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YMG12_ARATH
ID   YMG12_ARATH             Reviewed;         218 AA.
AC   Q9SUE0; Q8LBK0;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=YlmG homolog protein 1-2, chloroplastic {ECO:0000305};
DE            Short=AtYLMG1-2 {ECO:0000303|PubMed:20359373};
DE   AltName: Full=YGGT family protein YLMG1-2 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=YLMG1-2 {ECO:0000303|PubMed:20359373};
GN   Synonyms=YGGT-B {ECO:0000303|PubMed:18593701};
GN   OrderedLocusNames=At4g27990 {ECO:0000312|Araport:AT4G27990};
GN   ORFNames=T13J8.100 {ECO:0000312|EMBL:CAB36768.1};
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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;
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   [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   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18593701; DOI=10.1074/jbc.m803869200;
RA   Lezhneva L., Kuras R., Ephritikhine G., de Vitry C.;
RT   "A novel pathway of cytochrome c biogenesis is involved in the assembly of
RT   the cytochrome b6f complex in arabidopsis chloroplasts.";
RL   J. Biol. Chem. 283:24608-24616(2008).
RN   [6]
RP   GENE FAMILY.
RX   PubMed=20359373; DOI=10.1186/1471-2229-10-57;
RA   Kabeya Y., Nakanishi H., Suzuki K., Ichikawa T., Kondou Y., Matsui M.,
RA   Miyagishima S.Y.;
RT   "The YlmG protein has a conserved function related to the distribution of
RT   nucleoids in chloroplasts and cyanobacteria.";
RL   BMC Plant Biol. 10:57-57(2010).
CC   -!- FUNCTION: Not required for the biogenesis and accumulation of native
CC       cytochrome b6 in the thylakoid membrane. Not functionally involved in
CC       the pathway for covalent binding of the c-type heme to cytochrome b6.
CC       {ECO:0000269|PubMed:18593701}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250|UniProtKB:Q9SRS3}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions. {ECO:0000269|PubMed:18593701}.
CC   -!- SIMILARITY: Belongs to the YggT family. {ECO:0000305}.
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DR   EMBL; AL035524; CAB36768.1; -; Genomic_DNA.
DR   EMBL; AL161572; CAB79601.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85417.1; -; Genomic_DNA.
DR   EMBL; AK226522; BAE98662.1; -; mRNA.
DR   EMBL; AY087165; AAM64721.1; -; mRNA.
DR   PIR; T02900; T02900.
DR   RefSeq; NP_194528.1; NM_118937.2.
DR   AlphaFoldDB; Q9SUE0; -.
DR   STRING; 3702.AT4G27990.1; -.
DR   PaxDb; Q9SUE0; -.
DR   PRIDE; Q9SUE0; -.
DR   ProteomicsDB; 242929; -.
DR   EnsemblPlants; AT4G27990.1; AT4G27990.1; AT4G27990.
DR   GeneID; 828912; -.
DR   Gramene; AT4G27990.1; AT4G27990.1; AT4G27990.
DR   KEGG; ath:AT4G27990; -.
DR   Araport; AT4G27990; -.
DR   TAIR; locus:2132907; AT4G27990.
DR   eggNOG; ENOG502S1YI; Eukaryota.
DR   HOGENOM; CLU_092220_1_0_1; -.
DR   InParanoid; Q9SUE0; -.
DR   OMA; IQASIRV; -.
DR   OrthoDB; 1546310at2759; -.
DR   PhylomeDB; Q9SUE0; -.
DR   PRO; PR:Q9SUE0; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SUE0; baseline and differential.
DR   Genevisible; Q9SUE0; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0010020; P:chloroplast fission; IBA:GO_Central.
DR   GO; GO:0090143; P:nucleoid organization; IBA:GO_Central.
DR   InterPro; IPR003425; CCB3/YggT.
DR   PANTHER; PTHR33219; PTHR33219; 1.
DR   Pfam; PF02325; YGGT; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Membrane; Plastid; Reference proteome; Thylakoid;
KW   Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..83
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           84..218
FT                   /note="YlmG homolog protein 1-2, chloroplastic"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000433267"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        79
FT                   /note="T -> N (in Ref. 4; AAM64721)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        167
FT                   /note="R -> G (in Ref. 4; AAM64721)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   218 AA;  23705 MW;  8F54991DDA2FFB49 CRC64;
     MASFTTNSLA LRASILANPR LPPPIIRPRL SLPRKLSFNL SLHNARTIVS SAVTSSSPVL
     SSKPPSQFPF SDSTRSITTL VLLAGVVIKS LIQKLSVAIV NLSPQIQASF RTASPLFFAS
     LRDRPAGYLN TPLTVVAAGL SKWLDIYSGV LMVRVLLSWF PNIPWDRQPL SAIRDLCDPY
     LNLFRNIIPP VFDTLDVSPL LAFAVLGTLG SILNNSRG
 
 
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