CALX_YEAST
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 03-AUG-2022, entry version 183.
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; Saccharomycetes;
OC 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 mammalian
RT 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 and
RT 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 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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and 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., 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 [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 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 monoglucosylated
CC glycoproteins in the endoplasmic reticulum. It may act in assisting
CC protein assembly and/or in the retention within the ER of unassembled
CC protein subunits. It seems to play a major role in the quality control
CC apparatus of the ER by the retention of incorrectly folded proteins.
CC {ECO:0000269|PubMed:16002399}.
CC -!- SUBUNIT: Interacts with MPD1. {ECO:0000269|PubMed:16002399}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}.
CC -!- MISCELLANEOUS: In contrast with other calnexin, yeast CNE1 does not
CC seem to bind calcium.
CC -!- MISCELLANEOUS: Present with 4760 molecules/cell in log phase SD medium.
CC {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 AlphaFoldDB; P27825; -.
DR SMR; P27825; -.
DR BioGRID; 31772; 201.
DR DIP; DIP-4121N; -.
DR STRING; 4932.YAL058W; -.
DR MaxQB; P27825; -.
DR PaxDb; P27825; -.
DR PRIDE; P27825; -.
DR TopDownProteomics; P27825; -.
DR EnsemblFungi; YAL058W_mRNA; YAL058W; YAL058W.
DR GeneID; 851241; -.
DR KEGG; sce:YAL058W; -.
DR SGD; S000000054; CNE1.
DR VEuPathDB; FungiDB:YAL058W; -.
DR eggNOG; KOG0675; Eukaryota.
DR GeneTree; ENSGT00950000182915; -.
DR HOGENOM; CLU_018224_1_2_1; -.
DR InParanoid; P27825; -.
DR OMA; SGCGKWE; -.
DR BioCyc; YEAST:G3O-28861-MON; -.
DR Reactome; R-SCE-901042; Calnexin/calreticulin cycle.
DR PRO; PR:P27825; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P27825; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
DR GO; GO:0006457; P:protein folding; IMP:SGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
DR Gene3D; 2.10.250.10; -; 1.
DR InterPro; IPR001580; Calret/calnex.
DR InterPro; IPR018124; Calret/calnex_CS.
DR InterPro; IPR009033; Calreticulin/calnexin_P_dom_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Lectin;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..502
FT /note="Calnexin homolog"
FT /id="PRO_0000004208"
FT TOPO_DOM 20..481
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 250..261
FT /note="1-1"
FT REPEAT 267..278
FT /note="1-2"
FT REPEAT 286..297
FT /note="1-3"
FT REPEAT 305..316
FT /note="1-4"
FT REPEAT 320..330
FT /note="2-1"
FT REPEAT 339..349
FT /note="2-2"
FT REPEAT 353..363
FT /note="2-3"
FT REPEAT 367..377
FT /note="2-4"
FT REGION 248..381
FT /note="P domain (Extended arm)"
FT /evidence="ECO:0000250"
FT REGION 250..316
FT /note="4 X approximate repeats"
FT REGION 320..377
FT /note="4 X approximate repeats"
FT BINDING 131
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 159
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 398
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 125..161
FT /evidence="ECO:0000250"
FT DISULFID 332..338
FT /evidence="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
