CY24A_MOUSE
ID CY24A_MOUSE Reviewed; 192 AA.
AC Q61462; Q3U820; Q9CWB9; Q9D2W2;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Cytochrome b-245 light chain;
DE AltName: Full=Cytochrome b(558) alpha chain;
DE AltName: Full=Cytochrome b558 subunit alpha;
DE AltName: Full=Neutrophil cytochrome b 22 kDa polypeptide;
DE AltName: Full=Superoxide-generating NADPH oxidase light chain subunit;
DE AltName: Full=p22 phagocyte B-cytochrome;
DE AltName: Full=p22-phox;
DE Short=p22phox;
GN Name=Cyba {ECO:0000312|MGI:MGI:1316658};
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] OF 3-192 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Macrophage;
RX PubMed=2597164; DOI=10.1016/s0006-291x(89)80051-8;
RA Sumimoto H., Nozaki M., Sasaki H., Takeshige K., Sakaki Y., Minakami S.;
RT "Complementary DNA for the mouse homolog of the small subunit of human
RT cytochrome b558.";
RL Biochem. Biophys. Res. Commun. 165:902-906(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryonic stem cell, and Kidney;
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 MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND SER-176, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH SH3PXD2A.
RX PubMed=19755709; DOI=10.1126/scisignal.2000368;
RA Diaz B., Shani G., Pass I., Anderson D., Quintavalle M., Courtneidge S.A.;
RT "Tks5-dependent, nox-mediated generation of reactive oxygen species is
RT necessary for invadopodia formation.";
RL Sci. Signal. 2:RA53-RA53(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND SER-176, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, and Spleen;
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).
RN [7]
RP INTERACTION WITH GBP7.
RX PubMed=21551061; DOI=10.1126/science.1201711;
RA Kim B.H., Shenoy A.R., Kumar P., Das R., Tiwari S., MacMicking J.D.;
RT "A family of IFN-gamma-inducible 65-kD GTPases protects against bacterial
RT infection.";
RL Science 332:717-721(2011).
RN [8]
RP UBIQUITINATION AT LYS-149.
RX PubMed=26194095; DOI=10.1038/ncomms8838;
RA Graham D.B., Becker C.E., Doan A., Goel G., Villablanca E.J., Knights D.,
RA Mok A., Ng A.C., Doench J.G., Root D.E., Clish C.B., Xavier R.J.;
RT "Functional genomics identifies negative regulatory nodes controlling
RT phagocyte oxidative burst.";
RL Nat. Commun. 6:7838-7838(2015).
RN [9]
RP DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=28351984; DOI=10.1084/jem.20161382;
RA Thomas D.C., Clare S., Sowerby J.M., Pardo M., Juss J.K., Goulding D.A.,
RA van der Weyden L., Storisteanu D., Prakash A., Espeli M., Flint S.,
RA Lee J.C., Hoenderdos K., Kane L., Harcourt K., Mukhopadhyay S., Umrania Y.,
RA Antrobus R., Nathan J.A., Adams D.J., Bateman A., Choudhary J.S.,
RA Lyons P.A., Condliffe A.M., Chilvers E.R., Dougan G., Smith K.G.;
RT "Eros is a novel transmembrane protein that controls the phagocyte
RT respiratory burst and is essential for innate immunity.";
RL J. Exp. Med. 214:1111-1128(2017).
CC -!- FUNCTION: Critical component of the membrane-bound oxidase of
CC phagocytes that generates superoxide. Associates with NOX3 to form a
CC functional NADPH oxidase constitutively generating superoxide.
CC {ECO:0000269|PubMed:19755709}.
CC -!- SUBUNIT: Composed of a heavy chain (beta) and a light chain (alpha).
