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CYB5_MOUSE
ID   CYB5_MOUSE              Reviewed;         134 AA.
AC   P56395;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 168.
DE   RecName: Full=Cytochrome b5;
GN   Name=Cyb5a; Synonyms=Cyb5;
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=FVB/N; TISSUE=Kidney;
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   [2]
RP   PROTEIN SEQUENCE OF 2-10; 25-73 AND 78-89, CLEAVAGE OF INITIATOR
RP   METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RA   Bienvenut W.V.;
RL   Submitted (JUL-2005) to UniProtKB.
RN   [3]
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).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-19, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-7; LYS-10 AND LYS-19, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA   Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT   identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC   -!- FUNCTION: Cytochrome b5 is a membrane-bound hemoprotein functioning as
CC       an electron carrier for several membrane-bound oxygenases. It is also
CC       involved in several steps of the sterol biosynthesis pathway,
CC       particularly in the C-5 double bond introduction during the C-5
CC       desaturation.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome b5 family. {ECO:0000305}.
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DR   EMBL; BC024341; AAH24341.1; -; mRNA.
DR   CCDS; CCDS29385.1; -.
DR   RefSeq; NP_080073.1; NM_025797.4.
DR   AlphaFoldDB; P56395; -.
DR   BMRB; P56395; -.
DR   SMR; P56395; -.
DR   BioGRID; 224948; 6.
DR   STRING; 10090.ENSMUSP00000124480; -.
DR   iPTMnet; P56395; -.
DR   PhosphoSitePlus; P56395; -.
DR   REPRODUCTION-2DPAGE; IPI00230113; -.
DR   REPRODUCTION-2DPAGE; P56395; -.
DR   SWISS-2DPAGE; P56395; -.
DR   CPTAC; non-CPTAC-3700; -.
DR   EPD; P56395; -.
DR   jPOST; P56395; -.
DR   PaxDb; P56395; -.
DR   PeptideAtlas; P56395; -.
DR   PRIDE; P56395; -.
DR   ProteomicsDB; 279251; -.
DR   TopDownProteomics; P56395; -.
DR   Antibodypedia; 23308; 373 antibodies from 31 providers.
DR   DNASU; 109672; -.
DR   Ensembl; ENSMUST00000160180; ENSMUSP00000124480; ENSMUSG00000024646.
DR   GeneID; 109672; -.
DR   KEGG; mmu:109672; -.
DR   UCSC; uc008fuw.1; mouse.
DR   CTD; 1528; -.
DR   MGI; MGI:1926952; Cyb5a.
DR   VEuPathDB; HostDB:ENSMUSG00000024646; -.
DR   eggNOG; KOG0537; Eukaryota.
DR   GeneTree; ENSGT00940000156770; -.
DR   HOGENOM; CLU_102602_3_3_1; -.
DR   InParanoid; P56395; -.
DR   OMA; YRFYFTQ; -.
DR   OrthoDB; 1566561at2759; -.
DR   PhylomeDB; P56395; -.
DR   TreeFam; TF314537; -.
DR   Reactome; R-MMU-196836; Vitamin C (ascorbate) metabolism.
DR   Reactome; R-MMU-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR   BioGRID-ORCS; 109672; 1 hit in 74 CRISPR screens.
DR   ChiTaRS; Cyb5a; mouse.
DR   PRO; PR:P56395; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; P56395; protein.
DR   Bgee; ENSMUSG00000024646; Expressed in right kidney and 258 other tissues.
DR   ExpressionAtlas; P56395; baseline and differential.
DR   Genevisible; P56395; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; TAS:MGI.
DR   GO; GO:0006631; P:fatty acid metabolic process; IC: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; Direct protein sequencing; Electron transport;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           2..134
FT                   /note="Cytochrome b5"
FT                   /id="PRO_0000166011"
FT   TRANSMEM        109..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          9..85
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT   BINDING         44
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         68
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         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|Ref.2"
FT   MOD_RES         7
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         10
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         19
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753,
FT                   ECO:0007744|PubMed:23806337"
SQ   SEQUENCE   134 AA;  15241 MW;  C2540A68320107C8 CRC64;
     MAGQSDKDVK YYTLEEIQKH KDSKSTWVIL HHKVYDLTKF LEEHPGGEEV LREQAGGDAT
     ENFEDVGHST DARELSKTYI IGELHPDDRS KIAKPSDTLI TTVESNSSWW TNWVIPAISA
     LAVALMYRLY MAED
 
 
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