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Cytochrome b5 isoform E (AtCb5-E) (Cytochrome b5 isoform 1) (Cytochrome b5 isoform A) (AtCb5-A)

 CYB5E_ARATH             Reviewed;         134 AA.
Q42342; Q9SB05;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
11-JAN-2001, sequence version 2.
23-MAY-2018, entry version 143.
RecName: Full=Cytochrome b5 isoform E {ECO:0000303|PubMed:19054355};
Short=AtCb5-E {ECO:0000303|PubMed:19054355};
AltName: Full=Cytochrome b5 isoform 1;
AltName: Full=Cytochrome b5 isoform A {ECO:0000303|PubMed:22384013};
Short=AtCb5-A {ECO:0000303|PubMed:22384013};
Name=CYTB5-E;
Synonyms=B5-A, CB5-A {ECO:0000303|PubMed:22384013},
CB5-E {ECO:0000303|PubMed:19054355}; OrderedLocusNames=At5g53560;
ORFNames=MNC6.10;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=9880378; DOI=10.1104/pp.119.1.353;
Fukuchi-Mizutani M., Mizutani M., Tanaka Y., Kusumi T., Ohta D.;
"Microsomal electron transfer in higher plants: cloning and
heterologous expression of NADH-cytochrome b5 reductase from
Arabidopsis.";
Plant Physiol. 119:353-361(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9872454; DOI=10.1093/dnares/5.5.297;
Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. VII.
Sequence features of the regions of 1,013,767 bp covered by sixteen
physically assigned P1 and TAC clones.";
DNA Res. 5:297-308(1998).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-113.
STRAIN=cv. Columbia;
PubMed=8580968; DOI=10.1046/j.1365-313X.1996.09010101.x;
Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y.,
Marbach J., Fleck J., Clement B., Philipps G., Herve C., Bardet C.,
Tremousaygue D., Lescure B., Lacomme C., Roby D., Jourjon M.-F.,
Chabrier P., Charpenteau J.-L., Desprez T., Amselem J., Chiapello H.,
Hoefte H.;
"Further progress towards a catalogue of all Arabidopsis genes:
analysis of a set of 5000 non-redundant ESTs.";
Plant J. 9:101-124(1996).
[7]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=15060130; DOI=10.1074/mcp.M400001-MCP200;
Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
Garin J., Barbier-Brygoo H., Ephritikhine G.;
"Identification of new intrinsic proteins in Arabidopsis plasma
membrane proteome.";
Mol. Cell. Proteomics 3:675-691(2004).
[8]
INTERACTION WITH BI-1; FAH1 AND FAH2, AND NOMENCLATURE.
PubMed=19054355; DOI=10.1111/j.1365-313X.2008.03765.x;
Nagano M., Ihara-Ohori Y., Imai H., Inada N., Fujimoto M.,
Tsutsumi N., Uchimiya H., Kawai-Yamada M.;
"Functional association of cell death suppressor, Arabidopsis Bax
inhibitor-1, with fatty acid 2-hydroxylation through cytochrome
b(5).";
Plant J. 58:122-134(2009).
[9]
INTERACTION WITH AKR2A.
STRAIN=cv. C24, and cv. Columbia;
PubMed=20215589; DOI=10.1105/tpc.109.065979;
Shen G., Kuppu S., Venkataramani S., Wang J., Yan J., Qiu X.,
Zhang H.;
"ANKYRIN REPEAT-CONTAINING PROTEIN 2A is an essential molecular
chaperone for peroxisomal membrane-bound ASCORBATE PEROXIDASE3 in
Arabidopsis.";
Plant Cell 22:811-831(2010).
[10]
AKR2A-BINDING SEQUENCE, AND REVIEW.
PubMed=21057222; DOI=10.4161/psb.5.11.13714;
Zhang H., Li X., Zhang Y., Kuppu S., Shen G.;
"Is AKR2A an essential molecular chaperone for a class of membrane-
bound proteins in plants?";
Plant Signal. Behav. 5:1520-1522(2010).
[11]
INTERACTION WITH CER1, AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
PubMed=22773744; DOI=10.1105/tpc.112.099796;
Bernard A., Domergue F., Pascal S., Jetter R., Renne C., Faure J.D.,
Haslam R.P., Napier J.A., Lessire R., Joubes J.;
"Reconstitution of plant alkane biosynthesis in yeast demonstrates
that Arabidopsis ECERIFERUM1 and ECERIFERUM3 are core components of a
very-long-chain alkane synthesis complex.";
Plant Cell 24:3106-3118(2012).
[12]
FUNCTION, AND NOMENCLATURE.
