CALX_MOUSE
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 03-AUG-2022, entry version 202.
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, Pancreas,
RC 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 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 [14]
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).
CC {ECO:0000250|UniProtKB:P27824, ECO:0000250|UniProtKB:P35565,
CC ECO:0000269|PubMed:21747946, 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}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P27824}.
CC Melanosome {ECO:0000250|UniProtKB:P27824}. Note=The palmitoylated form
CC preferentially localizes to the perinuclear rough ER (By similarity).
CC When bound to CD3 epsilon chains, calnexin's ER retention signal can be
CC masked, permitting it to escape ER retention.
CC {ECO:0000250|UniProtKB:P27824}.
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; 46.
DR CORUM; P35564; -.
DR IntAct; P35564; 15.
DR MINT; P35564; -.
DR STRING; 10090.ENSMUSP00000020637; -.
DR iPTMnet; P35564; -.
DR PhosphoSitePlus; P35564; -.
DR SwissPalm; P35564; -.
DR EPD; P35564; -.
DR jPOST; P35564; -.
DR PaxDb; P35564; -.
DR PeptideAtlas; P35564; -.
DR PRIDE; P35564; -.
DR ProteomicsDB; 265514; -.
DR Antibodypedia; 2421; 1151 antibodies from 46 providers.
DR DNASU; 12330; -.
DR Ensembl; ENSMUST00000020637; ENSMUSP00000020637; ENSMUSG00000020368.
DR Ensembl; ENSMUST00000179865; ENSMUSP00000137440; ENSMUSG00000020368.
DR GeneID; 12330; -.
DR KEGG; mmu:12330; -.
DR UCSC; uc007isf.2; mouse.
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; ANPKCEA; -.
DR OrthoDB; 775337at2759; -.
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-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR BioGRID-ORCS; 12330; 2 hits in 74 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 254 other tissues.
DR ExpressionAtlas; P35564; baseline and differential.
DR Genevisible; P35564; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; 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:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; ISO:MGI.
DR GO; GO:0042470; C:melanosome; 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:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005840; C:ribosome; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; 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:0007568; P:aging; IEA:Ensembl.
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; 2.10.250.10; -; 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; PTHR11073; 1.
DR Pfam; PF00262; Calreticulin; 1.
DR PRINTS; PR00626; CALRETICULIN.
DR SUPFAM; SSF49899; SSF49899; 2.
DR SUPFAM; SSF63887; SSF63887; 1.
DR PROSITE; PS00803; CALRETICULIN_1; 1.
DR PROSITE; PS00804; CALRETICULIN_2; 1.
DR PROSITE; PS00805; CALRETICULIN_REPEAT; 3.
PE 1: Evidence at protein level;
KW Acetylation; Calcium; Chaperone; Disulfide bond; Endoplasmic reticulum;
KW Lectin; Lipoprotein; Membrane; Metal-binding; Palmitate; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW 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"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
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"
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"
FT DISULFID 361..367
FT /evidence="ECO:0000250"
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
