ID CALX_MOUSE Reviewed; 591 AA. AC P35564; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 27-MAR-2024, entry version 211. DE RecName: Full=Calnexin; DE Flags: Precursor; GN Name=Canx; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8136357; DOI=10.1021/bi00177a013; RA Tjoelker L.W., Seyfried C.E., Eddy R.L. Jr., Shows T.B. Jr., Calderon J., RA Schreiber R.B., Gray P.W.; RT "Human, mouse, and rat calnexin cDNA cloning: identification of potential RT calcium binding motifs and gene localization to human chromosome 5."; RL Biochemistry 33:3229-3236(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-155. RC STRAIN=C57BL/6J; TISSUE=Eye; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-591. RC STRAIN=BALB/cJ; RX PubMed=8148318; DOI=10.1093/intimm/6.1.101; RA Schreiber K.L., Bell M.P., Huntoon C.J., Rajagopalan S., Brenner M.B., RA McKean D.J.; RT "Class II histocompatibility molecules associate with calnexin during RT assembly in the endoplasmic reticulum."; RL Int. Immunol. 6:101-111(1994). RN [5] RP FUNCTION IN THYMOCYTE MATURATION, AND SUBCELLULAR LOCATION. RX PubMed=7628443; DOI=10.1002/j.1460-2075.1995.tb07348.x; RA Wiest D.L., Burgess W.H., McKean D., Kearse K.P., Singer A.; RT "The molecular chaperone calnexin is expressed on the surface of immature RT thymocytes in association with clonotype-independent CD3 complexes."; RL EMBO J. 14:3425-3433(1995). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Teratocarcinoma; RX PubMed=17622165; DOI=10.1021/pr070122r; RA Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.; RT "A differential phosphoproteomic analysis of retinoic acid-treated P19 RT cells."; RL J. Proteome Res. 6:3174-3186(2007). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain cortex; RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200; RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., RA Panse C., Schlapbach R., Mansuy I.M.; RT "Qualitative and quantitative analyses of protein phosphorylation in naive RT and stimulated mouse synaptosomal preparations."; RL Mol. Cell. Proteomics 6:283-293(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553; SER-563 AND SER-582, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200; RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.; RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and RT MS/MS/MS."; RL Mol. Cell. Proteomics 6:669-676(2007). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18630941; DOI=10.1021/pr800223m; RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity RT chromatography adsorbent for phosphoproteome analysis."; RL J. Proteome Res. 7:3957-3967(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553; SER-563 AND SER-582, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of electron RT capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553 AND SER-563, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [13] RP INTERACTION WITH ADAM7, AND TISSUE SPECIFICITY. RX PubMed=20945367; DOI=10.1002/jcp.22444; RA Han C., Park I., Lee B., Jin S., Choi H., Kwon J.T., Kwon Y.I., Kim D.H., RA Park Z.Y., Cho C.; RT "Identification of heat shock protein 5, calnexin and integral membrane RT protein 2B as Adam7-interacting membrane proteins in mouse sperm."; RL J. Cell. Physiol. 226:1186-1195(2011). RN [14] RP FUNCTION, AND INTERACTION WITH SGIP1. RX PubMed=21747946; DOI=10.1371/journal.pone.0021678; RA Li H.D., Liu W.X., Michalak M.; RT "Enhanced clathrin-dependent endocytosis in the absence of calnexin."; RL PLoS ONE 6:E21678-E21678(2011). RN [15] RP INTERACTION WITH TMEM35A/NACHO. RX PubMed=32783947; DOI=10.1016/j.celrep.2020.108025; RA Kweon H.J., Gu S., Witham E., Dhara M., Yu H., Mandon E.D., Jawhari A., RA Bredt D.S.; RT "NACHO Engages N-Glycosylation ER Chaperone Pathways for alpha7 Nicotinic RT Receptor Assembly."; RL Cell Rep. 32:108025-108025(2020). CC -!