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PEX7_ARATH
ID   PEX7_ARATH              Reviewed;         317 AA.
AC   Q9XF57; Q9LP54;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   25-MAY-2022, entry version 136.
DE   RecName: Full=Peroxisome biogenesis protein 7;
DE   AltName: Full=Peroxin-7;
DE            Short=AtPEX7;
DE   AltName: Full=Peroxisomal targeting signal type 2 receptor;
DE   AltName: Full=Pex7p;
GN   Name=PEX7; OrderedLocusNames=At1g29260; ORFNames=F28N24.6;
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].
RA   Schumann U., Gietl C., Schmid M.;
RT   "Sequence analysis of a cDNA encoding Pex7p, a peroxisomal targeting signal
RT   2 receptor from Arabidopsis thaliana.";
RL   (er) Plant Gene Register PGR99-060(1999).
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].
RA   Kim C.J., Chen H., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   INTERACTION WITH PEX5 AND PEX14, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=11978862; DOI=10.1093/pcp/pcf057;
RA   Nito K., Hayashi M., Nishimura M.;
RT   "Direct interaction and determination of binding domains among peroxisomal
RT   import factors in Arabidopsis thaliana.";
RL   Plant Cell Physiol. 43:355-366(2002).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH PEX5.
RX   PubMed=15637057; DOI=10.1074/jbc.m411005200;
RA   Hayashi M., Yagi M., Nito K., Kamada T., Nishimura M.;
RT   "Differential contribution of two peroxisomal protein receptors to the
RT   maintenance of peroxisomal functions in Arabidopsis.";
RL   J. Biol. Chem. 280:14829-14835(2005).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15548601; DOI=10.1091/mbc.e04-05-0422;
RA   Woodward A.W., Bartel B.;
RT   "The Arabidopsis peroxisomal targeting signal type 2 receptor PEX7 is
RT   necessary for peroxisome function and dependent on PEX5.";
RL   Mol. Biol. Cell 16:573-583(2005).
RN   [8]
RP   INTERACTION WITH PEX13.
RX   PubMed=16813573; DOI=10.1111/j.1365-313x.2006.02809.x;
RA   Mano S., Nakamori C., Nito K., Kondo M., Nishimura M.;
RT   "The Arabidopsis pex12 and pex13 mutants are defective in both PTS1- and
RT   PTS2-dependent protein transport to peroxisomes.";
RL   Plant J. 47:604-618(2006).
RN   [9]
RP   FUNCTION.
RX   PubMed=17478547; DOI=10.1093/pcp/pcm053;
RA   Nito K., Kamigaki A., Kondo M., Hayashi M., Nishimura M.;
RT   "Functional classification of Arabidopsis peroxisome biogenesis factors
RT   proposed from analyses of knockdown mutants.";
RL   Plant Cell Physiol. 48:763-774(2007).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PEX12 AND
RP   PTS2-CONTAINING PROTEINS.
RX   PubMed=19594707; DOI=10.1111/j.1365-313x.2009.03970.x;
RA   Singh T., Hayashi M., Mano S., Arai Y., Goto S., Nishimura M.;
RT   "Molecular components required for the targeting of PEX7 to peroxisomes in
RT   Arabidopsis thaliana.";
RL   Plant J. 60:488-498(2009).
RN   [11]
RP   FUNCTION, MUTAGENESIS OF THR-124, AND INTERACTION WITH PEX5 AND
RP   PTS2-CONTAINING PROTEINS.
RX   PubMed=20130089; DOI=10.1091/mbc.e09-08-0672;
RA   Ramon N.M., Bartel B.;
RT   "Interdependence of the peroxisome-targeting receptors in Arabidopsis
RT   thaliana: PEX7 facilitates PEX5 accumulation and import of PTS1 cargo into
RT   peroxisomes.";
RL   Mol. Biol. Cell 21:1263-1271(2010).
CC   -!- FUNCTION: Import receptor for peroxisomal-targeting signal two (PTS2).
CC       A receptor-cargo complex composed of PEX5, PEX7, a PTS1-containing
CC       protein and a PTS2-containing protein is targeted to peroxisomes during
CC       import. {ECO:0000269|PubMed:15548601, ECO:0000269|PubMed:15637057,
CC       ECO:0000269|PubMed:17478547, ECO:0000269|PubMed:19594707,
CC       ECO:0000269|PubMed:20130089}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with PEX5 (via N-terminus), PEX13
CC       (via N-terminus) and PEX12 (via C-terminus), but not with PEX14.
CC       Interacts with PTS2-containing proteins. {ECO:0000269|PubMed:11978862,
CC       ECO:0000269|PubMed:15637057, ECO:0000269|PubMed:16813573,
CC       ECO:0000269|PubMed:19594707, ECO:0000269|PubMed:20130089}.
CC   -!- INTERACTION:
CC       Q9XF57; Q8LF48: KAT1; NbExp=3; IntAct=EBI-9536794, EBI-25521360;
CC       Q9XF57; Q56WD9: PED1; NbExp=3; IntAct=EBI-9536794, EBI-4468126;
CC       Q9XF57; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-9536794, EBI-4426557;
CC       Q9XF57; Q5CCK4: VAL2; NbExp=3; IntAct=EBI-9536794, EBI-15193683;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19594707}.
