P24643 (CALX_CANFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Calnexin

Alternative name(s):
pp90

Gene names

Name:

CANX

Organism

Canis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis › Canis lupus

Protein attributes

Sequence length	593 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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.
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-565 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. Ref.3
Sequence similarities	Belongs to the calreticulin family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium Lectin Metal-binding
Molecular function	Chaperone
PTM	Acetylation Disulfide bond Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	clathrin-mediated endocytosis Inferred from sequence or structural similarity. Source: UniProtKB protein folding Inferred from electronic annotation. Source: InterPro synaptic vesicle endocytosis Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Chain

21 – 593

573

Calnexin

PRO_0000004197

Regions

Topological domain

21 – 482

462

Lumenal Potential

Transmembrane

483 – 503

21

Helical; Potential

Topological domain

504 – 593

90

Cytoplasmic Potential

Repeat

279 – 290

12

1-1

Repeat

296 – 307

12

1-2

Repeat

315 – 326

12

1-3

Repeat

334 – 345

12

1-4

Repeat

349 – 359

11

2-1

Repeat

368 – 378

11

2-2

Repeat

382 – 392

11

2-3

Repeat

396 – 406

11

2-4

Region

277 – 410

134

P domain (Extended arm)

Region

279 – 345

67

4 X approximate repeats

Region

349 – 406

58

4 X approximate repeats

Region

504 – 593

90

Sufficient to mediate interaction with SGIP1 By similarity

Sites

Metal binding

75

1

Calcium; via carbonyl oxygen

Metal binding

118

1

Calcium; via carbonyl oxygen

Metal binding

437

1

Calcium

Binding site

165

1

Carbohydrate Probable

Binding site

167

1

Carbohydrate Probable

Binding site

186

1

Carbohydrate Probable

Binding site

217

1

Carbohydrate Probable

Amino acid modifications

Modified residue

138

1

N6-acetyllysine By similarity

Modified residue

555

1

Phosphoserine By similarity

Modified residue

563

1

Phosphothreonine By similarity

Modified residue

565

1

Phosphoserine; by MAPK3 By similarity

Modified residue

584

1

Phosphoserine By similarity

Lipidation

503

1

S-palmitoyl cysteine By similarity

Lipidation

504

1

S-palmitoyl cysteine By similarity

Disulfide bond

161 ↔ 195

Ref.3

Disulfide bond

361 ↔ 367

Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

593

Helix Strand Turn

Details...

Beta strand

71 – 74

4

Beta strand

78 – 80

3

Beta strand

104 – 106

3

Beta strand

122 – 124

3

Beta strand

131 – 140

10

Beta strand

142 – 145

4

Beta strand

147 – 153

7

Beta strand

160 – 163

4

Beta strand

166 – 170

5

Helix

177 – 179

3

Beta strand

186 – 197

12

Beta strand

200 – 208

9

Turn

210 – 212

3

Beta strand

215 – 218

4

Helix

229 – 232

4

Beta strand

237 – 244

8

Turn

245 – 247

3

Beta strand

248 – 253

6

Beta strand

256 – 261

6

Beta strand

292 – 295

4

Beta strand

311 – 314

4

Beta strand

325 – 328

4

Turn

345 – 347

3

Helix

359 – 361

3

Beta strand

367 – 369

3

Beta strand

374 – 376

3

Beta strand

388 – 390

3

Beta strand

420 – 425

6

Beta strand

430 – 432

3

Beta strand

437 – 445

9

Helix

446 – 454

9

Turn

455 – 457

3

Sequences

	Sequence		Length	Mass (Da)
	P24643 [UniParc]. Last modified July 15, 1998. Version 3. Checksum: A2969701B1EB7B6A	FASTA	593	67,603
	10 20 30 40 50 60 MEGKWLLCML LVLGTTIVQA HEGHDDDMID IEDDLDDVIE EVEDSKSKPD TSAPTSPKVT 70 80 90 100 110 120 YKAPVPTGEV YFADSFDRGT LSGWILSKAK KDDTDDEIAK YDGKWEVDEM KETKLPGDKG 130 140 150 160 170 180 LVLMSRAKHH AISAKLNKPF LFDTKPLIVQ YEVNFQNGIE CGGAYVKLLS KTPELNLDQF 190 200 210 220 230 240 HDKTPYTIMF GPDKCGEDYK LHFIFRHKNP KTGVYEEKHA KRPDADLKTY FTDKKTHLYT 250 260 270 280 290 300 LILNPDNSFE ILVDQSIVNS GNLLNDMTPP VNPSREIEDP EDQKPEDWDE RPKIPDPDAV 310 320 330 340 350 360 KPDDWNEDAP AKIPDEEATK PDGWLDDEPE YVPDPDAEKP EDWDEDMDGE WEAPQIANPK 370 380 390 400 410 420 CESAPGCGVW QRPMIDNPNY KGKWKPPMID NPNYQGIWKP RKIPNPDFFE DLEPFKMTPF 430 440 450 460 470 480 SAIGLELWSM TSDIFFDNFI VCGDRRVVDD WANDGWGLKK AADGAAEPGV VGQMIEAAEE 490 500 510 520 530 540 RPWLWVVYVL TVALPVFLVI LFCCSGKKQS SPVEYKKTDA PQPDVKEEEE EKEEEKDKGD 550 560 570 580 590 EEEEGEEKLE EKQKSDAEED GGTASQEEDD RKPKAEEDEI LNRSPRNRKP RRE

References

[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]	"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X53616 mRNA. Translation: CAA37678.1.

PIR

A37273.

RefSeq

NP_001003232.1. NM_001003232.1.

UniGene

Cfa.3766.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JHN	X-ray	2.90	A	45-468	[»]

ProteinModelPortal

P24643.

SMR

P24643. Positions 61-458.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29133N.

STRING

9615.ENSCAFP00000000498.

Proteomic databases

PaxDb

P24643.

PRIDE

P24643.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

403908.

KEGG

cfa:403908.

Organism-specific databases

CTD

821.

Phylogenomic databases

eggNOG

NOG305105.

HOGENOM

HOG000192436.

HOVERGEN

HBG005407.

InParanoid

P24643.

KO

K08054.

OrthoDB

EOG4DBTDB.

Family and domain databases

Gene3D

2.10.250.10. 1 hit.
2.60.120.200. 1 hit.

InterPro

IPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009033. Calreticulin/calnexin_P_dom.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
[Graphical view]

PANTHER

PTHR11073. PTHR11073. 1 hit.

Pfam

PF00262. Calreticulin. 1 hit.
[Graphical view]

PRINTS

PR00626. CALRETICULIN.

SUPFAM

SSF63887. Calret_calnex_P. 1 hit.
SSF49899. ConA_like_lec_gl. 2 hits.

PROSITE

PS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P24643.

NextBio

20817400.

Entry information

Entry name

CALX_CANFA

Accession

Primary (citable) accession number: P24643
Secondary accession number(s): P79140

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	July 15, 1998
Last modified:	April 3, 2013
This is version 111 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program