UniProt Accession

 CALX_MOUSE; P35564 

Genbank Protein ID

 L18888; BC012408; BC040244; AK084175; L23865 

Genbank Nucleotide ID

 AAA21014.1; AAH12408.1; AAH40244.1; BAC39133.1; AAA62450.1 

Protein Name

 Calnexin 

Protein Synonyms/Alias

  

Gene Name

 Canx 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
48	EVEDSKSKSDASTPP	acetylation	[1]
48	EVEDSKSKSDASTPP	succinylation	[1]
171	AYVKLLSKTAELSLD	ubiquitination	[2]
218	KTGVYEEKHAKRPDA	acetylation	[3, 4]
517	SNAMEYKKTDAPQPD	ubiquitination	[2]
526	DAPQPDVKDEEGKEE	ubiquitination	[2]
535	EEGKEEEKNKRDEEE	ubiquitination	[2]
537	GKEEEKNKRDEEEEE	ubiquitination	[2]
546	DEEEEEEKLEEKQKS	ubiquitination	[2]
550	EEEKLEEKQKSDAEE	ubiquitination	[2]

Reference

 [1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [4] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123] 

Functional Description

 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. 

Sequence Annotation

 REPEAT 279 291 1-1.
 REPEAT 296 308 1-2.
 REPEAT 315 327 1-3.
 REPEAT 334 346 1-4.
 REPEAT 349 359 2-1.
 REPEAT 368 378 2-2.
 REPEAT 382 392 2-3.
 REPEAT 396 406 2-4.
 REGION 277 410 P domain (Extended arm) (By similarity).
 REGION 279 346 4 X approximate repeats.
 REGION 349 406 4 X approximate repeats.
 REGION 504 591 Sufficient to mediate interaction with
 METAL 75 75 Calcium; via carbonyl oxygen (By
 METAL 118 118 Calcium; via carbonyl oxygen (By
 METAL 437 437 Calcium (By similarity).
 BINDING 165 165 Carbohydrate (By similarity).
 BINDING 167 167 Carbohydrate (By similarity).
 BINDING 186 186 Carbohydrate (By similarity).
 BINDING 217 217 Carbohydrate (By similarity).
 MOD_RES 138 138 N6-acetyllysine (By similarity).
 MOD_RES 553 553 Phosphoserine.
 MOD_RES 561 561 Phosphothreonine.
 MOD_RES 563 563 Phosphoserine; by MAPK3.
 MOD_RES 569 569 Phosphoserine.
 MOD_RES 582 582 Phosphoserine.
 LIPID 503 503 S-palmitoyl cysteine (By similarity).
 LIPID 504 504 S-palmitoyl cysteine (By similarity).
 DISULFID 161 195 By similarity.
 DISULFID 361 367 By similarity.  

Keyword

 Acetylation; Calcium; Chaperone; Complete proteome; Disulfide bond; Endoplasmic reticulum; Lectin; Lipoprotein; Membrane; Metal-binding; Palmitate; Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 591 AA 

Protein Sequence

Gene Ontology

 GO:0030424; C:axon; IEA:Compara.
 GO:0032839; C:dendrite cytoplasm; IEA:Compara.
 GO:0043197; C:dendritic spine; IEA:Compara.
 GO:0071556; C:integral to lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0043025; C:neuronal cell body; IEA:Compara.
 GO:0005840; C:ribosome; IEA:Compara.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0007568; P:aging; IEA:Compara.
 GO:0072583; P:clathrin-mediated endocytosis; IMP:UniProtKB.
 GO:0006457; P:protein folding; IEA:InterPro.
 GO:0048488; P:synaptic vesicle endocytosis; IMP:UniProtKB. 

Interpro

 IPR001580; Calret/calnex.
 IPR018124; Calret/calnex_CS.
 IPR009033; Calreticulin/calnexin_P_dom.
 IPR008985; ConA-like_lec_gl_sf.
 IPR013320; ConA-like_subgrp. 

Pfam

 PF00262; Calreticulin 

SMART

  

PROSITE

 PS00803; CALRETICULIN_1
 PS00804; CALRETICULIN_2
 PS00805; CALRETICULIN_REPEAT 

PRINTS

 PR00626; CALRETICULIN.