CYB5_RAT
ID CYB5_RAT Reviewed; 134 AA.
AC P00173; O35768;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Cytochrome b5;
GN Name=Cyb5a; Synonyms=Cyb5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1396600; DOI=10.1002/j.1460-2075.1992.tb05513.x;
RA Mitoma J.-Y., Ito A.;
RT "The carboxy-terminal 10 amino acid residues of cytochrome b5 are necessary
RT for its targeting to the endoplasmic reticulum.";
RL EMBO J. 11:4197-4203(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=9245704; DOI=10.1006/bbrc.1997.7023;
RA Yoo M.;
RT "Identification of two homologous cytochrome b5s in rat brain.";
RL Biochem. Biophys. Res. Commun. 236:641-642(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC TISSUE=Liver;
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 [4]
RP PROTEIN SEQUENCE OF 2-134, CLEAVAGE OF INITIATOR METHIONINE, AND
RP ACETYLATION AT ALA-2.
RX PubMed=7093287; DOI=10.1016/0167-4838(82)90143-1;
RA Ozols J., Heinemann F.S.;
RT "Chemical structure of rat liver cytochrome b5. Isolation of peptides by
RT high-pressure liquid chromatography.";
RL Biochim. Biophys. Acta 704:163-173(1982).
RN [5]
RP PROTEIN SEQUENCE OF 2-11.
RX PubMed=2752049; DOI=10.1016/0167-4838(89)90143-x;
RA Ozols J.;
RT "Structure of cytochrome b5 and its topology in the microsomal membrane.";
RL Biochim. Biophys. Acta 997:121-130(1989).
RN [6]
RP PROTEIN SEQUENCE OF 7-89.
RX PubMed=6840088; DOI=10.1111/j.1432-1033.1983.tb07330.x;
RA Lederer F., Ghrir R., Guiard B., Cortial S., Ito A.;
RT "Two homologous cytochromes b5 in a single cell.";
RL Eur. J. Biochem. 132:95-102(1983).
RN [7]
RP STRUCTURE BY NMR OF 1-99.
RX PubMed=8639599; DOI=10.1021/bi960501q;
RA Falzone C.J., Mayer M.R., Whiteman E.L., Moore C.D., Lecomte J.T.J.;
RT "Design challenges for hemoproteins: the solution structure of
RT apocytochrome b5.";
RL Biochemistry 35:6519-6526(1996).
RN [8]
RP STRUCTURE BY NMR OF 6-99.
RX PubMed=9363779; DOI=10.1111/j.1432-1033.1997.t01-1-00270.x;
RA Banci L., Bertini I., Ferroni F., Rosato A.;
RT "Solution structure of reduced microsomal rat cytochrome b5.";
RL Eur. J. Biochem. 249:270-279(1997).
RN [9]
RP STRUCTURE BY NMR OF 6-99.
RX PubMed=9425037; DOI=10.1021/bi971896w;
RA Arnesano F., Banci L., Bertini I., Felli I.C.;
RT "The solution structure of oxidized rat microsomal cytochrome b5.";
RL Biochemistry 37:173-184(1998).
RN [10]
RP STRUCTURE BY NMR OF 6-99.
RX PubMed=9622481; DOI=10.1021/bi9801964;
RA Dangi B., Sarma S., Yan C., Banville D.L., Guiles R.D.;
RT "The origin of differences in the physical properties of the equilibrium
RT forms of cytochrome b5 revealed through high-resolution NMR structures and
RT backbone dynamic analyses.";
RL Biochemistry 37:8289-8302(1998).
RN [11]
RP STRUCTURE BY NMR OF 1-99.
RX PubMed=11294656; DOI=10.1021/bi002681g;
RA Falzone C.J., Wang Y., Vu B.C., Scott N.L., Bhattacharya S.,
RA Lecomte J.T.J.;
RT "Structural and dynamic perturbations induced by heme binding in cytochrome
RT b5.";
RL Biochemistry 40:4879-4891(2001).
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-6 double bond introduction during the C-6
CC desaturation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC membrane protein; Cytoplasmic side. Microsome membrane; Single-pass
CC membrane protein; Cytoplasmic side.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P00173-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P00173-2; Sequence=VSP_001246, VSP_001247;
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. {ECO:0000305}.
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DR EMBL; D13205; BAA02492.1; -; mRNA.
DR EMBL; AF007107; AAB67609.1; -; mRNA.
DR EMBL; AF007108; AAB67610.1; -; mRNA.
DR EMBL; BC086945; AAH86945.1; -; mRNA.
DR PIR; JC5596; JC5596.
DR PIR; S28404; CBRT5.
