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Q96L12

- CALR3_HUMAN

UniProt

Q96L12 - CALR3_HUMAN

Protein

Calreticulin-3

Gene

CALR3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    During spermatogenesis, may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Required for sperm fertility By similarity. CALR3 capacity for calcium-binding may be absent or much lower than that of CALR.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 sitei303 – 3031CarbohydrateBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. protein folding Source: InterPro
    3. spermatogenesis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Differentiation, Spermatogenesis

    Keywords - Ligandi

    Lectin, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calreticulin-3
    Alternative name(s):
    Calreticulin-2
    Calsperin
    Gene namesi
    Name:CALR3
    Synonyms:CRT2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:20407. CALR3.

    Subcellular locationi

    Endoplasmic reticulum lumen 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Involvement in diseasei

    Cardiomyopathy, familial hypertrophic 19 (CMH19) [MIM:613875]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti82 – 821K → R in CMH19. 1 Publication
    VAR_065476

    Keywords - Diseasei

    Cardiomyopathy, Disease mutation

    Organism-specific databases

    MIMi613875. phenotype.
    Orphaneti155. Familial isolated hypertrophic cardiomyopathy.
    PharmGKBiPA134922944.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 384365Calreticulin-3PRO_0000004178Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi42 – 421N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi105 ↔ 137By similarity
    Glycosylationi201 – 2011N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ96L12.
    PRIDEiQ96L12.

    PTM databases

    PhosphoSiteiQ96L12.

    Expressioni

    Tissue specificityi

    Testis specific.1 Publication

    Gene expression databases

    BgeeiQ96L12.
    CleanExiHS_CALR3.
    GenevestigatoriQ96L12.

    Organism-specific databases

    HPAiCAB025749.
    HPA043355.
    HPA048460.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi125941. 1 interaction.
    STRINGi9606.ENSP00000269881.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96L12.
    SMRiQ96L12. Positions 21-351.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati191 – 202121-1Add
    BLAST
    Repeati208 – 219121-2Add
    BLAST
    Repeati221 – 230101-3
    Repeati234 – 245121-4Add
    BLAST
    Repeati249 – 259112-1Add
    BLAST
    Repeati263 – 27192-2
    Repeati273 – 283112-3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni20 – 197178N-domainAdd
    BLAST
    Regioni191 – 245554 X approximate repeatsAdd
    BLAST
    Regioni198 – 29497P-domainAdd
    BLAST
    Regioni249 – 283353 X approximate repeatsAdd
    BLAST
    Regioni295 – 38490C-domainAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi381 – 3844Prevents secretion from ERPROSITE-ProRule annotation

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi337 – 36226Glu/Lys-richAdd
    BLAST

    Domaini

    Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity By similarity.By similarity
    The interaction with glycans occurs through a binding site in the globular lectin domain.By similarity
    The zinc binding sites are localized to the N-domain.By similarity

    Sequence similaritiesi

    Belongs to the calreticulin family.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG268919.
    HOGENOMiHOG000192435.
    HOVERGENiHBG005407.
    InParanoidiQ96L12.
    KOiK10098.
    OMAiQDWEKHF.
    OrthoDBiEOG77126Z.
    PhylomeDBiQ96L12.
    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.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    [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.
    PS00014. ER_TARGET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q96L12-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARALVQLWA ICMLRVALAT VYFQEEFLDG EHWRNRWLQS TNDSRFGHFR    50
    LSSGKFYGHK EKDKGLQTTQ NGRFYAISAR FKPFSNKGKT LVIQYTVKHE 100
    QKMDCGGGYI KVFPADIDQK NLNGKSQYYI MFGPDICGFD IKKVHVILHF 150
    KNKYHENKKL IRCKVDGFTH LYTLILRPDL SYDVKIDGQS IESGSIEYDW 200
    NLTSLKKETS PAESKDWEQT KDNKAQDWEK HFLDASTSKQ SDWNGDLDGD 250
    WPAPMLQKPP YQDGLKPEGI HKDVWLHRKM KNTDYLTQYD LSEFENIGAI 300
    GLELWQVRSG TIFDNFLITD DEEYADNFGK ATWGETKGPE REMDAIQAKE 350
    EMKKAREEEE EELLSGKINR HEHYFNQFHR RNEL 384
    Length:384
    Mass (Da):44,996
    Last modified:October 17, 2006 - v2
    Checksum:i32D8AFB23D1DF7C5
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti8 – 81L → F.1 Publication
    Corresponds to variant rs11544148 [ dbSNP | Ensembl ].
    VAR_027944
    Natural varianti82 – 821K → R in CMH19. 1 Publication
    VAR_065476
    Natural varianti248 – 2481D → G.
    Corresponds to variant rs10411092 [ dbSNP | Ensembl ].
    VAR_027945
    Natural varianti274 – 2741V → I.
    Corresponds to variant rs12459238 [ dbSNP | Ensembl ].
    VAR_027946
    Natural varianti284 – 2841D → N.
    Corresponds to variant rs10404156 [ dbSNP | Ensembl ].
    VAR_048589

