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OEP7_ARATH
ID   OEP7_ARATH              Reviewed;          64 AA.
AC   Q9SVC4;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Outer envelope membrane protein 7 {ECO:0000303|PubMed:11595795};
DE            Short=AtOEP7 {ECO:0000303|PubMed:11595795};
GN   Name=OEP7 {ECO:0000303|PubMed:11595795};
GN   OrderedLocusNames=At3g52420 {ECO:0000312|EMBL:AEE78944.1};
GN   ORFNames=F22O6.200 {ECO:0000312|EMBL:CAB43440.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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].
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   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, AND MUTAGENESIS OF
RP   10-ALA--LEU-22; ALA-15; LEU-19; ALA-23; LYS-29; ASP-33 AND LYS-34.
RC   STRAIN=cv. Columbia;
RX   PubMed=11595795; DOI=10.2307/3871501;
RA   Lee Y.J., Kim D.H., Kim Y.-W., Hwang I.;
RT   "Identification of a signal that distinguishes between the chloroplast
RT   outer envelope membrane and the endomembrane system in vivo.";
RL   Plant Cell 13:2175-2190(2001).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17337631; DOI=10.1105/tpc.106.047407;
RA   Duy D., Wanner G., Meda A.R., von Wiren N., Soll J., Philippar K.;
RT   "PIC1, an ancient permease in Arabidopsis chloroplasts, mediates iron
RT   transport.";
RL   Plant Cell 19:986-1006(2007).
RN   [7]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH AKR2A.
RC   STRAIN=cv. Columbia;
RX   PubMed=18193034; DOI=10.1038/ncb1683;
RA   Bae W., Lee Y.J., Kim D.H., Lee J., Kim S., Sohn E.J., Hwang I.;
RT   "AKR2A-mediated import of chloroplast outer membrane proteins is essential
RT   for chloroplast biogenesis.";
RL   Nat. Cell Biol. 10:220-227(2008).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18715957; DOI=10.1104/pp.108.123075;
RA   Oikawa K., Yamasato A., Kong S.-G., Kasahara M., Nakai M., Takahashi F.,
RA   Ogura Y., Kagawa T., Wada M.;
RT   "Chloroplast outer envelope protein CHUP1 is essential for chloroplast
RT   anchorage to the plasma membrane and chloroplast movement.";
RL   Plant Physiol. 148:829-842(2008).
RN   [9]
RP   AKR2A-BINDING SEQUENCE, AND REVIEW.
RX   PubMed=21057222; DOI=10.4161/psb.5.11.13714;
RA   Zhang H., Li X., Zhang Y., Kuppu S., Shen G.;
RT   "Is AKR2A an essential molecular chaperone for a class of membrane-bound
RT   proteins in plants?";
RL   Plant Signal. Behav. 5:1520-1522(2010).
RN   [10]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=21730198; DOI=10.1104/pp.111.178681;
RA   Kim D.H., Xu Z.-Y., Na Y.J., Yoo Y.-J., Lee J., Sohn E.-J., Hwang I.;
RT   "Small heat shock protein Hsp17.8 functions as an AKR2A cofactor in the
RT   targeting of chloroplast outer membrane proteins in Arabidopsis.";
RL   Plant Physiol. 157:132-146(2011).
CC   -!- SUBUNIT: Interacts with AKR2A. {ECO:0000269|PubMed:18193034}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC       {ECO:0000269|PubMed:11595795, ECO:0000269|PubMed:17337631,
CC       ECO:0000269|PubMed:18715957, ECO:0000269|PubMed:21730198}; Single-pass
CC       membrane protein {ECO:0000269|PubMed:11595795}. Note=The targeting to
CC       chloroplasts is facilitated by AKR2A and HSP17.8.
CC       {ECO:0000269|PubMed:18193034, ECO:0000269|PubMed:21730198}.
CC   -!- TISSUE SPECIFICITY: Confined to green tissues.
CC       {ECO:0000269|PubMed:11595795}.
CC   -!- DOMAIN: The transmembrane plays critical roles in migration to the
CC       chloroplasts and/or subsequent insertion into the membrane.
CC       {ECO:0000269|PubMed:11595795}.
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DR   EMBL; AL050300; CAB43440.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78944.1; -; Genomic_DNA.
DR   EMBL; BT010511; AAQ65134.1; -; mRNA.
DR   EMBL; AK175275; BAD43038.1; -; mRNA.
DR   EMBL; AK175812; BAD43575.1; -; mRNA.
DR   PIR; T08457; T08457.
