CYB5B_MOUSE
ID CYB5B_MOUSE Reviewed; 146 AA.
AC Q9CQX2; Q9D1M6; Q9D8R3;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Cytochrome b5 type B;
DE AltName: Full=Cytochrome b5 outer mitochondrial membrane isoform;
DE Flags: Precursor;
GN Name=Cyb5b; Synonyms=Cyb5m;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Mammary gland, Pancreas, and Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Colon;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-80, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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: Cytochrome b5 is a membrane-bound hemoprotein functioning as
CC an electron carrier for several membrane-bound oxygenases.
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of a complex composed of cytochrome b5, NADH-
CC cytochrome b5 reductase (CYB5R3) and MTARC2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:P04166}.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK003333; BAB22721.1; -; mRNA.
DR EMBL; AK003815; BAB23012.1; -; mRNA.
DR EMBL; AK007780; BAB25251.1; -; mRNA.
DR EMBL; AK019263; BAB31635.1; -; mRNA.
DR EMBL; AK052810; BAC35156.1; -; mRNA.
DR EMBL; AK088970; BAC40677.1; -; mRNA.
DR EMBL; BC054749; AAH54749.1; -; mRNA.
DR EMBL; BC058812; AAH58812.1; -; mRNA.
DR EMBL; BC062980; AAH62980.1; -; mRNA.
DR CCDS; CCDS22647.1; -.
DR RefSeq; NP_079834.2; NM_025558.5.
DR AlphaFoldDB; Q9CQX2; -.
DR SMR; Q9CQX2; -.
DR BioGRID; 211466; 3.
DR IntAct; Q9CQX2; 1.
DR STRING; 10090.ENSMUSP00000034400; -.
DR iPTMnet; Q9CQX2; -.
DR PhosphoSitePlus; Q9CQX2; -.
DR SwissPalm; Q9CQX2; -.
DR EPD; Q9CQX2; -.
DR jPOST; Q9CQX2; -.
DR MaxQB; Q9CQX2; -.
DR PaxDb; Q9CQX2; -.
DR PRIDE; Q9CQX2; -.
DR ProteomicsDB; 279250; -.
DR TopDownProteomics; Q9CQX2; -.
DR Antibodypedia; 2014; 89 antibodies from 21 providers.
DR DNASU; 66427; -.
DR Ensembl; ENSMUST00000034400; ENSMUSP00000034400; ENSMUSG00000031924.
DR GeneID; 66427; -.
DR KEGG; mmu:66427; -.
DR UCSC; uc009nhg.1; mouse.
DR CTD; 80777; -.
DR MGI; MGI:1913677; Cyb5b.
DR VEuPathDB; HostDB:ENSMUSG00000031924; -.
DR eggNOG; KOG0537; Eukaryota.
DR GeneTree; ENSGT00940000155584; -.
DR HOGENOM; CLU_102602_3_3_1; -.
DR InParanoid; Q9CQX2; -.
DR OMA; KNNTCKS; -.
DR OrthoDB; 1566561at2759; -.
DR PhylomeDB; Q9CQX2; -.
DR TreeFam; TF314537; -.
DR Reactome; R-MMU-211945; Phase I - Functionalization of compounds.
DR BioGRID-ORCS; 66427; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Cyb5b; mouse.
DR PRO; PR:Q9CQX2; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9CQX2; protein.
DR Bgee; ENSMUSG00000031924; Expressed in adrenal gland and 257 other tissues.
DR Genevisible; Q9CQX2; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:1903958; C:nitric-oxide synthase complex; ISO:MGI.
DR GO; GO:0008047; F:enzyme activator activity; ISO:MGI.
DR GO; GO:0020037; F:heme binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050421; F:nitrite reductase (NO-forming) activity; ISO:MGI.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; ISO:MGI.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR Pfam; PF00173; Cyt-b5; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT PROPEP 1..11
FT /evidence="ECO:0000250|UniProtKB:P04166"
FT /id="PRO_0000006473"
FT CHAIN 12..146
FT /note="Cytochrome b5 type B"
FT /id="PRO_0000006474"
FT TRANSMEM 119..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 20..96
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 55
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|PROSITE-ProRule:PRU00279"
FT BINDING 79
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|PROSITE-ProRule:PRU00279"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43169"
FT MOD_RES 30
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43169"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 31
FT /note="R -> E (in Ref. 1; BAB25251)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="D -> G (in Ref. 1; BAB22721)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 146 AA; 16318 MW; 4ADA7C96A5F311DD CRC64;
MATPEASGSG EKVEGSEPSV TYYRLEEVAK RNSAEETWMV IHGRVYDITR FLSEHPGGEE
VLLEQAGADA TESFEDVGHS PDAREMLKQY YIGDVHPSDL KPKGDDKDPS KNNSCQSSWA
YWFVPIVGAI LIGFLYRHFW ADSKSS
