CYB5_PIG
ID CYB5_PIG Reviewed; 134 AA.
AC P00172; O18813;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Cytochrome b5;
GN Name=CYB5A; Synonyms=CYB5;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Blood, and Liver;
RX PubMed=9367886; DOI=10.1006/bbrc.1997.7599;
RA Vandermark P.K., Steggles A.W.;
RT "The isolation and characterization of the soluble and membrane-bound
RT porcine cytochrome b5 cDNAs.";
RL Biochem. Biophys. Res. Commun. 240:80-83(1997).
RN [2]
RP PROTEIN SEQUENCE OF 2-134.
RC TISSUE=Erythrocyte, and Liver;
RX PubMed=4030743; DOI=10.1093/oxfordjournals.jbchem.a135224;
RA Abe K., Kimura S., Kizawa R., Anan F.K., Sugita Y.;
RT "Amino acid sequences of cytochrome b5 from human, porcine, and bovine
RT erythrocytes and comparison with liver microsomal cytochrome b5.";
RL J. Biochem. 97:1659-1668(1985).
RN [3]
RP PROTEIN SEQUENCE OF 2-7.
RX PubMed=4810060; DOI=10.1021/bi00700a005;
RA Ozols J.;
RT "Cytochrome b5 from microsomal membranes of equine, bovine, and porcine
RT livers. Isolation and properties of preparations containing the membranous
RT segment.";
RL Biochemistry 13:426-434(1974).
RN [4]
RP PROTEIN SEQUENCE OF 8-89.
RX PubMed=4993957; DOI=10.1016/s0021-9258(18)62368-3;
RA Nobrega F.G., Ozols J.;
RT "Amino acid sequences of tryptic peptides of cytochromes b5 from microsomes
RT of human, monkey, porcine, and chicken liver.";
RL J. Biol. Chem. 246:1706-1717(1971).
RN [5]
RP PROTEIN SEQUENCE OF 90-134, AND SEQUENCE REVISION TO 14; 15 AND 61.
RX PubMed=269425; DOI=10.1073/pnas.74.9.3725;
RA Ozols J., Gerard C.;
RT "Primary structure of the membranous segment of cytochrome b5.";
RL Proc. Natl. Acad. Sci. U.S.A. 74:3725-3729(1977).
RN [6]
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).
CC -!- FUNCTION: Cytochrome b5 is a membrane-bound hemoprotein functioning as
CC an electron carrier for several membrane-bound oxygenases.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane;
CC Single-pass membrane protein; Cytoplasmic side. Microsome membrane;
CC Single-pass membrane protein; Cytoplasmic side.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Liver, Membrane-bound;
CC IsoId=P00172-1; Sequence=Displayed;
CC Name=2; Synonyms=Erythrocyte, Cytoplasmic;
CC IsoId=P00172-2; Sequence=VSP_001242, VSP_001243;
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. {ECO:0000305}.
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DR EMBL; AF016388; AAC48779.1; -; mRNA.
DR EMBL; AF016389; AAC48780.1; -; mRNA.
DR PIR; JC5782; CBPG5.
DR PIR; JC5783; JC5783.
DR RefSeq; NP_001001770.1; NM_001001770.1. [P00172-1]
DR PDB; 3X32; X-ray; 0.83 A; A=1-94.
DR PDB; 3X33; X-ray; 0.93 A; A=1-94.
DR PDB; 3X34; X-ray; 0.76 A; A=1-94.
DR PDB; 3X35; X-ray; 0.95 A; A=1-94.
DR PDBsum; 3X32; -.
DR PDBsum; 3X33; -.
DR PDBsum; 3X34; -.
DR PDBsum; 3X35; -.
DR AlphaFoldDB; P00172; -.
DR BMRB; P00172; -.
DR SMR; P00172; -.
DR STRING; 9823.ENSSSCP00000005246; -.
DR PaxDb; P00172; -.
DR PeptideAtlas; P00172; -.
DR PRIDE; P00172; -.
DR Ensembl; ENSSSCT00000005381; ENSSSCP00000005246; ENSSSCG00000004875. [P00172-2]
DR Ensembl; ENSSSCT00000051381; ENSSSCP00000032988; ENSSSCG00000004875. [P00172-2]
DR Ensembl; ENSSSCT00000069977; ENSSSCP00000064236; ENSSSCG00000004875. [P00172-1]
DR Ensembl; ENSSSCT00005043160; ENSSSCP00005026456; ENSSSCG00005027050. [P00172-1]
DR Ensembl; ENSSSCT00005043213; ENSSSCP00005026490; ENSSSCG00005027050. [P00172-2]
DR Ensembl; ENSSSCT00005043255; ENSSSCP00005026518; ENSSSCG00005027050. [P00172-2]
DR Ensembl; ENSSSCT00015071088; ENSSSCP00015028491; ENSSSCG00015053340. [P00172-2]
DR Ensembl; ENSSSCT00015071479; ENSSSCP00015028646; ENSSSCG00015053340. [P00172-2]
DR Ensembl; ENSSSCT00015071689; ENSSSCP00015028726; ENSSSCG00015053340. [P00172-1]
DR Ensembl; ENSSSCT00025039117; ENSSSCP00025016554; ENSSSCG00025028776. [P00172-2]
DR Ensembl; ENSSSCT00025039266; ENSSSCP00025016617; ENSSSCG00025028776. [P00172-2]
DR Ensembl; ENSSSCT00025039386; ENSSSCP00025016673; ENSSSCG00025028776. [P00172-1]
DR Ensembl; ENSSSCT00030099570; ENSSSCP00030045855; ENSSSCG00030071172. [P00172-2]
DR Ensembl; ENSSSCT00030099618; ENSSSCP00030045889; ENSSSCG00030071172. [P00172-2]
DR Ensembl; ENSSSCT00030099647; ENSSSCP00030045907; ENSSSCG00030071172. [P00172-1]
DR Ensembl; ENSSSCT00035034696; ENSSSCP00035013749; ENSSSCG00035026302. [P00172-2]