- FUNCTION: Calcium-binding protein that interacts with newly synthesized CC monoglucosylated glycoproteins in the endoplasmic reticulum. It may act CC in assisting protein assembly and/or in the retention within the ER of CC unassembled protein subunits. It seems to play a major role in the CC quality control apparatus of the ER by the retention of incorrectly CC folded proteins. Associated with partial T-cell antigen receptor CC complexes that escape the ER of immature thymocytes, it may function as CC a signaling complex regulating thymocyte maturation. Additionally it CC may play a role in receptor-mediated endocytosis at the synapse. CC {ECO:0000269|PubMed:21747946, ECO:0000269|PubMed:7628443}. CC -!- SUBUNIT: Interacts with MAPK3/ERK1 (By similarity). Interacts with CC KCNH2 (By similarity). Associates with ribosomes (By similarity). The CC palmitoylated form interacts with the ribosome-translocon complex CC component SSR1, promoting efficient folding of glycoproteins (By CC similarity). Interacts with SERPINA2P/SERPINA2 and with the S and Z CC variants of SERPINA1 (By similarity). Interacts with SGIP1; involved in CC negative regulation of endocytosis (PubMed:21747946). Interacts with CC PPIB (By similarity). Interacts with SMIM22 (By similarity). Interacts CC with TMX2 (By similarity). Interacts with TMEM35A/NACHO CC (PubMed:32783947). Interacts with CHRNA7 (By similarity). Interacts CC with reticulophagy regulators RETREG2 and RETREG3 (By similarity). CC Interacts with DNM1L; may form part of a larger protein complex at the CC ER-mitochondrial interface during mitochondrial fission (By CC similarity). Interacts with ADAM7 (PubMed:20945367). CC {ECO:0000250|UniProtKB:P27824, ECO:0000250|UniProtKB:P35565, CC ECO:0000269|PubMed:20945367, ECO:0000269|PubMed:21747946, CC ECO:0000269|PubMed:32783947}. CC -!- INTERACTION: CC P35564; Q8VD37: Sgip1; NbExp=3; IntAct=EBI-738422, EBI-776269; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:7628443}; Single-pass type I membrane protein CC {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:P24643}; CC Single-pass type I membrane protein {ECO:0000255}. Melanosome membrane CC {ECO:0000250|UniProtKB:P27824}; Single-pass type I membrane protein CC {ECO:0000255}. Note=The palmitoylated form preferentially localizes to CC the perinuclear rough ER (By similarity). When bound to CD3 epsilon CC chains, calnexin's ER retention signal can be masked, permitting it to CC escape ER retention (By similarity). Localizes to endoplasmic reticulum CC mitochondria-associated membrane (MAMs) that connect the endoplasmic CC reticulum and the mitochondria (By similarity). CC {ECO:0000250|UniProtKB:P24643, ECO:0000250|UniProtKB:P27824}. CC -!- TISSUE SPECIFICITY: Expressed in sperm (at protein level). CC {ECO:0000269|PubMed:20945367}. CC -!- PTM: Phosphorylated at Ser-563 by MAPK3/ERK1. Phosphorylation by CC MAPK3/ERK1 increases its association with ribosomes (By similarity). CC {ECO:0000250}. CC -!- PTM: Palmitoylation by DHHC6 leads to the preferential localization to CC the perinuclear rough ER. It mediates the association of calnexin with CC the ribosome-translocon complex (RTC) which is required for efficient CC folding of glycosylated proteins (By similarity). {ECO:0000250}. CC -!