CYB5E_ARATH
ID CYB5E_ARATH Reviewed; 134 AA.
AC Q42342; Q9SB05;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Cytochrome b5 isoform E {ECO:0000303|PubMed:19054355};
DE Short=AtCb5-E {ECO:0000303|PubMed:19054355};
DE AltName: Full=Cytochrome b5 isoform 1;
DE AltName: Full=Cytochrome b5 isoform A {ECO:0000303|PubMed:22384013};
DE Short=AtCb5-A {ECO:0000303|PubMed:22384013};
GN Name=CYTB5-E;
GN Synonyms=B5-A, CB5-A {ECO:0000303|PubMed:22384013},
GN CB5-E {ECO:0000303|PubMed:19054355}; OrderedLocusNames=At5g53560;
GN ORFNames=MNC6.10;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9880378; DOI=10.1104/pp.119.1.353;
RA Fukuchi-Mizutani M., Mizutani M., Tanaka Y., Kusumi T., Ohta D.;
RT "Microsomal electron transfer in higher plants: cloning and heterologous
RT expression of NADH-cytochrome b5 reductase from Arabidopsis.";
RL Plant Physiol. 119:353-361(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-113.
RC STRAIN=cv. Columbia;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=15060130; DOI=10.1074/mcp.m400001-mcp200;
RA Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
RA Garin J., Barbier-Brygoo H., Ephritikhine G.;
RT "Identification of new intrinsic proteins in Arabidopsis plasma membrane
RT proteome.";
RL Mol. Cell. Proteomics 3:675-691(2004).
RN [8]
RP INTERACTION WITH BI-1; FAH1 AND FAH2, AND NOMENCLATURE.
RX PubMed=19054355; DOI=10.1111/j.1365-313x.2008.03765.x;
RA Nagano M., Ihara-Ohori Y., Imai H., Inada N., Fujimoto M., Tsutsumi N.,
RA Uchimiya H., Kawai-Yamada M.;
RT "Functional association of cell death suppressor, Arabidopsis Bax
RT inhibitor-1, with fatty acid 2-hydroxylation through cytochrome b(5).";
RL Plant J. 58:122-134(2009).
RN [9]
RP INTERACTION WITH AKR2A.
RC STRAIN=cv. C24, and cv. Columbia;
RX PubMed=20215589; DOI=10.1105/tpc.109.065979;
RA Shen G., Kuppu S., Venkataramani S., Wang J., Yan J., Qiu X., Zhang H.;
RT "ANKYRIN REPEAT-CONTAINING PROTEIN 2A is an essential molecular chaperone
RT for peroxisomal membrane-bound ASCORBATE PEROXIDASE3 in Arabidopsis.";
RL Plant Cell 22:811-831(2010).
RN [10]
RP AKR2A-BINDING SEQUENCE, AND REVIEW.
RX PubMed=21057222; DOI=10.4161/psb.5.11.13714;
RA Zhang H., Li X., Zhang Y., Kuppu S., Shen G.;
RT "Is AKR2A an essential molecular chaperone for a class of membrane-bound
RT proteins in plants?";
RL Plant Signal. Behav. 5:1520-1522(2010).
RN [11]
RP INTERACTION WITH CER1, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=22773744; DOI=10.1105/tpc.112.099796;
RA Bernard A., Domergue F., Pascal S., Jetter R., Renne C., Faure J.D.,
RA Haslam R.P., Napier J.A., Lessire R., Joubes J.;
RT "Reconstitution of plant alkane biosynthesis in yeast demonstrates that
RT Arabidopsis ECERIFERUM1 and ECERIFERUM3 are core components of a very-long-
RT chain alkane synthesis complex.";
RL Plant Cell 24:3106-3118(2012).
RN [12]
RP FUNCTION, AND NOMENCLATURE.
RX PubMed=22384013; DOI=10.1371/journal.pone.0031370;
RA Kumar R., Tran L.S., Neelakandan A.K., Nguyen H.T.;
RT "Higher plant cytochrome b5 polypeptides modulate fatty acid
RT desaturation.";
RL PLoS ONE 7:E31370-E31370(2012).
CC -!- FUNCTION: Membrane bound hemoprotein which function as an electron
CC carrier for several membrane bound oxygenases, including fatty acid
CC desaturases. {ECO:0000269|PubMed:22384013, ECO:0000269|PubMed:9880378}.
CC -!- SUBUNIT: Interacts with CER1, BI-1, FAH1 and FAH2. Interacts with AKR2A
CC (PubMed:20215589). {ECO:0000269|PubMed:19054355,
CC ECO:0000269|PubMed:20215589, ECO:0000269|PubMed:22773744}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060130}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:22773744}; Single-
CC pass membrane protein {ECO:0000269|PubMed:22773744}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC siliques. {ECO:0000269|PubMed:9880378}.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. {ECO:0000305}.
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DR EMBL; AB007801; BAA74839.1; -; mRNA.
DR EMBL; AB015476; BAB09732.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96377.1; -; Genomic_DNA.
DR EMBL; AY080878; AAL87348.1; -; mRNA.
DR EMBL; AY114045; AAM45093.1; -; mRNA.
DR EMBL; AY087070; AAM64631.1; -; mRNA.
DR EMBL; F20001; CAA23377.1; -; mRNA.
DR PIR; T52469; T52469.
DR RefSeq; NP_200168.1; NM_124736.4.
DR AlphaFoldDB; Q42342; -.
DR SMR; Q42342; -.
DR BioGRID; 20682; 13.
DR IntAct; Q42342; 9.
DR STRING; 3702.AT5G53560.1; -.
DR SwissPalm; Q42342; -.
DR PaxDb; Q42342; -.
DR PRIDE; Q42342; -.
DR ProteomicsDB; 220435; -.
DR EnsemblPlants; AT5G53560.1; AT5G53560.1; AT5G53560.
DR GeneID; 835438; -.
DR Gramene; AT5G53560.1; AT5G53560.1; AT5G53560.
DR KEGG; ath:AT5G53560; -.
DR Araport; AT5G53560; -.
DR TAIR; locus:2168666; AT5G53560.
DR eggNOG; KOG0537; Eukaryota.
DR HOGENOM; CLU_102602_3_0_1; -.
DR InParanoid; Q42342; -.
DR OMA; YIGEIDM; -.
DR OrthoDB; 1566561at2759; -.
DR PhylomeDB; Q42342; -.
DR PRO; PR:Q42342; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q42342; baseline and differential.
DR Genevisible; Q42342; AT.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; NAS:TAIR.
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; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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 Cell membrane; Electron transport; Endoplasmic reticulum; Heme; Iron;
KW Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..134
FT /note="Cytochrome b5 isoform E"
FT /id="PRO_0000166020"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 5..81
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT MOTIF 128..134
FT /note="AKR2A-binding sequence (ABS) required for
FT endoplasmic reticulum membrane targeting"
FT /evidence="ECO:0000269|PubMed:21057222"
FT BINDING 40
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 64
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 CONFLICT 1..3
FT /note="MSS -> ARA (in Ref. 6; CAA23377)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 134 AA; 15084 MW; 9CC01C60F7C873FD CRC64;
MSSDRKVLSF EEVSKHNKTK DCWLIISGKV YDVTPFMDDH PGGDEVLLSS TGKDATNDFE
DVGHSDTARD MMDKYFIGEI DSSSVPATRT YVAPQQPAYN QDKTPEFIIK ILQFLVPILI
LGLALVVRHY TKKD
