Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P24643

- CALX_CANFA

UniProt

P24643 - CALX_CANFA

Protein

Calnexin

Gene

CANX

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 3 (15 Jul 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor-mediated endocytosis at the synapse By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi75 – 751Calcium; via carbonyl oxygen
    Metal bindingi118 – 1181Calcium; via carbonyl oxygen
    Binding sitei165 – 1651CarbohydrateCurated
    Binding sitei167 – 1671CarbohydrateCurated
    Binding sitei186 – 1861CarbohydrateCurated
    Binding sitei217 – 2171CarbohydrateCurated
    Metal bindingi437 – 4371Calcium

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro

    GO - Biological processi

    1. clathrin-mediated endocytosis Source: UniProtKB
    2. protein folding Source: InterPro
    3. synaptic vesicle endocytosis Source: UniProtKB

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    Calcium, Lectin, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calnexin
    Alternative name(s):
    pp90
    Gene namesi
    Name:CANX
    OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
    Taxonomic identifieri9615 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
    ProteomesiUP000002254: Unplaced

    Subcellular locationi

    Endoplasmic reticulum membrane; Single-pass type I membrane protein. Endoplasmic reticulum By similarity. Melanosome By similarity
    Note: The palmitoylated form preferentially localizes to the perinuclear rough ER.By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. melanosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi348 – 3481D → K: Abolishes interaction with PPIB. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Add
    BLAST
    Chaini21 – 593573CalnexinPRO_0000004197Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei138 – 1381N6-acetyllysineBy similarity
    Disulfide bondi161 ↔ 1951 Publication
    Disulfide bondi361 ↔ 3671 Publication
    Lipidationi503 – 5031S-palmitoyl cysteineBy similarity
    Lipidationi504 – 5041S-palmitoyl cysteineBy similarity
    Modified residuei555 – 5551PhosphoserineBy similarity
    Modified residuei563 – 5631PhosphothreonineBy similarity
    Modified residuei565 – 5651Phosphoserine; by MAPK3By similarity
    Modified residuei584 – 5841PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated at Ser-565 by MAPK3/ERK1. phosphorylation by MAPK3/ERK1 increases its association with ribosomes By similarity.By similarity
    Palmitoylation by DHHC6 leads to the preferential localization to the perinuclear rough ER. It mediates the association of calnexin with the ribosome-translocon complex (RTC) which is required for efficient folding of glycosylated proteins By similarity.By similarity

    Keywords - PTMi

    Acetylation, Disulfide bond, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    PaxDbiP24643.
    PRIDEiP24643.

    Interactioni

    Subunit structurei

    Interacts with MAPK3/ERK1. Interacts with KCNH2. Associates with ribosomes. Interacts with SGIP1; involved in negative regulation of endocytosis. The palmitoylated form interacts with the ribosome-translocon complex component SSR1, promoting efficient folding of glycoproteins By similarity. Interacts with SERPINA2P/SERPINA2 and with the S and Z variants of SERPINA1 By similarity. Interacts with PPIB.By similarity1 Publication

    Protein-protein interaction databases

    DIPiDIP-29133N.
    STRINGi9615.ENSCAFP00000000498.

    Structurei

    Secondary structure

    1
    593
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi71 – 744
    Beta strandi78 – 803
    Beta strandi104 – 1063
    Beta strandi122 – 1243
    Beta strandi131 – 14010
    Beta strandi142 – 1454
    Beta strandi147 – 1537
    Beta strandi160 – 1634
    Beta strandi166 – 1705
    Helixi177 – 1793
    Beta strandi186 – 19712
    Beta strandi200 – 2089
    Turni210 – 2123
    Beta strandi215 – 2184
    Helixi229 – 2324
    Beta strandi237 – 2448
    Turni245 – 2473
    Beta strandi248 – 2536
    Beta strandi256 – 2616
    Beta strandi292 – 2954
    Beta strandi311 – 3144
    Beta strandi325 – 3284
    Turni345 – 3473
    Helixi359 – 3613
    Beta strandi367 – 3693
    Beta strandi374 – 3763
    Beta strandi388 – 3903
    Beta strandi420 – 4256
    Beta strandi430 – 4323
    Beta strandi437 – 4459
    Helixi446 – 4549
    Turni455 – 4573

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JHNX-ray2.90A45-468[»]
    ProteinModelPortaliP24643.
    SMRiP24643. Positions 61-458.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP24643.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 482462LumenalSequence AnalysisAdd
    BLAST
    Topological domaini504 – 59390CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei483 – 50321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati279 – 290121-1Add
    BLAST
    Repeati296 – 307121-2Add
    BLAST
    Repeati315 – 326121-3Add
    BLAST
    Repeati334 – 345121-4Add
    BLAST
    Repeati349 – 359112-1Add
    BLAST
    Repeati368 – 378112-2Add
    BLAST
    Repeati382 – 392112-3Add
    BLAST
    Repeati396 – 406112-4Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni277 – 410134P domain (Extended arm)Add
    BLAST
    Regioni279 – 345674 X approximate repeatsAdd
    BLAST
    Regioni327 – 36034Interaction with PPIBAdd
    BLAST
    Regioni349 – 406584 X approximate repeatsAdd
    BLAST
    Regioni504 – 59390Sufficient to mediate interaction with SGIP1By similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the calreticulin family.Curated

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG305105.
    HOGENOMiHOG000192436.
    HOVERGENiHBG005407.
    InParanoidiP24643.
    KOiK08054.