- PTM: Ubiquitinated, leading to proteasomal degradation. Probably CC ubiquitinated by ZNRF4. {ECO:0000250|UniProtKB:P27824}. CC -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L18888; AAA21014.1; -; mRNA. DR EMBL; BC012408; AAH12408.1; -; mRNA. DR EMBL; BC040244; AAH40244.1; -; mRNA. DR EMBL; AK084175; BAC39133.1; -; mRNA. DR EMBL; L23865; AAA62450.1; -; mRNA. DR CCDS; CCDS24633.1; -. DR PIR; B54354; B54354. DR RefSeq; NP_001103969.1; NM_001110499.1. DR RefSeq; NP_001103970.1; NM_001110500.1. DR RefSeq; NP_031623.1; NM_007597.3. DR AlphaFoldDB; P35564; -. DR SMR; P35564; -. DR BioGRID; 198467; 53. DR CORUM; P35564; -. DR IntAct; P35564; 15. DR MINT; P35564; -. DR STRING; 10090.ENSMUSP00000137440; -. DR GlyGen; P35564; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P35564; -. DR PhosphoSitePlus; P35564; -. DR SwissPalm; P35564; -. DR EPD; P35564; -. DR jPOST; P35564; -. DR PaxDb; 10090-ENSMUSP00000020637; -. DR PeptideAtlas; P35564; -. DR ProteomicsDB; 265514; -. DR Pumba; P35564; -. DR Antibodypedia; 2421; 1301 antibodies from 46 providers. DR DNASU; 12330; -. DR Ensembl; ENSMUST00000020637.9; ENSMUSP00000020637.9; ENSMUSG00000020368.16. DR Ensembl; ENSMUST00000179865.8; ENSMUSP00000137440.2; ENSMUSG00000020368.16. DR GeneID; 12330; -. DR KEGG; mmu:12330; -. DR UCSC; uc007isf.2; mouse. DR AGR; MGI:88261; -. DR CTD; 821; -. DR MGI; MGI:88261; Canx. DR VEuPathDB; HostDB:ENSMUSG00000020368; -. DR eggNOG; KOG0675; Eukaryota. DR GeneTree; ENSGT00950000182915; -. DR HOGENOM; CLU_018224_2_0_1; -. DR InParanoid; P35564; -. DR OMA; SGCGKWE; -. DR OrthoDB; 5489154at2759; -. DR PhylomeDB; P35564; -. DR TreeFam; TF300618; -. DR Reactome; R-MMU-2132295; MHC class II antigen presentation. DR Reactome; R-MMU-901042; Calnexin/calreticulin cycle. DR Reactome; R-MMU-9020956; Interleukin-27 signaling. DR Reactome; R-MMU-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC. DR BioGRID-ORCS; 12330; 2 hits in 79 CRISPR screens. DR ChiTaRS; Canx; mouse. DR PRO; PR:P35564; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; P35564; Protein. DR Bgee; ENSMUSG00000020368; Expressed in ureteric bud tip and 257 other cell types or tissues. DR ExpressionAtlas; P35564; baseline and differential. DR GO; GO:0030424; C:axon; ISO:MGI. DR GO; GO:0032839; C:dendrite cytoplasm; ISO:MGI. DR GO; GO:0043197; C:dendritic spine; ISO:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:AgBase. DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IDA:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI. DR GO; GO:0098553; C:lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISO:MGI. DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB. DR GO; GO:0043025; C:neuronal cell body; ISO:MGI. DR GO; GO:0031965; C:nuclear membrane; IDA:MGI. DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI. DR GO; GO:0048787; C:presynaptic active zone membrane; ISO:MGI. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0005840; C:ribosome; ISO:MGI. DR GO; GO:0005790; C:smooth endoplasmic reticulum; ISO:MGI. DR GO; GO:0034185; F:apolipoprotein binding; ISO:MGI. DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI. DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro. DR GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:UniProtKB. DR GO; GO:0006457; P:protein folding; IBA:GO_Central. DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:SynGO. DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central. DR Gene3D; 2.60.120.200; -; 1. DR Gene3D; 2.10.250.10; Calreticulin/calnexin, P domain; 1. DR InterPro; IPR001580; Calret/calnex. DR InterPro; IPR018124; Calret/calnex_CS. DR InterPro; IPR009033; Calreticulin/calnexin_P_dom_sf. DR InterPro; IPR013320; ConA-like_dom_sf. DR PANTHER; PTHR11073:SF11; CALNEXIN; 1. DR PANTHER; PTHR11073; CALRETICULIN AND CALNEXIN; 1. DR Pfam; PF00262; Calreticulin; 1. DR PRINTS; PR00626; CALRETICULIN. