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P24643

- CALX_CANFA

UniProt

P24643 - CALX_CANFA

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Protein

Calnexin

Gene

CANX

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
  2. carbohydrate binding Source: UniProtKB-KW

GO - Biological processi

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

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 482462LumenalSequence AnalysisAdd
BLAST
Transmembranei483 – 50321HelicalSequence AnalysisAdd
BLAST
Topological domaini504 – 59390CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

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 – 744Combined sources
Beta strandi78 – 803Combined sources
Beta strandi104 – 1063Combined sources
Beta strandi122 – 1243Combined sources
Beta strandi131 – 14010Combined sources
Beta strandi142 – 1454Combined sources
Beta strandi147 – 1537Combined sources
Beta strandi160 – 1634Combined sources
Beta strandi166 – 1705Combined sources
Helixi177 – 1793Combined sources
Beta strandi186 – 19712Combined sources
Beta strandi200 – 2089Combined sources
Turni210 – 2123Combined sources
Beta strandi215 – 2184Combined sources
Helixi229 – 2324Combined sources
Beta strandi237 – 2448Combined sources
Turni245 – 2473Combined sources
Beta strandi248 – 2536Combined sources
Beta strandi256 – 2616Combined sources
Beta strandi292 – 2954Combined sources
Beta strandi311 – 3144Combined sources
Beta strandi325 – 3284Combined sources
Turni345 – 3473Combined sources
Helixi359 – 3613Combined sources
Beta strandi367 – 3693Combined sources
Beta strandi374 – 3763Combined sources
Beta strandi388 – 3903Combined sources
Beta strandi420 – 4256Combined sources
Beta strandi430 – 4323Combined sources
Beta strandi437 – 4459Combined sources
Helixi446 – 4549Combined sources
Turni455 – 4573Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP24643.

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.
IPR013320. ConA-like_dom.
[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

        10         20         30         40         50
MEGKWLLCML LVLGTTIVQA HEGHDDDMID IEDDLDDVIE EVEDSKSKPD
60 70 80 90 100
TSAPTSPKVT YKAPVPTGEV YFADSFDRGT LSGWILSKAK KDDTDDEIAK
110 120 130 140 150
YDGKWEVDEM KETKLPGDKG LVLMSRAKHH AISAKLNKPF LFDTKPLIVQ
160 170 180 190 200
YEVNFQNGIE CGGAYVKLLS KTPELNLDQF HDKTPYTIMF GPDKCGEDYK
210 220 230 240 250
LHFIFRHKNP KTGVYEEKHA KRPDADLKTY FTDKKTHLYT LILNPDNSFE
260 270 280 290 300
ILVDQSIVNS GNLLNDMTPP VNPSREIEDP EDQKPEDWDE RPKIPDPDAV
310 320 330 340 350
KPDDWNEDAP AKIPDEEATK PDGWLDDEPE YVPDPDAEKP EDWDEDMDGE
360 370 380 390 400
WEAPQIANPK CESAPGCGVW QRPMIDNPNY KGKWKPPMID NPNYQGIWKP
410 420 430 440 450
RKIPNPDFFE DLEPFKMTPF SAIGLELWSM TSDIFFDNFI VCGDRRVVDD
460 470 480 490 500
WANDGWGLKK AADGAAEPGV VGQMIEAAEE RPWLWVVYVL TVALPVFLVI
510 520 530 540 550
LFCCSGKKQS SPVEYKKTDA PQPDVKEEEE EKEEEKDKGD EEEEGEEKLE
560 570 580 590
EKQKSDAEED GGTASQEEDD RKPKAEEDEI LNRSPRNRKP RRE
Length:593
Mass (Da):67,603
Last modified:July 15, 1998 - v3
Checksum:iA2969701B1EB7B6A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
IPR013320. ConA-like_dom.
[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: November 26, 2014
This is version 121 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