CYB5C_ARATH
ID CYB5C_ARATH Reviewed; 132 AA.
AC Q9ZNV4; Q682C5;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Cytochrome B5 isoform C {ECO:0000303|PubMed:19054355, ECO:0000303|PubMed:22384013};
DE Short=AtCb5-C {ECO:0000303|PubMed:19054355, ECO:0000303|PubMed:22384013};
GN Name=CYTB5-C {ECO:0000305};
GN Synonyms=CB5-C {ECO:0000303|PubMed:19054355, ECO:0000303|PubMed:22384013};
GN OrderedLocusNames=At2g46650; ORFNames=T3A4.3;
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].
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 [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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
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, BI-1, FAH1 and FAH2.
CC {ECO:0000269|PubMed:19054355, ECO:0000269|PubMed:22773744}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22773744}; Single-pass membrane protein
CC {ECO:0000269|PubMed:22773744}.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD43205.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC005819; AAC69922.1; -; Genomic_DNA.
DR EMBL; AC006418; AAM15242.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10735.1; -; Genomic_DNA.
DR EMBL; AY087658; AAM65196.1; -; mRNA.
DR EMBL; AK175189; BAD42952.1; -; mRNA.
DR EMBL; AK175442; BAD43205.1; ALT_INIT; mRNA.
DR EMBL; BT025600; ABF59018.1; -; mRNA.
DR PIR; E84905; E84905.
DR RefSeq; NP_182188.1; NM_130230.3.
DR AlphaFoldDB; Q9ZNV4; -.
DR SMR; Q9ZNV4; -.
DR BioGRID; 4612; 4.
DR IntAct; Q9ZNV4; 1.
DR STRING; 3702.AT2G46650.1; -.
DR PaxDb; Q9ZNV4; -.
DR PRIDE; Q9ZNV4; -.
DR ProteomicsDB; 222738; -.
DR EnsemblPlants; AT2G46650.1; AT2G46650.1; AT2G46650.
DR GeneID; 819277; -.
DR Gramene; AT2G46650.1; AT2G46650.1; AT2G46650.
DR KEGG; ath:AT2G46650; -.
DR Araport; AT2G46650; -.
DR TAIR; locus:2039939; AT2G46650.
DR eggNOG; KOG0537; Eukaryota.
DR HOGENOM; CLU_102602_3_0_1; -.
DR InParanoid; Q9ZNV4; -.
DR OMA; CIGDVDQ; -.
DR OrthoDB; 1566561at2759; -.
DR PRO; PR:Q9ZNV4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZNV4; baseline and differential.
DR Genevisible; Q9ZNV4; AT.
DR GO; GO:0005829; C:cytosol; 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 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..132
FT /note="Cytochrome B5 isoform C"
FT /id="PRO_0000419612"
FT TRANSMEM 110..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 2..78
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 37
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 61
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 89
FT /note="I -> V (in Ref. 4; BAD43205)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 132 AA; 14873 MW; 894A1133E88596BC CRC64;
MANLISFHDV AKHKCKNDCW ILIHGKVYDI STFMDEHPGG DNVLLAVTGK DASIDFEDVN
HSKDAKELMK KYCIGDVDQS TVPVTQQYIP PWEKESTAAE TTKEESGKKL LIYLIPLLIL
GVAFALRFYN NK