    Family and domain databases

    Gene3Di2.10.250.10. 1 hit.
    2.60.120.200. 1 hit.
    InterProiIPR001580. Calret/calnex.
    IPR018124. Calret/calnex_CS.
    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]
    PRINTSiPR00626. CALRETICULIN.
    SUPFAMiSSF49899. SSF49899. 2 hits.
    SSF63887. SSF63887. 1 hit.
    PROSITEiPS00803. CALRETICULIN_1. 1 hit.
    PS00804. CALRETICULIN_2. 1 hit.
    PS00805. CALRETICULIN_REPEAT. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P24643-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEGKWLLCML LVLGTTIVQA HEGHDDDMID IEDDLDDVIE EVEDSKSKPD    50
    TSAPTSPKVT YKAPVPTGEV YFADSFDRGT LSGWILSKAK KDDTDDEIAK 100
    YDGKWEVDEM KETKLPGDKG LVLMSRAKHH AISAKLNKPF LFDTKPLIVQ 150
    YEVNFQNGIE CGGAYVKLLS KTPELNLDQF HDKTPYTIMF GPDKCGEDYK 200
    LHFIFRHKNP KTGVYEEKHA KRPDADLKTY FTDKKTHLYT LILNPDNSFE 250
    ILVDQSIVNS GNLLNDMTPP VNPSREIEDP EDQKPEDWDE RPKIPDPDAV 300
    KPDDWNEDAP AKIPDEEATK PDGWLDDEPE YVPDPDAEKP EDWDEDMDGE 350
    WEAPQIANPK CESAPGCGVW QRPMIDNPNY KGKWKPPMID NPNYQGIWKP 400
    RKIPNPDFFE DLEPFKMTPF SAIGLELWSM TSDIFFDNFI VCGDRRVVDD 450
    WANDGWGLKK AADGAAEPGV VGQMIEAAEE RPWLWVVYVL TVALPVFLVI 500
    LFCCSGKKQS SPVEYKKTDA PQPDVKEEEE EKEEEKDKGD EEEEGEEKLE 550
    EKQKSDAEED GGTASQEEDD RKPKAEEDEI LNRSPRNRKP RRE 593
    Length:593
    Mass (Da):67,603
    Last modified:July 15, 1998 - v3
    Checksum:iA2969701B1EB7B6A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53616 mRNA. Translation: CAA37678.1.
    PIRiA37273.
    RefSeqiNP_001003232.1. NM_001003232.1.
    UniGeneiCfa.3766.

    Genome annotation databases

    GeneIDi403908.
    KEGGicfa:403908.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53616 mRNA. Translation: CAA37678.1 .
    PIRi A37273.
    RefSeqi NP_001003232.1. NM_001003232.1.
    UniGenei Cfa.3766.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JHN X-ray 2.90 A 45-468 [» ]
    ProteinModelPortali P24643.
    SMRi P24643. Positions 61-458.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-29133N.
    STRINGi 9615.ENSCAFP00000000498.

    Proteomic databases

    PaxDbi P24643.
    PRIDEi P24643.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 403908.
    KEGGi cfa:403908.

    Organism-specific databases

    CTDi 821.

    Phylogenomic databases

    eggNOGi NOG305105.
    HOGENOMi HOG000192436.
    HOVERGENi HBG005407.
    InParanoidi P24643.
    KOi K08054.

    Miscellaneous databases

    EvolutionaryTracei P24643.
    NextBioi 20817400.

    Family and domain databases

    Gene3Di 2.10.250.10. 1 hit.
    2.60.120.200. 1 hit.
    InterProi IPR001580. Calret/calnex.
    IPR018124. Calret/calnex_CS.
    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 ]
    PRINTSi PR00626. CALRETICULIN.
    SUPFAMi SSF49899. SSF49899. 2 hits.
    SSF63887. SSF63887. 1 hit.
    PROSITEi PS00803. CALRETICULIN_1. 1 hit.
    PS00804. CALRETICULIN_2. 1 hit.
    PS00805. CALRETICULIN_REPEAT. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane."
      Wada I., Rindress D., Cameron P.H., Ou W.-J., Doherty J.J. II, Louvard D., Bell A.W., Dignard D., Thomas D.Y., Bergeron J.J.M.
      J. Biol. Chem. 266:19599-19610(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    2. Dignard D.
      Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 67.
    3. Cited for: INTERACTION WITH PPIB, MUTAGENESIS OF ASP-348.
    4. "The Structure of calnexin, an ER chaperone involved in quality control of protein folding."
      Schrag J.D., Bergeron J.J., Li Y., Borisova S., Hahn M., Thomas D.Y., Cygler M.
      Mol. Cell 8:633-644(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 45-468, DISULFIDE BONDS CALCIUM-BINDING SITES, PROBABLE CARBOHYDRATE-INTERACTING SITES.

    Entry informationi

    Entry nameiCALX_CANFA
    AccessioniPrimary (citable) accession number: P24643
    Secondary accession number(s): P79140
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 119 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3