CALR_CAEBR
ID CALR_CAEBR Reviewed; 396 AA.
AC Q61KR9; A8X9I9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Calreticulin;
DE Flags: Precursor;
GN Name=crt-1; ORFNames=CBG09253;
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: Molecular calcium-binding chaperone promoting folding,
CC oligomeric assembly and quality control in the ER via the
CC calreticulin/calnexin cycle. This lectin may interact transiently with
CC almost all of the monoglucosylated glycoproteins that are synthesized
CC in the ER. Probably by controlling the folding of extracellular matrix
CC protein unc-52/Perlecan, may play a role in the formation of fibrous
CC organelles, a hemidesmosome-like structure attaching muscles to the
CC epidermis. Protects dopaminergic neurons against oxidative stress-
CC induced neurodegeneration (By similarity).
CC {ECO:0000250|UniProtKB:P14211, ECO:0000250|UniProtKB:P27798}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- DOMAIN: Can be divided into a N-terminal globular domain, a proline-
CC rich P-domain forming an elongated arm-like structure and a C-terminal
CC acidic domain. The P-domain binds one molecule of calcium with high
CC affinity, whereas the acidic C-domain binds multiple calcium ions with
CC low affinity (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The interaction with glycans occurs through a binding site in
CC the globular lectin domain. {ECO:0000250}.
CC -!- DOMAIN: The zinc binding sites are localized to the N-domain.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
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DR EMBL; HE600954; CAP29301.1; -; Genomic_DNA.
DR RefSeq; XP_002636809.1; XM_002636763.1.
DR AlphaFoldDB; Q61KR9; -.
DR SMR; Q61KR9; -.
DR STRING; 6238.CBG09253; -.
DR EnsemblMetazoa; CBG09253.1; CBG09253.1; WBGene00030869.
DR GeneID; 8578804; -.
DR KEGG; cbr:CBG_09253; -.
DR CTD; 8578804; -.
DR WormBase; CBG09253; CBP02265; WBGene00030869; Cbr-crt-1.
DR eggNOG; KOG0674; Eukaryota.
DR HOGENOM; CLU_018224_0_2_1; -.
DR InParanoid; Q61KR9; -.
DR OMA; DANEVSH; -.
DR OrthoDB; 822188at2759; -.
DR Proteomes; UP000008549; Chromosome V.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
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; IEA:InterPro.
DR GO; GO:0030421; P:defecation; IEA:EnsemblMetazoa.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:EnsemblMetazoa.
DR GO; GO:0031581; P:hemidesmosome assembly; IEA:EnsemblMetazoa.
DR GO; GO:0048609; P:multicellular organismal reproductive process; IEA:EnsemblMetazoa.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IEA:EnsemblMetazoa.
DR GO; GO:0012501; P:programmed cell death; IEA:EnsemblMetazoa.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IEA:EnsemblMetazoa.
DR GO; GO:0045471; P:response to ethanol; IEA:EnsemblMetazoa.
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; IPR009169; Calreticulin.
DR InterPro; IPR009033; Calreticulin/calnexin_P_dom_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR PANTHER; PTHR11073; PTHR11073; 1.
DR Pfam; PF00262; Calreticulin; 2.
DR PIRSF; PIRSF002356; 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; 3.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 3: Inferred from homology;
KW Calcium; Chaperone; Disulfide bond; Endoplasmic reticulum; Lectin;
KW Metal-binding; Reference proteome; Repeat; Signal; Zinc.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..396
FT /note="Calreticulin"
FT /id="PRO_0000246154"
FT REPEAT 186..197
FT /note="1-1"
FT REPEAT 205..216
FT /note="1-2"
FT REPEAT 222..233
FT /note="1-3"
FT REPEAT 239..250
FT /note="1-4"
FT REPEAT 254..264
FT /note="2-1"
FT REPEAT 268..278
FT /note="2-2"
FT REPEAT 282..292
FT /note="2-3"
FT REGION 186..250
FT /note="4 X approximate repeats"
FT REGION ?..192
FT /note="N-domain"
FT REGION 193..301
FT /note="P-domain"
FT REGION 202..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..292
FT /note="3 X approximate repeats"
FT REGION 302..396
FT /note="C-domain"
FT REGION 342..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 393..396
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 202..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..396
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 105
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 107
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 124
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 131
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 312
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT DISULFID 101..133
FT /evidence="ECO:0000250"
SQ SEQUENCE 396 AA; 45809 MW; CE7E53118485EFF7 CRC64;
MKSLCLLAIV AVVSAEVYFK EEFNDASWEK RWVQSKHKDD FGAFKLSAGK FFDVESRDQG
IQTSQDAKFY SRAAKFDKEF SNKGKTLVIQ YTVKHEQGID CGGGYVKVMR GDADLADFHG
ETPYNVMFGP DICGPTRRVH VILNYKGENK LIKKEITCKS DELTHLYTLI LNADNTYEVK
IDGESAQTGS LEEDWDLLPA KKIKDPDAKK PEDWDEREYI DDAEDVKPED WEKPEHIPDP
DAKKPEDWDD EMDGEWEPPM IDNPEYKGEW KPKQIKNPAY KGKWIHPEIE NPEYTPDDEL
YLYENWGAIG FDLWQVKSGT IFDNVLITDS VEEAEAHAAE TFDKLKTVEK EKKEKADEEA
RKVEEEARKK AEEEKEAKKD DDEEEEKEEE EGHDEL
