CALX_CAEEL
ID CALX_CAEEL Reviewed; 619 AA.
AC P34652;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Calnexin;
DE Short=CeCNX-1;
DE Flags: Precursor;
GN Name=cnx-1; ORFNames=ZK632.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, DISRUPTION PHENOTYPE,
RP GLYCOSYLATION AT ASN-203 AND ASN-571, AND MUTAGENESIS OF ASN-203 AND
RP ASN-571.
RC STRAIN=Bristol N2;
RX PubMed=16256074; DOI=10.1016/j.bbrc.2005.10.041;
RA Lee W., Lee T.H., Park B.J., Chang J.W., Yu J.R., Koo H.S., Park H.,
RA Yoo Y.J., Ahnn J.;
RT "Caenorhabditis elegans calnexin is N-glycosylated and required for stress
RT response.";
RL Biochem. Biophys. Res. Commun. 338:1018-1030(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP FUNCTION.
RX PubMed=11580896; DOI=10.1016/s0896-6273(01)00432-9;
RA Xu K., Tavernarakis N., Driscoll M.;
RT "Necrotic cell death in C. elegans requires the function of calreticulin
RT and regulators of Ca(2+) release from the endoplasmic reticulum.";
RL Neuron 31:957-971(2001).
CC -!- FUNCTION: Calcium-binding protein that interacts with newly synthesized
CC monoglucosylated glycoproteins in the endoplasmic reticulum. It may act
CC in assisting protein assembly and/or in the retention within the ER of
CC unassembled protein subunits. It seems to play a major role in the
CC quality control apparatus of the ER by the retention of incorrectly
CC folded proteins (By similarity). Required for embryogenesis and larval
CC development under heat and ER stress conditions. May be important for
CC germ cell development. Involved in neuronal necrotic cell death.
CC {ECO:0000250, ECO:0000269|PubMed:11580896,
CC ECO:0000269|PubMed:16256074}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}. Cytoplasm,
CC perinuclear region {ECO:0000269|PubMed:16256074}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:16256074}. Note=Perinuclear localization in
CC excretory and germ cells. In intestinal cells, clustered signals around
CC vacuoles with vesicles are detected.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously in every blastomere of the
CC embryo up to the gastrulation stage. Expression becomes gradually
CC restricted to the head and tail regions at the comma stage during
CC embryogenesis. During postembryonic development, expressed prominently
CC in the H-shaped excretory cell, in the neurons of head (including ASK
CC and ADL) and tail (including PHA and PHB), in the dorsal and ventral
CC nerve cords, and in the spermatheca. Expressed in the spicules of the
CC male tail (at protein level). {ECO:0000269|PubMed:16256074}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:16256074}.
CC -!- INDUCTION: By stress conditions, such as higher temperature, EGTA, DTT
CC or tunicamycin (at protein level). {ECO:0000269|PubMed:16256074}.
CC -!- PTM: Glycosylation is important for its biological activity.
CC {ECO:0000269|PubMed:16256074}.
CC -!- DISRUPTION PHENOTYPE: Reduced fertility and slowed development.
CC Temperature-sensitive reproduction defects.
CC {ECO:0000269|PubMed:16256074}.
CC -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
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DR EMBL; Z22181; CAA80183.1; -; Genomic_DNA.
DR PIR; S40938; S40938.
DR RefSeq; NP_499176.1; NM_066775.4.
DR AlphaFoldDB; P34652; -.
DR SMR; P34652; -.
DR BioGRID; 41584; 6.
DR DIP; DIP-25990N; -.
DR IntAct; P34652; 2.
DR STRING; 6239.ZK632.6; -.
DR iPTMnet; P34652; -.
DR EPD; P34652; -.
DR PaxDb; P34652; -.
DR PeptideAtlas; P34652; -.
DR EnsemblMetazoa; ZK632.6a.1; ZK632.6a.1; WBGene00000567.
DR GeneID; 176390; -.
