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Q2TBR8

- CALR3_BOVIN

UniProt

Q2TBR8 - CALR3_BOVIN

Protein

Calreticulin-3

Gene

CALR3

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (24 Jan 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. CALR3 capacity for calcium-binding may be absent or much lower than that of CALR. Required for sperm fertility By similarity.By similarity

    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):
    Calsperin
    Gene namesi
    Name:CALR3
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 384365Calreticulin-3PRO_0000282867Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ2TBR8.

    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

    STRINGi9913.ENSBTAP00000013175.

    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 – 260112-1Add
    BLAST
    Repeati264 – 27292-2
    Repeati274 – 284112-3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni20 – 197178N-domainAdd
    BLAST
    Regioni191 – 246564 X approximate repeatsAdd
    BLAST
    Regioni198 – 29497P-domainAdd
    BLAST
    Regioni250 – 284353 X approximate repeatsAdd
    BLAST
    Regioni295 – 38490C-domainAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi381 – 3844Prevents secretion from ERSequence Analysis

    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.
    InParanoidiQ2TBR8.
    KOiK10098.

    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.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q2TBR8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAARVPLWA ICVRRVALAT VYFQEEFLDG ERWRNRWVHS TNDSQFGHFR    50
    LSSGNFYGHK EKDKGLQTTQ NSRFYAISAR FKPFSNKGKT LIIQYTVKHE 100
    QKMDCGGGYI KLFPADVDQK NLNGKSQYYI MFGPDICGFD IKTVHVILHF 150
    KNQYHANKKS IRCKVDSFTH LYTLVLRPDL TYEVKIDGQS IESGSIEYDW 200
    QLTSLKKMEK ASAEAEGWDQ AAKDKSQDWE KHFLDASASK PSDWKGELDG 250
    DWQAAMLQKP PYQDGLKPEG IDKDVWLHQK MKNSYLTEYD LSEFENIGAV 300
    GLELWQVRSG TIFDNFLITD DEEYAENFGK ATWGETKGPE KEMDAIQAKE 350
    EVKKAQEEDE DDMLMGRFRG RENSFKGFHR RNEF 384
    Length:384
    Mass (Da):44,512
    Last modified:January 24, 2006 - v1
    Checksum:iBAE01C8F353718C2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC109750 mRNA. Translation: AAI09751.1.
    RefSeqiNP_001033603.1. NM_001038514.2.
    UniGeneiBt.54234.

    Genome annotation databases

    GeneIDi508555.
    KEGGibta:508555.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC109750 mRNA. Translation: AAI09751.1 .
    RefSeqi NP_001033603.1. NM_001038514.2.
    UniGenei Bt.54234.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000013175.

    Proteomic databases

    PRIDEi Q2TBR8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 508555.
    KEGGi bta:508555.

    Organism-specific databases

    CTDi 125972.

    Phylogenomic databases

    eggNOGi NOG268919.
    HOGENOMi HOG000192435.
    HOVERGENi HBG005407.
    InParanoidi Q2TBR8.
    KOi K10098.

    Miscellaneous databases

    NextBioi 20868571.

    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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. NIH - Mammalian Gene Collection (MGC) project
      Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Crossbred X Angus.
      Tissue: Liver.

    Entry informationi

    Entry nameiCALR3_BOVIN
    AccessioniPrimary (citable) accession number: Q2TBR8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2007
    Last sequence update: January 24, 2006
    Last modified: October 1, 2014
    This is version 70 of the entry and version 1 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3