LOCUS       NP_085075                146 aa            linear   ROD 31-MAY-2024
DEFINITION  cytochrome b5 type B precursor [Rattus norvegicus].
ACCESSION   NP_085075
VERSION     NP_085075.1
DBSOURCE    REFSEQ: accession NM_030586.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Neve,E.P., Nordling,A., Andersson,T.B., Hellman,U., Diczfalusy,U.,
            Johansson,I. and Ingelman-Sundberg,M.
  TITLE     Amidoxime reductase system containing cytochrome b5 type B (CYB5B)
            and MOSC2 is of importance for lipid synthesis in adipocyte
            mitochondria
  JOURNAL   J Biol Chem 287 (9), 6307-6317 (2012)
   PUBMED   22203676
  REMARK    GeneRIF: The presence of a novel reductive enzyme system of
            importance for lipid synthesis that is exclusively localized to the
            outer mitochondrial membrane and is composed of CYB5B, MOSC2, and a
            third unknown component (a CYB5B reductase).
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Parthasarathy,S., Altuve,A., Terzyan,S., Zhang,X., Kuczera,K.,
            Rivera,M. and Benson,D.R.
  TITLE     Accommodating a nonconservative internal mutation by water-mediated
            hydrogen bonding between beta-sheet strands: a comparison of human
            and rat type B (mitochondrial) cytochrome b5
  JOURNAL   Biochemistry 50 (24), 5544-5554 (2011)
   PUBMED   21574570
  REMARK    GeneRIF: comparison of X-ray crystal structures of human and rat
            CYB5B reveals a striking difference in packing involving the
            five-strand beta-sheet, which can be attributed to fully buried
            residue 21 in strand beta4
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Wahl,B., Reichmann,D., Niks,D., Krompholz,N., Havemeyer,A.,
            Clement,B., Messerschmidt,T., Rothkegel,M., Biester,H., Hille,R.,
            Mendel,R.R. and Bittner,F.
  TITLE     Biochemical and spectroscopic characterization of the human
            mitochondrial amidoxime reducing components hmARC-1 and hmARC-2
            suggests the existence of a new molybdenum enzyme family in
            eukaryotes
  JOURNAL   J Biol Chem 285 (48), 37847-37859 (2010)
   PUBMED   20861021
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 146)
  AUTHORS   Cheng,Q., Benson,D.R., Rivera,M. and Kuczera,K.
  TITLE     Influence of point mutations on the flexibility of cytochrome b5:
            molecular dynamics simulations of holoproteins
  JOURNAL   Biopolymers 83 (3), 297-312 (2006)
   PUBMED   16807901
  REMARK    GeneRIF: simulations provided qualitative microscopic explanations
            of many of the differences in physical properties between outer
            mitochondrial membrane CYB5 isoform and microsomal CYB5 and two
            mutants in terms of localized changes in structure and flexibility
REFERENCE   6  (residues 1 to 146)
  AUTHORS   Wirtz,M., Oganesyan,V., Zhang,X., Studer,J. and Rivera,M.
  TITLE     Modulation of redox potential in electron transfer proteins:
            effects of complex formation on the active site microenvironment of
            cytochrome b5
  JOURNAL   Faraday Discuss (116), 221-34 (2000)
   PUBMED   11197480
REFERENCE   7  (residues 1 to 146)
  AUTHORS   Rivera,M., Seetharaman,R., Girdhar,D., Wirtz,M., Zhang,X., Wang,X.
            and White,S.
  TITLE     The reduction potential of cytochrome b5 is modulated by its
            exposed heme edge
  JOURNAL   Biochemistry 37 (6), 1485-1494 (1998)
   PUBMED   9484218
REFERENCE   8  (residues 1 to 146)
  AUTHORS   Rodriguez-Maranon,M.J., Qiu,F., Stark,R.E., White,S.P., Zhang,X.,
            Foundling,S.I., Rodriguez,V., Schilling,C.L. 3rd, Bunce,R.A. and
            Rivera,M.
  TITLE     13C NMR spectroscopic and X-ray crystallographic study of the role
            played by mitochondrial cytochrome b5 heme propionates in the
            electrostatic binding to cytochrome c
  JOURNAL   Biochemistry 35 (50), 16378-16390 (1996)
   PUBMED   8973214
REFERENCE   9  (residues 1 to 146)
  AUTHORS   De Silvestris,M., D'Arrigo,A. and Borgese,N.
  TITLE     The targeting information of the mitochondrial outer membrane
            isoform of cytochrome b5 is contained within the carboxyl-terminal
            region
  JOURNAL   FEBS Lett 370 (1-2), 69-74 (1995)
   PUBMED   7649306
REFERENCE   10 (residues 1 to 146)
  AUTHORS   Lederer,F., Ghrir,R., Guiard,B., Cortial,S. and Ito,A.
  TITLE     Two homologous cytochromes b5 in a single cell
  JOURNAL   Eur J Biochem 132 (1), 95-102 (1983)
   PUBMED   6840088
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC072535.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072535.1, EV775749.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..146
                     /product="cytochrome b5 type B precursor"
                     /note="cytochrome b5 type B (outer mitochondrial
                     membrane)"
                     /calculated_mol_wt=16134
     mat_peptide     12..146
                     /product="Cytochrome b5 type B. /id=PRO_0000006478"
                     /note="propagated from UniProtKB/Swiss-Prot (P04166.2)"
                     /calculated_mol_wt=15220
     Region          24..96
                     /region_name="Cyt-b5"
                     /note="Cytochrome b5-like Heme/Steroid binding domain;
                     pfam00173"
                     /db_xref="CDD:459698"
     Site            30
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O43169; propagated from
                     UniProtKB/Swiss-Prot (P04166.2)"
     Site            80
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CQX2; propagated from
                     UniProtKB/Swiss-Prot (P04166.2)"
     Region          <119..139
                     /region_name="MIP"
                     /note="Major intrinsic protein (MIP) superfamily. Members
                     of the MIP superfamily function as membrane channels that
                     selectively transport water, small neutral molecules, and
                     ions out of and between cells. The channel proteins share
                     a common fold: the N-terminal...; cl00200"
                     /db_xref="CDD:444743"
     Site            119..136
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04166.2)"
     CDS             1..146
                     /gene="Cyb5b"
                     /gene_synonym="Cyb5m; omb5"
                     /coded_by="NM_030586.2:7..447"
                     /db_xref="GeneID:80773"
                     /db_xref="RGD:621551"
ORIGIN      
        1 matpeasgsg rngqgsdpav tyyrleevak rntaeetwmv ihgrvyditr flsehpggee
       61 vlleqagada tesfedvghs pdaremlkqy yigdvhpndl kpkdgdkdps knnscqsswa
      121 ywivpivgai ligflyrhfw adskss
//
