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EMC10_YEAST
ID   EMC10_YEAST             Reviewed;         205 AA.
AC   Q12025; D6VS42;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Endoplasmic reticulum membrane protein complex subunit 10 {ECO:0000303|PubMed:26512320};
DE   Flags: Precursor;
GN   Name=EMC10 {ECO:0000303|PubMed:26512320}; OrderedLocusNames=YDR056C;
GN   ORFNames=D4219;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8789263;
RX   DOI=10.1002/(sici)1097-0061(199601)12:1<85::aid-yea890>3.0.co;2-u;
RA   Brandt P., Ramlow S., Otto B., Bloecker H.;
RT   "Nucleotide sequence analysis of a 32,500 bp region of the right arm of
RT   Saccharomyces cerevisiae chromosome IV.";
RL   Yeast 12:85-90(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   IDENTIFICATION, AND FUNCTION.
RX   PubMed=26512320; DOI=10.12688/f1000research.6944.2;
RA   Wideman J.G.;
RT   "The ubiquitous and ancient ER membrane protein complex (EMC): tether or
RT   not?";
RL   F1000Research 4:624-624(2015).
RN   [8]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=29809151; DOI=10.7554/elife.37018;
RA   Shurtleff M.J., Itzhak D.N., Hussmann J.A., Schirle Oakdale N.T.,
RA   Costa E.A., Jonikas M., Weibezahn J., Popova K.D., Jan C.H., Sinitcyn P.,
RA   Vembar S.S., Hernandez H., Cox J., Burlingame A.L., Brodsky J.L., Frost A.,
RA   Borner G.H., Weissman J.S.;
RT   "The ER membrane protein complex interacts cotranslationally to enable
RT   biogenesis of multipass membrane proteins.";
RL   Elife 7:0-0(2018).
CC   -!- FUNCTION: Part of the endoplasmic reticulum membrane protein complex
CC       (EMC) that enables the energy-independent insertion into endoplasmic
CC       reticulum membranes of newly synthesized membrane proteins
CC       (PubMed:29809151). Preferentially accommodates proteins with
CC       transmembrane domains that are weakly hydrophobic or contain
CC       destabilizing features such as charged and aromatic residues
CC       (PubMed:29809151). Involved in the cotranslational insertion of multi-
CC       pass membrane proteins in which stop-transfer membrane-anchor sequences
CC       become ER membrane spanning helices (PubMed:29809151). It is also
CC       required for the post-translational insertion of tail-anchored/TA
CC       proteins in endoplasmic reticulum membranes. By mediating the proper
CC       cotranslational insertion of N-terminal transmembrane domains in an N-
CC       exo topology, with translocated N-terminus in the lumen of the ER,
CC       controls the topology of multi-pass membrane proteins (By similarity).
CC       {ECO:0000250|UniProtKB:Q5J8M3, ECO:0000269|PubMed:29809151}.
CC   -!- SUBUNIT: Component of the ER membrane protein complex (EMC).
CC       {ECO:0000269|PubMed:29809151, ECO:0000305|PubMed:26512320}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:14562095}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:Q5UCC4}.
CC   -!- MISCELLANEOUS: Present with 1600 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; X84162; CAA58972.1; -; Genomic_DNA.
DR   EMBL; Z49209; CAA89085.1; -; Genomic_DNA.
DR   EMBL; Z74352; CAA98874.1; -; Genomic_DNA.
DR   EMBL; AY557649; AAS55975.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11902.1; -; Genomic_DNA.
DR   PIR; S54040; S54040.
DR   RefSeq; NP_010341.3; NM_001180364.3.
DR   PDB; 6WB9; EM; 3.00 A; 0=1-205.
DR   PDB; 7KRA; EM; 3.20 A; H=1-205.
DR   PDB; 7KTX; EM; 4.30 A; H=1-205.
DR   PDBsum; 6WB9; -.
DR   PDBsum; 7KRA; -.
DR   PDBsum; 7KTX; -.
DR   AlphaFoldDB; Q12025; -.
DR   SMR; Q12025; -.
DR   BioGRID; 32109; 84.
DR   DIP; DIP-5465N; -.
DR   IntAct; Q12025; 8.
DR   MINT; Q12025; -.
DR   STRING; 4932.YDR056C; -.
DR   TCDB; 3.A.27.1.2; the endoplasmic reticulum membrane protein insertion complex (emc) family.
DR   iPTMnet; Q12025; -.
DR   MaxQB; Q12025; -.
DR   PaxDb; Q12025; -.
DR   PRIDE; Q12025; -.
DR   TopDownProteomics; Q12025; -.
DR   EnsemblFungi; YDR056C_mRNA; YDR056C; YDR056C.
DR   GeneID; 851626; -.
DR   KEGG; sce:YDR056C; -.
DR   SGD; S000002463; EMC10.
DR   VEuPathDB; FungiDB:YDR056C; -.
DR   eggNOG; ENOG502S1Z2; Eukaryota.
DR   HOGENOM; CLU_117308_0_0_1; -.
DR   InParanoid; Q12025; -.
DR   OMA; SFIQKNW; -.
DR   BioCyc; YEAST:G3O-29665-MON; -.
DR   PRO; PR:Q12025; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q12025; protein.
DR   GO; GO:0072546; C:EMC complex; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0045050; P:protein insertion into ER membrane by stop-transfer membrane-anchor sequence; IMP:UniProtKB.
PE   1: Evidence at protein level;
KW   3D-structure; Endoplasmic reticulum; Glycoprotein; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..205
FT                   /note="Endoplasmic reticulum membrane protein complex
FT                   subunit 10"
FT                   /id="PRO_0000244437"
FT   TOPO_DOM        18..172
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q5UCC4"
FT   TRANSMEM        173..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        191..205
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q5UCC4"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   STRAND          20..26
FT                   /evidence="ECO:0007829|PDB:6WB9"
FT   STRAND          28..30
FT                   /evidence="ECO:0007829|PDB:6WB9"
FT   STRAND          32..39
FT                   /evidence="ECO:0007829|PDB:6WB9"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:6WB9"
FT   STRAND          51..55
FT                   /evidence="ECO:0007829|PDB:6WB9"
FT   STRAND          62..73
FT                   /evidence="ECO:0007829|PDB:6WB9"
FT   STRAND          74..77
FT                   /evidence="ECO:0007829|PDB:7KRA"
FT   STRAND          79..84
FT                   /evidence="ECO:0007829|PDB:6WB9"
FT   STRAND          90..96
FT                   /evidence="ECO:0007829|PDB:6WB9"
FT   STRAND          102..109
FT                   /evidence="ECO:0007829|PDB:6WB9"
FT   STRAND          117..121
FT                   /evidence="ECO:0007829|PDB:6WB9"
SQ   SEQUENCE   205 AA;  22769 MW;  5B995CE50EF1B725 CRC64;
     MLVRLLRVIL LASMVFCADI LQLSYSDDAK DAIPLGTFEI DSTSDGNVTV TTVNIQDVEV
     SGEYCLNAQI EGKLDMPCFS YMKLRTPLKY DLIVDVDEDN EVKQVSLSYD ETNDAITATV
     RYPEAGPTAP VTKLKKKTKT YADKKASKNK DGSTAQFEED EEVKEVSWFQ KNWKMLLLGL
     LIYNFVAGSA KKQQQGGAGA DQKTE
 
 
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