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB576176 mRNA. Translation: BAJ14705.1.
    AK058084 mRNA. Translation: BAB71655.1.
    AC008764 Genomic DNA. No translation available.
    CH471106 Genomic DNA. Translation: EAW84546.1.
    BC014595 mRNA. Translation: AAH14595.1.
    CCDSiCCDS12344.1.
    RefSeqiNP_659483.2. NM_145046.4.
    UniGeneiHs.304020.

    Genome annotation databases

    EnsembliENST00000269881; ENSP00000269881; ENSG00000269058.
    GeneIDi125972.
    KEGGihsa:125972.
    UCSCiuc002ned.3. human.

    Polymorphism databases

    DMDMi116241279.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB576176 mRNA. Translation: BAJ14705.1 .
    AK058084 mRNA. Translation: BAB71655.1 .
    AC008764 Genomic DNA. No translation available.
    CH471106 Genomic DNA. Translation: EAW84546.1 .
    BC014595 mRNA. Translation: AAH14595.1 .
    CCDSi CCDS12344.1.
    RefSeqi NP_659483.2. NM_145046.4.
    UniGenei Hs.304020.

    3D structure databases

    ProteinModelPortali Q96L12.
    SMRi Q96L12. Positions 21-351.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125941. 1 interaction.
    STRINGi 9606.ENSP00000269881.

    PTM databases

    PhosphoSitei Q96L12.

    Polymorphism databases

    DMDMi 116241279.

    Proteomic databases

    PaxDbi Q96L12.
    PRIDEi Q96L12.

    Protocols and materials databases

    DNASUi 125972.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000269881 ; ENSP00000269881 ; ENSG00000269058 .
    GeneIDi 125972.
    KEGGi hsa:125972.
    UCSCi uc002ned.3. human.

    Organism-specific databases

    CTDi 125972.
    GeneCardsi GC19M016589.
    H-InvDB HIX0080124.
    HGNCi HGNC:20407. CALR3.
    HPAi CAB025749.
    HPA043355.
    HPA048460.
    MIMi 611414. gene.
    613875. phenotype.
    neXtProti NX_Q96L12.
    Orphaneti 155. Familial isolated hypertrophic cardiomyopathy.
    PharmGKBi PA134922944.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG268919.
    HOGENOMi HOG000192435.
    HOVERGENi HBG005407.
    InParanoidi Q96L12.
    KOi K10098.
    OMAi QDWEKHF.
    OrthoDBi EOG77126Z.
    PhylomeDBi Q96L12.
    TreeFami TF338438.

    Miscellaneous databases

    GenomeRNAii 125972.
    NextBioi 81602.
    PROi Q96L12.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q96L12.
    CleanExi HS_CALR3.
    Genevestigatori Q96L12.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    InterProi IPR001580. Calret/calnex.
    IPR018124. Calret/calnex_CS.
    IPR009169. Calreticulin.
    IPR009033. Calreticulin/calnexin_P_dom.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    [Graphical view ]
    PANTHERi PTHR11073. PTHR11073. 1 hit.
    Pfami PF00262. Calreticulin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002356. Calreticulin. 1 hit.
    PRINTSi PR00626. CALRETICULIN.
    SUPFAMi SSF49899. SSF49899. 2 hits.
    SSF63887. SSF63887. 1 hit.
    PROSITEi PS00803. CALRETICULIN_1. 1 hit.
    PS00804. CALRETICULIN_2. 1 hit.
    PS00014. ER_TARGET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Calreticulin-2 is localized in the lumen of the endoplasmic reticulum but is not a Ca2+ -binding protein."
      Nomura R., Orii M., Senda T.
      Histochem. Cell Biol. 135:531-538(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, LACK OF CALCIUM-BINDING.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PHE-8.
      Tissue: Testis.
    6. "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.
    7. "Genetic screening of calcium regulation genes in familial hypertrophic cardiomyopathy."
      Chiu C., Tebo M., Ingles J., Yeates L., Arthur J.W., Lind J.M., Semsarian C.
      J. Mol. Cell. Cardiol. 43:337-343(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CMH19 ARG-82.

    Entry informationi

    Entry nameiCALR3_HUMAN
    AccessioniPrimary (citable) accession number: Q96L12
    Secondary accession number(s): D9N574, Q96LN3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 22, 2003
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3