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2. DR SUPFAM; SSF63887; P-domain of calnexin/calreticulin; 1. DR PROSITE; PS00803; CALRETICULIN_1; 1. DR PROSITE; PS00804; CALRETICULIN_2; 1. DR PROSITE; PS00805; CALRETICULIN_REPEAT; 3. DR Genevisible; P35564; MM. PE 1: Evidence at protein level; KW Acetylation; Calcium; Chaperone; Disulfide bond; Endoplasmic reticulum; KW Lectin; Lipoprotein; Membrane; Metal-binding; Mitochondrion; Palmitate; KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..591 FT /note="Calnexin" FT /id="PRO_0000004199" FT TOPO_DOM 21..482 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 483..503 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 504..591 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 279..291 FT /note="1-1" FT REPEAT 296..308 FT /note="1-2" FT REPEAT 315..327 FT /note="1-3" FT REPEAT 334..346 FT /note="1-4" FT REPEAT 349..359 FT /note="2-1" FT REPEAT 368..378 FT /note="2-2" FT REPEAT 382..392 FT /note="2-3" FT REPEAT 396..406 FT /note="2-4" FT REGION 261..347 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 277..410 FT /note="P domain (Extended arm)" FT /evidence="ECO:0000250" FT REGION 279..346 FT /note="4 X approximate repeats" FT REGION 327..360 FT /note="Interaction with PPIB" FT /evidence="ECO:0000250" FT REGION 349..406 FT /note="4 X approximate repeats" FT REGION 504..591 FT /note="Sufficient to mediate interaction with SGIP1" FT /evidence="ECO:0000269|PubMed:21747946" FT REGION 514..591 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 275..327 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 328..347 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 519..584 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 75 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P24643" FT BINDING 118 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P24643" FT BINDING 165 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 167 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 186 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 193 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 426 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 437 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P24643" FT MOD_RES 138 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P27824" FT MOD_RES 553 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17208939, FT ECO:0007744|PubMed:17622165, ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT MOD_RES 561 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P27824" FT MOD_RES 563 FT /note="Phosphoserine; by MAPK3" FT /evidence="ECO:0007744|PubMed:17208939, FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079" FT MOD_RES 582 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17208939, FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319" FT LIPID 503 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT LIPID 504 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT DISULFID 161..195 FT /evidence="ECO:0000250|UniProtKB:P24643" FT DISULFID 361..367 FT /evidence="ECO:0000250|UniProtKB:P24643" FT CONFLICT 416 FT /note="K -> R (in Ref. 4; AAA62450)" FT /evidence="ECO:0000305" FT CONFLICT 468 FT /note="P -> L (in Ref. 4; AAA62450)" FT /evidence="ECO:0000305" FT CONFLICT 472 FT /note="L -> G (in Ref. 4; AAA62450)" FT /evidence="ECO:0000305" FT CONFLICT 538 FT /note="R -> G (in Ref. 4; AAA62450)" FT /evidence="ECO:0000305" FT CONFLICT 560 FT /note="V -> G (in Ref. 4; AAA62450)" FT /evidence="ECO:0000305" SQ SEQUENCE 591 AA; 67278 MW; 0D9F8FE03434BADC CRC64; MEGKWLLCLL LVLGTAAVEA HDGHDDDAID IEDDLDDVIE EVEDSKSKSD ASTPPSPKVT YKAPVPTGEV YFADSFDRGS LSGWILSKAK KDDTDDEIAK YDGKWEVDEM KETKLPGDKG LVLMSRAKHH AISAKLNKPF LFDTKPLIVQ YEVNFQNGIE CGGAYVKLLS KTAELSLDQF HDKTPYTIMF GPDKCGEDYK LHFIFRHKNP KTGVYEEKHA KRPDADLKTY FTDKKTHLYT LILNPDNSFE ILVDQSVVNS GNLLNDMTPP VNPSREIEDP EDRKPEDWDE RPKIADPDAV KPDDWDEDAP SKIPDEEATK PEGWLDDEPE YIPDPDAEKP EDWDEDMDGE WEAPQIANPK CESAPGCGVW QRPMIDNPNY KGKWKPPMID NPNYQGIWKP RKIPNPDFFE DLEPFKMTPF SAIGLELWSM TSDIFFDNFI ISGDRRVVDD WANDGWGLKK AADGAAEPGV VLQMLEAAEE RPWLWVVYIL TVALPVFLVI LFCCSGKKQS NAMEYKKTDA PQPDVKDEEG KEEEKNKRDE EEEEEKLEEK QKSDAEEDGV TGSQDEEDSK PKAEEDEILN RSPRNRKPRR E //