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RER1_RAT
ID   RER1_RAT                Reviewed;         196 AA.
AC   Q498C8;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Protein RER1;
GN   Name=Rer1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-95, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Involved in the retrieval of endoplasmic reticulum membrane
CC       proteins from the early Golgi compartment. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-
CC       pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RER1 family. {ECO:0000305}.
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DR   EMBL; BC100270; AAI00271.1; -; mRNA.
DR   RefSeq; NP_001034101.1; NM_001039012.1.
DR   AlphaFoldDB; Q498C8; -.
DR   IntAct; Q498C8; 1.
DR   STRING; 10116.ENSRNOP00000019620; -.
DR   iPTMnet; Q498C8; -.
DR   PhosphoSitePlus; Q498C8; -.
DR   jPOST; Q498C8; -.
DR   PaxDb; Q498C8; -.
DR   PRIDE; Q498C8; -.
DR   GeneID; 298675; -.
DR   KEGG; rno:298675; -.
DR   CTD; 11079; -.
DR   RGD; 1306324; Rer1.
DR   VEuPathDB; HostDB:ENSRNOG00000014270; -.
DR   eggNOG; KOG1688; Eukaryota.
DR   HOGENOM; CLU_074889_1_0_1; -.
DR   InParanoid; Q498C8; -.
DR   OMA; WYIVAYS; -.
DR   OrthoDB; 1458086at2759; -.
DR   PhylomeDB; Q498C8; -.
DR   TreeFam; TF300029; -.
DR   PRO; PR:Q498C8; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000014270; Expressed in duodenum and 20 other tissues.
DR   Genevisible; Q498C8; RN.
DR   GO; GO:0009986; C:cell surface; ISO:RGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:GOC.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:RGD.
DR   GO; GO:0030173; C:integral component of Golgi membrane; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR   GO; GO:0033130; F:acetylcholine receptor binding; ISO:RGD.
DR   GO; GO:0007528; P:neuromuscular junction development; ISO:RGD.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; ISO:RGD.
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; Golgi apparatus; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O15258"
FT   CHAIN           2..196
FT                   /note="Protein RER1"
FT                   /id="PRO_0000261128"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:O15258"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O15258"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O15258"
FT   MOD_RES         95
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   196 AA;  22988 MW;  590374BB64FAD85B CRC64;
     MSEGDSVGDS VHGKPSVVYR FFSRLGQIYQ SWLDKSTPYT AVRWVVTLGL SFVYMIRVYL
     LQGWYIVTYA LGIYHLNLFI AFLSPKVDPS LMEDSDDGPS LPTKQNEEFR PFIRRLPEFK
     FWHAATKGIL VAMICTFFEA FNVPVFWPIL VMYFIMLFCI TMKRQIKHMI KYRYIPFTHG
     KRRYKGKEDV GKTFAS
 
 
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