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Q5R440 (CALX_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Calnexin
Gene names
Name:CANX
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length592 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subunit structure

Interacts with MAPK3/ERK1. Interacts with KCNH2 By similarity. 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 KCNH2 By similarity.

Subcellular location

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

Post-translational modification

Phosphorylated at Ser-564 by MAPK3/ERK1. phosphorylation by MAPK3/ERK1 increases its association with ribosomes 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.

Sequence similarities

Belongs to the calreticulin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 592572Calnexin
PRO_0000004200

Regions

Topological domain21 – 481461Lumenal Potential
Transmembrane482 – 50221Helical; Potential
Topological domain503 – 59290Cytoplasmic Potential
Repeat278 – 290131-1
Repeat295 – 307131-2
Repeat314 – 326131-3
Repeat333 – 345131-4
Repeat348 – 358112-1
Repeat367 – 377112-2
Repeat381 – 391112-3
Repeat395 – 405112-4
Region276 – 409134P domain (Extended arm) By similarity
Region278 – 345684 X approximate repeats
Region348 – 405584 X approximate repeats
Region503 – 59290Sufficient to mediate interaction with SGIP1 By similarity

Sites

Metal binding741Calcium; via carbonyl oxygen By similarity
Metal binding1171Calcium; via carbonyl oxygen By similarity
Metal binding4361Calcium By similarity
Binding site1641Carbohydrate By similarity
Binding site1661Carbohydrate By similarity
Binding site1851Carbohydrate By similarity
Binding site2161Carbohydrate By similarity

Amino acid modifications

Modified residue1371N6-acetyllysine By similarity
Modified residue5541Phosphoserine By similarity
Modified residue5621Phosphothreonine By similarity
Modified residue5641Phosphoserine; by MAPK3 By similarity
Modified residue5831Phosphoserine By similarity
Lipidation5021S-palmitoyl cysteine By similarity
Lipidation5031S-palmitoyl cysteine By similarity
Disulfide bond160 ↔ 194 By similarity
Disulfide bond360 ↔ 366 By similarity

Experimental info

Sequence conflict831W → R in CAH93476. Ref.1
Sequence conflict1431T → A in CAH92563. Ref.1
Sequence conflict2171K → R in CAH92697. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q5R440 [UniParc].

Last modified July 25, 2006. Version 2.
Checksum: 31875C853C202811

FASTA59267,572
        10         20         30         40         50         60 
MEGKWLLCML LVLGTAIVEA HDGHDDDVID IEDDLDDVIE EVEDSKPDTT APPSSPKVTY 

        70         80         90        100        110        120 
KAPVPTGEVY FADSFDRGTL SGWILSKAKK DDTDDEIAKY DGKWEVDEMK ESKLPGDKGL 

       130        140        150        160        170        180 
VLMSRAKHHA ISAKLNKPFL FDTKPLIVQY EVNFQNGIEC GGAYVKLLSK TPELNLDQFH 

       190        200        210        220        230        240 
DKTPYTIMFG PDKCGEDYKL HFIFRHKNPK TGIYEEKHAK RPDADLKTYF TDKKTHLYTL 

       250        260        270        280        290        300 
ILNPDNSFEI LVDQSVVNSG NLLNDMTPPV NPSREIEDPE DRKPEDWDER PKIPDPEAVK 

       310        320        330        340        350        360 
PDDWDEDAPA KIPDEEATKP EGWLDDEPEY VPDPDAEKPE DWDEDMDGEW EAPQIANPKC 

       370        380        390        400        410        420 
ESAPGCGVWQ RPMIDNPNYK GKWKPPMIDN PSYQGIWKPR KIPNPDFFED LEPFRMTPFS 

       430        440        450        460        470        480 
AIGLELWSMT SDIFFDNFII CADRRIVDDW ANDGWGLKKA ADGAAEPGVV GQMIEAAEER 

       490        500        510        520        530        540 
PWLWVVYILT VALPVFLVIL FCCSGKKQTS AMEYKKTDAP QPDVKEEEEE KEEEKDKGDE 

       550        560        570        580        590 
EEEGEEKLEE KQKSDAEEDG GTVSQEEEDR KPKAEEDEIL NRSPRNRKPR RE

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR860439 mRNA. Translation: CAH92563.1.
CR860572 mRNA. Translation: CAH92697.1.
CR861420 mRNA. Translation: CAH93476.1.
RefSeqNP_001127039.1. NM_001133567.1.
UniGenePab.359.

3D structure databases

ProteinModelPortalQ5R440.
SMRQ5R440. Positions 60-457.
ModBaseSearch...

Proteomic databases

PRIDEQ5R440.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100174065.
KEGGpon:100174065.

Organism-specific databases

CTD821.

Phylogenomic databases

HOVERGENHBG005407.
KOK08054.
OrthoDBEOG4DBTDB.

Family and domain databases

Gene3D2.10.250.10. 1 hit.
2.60.120.200. 1 hit.
InterProIPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009033. Calreticulin/calnexin_P_dom.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
[Graphical view]
PANTHERPTHR11073. PTHR11073. 1 hit.
PfamPF00262. Calreticulin. 1 hit.
[Graphical view]
PRINTSPR00626. CALRETICULIN.
SUPFAMSSF63887. Calret_calnex_P. 1 hit.
SSF49899. ConA_like_lec_gl. 2 hits.
PROSITEPS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCALX_PONAB
AccessionPrimary (citable) accession number: Q5R440
Secondary accession number(s): Q5R6B9, Q5R6P7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: July 25, 2006
Last modified: March 6, 2013
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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