ID CALR_RABIT Reviewed; 418 AA.
AC P15253;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-APR-2013, entry version 113.
DE RecName: Full=Calreticulin;
DE AltName: Full=CRP55;
DE AltName: Full=Calregulin;
DE AltName: Full=Endoplasmic reticulum resident protein 60;
DE Short=ERp60;
DE AltName: Full=HACBP;
DE Flags: Precursor;
GN Name=CALR;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Slow-twitch skeletal muscle;
RX PubMed=2600080;
RA Fliegel L., Burns K., Maclennan D.H., Reithmeier R.A.F., Michalak M.;
RT "Molecular cloning of the high affinity calcium-binding protein
RT (calreticulin) of skeletal muscle sarcoplasmic reticulum.";
RL J. Biol. Chem. 264:21522-21528(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fast-twitch skeletal muscle;
RX PubMed=2059224; DOI=10.1016/0006-291X(91)90634-J;
RA Fliegel L., Michalak M.;
RT "Fast-twitch and slow-twitch skeletal muscles express the same isoform
RT of calreticulin.";
RL Biochem. Biophys. Res. Commun. 177:979-984(1991).
RN [3]
RP PROTEIN SEQUENCE OF 18-36.
RX PubMed=2241926;
RA Treves S., de Mattei M., Lanfredi M., Villa A., Green N.M.,
RA Maclennan D.H., Meldolesi J., Pozzan T.;
RT "Calreticulin is a candidate for a calsequestrin-like function in
RT Ca2(+)-storage compartments (calciosomes) of liver and brain.";
RL Biochem. J. 271:473-480(1990).
RN [4]
RP PROTEIN SEQUENCE OF 18-46.
RX PubMed=2016321;
RA Milner R.E., Baksh S., Shemanko C., Carpenter M.R., Smillie L.,
RA Vance J.E., Opas M., Michalak M.;
RT "Calreticulin, and not calsequestrin, is the major calcium binding
RT protein of smooth muscle sarcoplasmic reticulum and liver endoplasmic
RT reticulum.";
RL J. Biol. Chem. 266:7155-7165(1991).
RN [5]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Lung;
RX PubMed=1911780; DOI=10.1021/bi00105a012;
RA Guan S., Falick A.M., Williams D.E., Cashman J.R.;
RT "Evidence for complex formation between rabbit lung flavin-containing
RT monooxygenase and calreticulin.";
RL Biochemistry 30:9892-9900(1991).
RN [6]
RP FUNCTION.
RX PubMed=10581245; DOI=10.1093/emboj/18.23.6718;
RA Saito Y., Ihara Y., Leach M.R., Cohen-Doyle M.F., Williams D.B.;
RT "Calreticulin functions in vitro as a molecular chaperone for both
RT glycosylated and non-glycosylated proteins.";
RL EMBO J. 18:6718-6729(1999).
RN [7]
RP ZINC-BINDING DOMAIN.
RX PubMed=8521965; DOI=10.1016/0014-5793(95)01246-4;
RA Baksh S., Spamer C., Heilmann C., Michalak M.;
RT "Identification of the Zn2+ binding region in calreticulin.";
RL FEBS Lett. 376:53-57(1995).
RN [8]
RP MUTAGENESIS OF HIS-170.
RX PubMed=14522955; DOI=10.1074/jbc.M309497200;
RA Guo L., Groenendyk J., Papp S., Dabrowska M., Knoblach B., Kay C.,
RA Parker J.M., Opas M., Michalak M.;
RT "Identification of an N-domain histidine essential for chaperone
RT function in calreticulin.";
RL J. Biol. Chem. 278:50645-50653(2003).
CC -!- FUNCTION: Calcium-binding chaperone that promotes folding,
CC oligomeric assembly and quality control in the endoplasmic
CC reticulum (ER) via the calreticulin/calnexin cycle. This lectin
CC interacts transiently with almost all of the monoglucosylated
CC glycoproteins that are synthesized in the ER. Interacts with the
CC DNA-binding domain of NR3C1 and mediates its nuclear export.
CC Involved in maternal gene expression regulation. May participate
CC in oocyte maturation via the regulation of calcium homeostasis (By
CC similarity).
CC -!- SUBUNIT: Monomer. Component of an EIF2 complex at least composed
CC of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5.
CC Interacts with GABARAP, NR3C1, PDIA3/ERp57 and TRIM21 (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Sarcoplasmic
CC reticulum lumen (By similarity).
CC -!- DOMAIN: Can be divided into a N-terminal globular domain, a
CC proline-rich P-domain forming an elongated arm-like structure and
CC a C-terminal acidic domain. The P-domain binds one molecule of
CC calcium with high affinity, whereas the acidic C-domain binds
CC multiple calcium ions with low affinity (By similarity).
