and a
CC regulatory (PIK3R5a/p101) subunit. Interacts with beta-gamma G protein
CC 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}. Note=Predominantly localized in the
CC nucleus in absence of PIK3CG/p120. Colocalizes with PIK3CG/p120 in the
CC cytoplasm. Translocated to the plasma membrane in a beta-gamma G
CC protein-dependent manner. {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; AY156924; AAN84787.1; -; mRNA.
DR EMBL; AK089483; BAC40901.2; -; mRNA.
DR EMBL; AK149847; BAE29119.1; -; mRNA.
DR EMBL; AK161050; BAE36171.1; -; mRNA.
DR EMBL; AL606831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS24865.1; -.
DR RefSeq; NP_796294.2; NM_177320.2.
DR RefSeq; XP_006533611.1; XM_006533548.2.
DR AlphaFoldDB; Q5SW28; -.
DR SMR; Q5SW28; -.
DR CORUM; Q5SW28; -.
DR IntAct; Q5SW28; 2.
DR STRING; 10090.ENSMUSP00000021283; -.
DR iPTMnet; Q5SW28; -.
DR PhosphoSitePlus; Q5SW28; -.
DR EPD; Q5SW28; -.
DR jPOST; Q5SW28; -.
DR MaxQB; Q5SW28; -.
DR PaxDb; 10090-ENSMUSP00000021283; -.
DR ProteomicsDB; 289417; -.
DR Antibodypedia; 24754; 513 antibodies from 31 providers.
DR DNASU; 320207; -.
DR Ensembl; ENSMUST00000021283.8; ENSMUSP00000021283.8; ENSMUSG00000020901.14.
DR GeneID; 320207; -.
DR KEGG; mmu:320207; -.
DR UCSC; uc007jno.1; mouse.
DR AGR; MGI:2443588; -.
DR CTD; 23533; -.
DR MGI; MGI:2443588; Pik3r5.
DR VEuPathDB; HostDB:ENSMUSG00000020901; -.
DR eggNOG; ENOG502QV4A; Eukaryota.
DR GeneTree; ENSGT00530000063753; -.
DR HOGENOM; CLU_337590_0_0_1; -.
DR InParanoid; Q5SW28; -.
DR OMA; VLCQHSL; -.
DR OrthoDB; 5349388at2759; -.
DR PhylomeDB; Q5SW28; -.
DR TreeFam; TF102035; -.
DR Reactome; R-MMU-114604; GPVI-mediated activation cascade.
DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-MMU-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-MMU-9027276; Erythropoietin activates Phosphoinositide-3-kinase (PI3K).
DR BioGRID-ORCS; 320207; 7 hits in 78 CRISPR screens.
DR ChiTaRS; Pik3r5; mouse.
DR PRO; PR:Q5SW28; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SW28; Protein.
DR Bgee; ENSMUSG00000020901; Expressed in granulocyte and 80 other cell types or tissues.
DR ExpressionAtlas; Q5SW28; baseline and differential.
DR Genevisible; Q5SW28; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; ISO:MGI.
DR GO; GO:0005943; C:phosphatidylinositol 3-kinase complex, class IA; ISO:MGI.
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; ISO:MGI.
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:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:UniProtKB.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; ISO:MGI.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:UniProtKB.
DR InterPro; IPR019522; PIK3R5/6.
DR PANTHER; PTHR15593; PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR15593:SF2; PHOSPHOINOSITIDE 3-KINASE REGULATORY SUBUNIT 5; 1.
DR Pfam; PF10486; PI3K_1B_p101; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..871
FT /note="Phosphoinositide 3-kinase regulatory subunit 5"
FT /id="PRO_0000058422"
FT REGION 25..101
FT /note="Heterodimerization"
FT /evidence="ECO:0000250"
FT REGION 381..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..746
FT /note="Interaction with beta-gamma G protein dimers"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O02696"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYR1"
FT CONFLICT 65
FT /note="K -> E (in Ref. 2; BAE29119)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="I -> T (in Ref. 2; BAC40901)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="M -> V (in Ref. 1; AAN84787)"
FT /evidence="ECO:0000305"
FT CONFLICT 642
FT /note="A -> V (in Ref. 1; AAN84787)"
FT /evidence="ECO:0000305"
FT CONFLICT 647
FT /note="I -> T (in Ref. 1; AAN84787)"
FT /evidence="ECO:0000305"
FT CONFLICT 651
FT /note="M -> V (in Ref. 1; AAN84787)"
FT /evidence="ECO:0000305"
FT CONFLICT 796
FT /note="D -> G (in Ref. 2; BAE29119)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 871 AA; 96954 MW; 1D0F36A3D4042D62 CRC64;
MQPAATTCTE DRIQHALERC LHGLSLGRRS APWSAGLCLN CWSLQELVSR DPGHFLILLE
QILQKTQEVQ EKGTYDLLAP LALLFYSTVL CTPHFPPDSD LLLKAASTYH CFLTWPVPYC
SICREMLTFI DAELKAPGIS YQRLVRAEQG LPVRSHRSST VTVLLLNPVE VQAEFLAVAD
KLSTPGQSPH GTYTTLLLHA FQATFGAHCD LPKLHRKLQS KTIEELEDIF TETTEAQELA
SGIGDVAEAR EWLRTKLQAV GEKAGFPGIL DTASPGKLHT IPIPVARCYT YSWNQDSFDI
LQEVLLKEQE LLQPGILGDD EEEEEEDLEM DRHCAERDSL LSTSSLVSHD STLLLTSSQA
SEPVLSRQML TTFVSGLSDG MDSGYVEDSE ENSEWPQKPG SQKRQGHRRP GQKFNRFYKL
LKSTSQLVLR RDSRSLESSV DPTLPLRRAG SLCSPLDCPA QLPSRAQRSR SLPQAKLTTQ
LPRWLLAPPS HHQRRRPFLS GDEDPKASTL RVVVFGSDRI SGKVARAYSK LRRLETSHPI
LTRFFKLQFF YVPVKRSHGT SPSACPSSLS QASPLPADSL KYPSPTDLGM APWEDSTNDI
SHYLGMLDPW YERNVLGLMH LPPEVLCQQS LKADSRPLEG SATQLPILAD MLLYYCRFAA
RPVLLQVYQT ELTFVTGEKT TEIFIQSLEL GHSATTRAIK ASGRGRKRLG IDDDREAVPL
TLQIIYSKGA ISGRSRWSNL EKVCTSVNLS KACQKPEELD SSMEALTLTL TEVVKRQNPK
SKKGFNQIST SYIKVDKVQI IGSSSCPFAV CLDQDERKIL QSVVRCEVSP CYKPEKSSLP
PERSFSQPAE TGSDLCSLLC LPIMTFSGAL P
//