DR KEGG; cel:CELE_ZK632.6; -.
DR UCSC; ZK632.6; c. elegans.
DR CTD; 176390; -.
DR WormBase; ZK632.6a; CE00423; WBGene00000567; cnx-1.
DR eggNOG; KOG0675; Eukaryota.
DR InParanoid; P34652; -.
DR OMA; RVGCGEW; -.
DR OrthoDB; 775337at2759; -.
DR PhylomeDB; P34652; -.
DR Reactome; R-CEL-901042; Calnexin/calreticulin cycle.
DR PRO; PR:P34652; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000567; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; P34652; baseline and differential.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:WormBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase.
DR GO; GO:0005509; F:calcium ion binding; IDA:WormBase.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:WormBase.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IEP:WormBase.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
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 Calcium; Chaperone; Cytoplasm; Cytoplasmic vesicle; Developmental protein;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Lectin; Membrane;
KW Metal-binding; Reference proteome; Repeat; Signal; Stress response;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..619
FT /note="Calnexin"
FT /id="PRO_0000004207"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 270..282
FT /note="1-1"
FT REPEAT 287..299
FT /note="1-2"
FT REPEAT 306..318
FT /note="1-3"
FT REPEAT 325..337
FT /note="1-4"
FT REPEAT 340..350
FT /note="2-1"
FT REPEAT 359..369
FT /note="2-2"
FT REPEAT 373..383
FT /note="2-3"
FT REPEAT 387..397
FT /note="2-4"
FT REGION 268..401
FT /note="P domain (Extended arm)"
FT /evidence="ECO:0000250"
FT REGION 270..337
FT /note="4 X approximate repeats"
FT REGION 340..397
FT /note="4 X approximate repeats"
FT REGION 538..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 158
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 177
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 184
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 417
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 428
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16256074"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16256074"
FT DISULFID 152..186
FT /evidence="ECO:0000250"
FT DISULFID 352..358
FT /evidence="ECO:0000250"
FT MUTAGEN 203
FT /note="N->Q: Impairs its biological function; when
FT associated with Q-571."
FT /evidence="ECO:0000269|PubMed:16256074"
FT MUTAGEN 571
FT /note="N->Q: Impairs its biological function; when
FT associated with Q-203."
FT /evidence="ECO:0000269|PubMed:16256074"
SQ SEQUENCE 619 AA; 69208 MW; 08903CE519A75B88 CRC64;
MVNRKWMYIF IQFLLVSSIR SDDDVFEDDE EEVTKGSDDK EEFVPSLFVA PKLSDKSTPN
FFDYFPVGSK IGLTWIKSLA KKDDVDSDIA KYNGEWSIGA PTKVSIEGDL GLIVKTKARH
HAIAAKLNTP FAFDANTFVV QYDIKFEEGQ ECGGGYLKLL SEGAEKDLAN FQDKTAYTIM
FGPDKCGATG KVHLIFRYKN PINGTISEYH ANQPTTIGST YWDDHNTHLF TLVVKPTGEY
SVSVDGKSLY YGNMMSDVTP ALTPPKQIFD ETDLKPVDWD ERENIEDESA VKPDDWDENE
PQSVVDEAAT KPYDWNEEEN ELIADPEAKK PQDWDEDMDG SWEAPLIDNP ACKGLSGCGT
WKAPTIKNPK YKGKWIRPKI SNPAFKGKWT ARLIDNPNYF EPKPFAGLAP ITAVGIEMWT
MSENILFDNI LITSSEEDSS DVAKQTFYVK QKEEYRLAAA TGNGNGFFQQ IIDATNEKPW
LWAVYILCVL LPLVAIGVFC FGKQSKPTPN FAKKSDAYSA DDDRVPNLVD DDEEEIIGDE
EDDVNQPGPS GSQSNPEPQD EEENAEQQSA NSSQSSAAEE EDDEHVVPEN EPVKPTEEFA
KKSPKNTGGA KRRTARRGD
