CNE1/YAL058W Protein Information

Standard Name	Cne1p
Systematic Name	Yal058wp
Alias	Fun48p
ORF Classification	Verified
Description	Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast (1, 2, 3, 4)
Name Description	CalNExin and calreticulin homolog

Experimental Data
Molecules/cell	4760 5

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	502
Molecular Weight (Da)	56,967
Isoelectric Point (pI)	5.04

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Cne1p (InterPro)
Transmembrane Domains	There are 1 total predicted transmembrane domains (TMHMM)
Signal Peptide(s)	There are 1 total predicted predicted signal peptide(s) (SignalP)
Physical Interactions	There are 3 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI0000126E86 \| P27825 MIPS: YAL058W NCBI: 115549 \| 171153 \| 51013291 \| 5511 \| 595528 \| 6319260 \| NP_009343.1 GenBank/EMBL/DDBJ: DAA06931.1 \| AY692920 \| L11012 \| U12980 \| X66470

Amino Acid Sequence (or in FASTA format)
1 MKFSAYLWWL FLNLALVKGT SLLSNVTLAE DSFWEHFQAY TNTKHLNQEW 51 ITSEAVNNEG SKIYGAQWRL SQGRLQGSAW DKGIAVRTGN AAAMIGHLLE 101 TPINVSETDT LVVQYEIKLD NSLTCGGAFI KLMSGFMNVE ALKHYAPDTE 151 GVELVFGPDY CAPEINGVQF AINKVDKITH ESKLRYLQEM PLSKLTDTSQ 201 SHLYTLIIDE SAQSFQILID GKTVMVREHI EDKKKVNFEP PITPPLMIPD 251 VSVAKPHDWD DRIRIPDPEA VKLSDRDERD PLMIPHPDGT EPPEWNSSIP 301 EYILDPNAQK PSWWKELEHG EWIPPMIKNP LCTAERGCGQ QIPGLINNAK 351 YKGPGELNEI INPNYMGEWH PPEIENPLYY EEQHPLRIEN VISGVILEFW 401 SGSPNMLISN IYVGKNVTEA QIIGNKTWLM RDRAFRGSDG PTERKFMNSR 451 LGNLQTTFHN ERESPNPFDR IIDRILEQPL KFVLTAAVVL LTTSVLCCVV 501 FT*

Amino Acid Sequence (or in FASTA format)

       1  MKFSAYLWWL FLNLALVKGT SLLSNVTLAE DSFWEHFQAY TNTKHLNQEW
      51  ITSEAVNNEG SKIYGAQWRL SQGRLQGSAW DKGIAVRTGN AAAMIGHLLE
     101  TPINVSETDT LVVQYEIKLD NSLTCGGAFI KLMSGFMNVE ALKHYAPDTE
     151  GVELVFGPDY CAPEINGVQF AINKVDKITH ESKLRYLQEM PLSKLTDTSQ
     201  SHLYTLIIDE SAQSFQILID GKTVMVREHI EDKKKVNFEP PITPPLMIPD
     251  VSVAKPHDWD DRIRIPDPEA VKLSDRDERD PLMIPHPDGT EPPEWNSSIP
     301  EYILDPNAQK PSWWKELEHG EWIPPMIKNP LCTAERGCGQ QIPGLINNAK
     351  YKGPGELNEI INPNYMGEWH PPEIENPLYY EEQHPLRIEN VISGVILEFW
     401  SGSPNMLISN IYVGKNVTEA QIIGNKTWLM RDRAFRGSDG PTERKFMNSR
     451  LGNLQTTFHN ERESPNPFDR IIDRILEQPL KFVLTAAVVL LTTSVLCCVV
     501  FT*

external links for Cne1p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	YPL+
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YeastGFP
YGOB	BioPIXIE	MIPS	YeastRC Public Image Repository
YOGY	CYC2008 (complexes)	Pfam domains
	Complexome	YeastRC Structure Prediction (Seattle)
	DIP
	GeneMANIA

References cited on this page View Complete Literature Guide for Cne1p

1)	Parlati F, et al. (1995) Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus. J Biol Chem 270(1):244-53
2)	Xu X, et al. (2004) Expression and characterization of Saccharomyces cerevisiae Cne1p, a calnexin homologue. J Biochem 135(5):615-8
3)	Xu X, et al. (2004) P-domain and lectin site are involved in the chaperone function of Saccharomyces cerevisiae calnexin homologue. FEBS Lett 570(1-3):155-60
4)	Kimura T, et al. (2005) Interactions among Yeast Protein-Disulfide Isomerase Proteins and Endoplasmic Reticulum Chaperone Proteins Influence Their Activities. J Biol Chem 280(36):31438-41
5)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41