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Database: UniProt
Entry: P27825
LinkDB: P27825
Original site: P27825 
ID   CALX_YEAST              Reviewed;         502 AA.
AC   P27825; D6VPG1;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   01-OCT-2014, entry version 133.
DE   RecName: Full=Calnexin homolog;
DE   Flags: Precursor;
GN   Name=CNE1; OrderedLocusNames=YAL058W; ORFNames=FUN48;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S288c / GRF88;
RX   PubMed=8465605; DOI=10.1002/yea.320090209;
RA   de Virgilio C., Buerckert N., Neuhaus J.-M., Boller T., Wiemken A.;
RT   "CNE1, a Saccharomyces cerevisiae homologue of the genes encoding
RT   mammalian calnexin and calreticulin.";
RL   Yeast 9:185-188(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7814381; DOI=10.1074/jbc.270.1.244;
RA   Parlati F., Dominguez M., Bergeron J.J.M., Thomas D.Y.;
RT   "Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER)
RT   membrane protein with sequence similarity to calnexin and calreticulin
RT   and functions as a constituent of the ER quality control apparatus.";
RL   J. Biol. Chem. 270:244-253(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA   Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA   Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA   Storms R.K.;
RT   "The nucleotide sequence of chromosome I from Saccharomyces
RT   cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN   [4]
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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
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.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
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.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH MPD1.
RX   PubMed=16002399; DOI=10.1074/jbc.M503377200;
RA   Kimura T., Hosoda Y., Sato Y., Kitamura Y., Ikeda T., Horibe T.,
RA   Kikuchi M.;
RT   "Interactions among yeast protein-disulfide isomerase proteins and
RT   endoplasmic reticulum chaperone proteins influence their activities.";
RL   J. Biol. Chem. 280:31438-31441(2005).
CC   -!- FUNCTION: Interacts with newly synthesized glycoproteins in the
CC       endoplasmic reticulum. It may act in assisting protein assembly
CC       and/or in the retention within the ER of unassembled protein
CC       subunits. It seems to play a major role in the quality control
CC       apparatus of the ER by the retention of incorrectly folded
CC       proteins. {ECO:0000269|PubMed:16002399}.
CC   -!- SUBUNIT: Interacts with MPD1. {ECO:0000269|PubMed:16002399}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC   -!- MISCELLANEOUS: In contrast with other calnexin, yeast CNE1 does
CC       not seem to bind calcium.
CC   -!- MISCELLANEOUS: Present with 4760 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
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DR   EMBL; X66470; CAA47100.1; -; Genomic_DNA.
DR   EMBL; L11012; AAA65967.1; -; Genomic_DNA.
DR   EMBL; U12980; AAC04976.1; -; Genomic_DNA.
DR   EMBL; AY692920; AAT92939.1; -; Genomic_DNA.
DR   EMBL; BK006935; DAA06931.1; -; Genomic_DNA.
DR   PIR; S29347; S29347.
DR   RefSeq; NP_009343.1; NM_001178200.1.
DR   ProteinModelPortal; P27825; -.
DR   SMR; P27825; 33-379.
DR   BioGrid; 31772; 138.
DR   DIP; DIP-4121N; -.
DR   MINT; MINT-532274; -.
DR   STRING; 4932.YAL058W; -.
DR   MaxQB; P27825; -.
DR   PaxDb; P27825; -.
DR   EnsemblFungi; YAL058W; YAL058W; YAL058W.
DR   GeneID; 851241; -.
DR   KEGG; sce:YAL058W; -.
DR   CYGD; YAL058w; -.
DR   SGD; S000000054; CNE1.
DR   eggNOG; NOG305105; -.
DR   GeneTree; ENSGT00430000030841; -.
DR   KO; K08054; -.
DR   OMA; DKITHES; -.
DR   OrthoDB; EOG73V6V4; -.
DR   BioCyc; YEAST:G3O-28861-MONOMER; -.
DR   NextBio; 968171; -.
DR   PRO; PR:P27825; -.
DR   Genevestigator; P27825; -.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:SGD.
DR   GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
DR   GO; GO:0030433; P:ER-associated ubiquitin-dependent protein catabolic process; IMP:SGD.
DR   GO; GO:0006457; P:protein folding; IMP:SGD.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR001580; Calret/calnex.
DR   InterPro; IPR018124; Calret/calnex_CS.
DR   InterPro; IPR009033; Calreticulin/calnexin_P_dom.
DR   InterPro; IPR008985; ConA-like_lec_gl_sf.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   PANTHER; PTHR11073; PTHR11073; 1.
DR   Pfam; PF00262; Calreticulin; 1.
DR   PRINTS; PR00626; CALRETICULIN.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF63887; SSF63887; 1.
DR   PROSITE; PS00803; CALRETICULIN_1; 1.
DR   PROSITE; PS00804; CALRETICULIN_2; 1.
DR   PROSITE; PS00805; CALRETICULIN_REPEAT; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Complete proteome; Disulfide bond; Endoplasmic reticulum;
KW   Glycoprotein; Lectin; Membrane; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    502       Calnexin homolog.
FT                                /FTId=PRO_0000004208.
FT   TOPO_DOM     20    481       Lumenal. {ECO:0000255}.
FT   TRANSMEM    482    502       Helical. {ECO:0000255}.
FT   REPEAT      250    261       1-1.
FT   REPEAT      267    278       1-2.
FT   REPEAT      286    297       1-3.
FT   REPEAT      305    316       1-4.
FT   REPEAT      320    330       2-1.
FT   REPEAT      339    349       2-2.
FT   REPEAT      353    363       2-3.
FT   REPEAT      367    377       2-4.
FT   REGION      248    381       P domain (Extended arm). {ECO:0000250}.
FT   REGION      250    316       4 X approximate repeats.
FT   REGION      320    377       4 X approximate repeats.
FT   BINDING     131    131       Carbohydrate. {ECO:0000250}.
FT   CARBOHYD     25     25       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    104    104       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    296    296       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    416    416       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    425    425       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    125    161       {ECO:0000250}.
FT   DISULFID    332    338       {ECO:0000250}.
SQ   SEQUENCE   502 AA;  56968 MW;  7A99030C147AB2F8 CRC64;
     MKFSAYLWWL FLNLALVKGT SLLSNVTLAE DSFWEHFQAY TNTKHLNQEW ITSEAVNNEG
     SKIYGAQWRL SQGRLQGSAW DKGIAVRTGN AAAMIGHLLE TPINVSETDT LVVQYEIKLD
     NSLTCGGAFI KLMSGFMNVE ALKHYAPDTE GVELVFGPDY CAPEINGVQF AINKVDKITH
     ESKLRYLQEM PLSKLTDTSQ SHLYTLIIDE SAQSFQILID GKTVMVREHI EDKKKVNFEP
     PITPPLMIPD VSVAKPHDWD DRIRIPDPEA VKLSDRDERD PLMIPHPDGT EPPEWNSSIP
     EYILDPNAQK PSWWKELEHG EWIPPMIKNP LCTAERGCGQ QIPGLINNAK YKGPGELNEI
     INPNYMGEWH PPEIENPLYY EEQHPLRIEN VISGVILEFW SGSPNMLISN IYVGKNVTEA
     QIIGNKTWLM RDRAFRGSDG PTERKFMNSR LGNLQTTFHN ERESPNPFDR IIDRILEQPL
     KFVLTAAVVL LTTSVLCCVV FT
//
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