CC Component of an NADPH oxidase complex composed of a heterodimer formed
CC by the membrane proteins CYBA and CYBB and the cytosolic subunits NCF1,
CC NCF2 and NCF4. Interacts with NCF1 (via SH3 domain). Interacts with
CC DUOX1, DUOX2 and TPO. Interacts with NOX3 and NOX4. Interacts with
CC calprotectin (S100A8/9) (By similarity). Interacts with SH3PXD2A
CC (PubMed:19755709). Interacts with GBP7 (PubMed:21551061).
CC {ECO:0000250|UniProtKB:P13498, ECO:0000269|PubMed:19755709,
CC ECO:0000269|PubMed:21551061}.
CC -!- INTERACTION:
CC Q61462; Q61093: Cybb; NbExp=4; IntAct=EBI-15795776, EBI-6654585;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P13498}.
CC Note=As unassembled monomer may localize to the endoplasmic reticulum.
CC {ECO:0000305|PubMed:19755709}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q61462-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q61462-2; Sequence=VSP_001248;
CC -!- TISSUE SPECIFICITY: The strongest level of expression is found in
CC kidney, peritoneal neutrophils and peritoneal macrophages, and a lower
CC level in spleen and small intestine. Very low level of expression can
CC be noted in brain, liver, testis, and heart.
CC {ECO:0000269|PubMed:2597164}.
CC -!- PTM: The heme prosthetic group could be coordinated with residues of
CC the light chain, the heavy chain, or both, and it is possible that more
CC than one heme is present per cytochrome b-245. {ECO:0000250}.
CC -!- PTM: Phosphorylation at Thr-147 enhances NADPH oxidase activity by
CC promoting p47phox binding. {ECO:0000250}.
CC -!- PTM: Ubiquitinated at Lys-149 likely by RNF145.
CC {ECO:0000269|PubMed:26194095}.
CC -!- DISRUPTION PHENOTYPE: Mice show defects in invadopodia biogenesis
CC (PubMed:19755709). Mutants have a very sever defect in controlling
CC bacterial replication (PubMed:28351984). Mice show spontaneous trunk
CC curland head bobbing and fail to exhibit contact-rghting reflex
CC (PubMed:28351984). {ECO:0000269|PubMed:19755709,
CC ECO:0000269|PubMed:28351984}.
CC -!- SIMILARITY: Belongs to the p22phox family. {ECO:0000305}.
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DR EMBL; M31775; AAA37513.1; -; mRNA.
DR EMBL; AK018713; BAB31361.1; -; mRNA.
DR EMBL; AK021200; BAB32327.1; -; mRNA.
DR EMBL; AK152414; BAE31199.1; -; mRNA.
DR EMBL; BC026791; AAH26791.1; -; mRNA.
DR CCDS; CCDS22737.1; -. [Q61462-1]
DR CCDS; CCDS85623.1; -. [Q61462-2]
DR PIR; A36747; A36747.
DR RefSeq; NP_001288213.1; NM_001301284.1. [Q61462-2]
DR RefSeq; NP_031832.2; NM_007806.3. [Q61462-1]
DR AlphaFoldDB; Q61462; -.
DR BioGRID; 198989; 2.
DR DIP; DIP-60456N; -.
DR IntAct; Q61462; 3.
DR MINT; Q61462; -.
DR STRING; 10090.ENSMUSP00000017604; -.
DR iPTMnet; Q61462; -.
DR PhosphoSitePlus; Q61462; -.
DR SwissPalm; Q61462; -.
DR EPD; Q61462; -.
DR MaxQB; Q61462; -.
DR PaxDb; Q61462; -.
DR PRIDE; Q61462; -.
DR ProteomicsDB; 285355; -. [Q61462-1]
DR ProteomicsDB; 285356; -. [Q61462-2]
DR Antibodypedia; 4009; 277 antibodies from 27 providers.
DR Ensembl; ENSMUST00000017604; ENSMUSP00000017604; ENSMUSG00000006519. [Q61462-1]
DR Ensembl; ENSMUST00000212600; ENSMUSP00000148320; ENSMUSG00000006519. [Q61462-2]
DR GeneID; 13057; -.
DR KEGG; mmu:13057; -.
