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Protein

Calreticulin-3

Gene

Calr3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

CALR3 capacity for calcium-binding may be absent or much lower than that of CALR (By similarity). During spermatogenesis, may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Required for sperm fertility.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei109 – 1091CarbohydrateBy similarity
Binding sitei111 – 1111CarbohydrateBy similarity
Binding sitei128 – 1281CarbohydrateBy similarity
Binding sitei135 – 1351CarbohydrateBy similarity
Binding sitei300 – 3001CarbohydrateBy similarity

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • protein binding involved in protein folding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Differentiation, Spermatogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Calreticulin-3
Alternative name(s):
Calreticulin-2
Calsperin
Gene namesi
Name:Calr3
Synonyms:Crt2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1920566. Calr3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Disruption phenotypei

Defective sperm migration from the uterus into the oviduct and defective binding to the zona pellucida.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 380361Calreticulin-3PRO_0000004179Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi42 – 421N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi137 ↔ 163By similarity
Glycosylationi201 – 2011N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9D9Q6.
PRIDEiQ9D9Q6.

PTM databases

PhosphoSiteiQ9D9Q6.

Expressioni

Tissue specificityi

Testis specific, absent in mature sperm.2 Publications

Gene expression databases

CleanExiMM_CALR3.
ExpressionAtlasiQ9D9Q6. baseline and differential.
GenevestigatoriQ9D9Q6.

Interactioni

Subunit structurei

Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5.1 Publication

Protein-protein interaction databases

DIPiDIP-60025N.

Structurei

3D structure databases

ProteinModelPortaliQ9D9Q6.
SMRiQ9D9Q6. Positions 21-348.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati191 – 202121-1Add
BLAST
Repeati209 – 220121-2Add
BLAST
Repeati222 – 231101-3
Repeati235 – 246121-4Add
BLAST
Repeati250 – 25672-1
Repeati260 – 26892-2
Repeati270 – 280112-3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 197178N-domainAdd
BLAST
Regioni191 – 246564 X approximate repeatsAdd
BLAST
Regioni198 – 29194P-domainAdd
BLAST
Regioni250 – 280313 X approximate repeatsAdd
BLAST
Regioni292 – 38089C-domainAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi377 – 3804Prevents secretion from ERSequence Analysis

Sequence similaritiesi

Belongs to the calreticulin family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG268919.
GeneTreeiENSGT00430000030841.
HOGENOMiHOG000192435.
HOVERGENiHBG005407.
InParanoidiQ9D9Q6.
KOiK10098.
OMAiQDWEKHF.
OrthoDBiEOG77126Z.
TreeFamiTF338438.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009169. Calreticulin.
IPR009033. Calreticulin/calnexin_P_dom.
IPR013320. ConA-like_dom.
[Graphical view]
PANTHERiPTHR11073. PTHR11073. 1 hit.
PfamiPF00262. Calreticulin. 1 hit.
[Graphical view]
PIRSFiPIRSF002356. Calreticulin. 1 hit.
PRINTSiPR00626. CALRETICULIN.
SUPFAMiSSF49899. SSF49899. 2 hits.
SSF63887. SSF63887. 1 hit.
PROSITEiPS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D9Q6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSARALLWA ICVLRVALAT VYFQEEFLDG ERWRNRWVQS TNDSQFGHFR
60 70 80 90 100
VSSGKFYGHK EKDKGLQTTQ NSRFYAISAS FKPFSNKGKT LVIQYTVKHE
110 120 130 140 150
QKMDCGGGYI KVFPSDLDQK KMNGKSQYYI MFGPDICGFD IKKVHVILYF
160 170 180 190 200
KNQYHENKKP IRCKVDGFTH LYTLILRPDL SYEVKVDGQS IESGSIEYDW
210 220 230 240 250
NLTSLRKTEK TSLDSRDWDQ VEGSKVQDWE KHFLDAGASK PSDWNSELDG
260 270 280 290 300
DWLQKPPYED GLKAEGIDKD VWLHQKMRPA GYLTQYDLSE FENIGAIGLE
310 320 330 340 350
LWQVRSGTIF DNFLITDDEE YAEKFGKATW GETKGPEKEM DAIQAKEEVK
360 370 380
KAREEDEEDL LMGKFHRHNH FSRFHRQGEL
Length:380
Mass (Da):44,232
Last modified:October 3, 2012 - v2
Checksum:iB13366ADB11B0442
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti371 – 3711F → L in BAB24660 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK006582 mRNA. Translation: BAB24660.1.
AC113182 Genomic DNA. No translation available.
CH466525 Genomic DNA. Translation: EDL10797.1.
CCDSiCCDS22413.1.
RefSeqiNP_082776.2. NM_028500.3.
UniGeneiMm.196315.