CC       Peroxisome membrane {ECO:0000269|PubMed:19594707}; Peripheral membrane
CC       protein {ECO:0000269|PubMed:19594707}. Note=The loss of PEX12, PEX13 or
CC       PEX14 prevents the targeting of PEX7 to peroxisomes.
CC   -!- TISSUE SPECIFICITY: Expressed in siliques and leaves, but barely
CC       detectable in flowers, stems and roots. {ECO:0000269|PubMed:11978862}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at the early stage of germination.
CC       {ECO:0000269|PubMed:11978862}.
CC   -!- DOMAIN: The WD40 repeats are involved in the binding of PTS2-containing
CC       proteins. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype, but reduced sensitivity to
CC       indole-3-butyric acid (IBA) and inefficient peroxisomal import of PTS2-
CC       containing proteins. {ECO:0000269|PubMed:15548601}.
CC   -!- MISCELLANEOUS: The binding of a cargo to PEX7 is necessary but not
CC       sufficient for the targeting of the complex to the peroxisome. PEX12,
CC       PEX13 and PEX14 play a critical role in this targeting. PEX7 is
CC       required for PEX5 stability in light-grown seedlings.
CC   -!- SIMILARITY: Belongs to the WD repeat peroxin-7 family. {ECO:0000305}.
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DR   EMBL; AF130973; AAD27848.1; -; mRNA.
DR   EMBL; AC021043; AAF88113.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE31066.1; -; Genomic_DNA.
DR   EMBL; BT024863; ABD65594.1; -; mRNA.
DR   PIR; B86415; B86415.
DR   RefSeq; NP_174220.1; NM_102666.4.
DR   AlphaFoldDB; Q9XF57; -.
DR   SMR; Q9XF57; -.
DR   BioGRID; 25035; 18.
DR   IntAct; Q9XF57; 8.
DR   MINT; Q9XF57; -.
DR   STRING; 3702.AT1G29260.1; -.
DR   TCDB; 3.A.20.1.2; the peroxisomal protein importer (ppi) family.
DR   PaxDb; Q9XF57; -.
DR   PRIDE; Q9XF57; -.
DR   ProteomicsDB; 236704; -.
DR   EnsemblPlants; AT1G29260.1; AT1G29260.1; AT1G29260.
DR   GeneID; 839800; -.
DR   Gramene; AT1G29260.1; AT1G29260.1; AT1G29260.
DR   KEGG; ath:AT1G29260; -.
DR   Araport; AT1G29260; -.
DR   TAIR; locus:2029939; AT1G29260.
DR   eggNOG; KOG0277; Eukaryota.
DR   HOGENOM; CLU_046581_0_0_1; -.
DR   InParanoid; Q9XF57; -.
DR   OMA; EKWNYHT; -.
DR   OrthoDB; 793152at2759; -.
DR   PhylomeDB; Q9XF57; -.
DR   PRO; PR:Q9XF57; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9XF57; baseline and differential.
DR   Genevisible; Q9XF57; AT.
DR   GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:TAIR.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005782; C:peroxisomal matrix; IBA:GO_Central.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005053; F:peroxisome matrix targeting signal-2 binding; IBA:GO_Central.
DR   GO; GO:0016558; P:protein import into peroxisome matrix; IBA:GO_Central.
DR   GO; GO:0006625; P:protein targeting to peroxisome; IMP:TAIR.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR044536; PEX7.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR46027; PTHR46027; 1.
DR   Pfam; PF00400; WD40; 5.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Membrane; Peroxisome; Peroxisome biogenesis; Protein transport;
KW   Receptor; Reference proteome; Repeat; Translocation; Transport; WD repeat.
FT   CHAIN           1..317
FT                   /note="Peroxisome biogenesis protein 7"
FT                   /id="PRO_0000403358"
FT   REPEAT          58..98
FT                   /note="WD 1"
FT   REPEAT          104..144
FT                   /note="WD 2"
FT   REPEAT          147..187
FT                   /note="WD 3"
FT   REPEAT          190..230
FT                   /note="WD 4"
FT   REPEAT          234..274
FT                   /note="WD 5"
FT   REPEAT          278..317
FT                   /note="WD 6"
FT   MUTAGEN         124
FT                   /note="T->I: In pex7-2; reduced sensitivity to indole-3-
FT                   butyric acid and loss of interaction with PEX5 and PST2-
FT                   cargo."
FT                   /evidence="ECO:0000269|PubMed:20130089"
FT   CONFLICT        80
FT                   /note="I -> N (in Ref. 1; AAD27848)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   317 AA;  35473 MW;  15DF55CE1F01B1A9 CRC64;
     MPVFKAPFNG YSVKFSPFYE SRLAVATAQN FGILGNGRIH VLELAPGAPG VTESVSYDTA
     DAVYDVCWSE SHDSVLIAAI GDGSVKIYDT ALPPPSNPIR SFQEHAREVQ SVDYNPTRRD
     SFLTSSWDDT VKLWAMDRPA SVRTFKEHAY CVYQAVWNPK HGDVFASASG DCTLRIWDVR
     EPGSTMIIPA HDFEILSCDW NKYDDCILAT SSVDKTVKVW DVRSYRVPLA VLNGHGYAVR
     KVKFSPHRRS LIASCSYDMS VCLWDYMVED ALVGRYDHHT EFAVGIDMSV LVEGLMASTG
     WDELVYVWQQ GMDPRAS
 
 
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