CALX_CAEBR
ID CALX_CAEBR Reviewed; 623 AA.
AC A8XA40;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 3.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Calnexin {ECO:0000250|UniProtKB:P34652};
DE Flags: Precursor;
GN Name=cnx-1 {ECO:0000312|WormBase:CBG09987}; ORFNames=CBG09987;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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. Required for embryogenesis and larval development
CC under heat and ER stress conditions. May be important for germ cell
CC development. Involved in neuronal necrotic cell death (By similarity).
CC {ECO:0000250|UniProtKB:P27824, ECO:0000250|UniProtKB:P34652}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P27824, ECO:0000250|UniProtKB:P34652}; Single-
CC pass type I membrane protein {ECO:0000250|UniProtKB:P27824,
CC ECO:0000250|UniProtKB:P34652}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P27824, ECO:0000250|UniProtKB:P34652}.
CC Cytoplasmic vesicle {ECO:0000250|UniProtKB:P27824,
CC ECO:0000250|UniProtKB:P34652}.
CC -!- PTM: Glycosylation is important for its biological activity.
CC {ECO:0000250|UniProtKB:P34652}.
CC -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAP29507.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; HE601459; CAP29507.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002641659.1; XM_002641613.1.
DR AlphaFoldDB; A8XA40; -.
DR SMR; A8XA40; -.
DR STRING; 6238.CBG09987; -.
DR EnsemblMetazoa; CBG09987.1; CBG09987.1; WBGene00031476.
DR GeneID; 8583652; -.
DR CTD; 8583652; -.
DR WormBase; CBG09987; CBP08355; WBGene00031476; Cbr-cnx-1.
DR eggNOG; KOG0675; Eukaryota.
DR HOGENOM; CLU_018224_2_1_1; -.
DR InParanoid; A8XA40; -.
DR OrthoDB; 775337at2759; -.
DR Proteomes; UP000008549; Chromosome III.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:EnsemblMetazoa.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IEA:EnsemblMetazoa.
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; 2.
PE 3: Inferred from homology;
KW Calcium; Chaperone; Cytoplasm; Cytoplasmic vesicle; Developmental protein;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Metal-binding; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..623
FT /note="Calnexin"
FT /evidence="ECO:0000255"
FT /id="PRO_0000416936"
FT TRANSMEM 480..500
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 269..281
FT /note="1-1"
FT /evidence="ECO:0000255"
FT REPEAT 286..298
FT /note="1-2"
FT /evidence="ECO:0000255"
FT REPEAT 305..317
FT /note="1-3"
FT /evidence="ECO:0000255"
FT REPEAT 324..336
FT /note="1-4"
FT /evidence="ECO:0000255"
FT REPEAT 339..349
FT /note="2-1"
FT /evidence="ECO:0000255"
FT REPEAT 358..368
FT /note="2-2"
FT /evidence="ECO:0000255"
FT REPEAT 372..382
FT /note="2-3"
FT /evidence="ECO:0000255"
FT REPEAT 386..396
FT /note="2-4"
FT /evidence="ECO:0000255"
FT REGION 260..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..400
FT /note="P domain (Extended arm)"
FT /evidence="ECO:0000250|UniProtKB:P24643"
FT REGION 269..336
FT /note="4 X approximate repeats"
FT /evidence="ECO:0000255"
FT REGION 339..396
FT /note="4 X approximate repeats"
FT /evidence="ECO:0000255"
FT REGION 536..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 108
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P24643"
FT BINDING 155
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 157
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 176
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 183
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 416
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 427
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P24643"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 151..185
FT /evidence="ECO:0000250|UniProtKB:P24643"
FT DISULFID 351..357
FT /evidence="ECO:0000250|UniProtKB:P24643"
SQ SEQUENCE 623 AA; 69593 MW; 7FF3E49D33C01F7B CRC64;
MLNRKWSFVF LTFLLVISVN ANDDVFEDED EASESGVEKD EFVPSNFVAP KLADTSKPNF
FDYFPVGSKI GQTWIKSLAK KDDVDSEIAK YNGEWSIGAP TKVSIEGDYG LIVKTKARHH
AIAAKLETPF VFGSNKFIAQ YDVKFEEGQE CGGGYLKLLS EGAEKDLASF QDKTPYTIMF
GPDKCGASGQ VHLIFRYKNP VNGTVSEYHA KQPASIGTAY WDDHNTHLFT LVVKPTGEYS
VSVDGKSLYY GNMLSDISPS LTPPKEIFDE TDLKPEDWDE REQIEDETAS KPDDWDENEP
QNVVDESATK PYDWNEEENE LIPDPEAQKP QDWDEDMDGS WEAPLIDNPA CKGLSGCGTW
KPPTIKNPKY RGKWVRPKIA NPAYKGKWSP RLIDNPNYFE PKPFDGLAPI SAVGIELWTM
SENILFDNIL ITSSEQDASE IAKQTFYIKQ QEEYRLAAAT GSSNGIFQQI VDATNEKPWL
WAVYILCILL PLIAIGVFCF GKGSKPAPNF AKKSDTYSPD DDRVPNLVDD QEEEIIAEDE
EDNQPGPSGT QNQPPIDEDE QDEVEQQPSS SKTASSESSS AAEEEDNDHV VHENEPVQPT
EEVAKKSPRV TGGAKRRTAR RGD
