ID   CYB5_MORAP              Reviewed;         130 AA.
AC   Q9Y706;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Cytochrome b5;
OS   Mortierella alpina (Oleaginous fungus) (Mortierella renispora).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC   Mortierellomycetes; Mortierellales; Mortierellaceae; Mortierella.
OX   NCBI_TaxID=64518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE, AND
RP   CHARACTERIZATION.
RC   STRAIN=1S-4;
RX   PubMed=10348912; DOI=10.1093/oxfordjournals.jbchem.a022391;
RA   Kobayashi M., Sakuradani E., Shimizu S.;
RT   "Genetic analysis of cytochrome b5 from arachidonic acid-producing fungus,
RT   Mortierella alpina 1S-4: cloning, RNA editing and expression of the gene in
RT   Escherichia coli, and purification and characterization of the gene
RT   product.";
RL   J. Biochem. 125:1094-1103(1999).
CC   -!- FUNCTION: Membrane bound hemoprotein which function as an electron
CC       carrier for several membrane bound oxygenases.
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; AB022444; BAA82441.1; -; Genomic_DNA.
DR   EMBL; AB022443; BAA82440.1; -; mRNA.
DR   AlphaFoldDB; Q9Y706; -.
DR   SMR; Q9Y706; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   Direct protein sequencing; Electron transport; Endoplasmic reticulum; Heme;
KW   Iron; Membrane; Metal-binding; Microsome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..130
FT                   /note="Cytochrome b5"
FT                   /id="PRO_0000166029"
FT   TRANSMEM        107..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          4..80
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT   REGION          80..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39
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         63
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"
SQ   SEQUENCE   130 AA;  13967 MW;  5A8DA82987C1FB16 CRC64;
     MAELKSFTLA DLSQHTTKDS LYLAIHGKVY DCTGFIDEHP GGEEVLIDEA GRDATESFED
     VGHSDEARDI MSKLLVGEFK TDSSEKPKAK SPSSSTPRPI PAAEPSDSGS LQYVLALAVV
     AGCVIWKVLL