CYB5_MUSDO
ID CYB5_MUSDO Reviewed; 134 AA.
AC P49096;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Cytochrome b5;
DE Short=CYTB5;
GN Name=Cyt-b5;
OS Musca domestica (House fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Musca.
OX NCBI_TaxID=7370;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Rutgers;
RA Guzov V., Feyereisen R.;
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cytochrome b5 is a membrane bound hemoprotein which function
CC as an electron 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; L38464; AAA56985.1; -; mRNA.
DR RefSeq; NP_001274474.1; NM_001287545.1.
DR PDB; 2IBJ; X-ray; 1.55 A; A=1-88.
DR PDBsum; 2IBJ; -.
DR AlphaFoldDB; P49096; -.
DR SMR; P49096; -.
DR STRING; 7370.XP_005176042.1; -.
DR GeneID; 101896437; -.
DR KEGG; mde:101896437; -.
DR VEuPathDB; VectorBase:MDOA006030; -.
DR eggNOG; KOG0537; Eukaryota.
DR EvolutionaryTrace; P49096; -.
DR Proteomes; UP000095301; Unplaced.
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 3D-structure; Electron transport; Endoplasmic reticulum; Heme; Iron;
KW Membrane; Metal-binding; Microsome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..134
FT /note="Cytochrome b5"
FT /id="PRO_0000166017"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 6..82
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 41
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 65
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 HELIX 11..15
FT /evidence="ECO:0007829|PDB:2IBJ"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:2IBJ"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:2IBJ"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:2IBJ"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:2IBJ"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:2IBJ"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:2IBJ"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:2IBJ"
FT HELIX 57..63
FT /evidence="ECO:0007829|PDB:2IBJ"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:2IBJ"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:2IBJ"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:2IBJ"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2IBJ"
SQ SEQUENCE 134 AA; 15401 MW; 11A1A23E235EC3AA CRC64;
MSSEDVKYFT RAEVAKNNTK DKNWFIIHNN VYDVTAFLNE HPGGEEVLIE QAGKDATEHF
EDVGHSSDAR EMMKQYKVGE LVAEERSNVP EKSEPTWNTE QKTEESSMKS WLMPFVLGLV
ATLIYKFFFG TKSQ
