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 29-MAY-2013, entry version 123.
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 204511 / S288c / AB972;
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;
RG Saccharomyces Genome Database;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
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.
CC -!- SUBUNIT: Interacts with MPD1.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type I membrane protein (By similarity).
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.
CC -!- SIMILARITY: Belongs to the calreticulin family.
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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 DIP; DIP-4121N; -.
DR MINT; MINT-532274; -.
DR STRING; 4932.YAL058W; -.
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; WVISELE; -.
DR OrthoDB; EOG4J14J7; -.
DR BioCyc; YEAST:G3O-28861-MONOMER; -.
DR NextBio; 968171; -.
DR Genevestigator; P27825; -.
DR GermOnline; YAL058W; Saccharomyces cerevisiae.
DR GO; GO:0030176; C:integral to endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IMP:SGD.
DR GO; GO:0030433; P:ER-associated 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; SSF63887; Calret_calnex_P; 1.
DR SUPFAM; SSF49899; ConA_like_lec_gl; 2.
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 Potential.
FT CHAIN 20 502 Calnexin homolog.
FT /FTId=PRO_0000004208.
FT TOPO_DOM 20 481 Lumenal (Potential).
FT TRANSMEM 482 502 Helical; (Potential).
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) (By similarity).
FT REGION 250 316 4 X approximate repeats.
FT REGION 320 377 4 X approximate repeats.
FT BINDING 131 131 Carbohydrate (By similarity).
FT CARBOHYD 25 25 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 104 104 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 296 296 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 416 416 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 425 425 N-linked (GlcNAc...) (Potential).
FT DISULFID 125 161 By similarity.
FT DISULFID 332 338 By similarity.
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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