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 27-MAR-2024, entry version 112. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; HE600954; CAP29301.1; -; Genomic_DNA. DR RefSeq; XP_002636809.1; XM_002636763.1. DR AlphaFoldDB; Q61KR9; -. DR SMR; Q61KR9; -. DR STRING; 6238.Q61KR9; -. 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; ESPYHIM; -. DR OrthoDB; 5489154at2759; -. 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: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; 2.60.120.200; -; 1. DR Gene3D; 2.10.250.10; Calreticulin/calnexin, P domain; 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:SF45; CALRETICULIN; 1. DR PANTHER; PTHR11073; CALRETICULIN AND CALNEXIN; 1. DR Pfam; PF00262; Calreticulin; 2. DR PIRSF; PIRSF002356; Calreticulin; 1. DR PRINTS; PR00626; CALRETICULIN. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR SUPFAM; SSF63887; P-domain of calnexin/calreticulin; 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 //