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Database: UniProt
Entry: P15253
LinkDB: P15253
Original site: P15253 
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   01-OCT-2014, entry version 118.
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). {ECO:0000250}.
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. Interacts
CC       with PPIB (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P05067:APP (xeno); NbExp=3; IntAct=EBI-9005200, EBI-77613;
CC       P12023:App (xeno); NbExp=2; IntAct=EBI-9005200, EBI-78814;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Sarcoplasmic
CC       reticulum lumen {ECO:0000250}.
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       {ECO:0000250}.
CC   -!- DOMAIN: The interaction with glycans occurs through a binding site
CC       in the globular lectin domain. {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
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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   BioGrid; 1172073; 1.
DR   IntAct; P15253; 4.
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:0005515; F:protein binding; IPI:IntAct.
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; IPR009033; Calreticulin/calnexin_P_dom.
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; 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   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       {ECO:0000269|PubMed:2016321,
FT                                ECO:0000269|PubMed:2241926}.
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      237    270       Interaction with PPIB. {ECO:0000250}.
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.
FT                                {ECO:0000250}.
FT   METAL        62     62       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL        64     64       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       328    328       Calcium. {ECO:0000250}.
FT   BINDING     109    109       Carbohydrate. {ECO:0000250}.
FT   BINDING     111    111       Carbohydrate. {ECO:0000250}.
FT   BINDING     128    128       Carbohydrate. {ECO:0000250}.
FT   BINDING     135    135       Carbohydrate. {ECO:0000250}.
FT   BINDING     317    317       Carbohydrate. {ECO:0000250}.
FT   MOD_RES      48     48       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     159    159       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     209    209       N6-acetyllysine. {ECO:0000250}.
FT   DISULFID    105    137       {ECO:0000250}.
FT   VARIANT      35     35       E -> D.
FT   MUTAGEN     170    170       H->A: Loss of activity.
FT                                {ECO:0000269|PubMed:14522955}.
FT   CONFLICT     90     90       P -> T (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
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
//
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