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MEB2_ARATH
ID   MEB2_ARATH              Reviewed;         550 AA.
AC   F4KFS7; B9DH25; Q8LCU6; Q9FNF3;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Membrane protein of ER body 2;
GN   Name=MEB2; OrderedLocusNames=At5g24290; ORFNames=MOP9.11;
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=9405937; DOI=10.1093/dnares/4.4.291;
RA   Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT   features of the regions of 1,044,062 bp covered by thirteen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:291-300(1997).
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] (ISOFORM 1).
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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] (ISOFORM 2).
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia; TISSUE=Root;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA   Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT   thaliana.";
RL   J. Proteomics 72:439-451(2009).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE, AND
RP   INTERACTION WITH NAI2.
RC   STRAIN=cv. Columbia;
RX   PubMed=23166355; DOI=10.1104/pp.112.207654;
RA   Yamada K., Nagano A.J., Nishina M., Hara-Nishimura I., Nishimura M.;
RT   "Identification of two novel endoplasmic reticulum body-specific integral
RT   membrane proteins.";
RL   Plant Physiol. 161:108-120(2013).
CC   -!- FUNCTION: May sequester excess cytosolic iron and manganese into
CC       endoplasmic reticulum to reduce metal ion toxicity. Not essential for
CC       the accumulation of ER body components, including PYK10.
CC       {ECO:0000269|PubMed:23166355}.
CC   -!- SUBUNIT: Interacts directly or indirectly with NAI2.
CC       {ECO:0000269|PubMed:23166355}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:23166355}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:23166355}. Note=Located in ER bodies.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=F4KFS7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=F4KFS7-2; Sequence=VSP_056762;
CC   -!- INDUCTION: Induced by NAI1. {ECO:0000269|PubMed:23166355}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype and no effect on pathogen
CC       sensitivity. {ECO:0000269|PubMed:23166355}.
CC   -!- SIMILARITY: Belongs to the CCC1 family. {ECO:0000305}.
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DR   EMBL; AB006701; BAB10395.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED93280.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED93281.1; -; Genomic_DNA.
DR   EMBL; AY086399; AAM64466.1; -; mRNA.
DR   EMBL; BT008326; AAP37685.1; -; mRNA.
DR   EMBL; AK228214; BAF00167.1; -; mRNA.
DR   EMBL; AK317370; BAH20042.1; -; mRNA.
DR   RefSeq; NP_568441.2; NM_122335.4. [F4KFS7-2]
DR   RefSeq; NP_851067.1; NM_180736.3. [F4KFS7-1]
DR   AlphaFoldDB; F4KFS7; -.
DR   BioGRID; 17771; 3.
DR   IntAct; F4KFS7; 3.
DR   STRING; 3702.AT5G24290.1; -.
DR   iPTMnet; F4KFS7; -.
DR   PaxDb; F4KFS7; -.
DR   PRIDE; F4KFS7; -.
DR   ProteomicsDB; 250840; -. [F4KFS7-1]
DR   EnsemblPlants; AT5G24290.1; AT5G24290.1; AT5G24290. [F4KFS7-1]
DR   EnsemblPlants; AT5G24290.2; AT5G24290.2; AT5G24290. [F4KFS7-2]
DR   GeneID; 832496; -.
DR   Gramene; AT5G24290.1; AT5G24290.1; AT5G24290. [F4KFS7-1]
DR   Gramene; AT5G24290.2; AT5G24290.2; AT5G24290. [F4KFS7-2]
DR   KEGG; ath:AT5G24290; -.
DR   Araport; AT5G24290; -.
DR   TAIR; locus:2169804; AT5G24290.
DR   eggNOG; ENOG502QQ85; Eukaryota.
DR   InParanoid; F4KFS7; -.
DR   OMA; IFTCLAC; -.
DR   OrthoDB; 953616at2759; -.
DR   PRO; PR:F4KFS7; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; F4KFS7; baseline and differential.
DR   Genevisible; F4KFS7; AT.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0010168; C:ER body; IDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005381; F:iron ion transmembrane transporter activity; IGI:TAIR.
DR   GO; GO:0005384; F:manganese ion transmembrane transporter activity; IGI:TAIR.
DR   GO; GO:0030026; P:cellular manganese ion homeostasis; IBA:GO_Central.
DR   GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central.
DR   InterPro; IPR008217; Ccc1_fam.
DR   PANTHER; PTHR31851; PTHR31851; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Endoplasmic reticulum; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..550
FT                   /note="Membrane protein of ER body 2"
FT                   /id="PRO_0000430468"
FT   TRANSMEM        374..394
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        425..445
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        458..478
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        500..520
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   REGION          46..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          134..165
FT                   /evidence="ECO:0000255"
FT   COILED          393..418
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        71..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..195
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         77..92
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172, ECO:0000303|Ref.5"
FT                   /id="VSP_056762"
FT   CONFLICT        91
FT                   /note="D -> G (in Ref. 6; BAH20042)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        202
FT                   /note="L -> F (in Ref. 3; AAM64466)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   550 AA;  61046 MW;  9F6E6C92E8FA2358 CRC64;
     MEKSNQPVHV TLSELKDGDK EIVDAEFLVD LLESYRFGKD NVPAREFRSK AAATAPAPVN
     TTEIELEEDN DGSQAQGNNS VSESTSSLFS DSDPIVLEST VSETGSNEES ETGSNEENGN
     NWLESSSTNL PNVENKRQRN GEDCEIEEEE ENNERSLSDS EEKSNLEKLL GTQENYELGN
     EDEEKNERSS SDSEEKSNLE NLLATQENYE LYCPSCSTCI TRNVVLKKRK RGKHVNSSLD
     LKPDIPVVEP DEPSDIEEME SPVKVYVPET RIEDDQEDKE GTIFTCLVCD LKYFIRLGTK
     FLQLDYIRGK PVEKSVEEYI DVRKSINTTQ SPPQIQPDGE RFAIELLKST VYGGLTETIT
     SLGVVSSASA SGSSTMNILA LAVANLAGGL IVLAQNFQDL RNSSDQEKDR YEELLGRRTK
     SRIHILVAVM SYIFFGLIPP LVYAFSFYET GIKNYKLISV FLGSLVCVIL LGSIKVYVRK
     PTNSCGSTKA YLKSAAYYTS IVVASCGISY VVGDIMGEYI EKLSLVGLDQ ISITSPCYGI
     KPEECRFTSF
 
 
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