DR RefSeq; NP_071581.1; NM_022245.1. [P00173-1]
DR PDB; 1AQA; NMR; -; A=6-99.
DR PDB; 1AW3; NMR; -; A=6-99.
DR PDB; 1AXX; NMR; -; A=6-99.
DR PDB; 1B5A; NMR; -; A=6-99.
DR PDB; 1B5B; NMR; -; A=6-99.
DR PDB; 1BFX; NMR; -; A=1-99.
DR PDB; 1BLV; NMR; -; A=6-99.
DR PDB; 1I87; NMR; -; A=2-99.
DR PDB; 1I8C; NMR; -; A=2-99.
DR PDB; 1IB7; NMR; -; A=6-99.
DR PDB; 1IET; NMR; -; A=2-99.
DR PDB; 1IEU; NMR; -; A=2-99.
DR PDB; 1JEX; NMR; -; A=6-99.
DR PDB; 1MNY; NMR; -; A=6-99.
DR PDB; 2AXX; NMR; -; A=6-99.
DR PDB; 5XE4; NMR; -; A=2-99.
DR PDB; 5XEE; NMR; -; A=2-99.
DR PDBsum; 1AQA; -.
DR PDBsum; 1AW3; -.
DR PDBsum; 1AXX; -.
DR PDBsum; 1B5A; -.
DR PDBsum; 1B5B; -.
DR PDBsum; 1BFX; -.
DR PDBsum; 1BLV; -.
DR PDBsum; 1I87; -.
DR PDBsum; 1I8C; -.
DR PDBsum; 1IB7; -.
DR PDBsum; 1IET; -.
DR PDBsum; 1IEU; -.
DR PDBsum; 1JEX; -.
DR PDBsum; 1MNY; -.
DR PDBsum; 2AXX; -.
DR PDBsum; 5XE4; -.
DR PDBsum; 5XEE; -.
DR AlphaFoldDB; P00173; -.
DR BMRB; P00173; -.
DR SMR; P00173; -.
DR IntAct; P00173; 1.
DR STRING; 10116.ENSRNOP00000020446; -.
DR iPTMnet; P00173; -.
DR PhosphoSitePlus; P00173; -.
DR jPOST; P00173; -.
DR PaxDb; P00173; -.
DR PRIDE; P00173; -.
DR GeneID; 64001; -.
DR KEGG; rno:64001; -.
DR CTD; 1528; -.
DR RGD; 620558; Cyb5a.
DR VEuPathDB; HostDB:ENSRNOG00000070068; -.
DR eggNOG; KOG0537; Eukaryota.
DR HOGENOM; CLU_102602_3_3_1; -.
DR InParanoid; P00173; -.
DR OMA; YRFYFTQ; -.
DR OrthoDB; 1566561at2759; -.
DR PhylomeDB; P00173; -.
DR TreeFam; TF314537; -.
DR Reactome; R-RNO-196836; Vitamin C (ascorbate) metabolism.
DR Reactome; R-RNO-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR EvolutionaryTrace; P00173; -.
DR PRO; PR:P00173; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000015205; Expressed in liver and 20 other tissues.
DR Genevisible; P00173; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HGNC-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0009055; F:electron transfer activity; TAS:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046686; P:response to cadmium ion; IEP:RGD.
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; Acetylation; Alternative splicing; Direct protein sequencing;
KW Electron transport; Endoplasmic reticulum; Heme; Iron; Membrane;
KW Metal-binding; Microsome; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2752049,
FT ECO:0000269|PubMed:7093287"
FT CHAIN 2..134
FT /note="Cytochrome b5"
FT /id="PRO_0000166014"
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 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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:7093287"
FT MOD_RES 7
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56395"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56395"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56395"
FT VAR_SEQ 97..100
FT /note="ETLI -> HSAL (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_001246"
FT VAR_SEQ 101..134
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_001247"
FT CONFLICT 18
FT /note="Q -> E (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:5XE4"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:5XE4"
FT HELIX 14..19
FT /evidence="ECO:0007829|PDB:1AQA"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:1AQA"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:1AQA"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:1AQA"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1AQA"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:1AQA"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:1AQA"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:1AQA"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:1B5A"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:1AQA"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:1AQA"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:1AW3"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1AQA"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:5XE4"
SQ SEQUENCE 134 AA; 15355 MW; 37568069CA88CCD2 CRC64;
MAEQSDKDVK YYTLEEIQKH KDSKSTWVIL HHKVYDLTKF LEEHPGGEEV LREQAGGDAT
ENFEDVGHST DARELSKTYI IGELHPDDRS KIAKPSETLI TTVESNSSWW TNWVIPAISA
LVVALMYRLY MAED
