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RER1B_ARATH
ID   RER1B_ARATH             Reviewed;         195 AA.
AC   O48671; Q541D3; Q9SIK0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 2.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Protein RER1B;
DE            Short=AtRER1B;
GN   Name=RER1B; OrderedLocusNames=At2g21600; ORFNames=F2G1.13;
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].
RC   STRAIN=cv. Columbia;
RX   PubMed=10737146; DOI=10.1023/a:1006329828395;
RA   Sato K., Ueda T., Nakano A.;
RT   "The Arabidopsis thaliana RER1 gene family: its potential role in the
RT   endoplasmic reticulum localization of membrane proteins.";
RL   Plant Mol. Biol. 41:815-824(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [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: Involved in the retrieval of endoplasmic reticulum membrane
CC       proteins from the early Golgi compartment. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the RER1 family. {ECO:0000305}.
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DR   EMBL; AB010946; BAA24804.1; -; mRNA.
DR   EMBL; AC007119; AAD23645.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07201.1; -; Genomic_DNA.
DR   EMBL; AY057644; AAL15275.1; -; mRNA.
DR   EMBL; AY113014; AAM47322.1; -; mRNA.
DR   EMBL; AY088719; AAM67037.1; -; mRNA.
DR   PIR; B84603; B84603.
DR   PIR; T51628; T51628.
DR   RefSeq; NP_179754.1; NM_127731.3.
DR   AlphaFoldDB; O48671; -.
DR   BioGRID; 2051; 1.
DR   STRING; 3702.AT2G21600.1; -.
DR   iPTMnet; O48671; -.
DR   PaxDb; O48671; -.
DR   PRIDE; O48671; -.
DR   ProteomicsDB; 236744; -.
DR   EnsemblPlants; AT2G21600.1; AT2G21600.1; AT2G21600.
DR   GeneID; 816698; -.
DR   Gramene; AT2G21600.1; AT2G21600.1; AT2G21600.
DR   KEGG; ath:AT2G21600; -.
DR   Araport; AT2G21600; -.
DR   TAIR; locus:2049354; AT2G21600.
DR   eggNOG; KOG1688; Eukaryota.
DR   HOGENOM; CLU_074889_1_1_1; -.
DR   InParanoid; O48671; -.
DR   OMA; HSAYRWI; -.
DR   OrthoDB; 1458086at2759; -.
DR   PhylomeDB; O48671; -.
DR   PRO; PR:O48671; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O48671; baseline and differential.
DR   Genevisible; O48671; AT.
DR   GO; GO:0005801; C:cis-Golgi network; TAS:TAIR.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR   GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR   GO; GO:0006621; P:protein retention in ER lumen; IBA:GO_Central.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:TAIR.
DR   InterPro; IPR004932; Rer1.
DR   PANTHER; PTHR10743; PTHR10743; 1.
DR   Pfam; PF03248; Rer1; 1.
DR   PIRSF; PIRSF016013; AtER_Rer1p; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..195
FT                   /note="Protein RER1B"
FT                   /id="PRO_0000207595"
FT   TRANSMEM        38..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CONFLICT        47
FT                   /note="F -> V (in Ref. 1; BAA24804 and 5; AAM67037)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   195 AA;  22418 MW;  5051FE91497D2746 CRC64;
     MEGSGGDSGS MATPVQKKVH EAWRVYQYYL DKTTPHSTNR WIGTLVFFLI YCLRVYSIHG
     FYIISYGLGI YLLNLLIGFL SPLVDPELEV SDGATLPTRG SDEFKPFIRR LPEFKFWYSM
     TKAFCIAFLM TFFSVFDVPV FWPILLCYWV VLFVLTMRRQ IAHMIKHKYI PFSIGKQKYS
     GRKSSANSGG GSRAD
 
 
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