PubMed=22384013; DOI=10.1371/journal.pone.0031370;
Kumar R., Tran L.S., Neelakandan A.K., Nguyen H.T.;
"Higher plant cytochrome b5 polypeptides modulate fatty acid
desaturation.";
PLoS ONE 7:E31370-E31370(2012).
-!- FUNCTION: Membrane bound hemoprotein which function as an electron
carrier for several membrane bound oxygenases, including fatty
acid desaturases. {ECO:0000269|PubMed:22384013,
ECO:0000269|PubMed:9880378}.
-!- SUBUNIT: Interacts with CER1, BI-1, FAH1 and FAH2. Interacts with
AKR2A (PubMed:20215589). {ECO:0000269|PubMed:19054355,
ECO:0000269|PubMed:20215589, ECO:0000269|PubMed:22773744}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060130}.
Endoplasmic reticulum membrane {ECO:0000269|PubMed:22773744};
Single-pass membrane protein {ECO:0000269|PubMed:22773744}.
-!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
siliques. {ECO:0000269|PubMed:9880378}.
-!- SIMILARITY: Belongs to the cytochrome b5 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB007801; BAA74839.1; -; mRNA.
EMBL; AB015476; BAB09732.1; -; Genomic_DNA.
EMBL; CP002688; AED96377.1; -; Genomic_DNA.
EMBL; AY080878; AAL87348.1; -; mRNA.
EMBL; AY114045; AAM45093.1; -; mRNA.
EMBL; AY087070; AAM64631.1; -; mRNA.
EMBL; F20001; CAA23377.1; -; mRNA.
PIR; T52469; T52469.
RefSeq; NP_200168.1; NM_124736.4.
UniGene; At.20842; -.
ProteinModelPortal; Q42342; -.
SMR; Q42342; -.
BioGrid; 20682; 12.
IntAct; Q42342; 9.
STRING; 3702.AT5G53560.1; -.
SwissPalm; Q42342; -.
PaxDb; Q42342; -.
PRIDE; Q42342; -.
EnsemblPlants; AT5G53560.1; AT5G53560.1; AT5G53560.
GeneID; 835438; -.
Gramene; AT5G53560.1; AT5G53560.1; AT5G53560.
KEGG; ath:AT5G53560; -.
Araport; AT5G53560; -.
TAIR; locus:2168666; AT5G53560.
eggNOG; KOG0537; Eukaryota.
eggNOG; COG5274; LUCA.
HOGENOM; HOG000039853; -.
InParanoid; Q42342; -.
OMA; YHIGQID; -.
OrthoDB; EOG09360S13; -.
PhylomeDB; Q42342; -.
Reactome; R-ATH-196836; Vitamin C (ascorbate) metabolism.
Reactome; R-ATH-211945; Phase I - Functionalization of compounds.
PRO; PR:Q42342; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q42342; baseline and differential.
Genevisible; Q42342; AT.
GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
GO; GO:0005789; C:endoplasmic reticulum membrane; NAS:TAIR.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
Gene3D; 3.10.120.10; -; 1.
InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
InterPro; IPR018506; Cyt_B5_heme-BS.
Pfam; PF00173; Cyt-b5; 1.
PRINTS; PR00363; CYTOCHROMEB5.
SMART; SM01117; Cyt-b5; 1.
SUPFAM; SSF55856; SSF55856; 1.
PROSITE; PS00191; CYTOCHROME_B5_1; 1.
PROSITE; PS50255; CYTOCHROME_B5_2; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Electron transport;
Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 134 Cytochrome b5 isoform E.
/FTId=PRO_0000166020.
TRANSMEM 107 127 Helical. {ECO:0000255}.
DOMAIN 5 81 Cytochrome b5 heme-binding.
{ECO:0000255|PROSITE-ProRule:PRU00279}.
MOTIF 128 134 AKR2A-binding sequence (ABS) required for
endoplasmic reticulum membrane targeting.
{ECO:0000269|PubMed:21057222}.
METAL 40 40 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00279}.
METAL 64 64 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00279}.
CONFLICT 1 3 MSS -> ARA (in Ref. 6; CAA23377).
{ECO:0000305}.
SEQUENCE 134 AA; 15084 MW; 9CC01C60F7C873FD CRC64;
MSSDRKVLSF EEVSKHNKTK DCWLIISGKV YDVTPFMDDH PGGDEVLLSS TGKDATNDFE
DVGHSDTARD MMDKYFIGEI DSSSVPATRT YVAPQQPAYN QDKTPEFIIK ILQFLVPILI
LGLALVVRHY TKKD


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