ID   CALR_PELLE              Reviewed;          13 AA.
AC   P31832;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   07-APR-2021, entry version 58.
DE   RecName: Full=Calreticulin;
DE   AltName: Full=Major microsomal calcium-binding protein;
DE   Flags: Fragment;
OS   Pelophylax lessonae (Pool frog) (Rana lessonae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX   NCBI_TaxID=45623;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Brain;
RX   PubMed=2018493; DOI=10.1016/0006-291x(91)91584-y;
RA   Treveso S., Zorzato F., Chiozzi P., Melandri P., Volpe P., Pozzan T.;
RT   "Frog brain expresses a 60 KDa Ca2+ binding protein similar to mammalian
RT   calreticulin.";
RL   Biochem. Biophys. Res. Commun. 175:444-450(1991).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC   -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
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DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Calcium; Chaperone; Direct protein sequencing; Endoplasmic reticulum;
KW   Lectin; Metal-binding; Zinc.
FT   CHAIN           1..>13
FT                   /note="Calreticulin"
FT                   /id="PRO_0000208522"
FT   NON_TER         13
SQ   SEQUENCE   13 AA;  1515 MW;  D0F62AD09EAEE339 CRC64;
     DPLVFFKXXF XXG