CYB5B_ARATH
ID CYB5B_ARATH Reviewed; 134 AA.
AC O48845; Q0WTX9;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Cytochrome b5 isoform B {ECO:0000303|PubMed:19054355};
DE Short=AtCb5-B {ECO:0000303|PubMed:19054355};
DE AltName: Full=Cytochrome b5 isoform 2;
DE AltName: Full=Cytochrome b5 isoform E {ECO:0000303|PubMed:22384013};
DE Short=AtCb5-E {ECO:0000303|PubMed:22384013};
GN Name=CYTB5-B {ECO:0000305};
GN Synonyms=CB5-B {ECO:0000303|PubMed:19054355},
GN CB5-E {ECO:0000303|PubMed:22384013}; OrderedLocusNames=At2g32720;
GN ORFNames=F24L7.14;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION, INTERACTION WITH BI-1; FAH1 AND FAH2, AND
RP 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 [6]
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 [7]
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}.
CC -!- SUBUNIT: Interacts with CER1, FAH1, FAH2 and BI-1.
CC {ECO:0000269|PubMed:19054355, ECO:0000269|PubMed:22773744}.
CC -!- INTERACTION:
CC O48845; Q9LD45: BI-1; NbExp=5; IntAct=EBI-2295402, EBI-1644586;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19054355, ECO:0000269|PubMed:22773744}; Single-pass
CC membrane protein {ECO:0000269|PubMed:19054355,
CC ECO:0000269|PubMed:22773744}; Cytoplasmic side
CC {ECO:0000269|PubMed:19054355, ECO:0000269|PubMed:22773744}.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. {ECO:0000305}.
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DR EMBL; AC003974; AAC04491.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08729.1; -; Genomic_DNA.
DR EMBL; AY128405; AAM91608.1; -; mRNA.
DR EMBL; BT000085; AAN15404.1; -; mRNA.
DR EMBL; AK227415; BAE99419.1; -; mRNA.
DR PIR; T00796; T00796.
DR RefSeq; NP_180831.1; NM_128831.4.
DR AlphaFoldDB; O48845; -.
DR SMR; O48845; -.
DR BioGRID; 3179; 10.
DR IntAct; O48845; 3.
DR STRING; 3702.AT2G32720.1; -.
DR PaxDb; O48845; -.
DR PRIDE; O48845; -.
DR ProteomicsDB; 222737; -.
DR EnsemblPlants; AT2G32720.1; AT2G32720.1; AT2G32720.
DR GeneID; 817832; -.
DR Gramene; AT2G32720.1; AT2G32720.1; AT2G32720.
DR KEGG; ath:AT2G32720; -.
DR Araport; AT2G32720; -.
DR TAIR; locus:2046417; AT2G32720.
DR eggNOG; KOG0537; Eukaryota.
DR HOGENOM; CLU_102602_3_0_1; -.
DR InParanoid; O48845; -.
DR OMA; MESVRYW; -.
DR OrthoDB; 1566561at2759; -.
DR PhylomeDB; O48845; -.
DR PRO; PR:O48845; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O48845; baseline and differential.
DR Genevisible; O48845; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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 GO; GO:0043447; P:alkane biosynthetic process; IDA:TAIR.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IPI:TAIR.
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..134
FT /note="Cytochrome b5 isoform B"
FT /id="PRO_0000166021"
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 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 134 AA; 15016 MW; B405F5430F5716C1 CRC64;
MGDEAKIFTL SEVSEHNQAH DCWIVINGKV YNVTKFLEDH PGGDDVLLSS TGKDATDDFE
DVGHSESARE MMEQYYVGEI DPTTIPKKVK YTPPKQPHYN QDKTSEFIIK LLQFLVPLAI
LGLAVGIRIY TKSG
