CX5B1_ARATH
ID CX5B1_ARATH Reviewed; 176 AA.
AC Q9LW15;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Cytochrome c oxidase subunit 5b-1, mitochondrial;
DE Short=AtCOX5b-1;
DE Flags: Precursor;
GN Name=COX5B-1; OrderedLocusNames=At3g15640; ORFNames=MSJ11.4;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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=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].
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP PHE-55.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
CC -!- FUNCTION: This protein is one of the nuclear-coded polypeptide chains
CC of cytochrome c oxidase, the terminal oxidase in mitochondrial electron
CC transport. {ECO:0000255|PROSITE-ProRule:PRU00692}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000255|PROSITE-ProRule:PRU00692, ECO:0000305|PubMed:25732537}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LW15-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 5B (TC
CC 3.D.4.11) 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; AB017071; BAB02295.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75706.1; -; Genomic_DNA.
DR EMBL; AF367258; AAK56247.1; -; mRNA.
DR EMBL; AY055100; AAL05900.1; -; mRNA.
DR EMBL; AY087329; AAM64879.1; -; mRNA.
DR RefSeq; NP_188185.1; NM_112434.3. [Q9LW15-1]
DR AlphaFoldDB; Q9LW15; -.
DR SMR; Q9LW15; -.
DR BioGRID; 6140; 2.
DR IntAct; Q9LW15; 1.
DR STRING; 3702.AT3G15640.1; -.
DR iPTMnet; Q9LW15; -.
DR MetOSite; Q9LW15; -.
DR PaxDb; Q9LW15; -.
DR PRIDE; Q9LW15; -.
DR ProteomicsDB; 220422; -. [Q9LW15-1]
DR EnsemblPlants; AT3G15640.1; AT3G15640.1; AT3G15640. [Q9LW15-1]
DR GeneID; 820806; -.
DR Gramene; AT3G15640.1; AT3G15640.1; AT3G15640. [Q9LW15-1]
DR KEGG; ath:AT3G15640; -.
DR Araport; AT3G15640; -.
DR TAIR; locus:2093267; AT3G15640.
DR eggNOG; KOG3352; Eukaryota.
DR PhylomeDB; Q9LW15; -.
DR PRO; PR:Q9LW15; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LW15; baseline and differential.
DR Genevisible; Q9LW15; AT.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR CDD; cd00924; Cyt_c_Oxidase_Vb; 1.
DR Gene3D; 2.60.11.10; -; 1.
DR InterPro; IPR002124; Cyt_c_oxidase_su5b.
DR InterPro; IPR036972; Cyt_c_oxidase_su5b_sf.
DR PANTHER; PTHR10122; PTHR10122; 1.
DR Pfam; PF01215; COX5B; 1.
DR PROSITE; PS51359; COX5B_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..55
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 56..176
FT /note="Cytochrome c oxidase subunit 5b-1, mitochondrial"
FT /id="PRO_0000412471"
FT REGION 157..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00692"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00692"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00692"
SQ SEQUENCE 176 AA; 19416 MW; 30946F0F0EADBEED CRC64;
MWRRIVSSQL KTLAADVVAA SPRRSIAATT RPVGFYLAAN RSAISASSFV IPRRFSSDSV
ETPATKKVED VMPIATGHEK EELEAELEGR RLDDIDFPEG PFGTKEAPAI VKSYYDKRIV
GCPGGEGEDE HDVVWFWLEK GKSFECPVCT QYFELEVVGP GGPPDGHGDE DDEHHH
