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CX6B1_ARATH
ID   CX6B1_ARATH             Reviewed;         191 AA.
AC   Q9S7L9; Q8LCP1;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=Cytochrome c oxidase subunit 6b-1;
DE            Short=AtCOX6b-1;
GN   Name=COX6B-1; OrderedLocusNames=At1g22450; ORFNames=F12K8.20;
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], GENE FAMILY, NOMENCLATURE, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=11250078; DOI=10.1016/s0378-1119(01)00334-1;
RA   Ohtsu K., Nakazono M., Tsutsumi N., Hirai A.;
RT   "Characterization and expression of the genes for cytochrome c oxidase
RT   subunit VIb (COX6b) from rice and Arabidopsis thaliana.";
RL   Gene 264:233-239(2001).
RN   [2]
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   [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   DEVELOPMENTAL STAGE.
RX   PubMed=11434463; DOI=10.1266/ggs.76.89;
RA   Saisho D., Nakazono M., Lee K.-H., Tsutsumi N., Akita S., Hirai A.;
RT   "The gene for alternative oxidase-2 (AOX2) from Arabidopsis thaliana
RT   consists of five exons unlike other AOX genes and is transcribed at an
RT   early stage during germination.";
RL   Genes Genet. Syst. 76:89-97(2001).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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. This protein may be one of the heme-binding subunits of the
CC       oxidase.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in the whole plant.
CC       {ECO:0000269|PubMed:11250078}.
CC   -!- DEVELOPMENTAL STAGE: Gradually expressed after germination.
CC       {ECO:0000269|PubMed:11434463}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 6B (TC 3.D.4.8)
CC       family. {ECO:0000305}.
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DR   EMBL; AB035444; BAA87883.1; -; mRNA.
DR   EMBL; AC006551; AAF18532.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE30243.1; -; Genomic_DNA.
DR   EMBL; AY063997; AAL36353.1; -; mRNA.
DR   EMBL; AY096696; AAM20330.1; -; mRNA.
DR   EMBL; AY086483; AAM63485.1; -; mRNA.
DR   PIR; F86357; F86357.
DR   RefSeq; NP_173661.1; NM_102094.4.
DR   AlphaFoldDB; Q9S7L9; -.
DR   SMR; Q9S7L9; -.
DR   BioGRID; 24090; 1.
DR   IntAct; Q9S7L9; 1.
DR   STRING; 3702.AT1G22450.1; -.
DR   iPTMnet; Q9S7L9; -.
DR   PaxDb; Q9S7L9; -.
DR   PRIDE; Q9S7L9; -.
DR   ProteomicsDB; 220429; -.
DR   EnsemblPlants; AT1G22450.1; AT1G22450.1; AT1G22450.
DR   GeneID; 838851; -.
DR   Gramene; AT1G22450.1; AT1G22450.1; AT1G22450.
DR   KEGG; ath:AT1G22450; -.
DR   Araport; AT1G22450; -.
DR   TAIR; locus:2009497; AT1G22450.
DR   eggNOG; KOG3057; Eukaryota.
DR   HOGENOM; CLU_084057_0_0_1; -.
DR   InParanoid; Q9S7L9; -.
DR   OMA; SWNEQRE; -.
DR   OrthoDB; 1586678at2759; -.
DR   PRO; PR:Q9S7L9; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9S7L9; baseline and differential.
DR   Genevisible; Q9S7L9; AT.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0045277; C:respiratory chain complex IV; IEA:InterPro.
DR   GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR   GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR   CDD; cd00926; Cyt_c_Oxidase_VIb; 1.
DR   Gene3D; 1.10.10.140; -; 1.
DR   InterPro; IPR003213; Cyt_c_oxidase_su6B.
DR   InterPro; IPR036549; Cyt_c_oxidase_su6B_sf.
DR   Pfam; PF02297; COX6B; 1.
DR   SUPFAM; SSF47694; SSF47694; 1.
DR   PROSITE; PS51808; CHCH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Disulfide bond; Mitochondrion; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..191
FT                   /note="Cytochrome c oxidase subunit 6b-1"
FT                   /id="PRO_0000412233"
FT   DOMAIN          134..177
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   REGION          1..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           137..147
FT                   /note="Cx9C motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           158..169
FT                   /note="Cx10C motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..74
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..110
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   DISULFID        137..169
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        147..158
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   CONFLICT        87
FT                   /note="E -> Q (in Ref. 5; AAM63485)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   191 AA;  21195 MW;  7592D7DBC94BC054 CRC64;
     MADAVNAQTP SLSEQYHLEK EVKQDTSAKP VEVKEVAPEV TTQAEEVKTE QAKEESPVEE
     AVSVVEEKSE SAPESTEVAS EAPAAAEDNA EETPAAAEEN NDENASEEVA EETPDEIKLE
     TAPADFRFPT TNQTRHCFTR YVEYHRCVAA KGDDAPECDK FAKFYRSLCP SEWVDRWNEQ
     RENGTFPGPL P
 
 
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