DR UCSC; uc009nsp.2; mouse. [Q61462-1]
DR UCSC; uc009nsq.2; mouse. [Q61462-2]
DR CTD; 1535; -.
DR MGI; MGI:1316658; Cyba.
DR VEuPathDB; HostDB:ENSMUSG00000006519; -.
DR eggNOG; ENOG502QVK1; Eukaryota.
DR GeneTree; ENSGT00390000002290; -.
DR HOGENOM; CLU_125024_0_0_1; -.
DR InParanoid; Q61462; -.
DR OMA; AYDNPIS; -.
DR PhylomeDB; Q61462; -.
DR TreeFam; TF328901; -.
DR Reactome; R-MMU-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-MMU-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
DR Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 13057; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Cyba; mouse.
DR PRO; PR:Q61462; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q61462; protein.
DR Bgee; ENSMUSG00000006519; Expressed in granulocyte and 225 other tissues.
DR ExpressionAtlas; Q61462; baseline and differential.
DR Genevisible; Q61462; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043020; C:NADPH oxidase complex; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0009055; F:electron transfer activity; ISO:MGI.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; ISO:MGI.
DR GO; GO:1904385; P:cellular response to angiotensin; IEA:Ensembl.
DR GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:1904845; P:cellular response to L-glutamine; IEA:Ensembl.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0071310; P:cellular response to organic substance; ISO:MGI.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0017004; P:cytochrome complex assembly; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0070254; P:mucus secretion; IMP:MGI.
DR GO; GO:0003106; P:negative regulation of glomerular filtration by angiotensin; ISO:MGI.
DR GO; GO:0045777; P:positive regulation of blood pressure; ISO:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; ISO:MGI.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:MGI.
DR GO; GO:0070257; P:positive regulation of mucus secretion; IMP:MGI.
DR GO; GO:0033864; P:positive regulation of NAD(P)H oxidase activity; ISO:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISO:MGI.
DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; ISO:MGI.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; ISO:MGI.
DR GO; GO:0034137; P:positive regulation of toll-like receptor 2 signaling pathway; ISO:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:MGI.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IMP:MGI.
DR GO; GO:0045730; P:respiratory burst; ISO:MGI.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:1904044; P:response to aldosterone; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0070555; P:response to interleukin-1; IEA:Ensembl.
DR GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0014895; P:smooth muscle hypertrophy; ISO:MGI.
DR GO; GO:0042554; P:superoxide anion generation; ISO:MGI.
DR GO; GO:0006801; P:superoxide metabolic process; ISO:MGI.
DR InterPro; IPR007732; Cyt_b558_asu.
DR PANTHER; PTHR15168; PTHR15168; 1.
DR Pfam; PF05038; Cytochrom_B558a; 1.
DR PIRSF; PIRSF019635; Cytochr_b558a; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Electron transport; Heme; Iron;
KW Isopeptide bond; Membrane; Metal-binding; NADP; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..192
FT /note="Cytochrome b-245 light chain"
FT /id="PRO_0000144908"
FT INTRAMEM 91..127
FT /evidence="ECO:0000250"
FT REGION 134..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 94
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT MOD_RES 147
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P13498"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 149
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:26194095"
FT VAR_SEQ 68..96
FT /note="CGQKYLTSVVKLFGPLTRNYYVRAALHFL -> W (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_001248"
FT CONFLICT 75
FT /note="S -> P (in Ref. 2; BAB32327)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 192 AA; 20748 MW; 10DA1F9A54F44E80 CRC64;
MGQIEWAMWA NEQALASGLI LITGGIVATA GRFTQWYFGA YSIAAGVLIC LLEYPRGKRK
KGSTMERCGQ KYLTSVVKLF GPLTRNYYVR AALHFLLSVP AGFLLATILG TVCLAIASVI
YLLAAIRGEQ WTPIEPKPKE RPQVGGTIKQ PPTNPPPRPP AEVRKKPSEG EEEAASAGGP
QVNPMPVTDE VV