DR   RefSeq; NP_190810.1; NM_115102.3.
DR   AlphaFoldDB; Q9SVC4; -.
DR   SMR; Q9SVC4; -.
DR   STRING; 3702.AT3G52420.1; -.
DR   iPTMnet; Q9SVC4; -.
DR   PaxDb; Q9SVC4; -.
DR   PRIDE; Q9SVC4; -.
DR   ProteomicsDB; 238921; -.
DR   EnsemblPlants; AT3G52420.1; AT3G52420.1; AT3G52420.
DR   GeneID; 824407; -.
DR   Gramene; AT3G52420.1; AT3G52420.1; AT3G52420.
DR   KEGG; ath:AT3G52420; -.
DR   Araport; AT3G52420; -.
DR   TAIR; locus:2079929; AT3G52420.
DR   eggNOG; ENOG502S8H4; Eukaryota.
DR   HOGENOM; CLU_187971_0_0_1; -.
DR   InParanoid; Q9SVC4; -.
DR   OMA; WWTIEIA; -.
DR   OrthoDB; 1644858at2759; -.
DR   PhylomeDB; Q9SVC4; -.
DR   PRO; PR:Q9SVC4; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SVC4; baseline and differential.
DR   Genevisible; Q9SVC4; AT.
DR   GO; GO:0009707; C:chloroplast outer membrane; IDA:UniProtKB.
DR   GO; GO:0031359; C:integral component of chloroplast outer membrane; IDA:TAIR.
DR   InterPro; IPR038944; OEP7-like.
DR   PANTHER; PTHR33982; PTHR33982; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Membrane; Plastid; Plastid outer membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..64
FT                   /note="Outer envelope membrane protein 7"
FT                   /id="PRO_0000434612"
FT   TOPO_DOM        1..11
FT                   /note="Chloroplast intermembrane"
FT                   /evidence="ECO:0000305|PubMed:11595795"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..64
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:11595795"
FT   REGION          39..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           29..35
FT                   /note="AKR2A-binding sequence (ABS) required for
FT                   chloroplast outer envelope membrane targeting"
FT                   /evidence="ECO:0000269|PubMed:11595795,
FT                   ECO:0000269|PubMed:21057222"
FT   MUTAGEN         10..21
FT                   /note="ATVVVAAMALGW->IIIIIIIIIIII: Normal targeting to the
FT                   chloroplast."
FT                   /evidence="ECO:0000269|PubMed:11595795"
FT   MUTAGEN         10..21
FT                   /note="ATVVVAAMALGW->MAMMMMMMAMMM,FFFFFFFFFFFF: Impaired
FT                   targeting to the chloroplast resulting in the formation of
FT                   large aggregates in the cytoplasm."
FT                   /evidence="ECO:0000269|PubMed:11595795"
FT   MUTAGEN         11..22
FT                   /note="TVVVAAMALGWL->AAAAAAAAAAAA,IIIIIIIIIIIIL: Normal
FT                   targeting to the chloroplast."
FT                   /evidence="ECO:0000269|PubMed:11595795"
FT   MUTAGEN         15
FT                   /note="A->P: Reduced efficiency of chloroplast-targeting."
FT                   /evidence="ECO:0000269|PubMed:11595795"
FT   MUTAGEN         19
FT                   /note="L->P: Impaired chloroplast-targeting."
FT                   /evidence="ECO:0000269|PubMed:11595795"
FT   MUTAGEN         23
FT                   /note="A->P: Reduced efficiency of chloroplast-targeting."
FT                   /evidence="ECO:0000269|PubMed:11595795"
FT   MUTAGEN         29
FT                   /note="K->G: Impaired targeting to the chloroplast outer
FT                   membrane leading to plasma membrane localization; when
FT                   associated with G-34."
FT                   /evidence="ECO:0000269|PubMed:11595795"
FT   MUTAGEN         33
FT                   /note="D->G: Impaired targeting to the chloroplast outer
FT                   membrane leading to plasma membrane localization."
FT                   /evidence="ECO:0000269|PubMed:11595795"
FT   MUTAGEN         34
FT                   /note="K->G: Impaired targeting to the chloroplast outer
FT                   membrane leading to plasma membrane localization; when
FT                   associated with G-29."
FT                   /evidence="ECO:0000269|PubMed:11595795"
SQ   SEQUENCE   64 AA;  6764 MW;  BA5B5D4340F9B006 CRC64;
     MGKTSGAKQA TVVVAAMALG WLAIEIAFKP FLDKFRSSID KSDPTKDPDD FDTAATATTS
     KEGL
 
 
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