CYB5D_ARATH
ID CYB5D_ARATH Reviewed; 140 AA.
AC Q9ZWT2;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cytochrome B5 isoform D {ECO:0000303|PubMed:19054355};
DE Short=AtCb5-D {ECO:0000303|PubMed:19054355};
DE AltName: Full=Cytochrome b5 isoform B {ECO:0000303|PubMed:22384013};
DE Short=AtCb5-B {ECO:0000303|PubMed:22384013};
GN Name=CYTB5-D {ECO:0000305};
GN Synonyms=B5-B, CB5-B {ECO:0000303|PubMed:22384013},
GN CB5-D {ECO:0000303|PubMed:19054355}; OrderedLocusNames=At5g48810;
GN ORFNames=K24G6.14;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(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 SUBCELLULAR LOCATION.
RX PubMed=17322552; DOI=10.1093/jxb/erl303;
RA Maggio C., Barbante A., Ferro F., Frigerio L., Pedrazzini E.;
RT "Intracellular sorting of the tail-anchored protein cytochrome b5 in
RT plants: a comparative study using different isoforms from rabbit and
RT Arabidopsis.";
RL J. Exp. Bot. 58:1365-1379(2007).
RN [7]
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 [8]
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 [9]
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.
CC {ECO:0000269|PubMed:19054355, ECO:0000269|PubMed:22773744}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17322552, ECO:0000269|PubMed:22773744}; Single-pass
CC membrane protein {ECO:0000269|PubMed:17322552,
CC 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; AB007802; BAA74840.1; -; mRNA.
DR EMBL; AB012242; BAB09434.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95727.1; -; Genomic_DNA.
DR EMBL; AF370256; AAK44071.1; -; mRNA.
DR EMBL; AY063073; AAL34247.1; -; mRNA.
DR EMBL; AY086738; AAM63789.1; -; mRNA.
DR PIR; T52468; T52468.
DR RefSeq; NP_199692.1; NM_124258.4.
DR AlphaFoldDB; Q9ZWT2; -.
DR SMR; Q9ZWT2; -.
DR BioGRID; 20185; 6.
DR IntAct; Q9ZWT2; 2.
DR STRING; 3702.AT5G48810.1; -.
DR iPTMnet; Q9ZWT2; -.
DR PaxDb; Q9ZWT2; -.
DR PRIDE; Q9ZWT2; -.
DR ProteomicsDB; 220330; -.
DR EnsemblPlants; AT5G48810.1; AT5G48810.1; AT5G48810.
DR GeneID; 834939; -.
DR Gramene; AT5G48810.1; AT5G48810.1; AT5G48810.
DR KEGG; ath:AT5G48810; -.
DR Araport; AT5G48810; -.
DR TAIR; locus:2156534; AT5G48810.
DR eggNOG; KOG0537; Eukaryota.
DR HOGENOM; CLU_102602_3_0_1; -.
DR InParanoid; Q9ZWT2; -.
DR OMA; HYERDKT; -.
DR OrthoDB; 1566561at2759; -.
DR PhylomeDB; Q9ZWT2; -.
DR PRO; PR:Q9ZWT2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9ZWT2; baseline and differential.
DR Genevisible; Q9ZWT2; AT.
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; IBA:GO_Central.
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 Electron transport; Endoplasmic reticulum; Heme; Iron; Membrane;
KW Metal-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..140
FT /note="Cytochrome B5 isoform D"
FT /id="PRO_0000419613"
FT TRANSMEM 109..129
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 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"
SQ SEQUENCE 140 AA; 15097 MW; 18C24FF8F7995E08 CRC64;
MGGDGKVFTL SEVSQHSSAK DCWIVIDGKV YDVTKFLDDH PGGDEVILTS TGKDATDDFE
DVGHSSTAKA MLDEYYVGDI DTATVPVKAK FVPPTSTKAV ATQDKSSDFV IKLLQFLVPL
LILGLAFGIR YYTKTKAPSS