Genome annotation databases

EnsembliENSMUST00000019876; ENSMUSP00000019876; ENSMUSG00000019732.
GeneIDi73316.
KEGGimmu:73316.
UCSCiuc009mfx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK006582 mRNA. Translation: BAB24660.1.
AC113182 Genomic DNA. No translation available.
CH466525 Genomic DNA. Translation: EDL10797.1.
CCDSiCCDS22413.1.
RefSeqiNP_082776.2. NM_028500.3.
UniGeneiMm.196315.

3D structure databases

ProteinModelPortaliQ9D9Q6.
SMRiQ9D9Q6. Positions 21-348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60025N.

PTM databases

PhosphoSiteiQ9D9Q6.

Proteomic databases

PaxDbiQ9D9Q6.
PRIDEiQ9D9Q6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019876; ENSMUSP00000019876; ENSMUSG00000019732.
GeneIDi73316.
KEGGimmu:73316.
UCSCiuc009mfx.1. mouse.

Organism-specific databases

CTDi125972.
MGIiMGI:1920566. Calr3.

Phylogenomic databases

eggNOGiNOG268919.
GeneTreeiENSGT00430000030841.
HOGENOMiHOG000192435.
HOVERGENiHBG005407.
InParanoidiQ9D9Q6.
KOiK10098.
OMAiQDWEKHF.
OrthoDBiEOG77126Z.
TreeFamiTF338438.

Miscellaneous databases

NextBioi337937.
PROiQ9D9Q6.
SOURCEiSearch...

Gene expression databases

CleanExiMM_CALR3.
ExpressionAtlasiQ9D9Q6. baseline and differential.
GenevestigatoriQ9D9Q6.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009169. Calreticulin.
IPR009033. Calreticulin/calnexin_P_dom.
IPR013320. ConA-like_dom.
[Graphical view]
PANTHERiPTHR11073. PTHR11073. 1 hit.
PfamiPF00262. Calreticulin. 1 hit.
[Graphical view]
PIRSFiPIRSF002356. Calreticulin. 1 hit.
PRINTSiPR00626. CALRETICULIN.
SUPFAMiSSF49899. SSF49899. 2 hits.
SSF63887. SSF63887. 1 hit.
PROSITEiPS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Identification of a novel calreticulin isoform (Crt2) in human and mouse."
    Persson S., Rosenquist M., Sommarin M.
    Gene 297:151-158(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, TISSUE SPECIFICITY.
  5. "Age-specific CUGBP1-eIF2 complex increases translation of CCAAT/enhancer-binding protein beta in old liver."
    Timchenko L.T., Salisbury E., Wang G.-L., Nguyen H., Albrecht J.H., Hershey J.W., Timchenko N.A.
    J. Biol. Chem. 281:32806-32819(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN AN EIF2 COMPLEX WITH EIF2S1; EIF2S2; CALR; CELF1; HSPA5 AND HSP90B1.
  6. "Calsperin is a testis-specific chaperone required for sperm fertility."
    Ikawa M., Tokuhiro K., Yamaguchi R., Benham A.M., Tamura T., Wada I., Satouh Y., Inoue N., Okabe M.
    J. Biol. Chem. 286:5639-5646(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiCALR3_MOUSE
AccessioniPrimary (citable) accession number: Q9D9Q6
Secondary accession number(s): G5E827
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2003
Last sequence update: October 3, 2012
Last modified: January 7, 2015
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.