CALR3_MOUSE
ID CALR3_MOUSE Reviewed; 380 AA.
AC Q9D9Q6; G5E827;
DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Calreticulin-3;
DE AltName: Full=Calreticulin-2;
DE AltName: Full=Calsperin;
DE Flags: Precursor;
GN Name=Calr3; Synonyms=Crt2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=12384296; DOI=10.1016/s0378-1119(02)00880-6;
RA Persson S., Rosenquist M., Sommarin M.;
RT "Identification of a novel calreticulin isoform (Crt2) in human and
RT mouse.";
RL Gene 297:151-158(2002).
RN [5]
RP IDENTIFICATION IN AN EIF2 COMPLEX WITH EIF2S1; EIF2S2; CALR; CELF1; HSPA5
RP AND HSP90B1.
RX PubMed=16931514; DOI=10.1074/jbc.m605701200;
RA Timchenko L.T., Salisbury E., Wang G.-L., Nguyen H., Albrecht J.H.,
RA Hershey J.W., Timchenko N.A.;
RT "Age-specific CUGBP1-eIF2 complex increases translation of CCAAT/enhancer-
RT binding protein beta in old liver.";
RL J. Biol. Chem. 281:32806-32819(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21131354; DOI=10.1074/jbc.m110.140152;
RA Ikawa M., Tokuhiro K., Yamaguchi R., Benham A.M., Tamura T., Wada I.,
RA Satouh Y., Inoue N., Okabe M.;
RT "Calsperin is a testis-specific chaperone required for sperm fertility.";
RL J. Biol. Chem. 286:5639-5646(2011).
CC -!- FUNCTION: CALR3 capacity for calcium-binding may be absent or much
CC lower than that of CALR (By similarity). During spermatogenesis, may
CC act as a lectin-independent chaperone for specific client proteins such
CC as ADAM3. Required for sperm fertility. {ECO:0000250,
CC ECO:0000269|PubMed:21131354}.
CC -!- SUBUNIT: Component of an EIF2 complex at least composed of
CC CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5.
CC {ECO:0000269|PubMed:16931514}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Testis specific, absent in mature sperm.
CC {ECO:0000269|PubMed:12384296, ECO:0000269|PubMed:21131354}.
CC -!- DISRUPTION PHENOTYPE: Defective sperm migration from the uterus into
CC the oviduct and defective binding to the zona pellucida.
CC {ECO:0000269|PubMed:21131354}.
CC -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
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DR EMBL; AK006582; BAB24660.1; -; mRNA.
DR EMBL; AC113182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466525; EDL10797.1; -; Genomic_DNA.
DR CCDS; CCDS22413.1; -.
DR RefSeq; NP_082776.2; NM_028500.3.
DR AlphaFoldDB; Q9D9Q6; -.
DR SMR; Q9D9Q6; -.
DR BioGRID; 215919; 4.
DR DIP; DIP-60025N; -.
DR IntAct; Q9D9Q6; 2.
DR STRING; 10090.ENSMUSP00000019876; -.
DR GlyGen; Q9D9Q6; 2 sites.
DR iPTMnet; Q9D9Q6; -.
DR PhosphoSitePlus; Q9D9Q6; -.
DR PaxDb; Q9D9Q6; -.
DR PeptideAtlas; Q9D9Q6; -.
DR PRIDE; Q9D9Q6; -.
DR ProteomicsDB; 281761; -.
DR Antibodypedia; 66699; 331 antibodies from 28 providers.
DR DNASU; 73316; -.
DR Ensembl; ENSMUST00000019876; ENSMUSP00000019876; ENSMUSG00000019732.
DR GeneID; 73316; -.
DR KEGG; mmu:73316; -.
DR UCSC; uc009mfx.1; mouse.
DR CTD; 125972; -.
DR MGI; MGI:1920566; Calr3.
DR VEuPathDB; HostDB:ENSMUSG00000019732; -.
DR eggNOG; KOG0674; Eukaryota.
DR GeneTree; ENSGT00950000182915; -.
DR HOGENOM; CLU_018224_0_0_1; -.
DR InParanoid; Q9D9Q6; -.
DR OMA; DWPAPML; -.
DR OrthoDB; 822188at2759; -.
DR PhylomeDB; Q9D9Q6; -.
DR TreeFam; TF338438; -.
DR BioGRID-ORCS; 73316; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Calr3; mouse.
DR PRO; PR:Q9D9Q6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9D9Q6; protein.
DR Bgee; ENSMUSG00000019732; Expressed in spermatid and 139 other tissues.
DR ExpressionAtlas; Q9D9Q6; baseline and differential.
DR Genevisible; Q9D9Q6; MM.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0044183; F:protein folding chaperone; IMP:MGI.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
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; 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.
PE 1: Evidence at protein level;
KW Chaperone; Differentiation; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Reference proteome; Repeat; Signal; Spermatogenesis.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..380
FT /note="Calreticulin-3"
FT /id="PRO_0000004179"
FT REPEAT 191..202
FT /note="1-1"
FT REPEAT 209..220
FT /note="1-2"
FT REPEAT 222..231
FT /note="1-3"
FT REPEAT 235..246
FT /note="1-4"
FT REPEAT 250..256
FT /note="2-1"
FT REPEAT 260..268
FT /note="2-2"
FT REPEAT 270..280
FT /note="2-3"
FT REGION 20..197
FT /note="N-domain"
FT REGION 191..246
FT /note="4 X approximate repeats"
FT REGION 198..291
FT /note="P-domain"
FT REGION 250..280
FT /note="3 X approximate repeats"
FT REGION 292..380
FT /note="C-domain"
FT MOTIF 377..380
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT BINDING 109
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 111
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 128
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 135
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 300
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 137..163
FT /evidence="ECO:0000250"
FT CONFLICT 371
FT /note="F -> L (in Ref. 1; BAB24660)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 44232 MW; B13366ADB11B0442 CRC64;
MVSARALLWA ICVLRVALAT VYFQEEFLDG ERWRNRWVQS TNDSQFGHFR VSSGKFYGHK
EKDKGLQTTQ NSRFYAISAS FKPFSNKGKT LVIQYTVKHE QKMDCGGGYI KVFPSDLDQK
KMNGKSQYYI MFGPDICGFD IKKVHVILYF KNQYHENKKP IRCKVDGFTH LYTLILRPDL
SYEVKVDGQS IESGSIEYDW NLTSLRKTEK TSLDSRDWDQ VEGSKVQDWE KHFLDAGASK
PSDWNSELDG DWLQKPPYED GLKAEGIDKD VWLHQKMRPA GYLTQYDLSE FENIGAIGLE
LWQVRSGTIF DNFLITDDEE YAEKFGKATW GETKGPEKEM DAIQAKEEVK KAREEDEEDL
LMGKFHRHNH FSRFHRQGEL