CC -!- DOMAIN: The interaction with glycans occurs through a binding site
CC in the globular lectin domain (By similarity).
CC -!- DOMAIN: The zinc binding sites are localized to the N-domain.
CC -!- DOMAIN: Associates with PDIA3 through the tip of the extended arm
CC formed by the P-domain (By similarity).
CC -!- SIMILARITY: Belongs to the calreticulin family.
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DR EMBL; J05138; AAA31188.1; -; mRNA.
DR PIR; A34154; A34154.
DR PIR; C33208; C33208.
DR PIR; D33208; D33208.
DR PIR; S13046; S13046.
DR RefSeq; NP_001075704.1; NM_001082235.1.
DR UniGene; Ocu.1840; -.
DR ProteinModelPortal; P15253; -.
DR SMR; P15253; 206-305.
DR PRIDE; P15253; -.
DR GeneID; 100009050; -.
DR CTD; 811; -.
DR HOVERGEN; HBG005407; -.
DR GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR Gene3D; 2.60.120.200; -; 2.
DR InterPro; IPR001580; Calret/calnex.
DR InterPro; IPR018124; Calret/calnex_CS.
DR InterPro; IPR009169; Calreticulin.
DR InterPro; IPR008985; ConA-like_lec_gl_sf.
DR InterPro; IPR013320; ConA-like_subgrp.
DR PANTHER; PTHR11073; PTHR11073; 1.
DR Pfam; PF00262; Calreticulin; 1.
DR PIRSF; PIRSF002356; Calreticulin; 1.
DR PRINTS; PR00626; CALRETICULIN.
DR SUPFAM; SSF49899; ConA_like_lec_gl; 2.
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 1: Evidence at protein level;
KW Acetylation; Calcium; Chaperone; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Lectin; Metal-binding; Reference proteome; Repeat;
KW Sarcoplasmic reticulum; Signal; Zinc.
FT SIGNAL 1 17
FT CHAIN 18 418 Calreticulin.
FT /FTId=PRO_0000004176.
FT REPEAT 191 202 1-1.
FT REPEAT 210 221 1-2.
FT REPEAT 227 238 1-3.
FT REPEAT 244 255 1-4.
FT REPEAT 259 269 2-1.
FT REPEAT 273 283 2-2.
FT REPEAT 287 297 2-3.
FT REGION 18 197 N-domain.
FT REGION 191 255 4 X approximate repeats.
FT REGION 198 308 P-domain.
FT REGION 259 297 3 X approximate repeats.
FT REGION 309 418 C-domain.
FT MOTIF 415 418 Prevents secretion from ER.
FT COMPBIAS 351 408 Asp/Glu/Lys-rich.
FT METAL 26 26 Calcium; via carbonyl oxygen (By
FT similarity).
FT METAL 62 62 Calcium; via carbonyl oxygen (By
FT similarity).
FT METAL 64 64 Calcium; via carbonyl oxygen (By
FT similarity).
FT METAL 328 328 Calcium (By similarity).
FT BINDING 109 109 Carbohydrate (By similarity).
FT BINDING 111 111 Carbohydrate (By similarity).
FT BINDING 128 128 Carbohydrate (By similarity).
FT BINDING 135 135 Carbohydrate (By similarity).
FT BINDING 317 317 Carbohydrate (By similarity).
FT MOD_RES 48 48 N6-acetyllysine (By similarity).
FT MOD_RES 159 159 N6-acetyllysine (By similarity).
FT MOD_RES 209 209 N6-acetyllysine (By similarity).
FT DISULFID 105 137 By similarity.
FT VARIANT 35 35 E -> D.
FT MUTAGEN 170 170 H->A: Loss of activity.
FT CONFLICT 90 90 P -> T (in Ref. 5; AA sequence).
SQ SEQUENCE 418 AA; 48275 MW; B6082B689DC763A6 CRC64;
MLLPVPLLLG LLGLAAAEPV VYFKEQFLDG DGWTERWIES KHKSDFGKFV LSSGKFYGDQ
EKDKGLQTSQ DARFYALSAR FEPFSNKGQP LVVQFTVKHE QNIDCGGGYV KLFPAGLDQK
DMHGDSEYNI MFGPDICGPG TKKVHVIFNY KGKNVLINKD IRCKDDEFTH LYTLIVRPDN
TYEVKIDNSQ VESGSLEDDW DFLPPKKIKD PDASKPEDWD ERAKIDDPTD SKPEDWDKPE
HIPDPDAKKP EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPDYKGTWI HPEIDNPEYS
PDANIYAYDS FAVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT KTAEKQMKDK
QDEEQRLKEE EEEKKRKEEE EAEEDEEDKD DKEDEDEDEE DKDEEEEEAA AGQAKDEL
//
