CYB5A_ARATH
ID CYB5A_ARATH Reviewed; 135 AA.
AC Q9FDW8;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Cytochrome b5 isoform A {ECO:0000303|PubMed:19054355};
DE Short=AtCb5-A {ECO:0000303|PubMed:19054355};
DE AltName: Full=Cytochrome b5 isoform D {ECO:0000303|PubMed:22384013};
DE Short=AtCb5-D {ECO:0000303|PubMed:22384013};
GN Name=CB5-A {ECO:0000303|PubMed:19054355};
GN Synonyms=CB5-D {ECO:0000303|PubMed:22384013};
GN OrderedLocusNames=At1g26340 {ECO:0000312|Araport:AT1G26340};
GN ORFNames=F28B23.1 {ECO:0000312|EMBL:AAG50683.1},
GN T1K7.28 {ECO:0000312|EMBL:AAF98581.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 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 -!- SUBUNIT: Interacts with BI-1, FAH1 and FAH2.
CC {ECO:0000269|PubMed:19054355}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:17322552}; Single-pass membrane protein
CC {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:17322552};
CC Single-pass membrane protein {ECO:0000255}. Note=Localizes
CC preferentially on the chloroplast envelope. Localizes in stromule
CC (stroma-filled tubular extensions of the plastid envelope membrane).
CC {ECO:0000269|PubMed:17322552}.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC013427; AAF98581.1; -; Genomic_DNA.
DR EMBL; AC079829; AAG50683.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30679.1; -; Genomic_DNA.
DR EMBL; AK117459; BAC42124.1; -; mRNA.
DR EMBL; AF332415; AAG48778.1; -; mRNA.
DR EMBL; AY084761; AAM61330.1; -; mRNA.
DR PIR; A86390; A86390.
DR RefSeq; NP_173958.1; NM_102398.3.
DR AlphaFoldDB; Q9FDW8; -.
DR SMR; Q9FDW8; -.
DR BioGRID; 24412; 2.
DR IntAct; Q9FDW8; 1.
DR STRING; 3702.AT1G26340.1; -.
DR iPTMnet; Q9FDW8; -.
DR PaxDb; Q9FDW8; -.
DR PRIDE; Q9FDW8; -.
DR ProMEX; Q9FDW8; -.
DR ProteomicsDB; 222736; -.
DR EnsemblPlants; AT1G26340.1; AT1G26340.1; AT1G26340.
DR GeneID; 839176; -.
DR Gramene; AT1G26340.1; AT1G26340.1; AT1G26340.
DR KEGG; ath:AT1G26340; -.
DR Araport; AT1G26340; -.
DR TAIR; locus:2028721; AT1G26340.
DR eggNOG; KOG0537; Eukaryota.
DR HOGENOM; CLU_102602_3_0_1; -.
DR InParanoid; Q9FDW8; -.
DR OMA; PCWLIIK; -.
DR OrthoDB; 1566561at2759; -.
DR PhylomeDB; Q9FDW8; -.
DR PRO; PR:Q9FDW8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FDW8; baseline and differential.
DR Genevisible; Q9FDW8; AT.
DR GO; GO:0009707; C:chloroplast outer membrane; IDA: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:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010319; C:stromule; IDA: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 Chloroplast; Heme; Iron; Membrane; Metal-binding; Mitochondrion; Plastid;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..135
FT /note="Cytochrome b5 isoform A"
FT /id="PRO_0000430955"
FT TRANSMEM 113..132
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 135 AA; 15220 MW; F88FCB6B5BBC8E9E CRC64;
MPTLTKLYSM EEAATHNKQD DCWVVIDGKV YDVSSYMDEH PGGDDVLLAV AGKDATDDFE
DAGHSKDARE LMEKYFIGEL DESSLPEIPE LKIYKKDQPQ DSVQKLFDLT KQYWVVPVSI
ITISVAVSVL FSRKT