DR Ensembl; ENSSSCT00035034718; ENSSSCP00035013756; ENSSSCG00035026302. [P00172-2]
DR Ensembl; ENSSSCT00035034725; ENSSSCP00035013759; ENSSSCG00035026302. [P00172-1]
DR Ensembl; ENSSSCT00040089118; ENSSSCP00040039170; ENSSSCG00040065260. [P00172-2]
DR Ensembl; ENSSSCT00040089271; ENSSSCP00040039243; ENSSSCG00040065260. [P00172-2]
DR Ensembl; ENSSSCT00040089418; ENSSSCP00040039311; ENSSSCG00040065260. [P00172-1]
DR Ensembl; ENSSSCT00045065718; ENSSSCP00045046521; ENSSSCG00045038001. [P00172-2]
DR Ensembl; ENSSSCT00045065748; ENSSSCP00045046545; ENSSSCG00045038001. [P00172-2]
DR Ensembl; ENSSSCT00045065776; ENSSSCP00045046571; ENSSSCG00045038001. [P00172-1]
DR Ensembl; ENSSSCT00050021872; ENSSSCP00050009185; ENSSSCG00050016076. [P00172-2]
DR Ensembl; ENSSSCT00050021904; ENSSSCP00050009201; ENSSSCG00050016076. [P00172-2]
DR Ensembl; ENSSSCT00050021932; ENSSSCP00050009217; ENSSSCG00050016076. [P00172-1]
DR Ensembl; ENSSSCT00055032691; ENSSSCP00055026041; ENSSSCG00055016520. [P00172-2]
DR Ensembl; ENSSSCT00055032834; ENSSSCP00055026154; ENSSSCG00055016520. [P00172-2]
DR Ensembl; ENSSSCT00055032886; ENSSSCP00055026197; ENSSSCG00055016520. [P00172-1]
DR Ensembl; ENSSSCT00060084000; ENSSSCP00060036408; ENSSSCG00060061551. [P00172-2]
DR Ensembl; ENSSSCT00060084064; ENSSSCP00060036428; ENSSSCG00060061551. [P00172-1]
DR Ensembl; ENSSSCT00060084160; ENSSSCP00060036459; ENSSSCG00060061551. [P00172-2]
DR Ensembl; ENSSSCT00065054245; ENSSSCP00065023564; ENSSSCG00065039699. [P00172-2]
DR Ensembl; ENSSSCT00065054262; ENSSSCP00065023571; ENSSSCG00065039699. [P00172-2]
DR Ensembl; ENSSSCT00065054273; ENSSSCP00065023579; ENSSSCG00065039699. [P00172-1]
DR Ensembl; ENSSSCT00070026151; ENSSSCP00070021708; ENSSSCG00070013386. [P00172-1]
DR Ensembl; ENSSSCT00070026160; ENSSSCP00070021714; ENSSSCG00070013386. [P00172-1]
DR Ensembl; ENSSSCT00070026170; ENSSSCP00070021722; ENSSSCG00070013386. [P00172-2]
DR Ensembl; ENSSSCT00070026186; ENSSSCP00070021735; ENSSSCG00070013386. [P00172-2]
DR GeneID; 414799; -.
DR KEGG; ssc:414799; -.
DR CTD; 1528; -.
DR eggNOG; KOG0537; Eukaryota.
DR GeneTree; ENSGT00940000156770; -.
DR HOGENOM; CLU_102602_3_3_1; -.
DR InParanoid; P00172; -.
DR OMA; RHKIAKP; -.
DR OrthoDB; 1566561at2759; -.
DR TreeFam; TF314537; -.
DR Reactome; R-SSC-196836; Vitamin C (ascorbate) metabolism.
DR Reactome; R-SSC-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR Proteomes; UP000008227; Chromosome 1.
DR Proteomes; UP000314985; Chromosome 1.
DR Bgee; ENSSSCG00000004875; Expressed in adult mammalian kidney and 47 other tissues.
DR ExpressionAtlas; P00172; baseline and differential.
DR Genevisible; P00172; SS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
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; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Electron transport; Endoplasmic reticulum; Heme;
KW Iron; Membrane; Metal-binding; Microsome; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00171,
FT ECO:0000269|PubMed:2752049, ECO:0000269|PubMed:4030743,
FT ECO:0000269|PubMed:4810060"
FT CHAIN 2..134
FT /note="Cytochrome b5"
FT /id="PRO_0000166012"
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:0000250|UniProtKB:P00171"
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 98
FT /note="T -> S (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9367886"
FT /id="VSP_001242"
FT VAR_SEQ 99..134
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9367886"
FT /id="VSP_001243"
FT CONFLICT 62
FT /note="N -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:3X34"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:3X34"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:3X34"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:3X34"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:3X34"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:3X34"
FT HELIX 60..66
FT /evidence="ECO:0007829|PDB:3X34"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:3X34"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:3X34"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:3X34"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:3X34"
SQ SEQUENCE 134 AA; 15310 MW; 016FE14A32CAC52A CRC64;
MAEQSDKAVK YYTLEEIQKH NNSKSTWLIL HHKVYDLTKF LEEHPGGEEV LREQAGGDAT
ENFEDVGHST DARELSKTFI IGELHPDDRS KIAKPSETLI TTVESNSSWW TNWVIPAISA
LVVSLMYHFY TSEN
