ID CALX_HUMAN Reviewed; 592 AA. AC P27824; B2R5V8; B4DGP8; B4E2T8; D3DWQ3; D6R9K3; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 2. DT 03-MAY-2023, entry version 239. DE RecName: Full=Calnexin; DE AltName: Full=IP90; DE AltName: Full=Major histocompatibility complex class I antigen-binding protein p88; DE AltName: Full=p90; DE Flags: Precursor; GN Name=CANX; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=8486646; DOI=10.1016/s0021-9258(18)98391-2; RA David V., Hochstenbach F., Rajagopalan S., Brenner M.B.; RT "Interaction with newly synthesized and retained proteins in the RT endoplasmic reticulum suggests a chaperone function for human integral RT membrane protein IP90 (calnexin)."; RL J. Biol. Chem. 268:9585-9592(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Lymph, and Placenta; 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Keratinocyte; RX PubMed=8055875; DOI=10.1002/elps.1150150166; RA Honore B., Rasmussen H.H., Celis A., Leffers H., Madsen P., Celis J.E.; RT "The molecular chaperones HSP28, GRP78, endoplasmin, and calnexin exhibit RT strikingly different levels in quiescent keratinocytes as compared to their RT proliferating normal and transformed counterparts: cDNA cloning and RT expression of calnexin."; RL Electrophoresis 15:482-490(1994). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Fibroblast; RA Hansen J.J., Jorgensen M.M., Bolund L., Gregersen N.; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC TISSUE=Brain, Cerebellum, and Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta; 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 [9] RP PROTEIN SEQUENCE OF 62-77; 171-193; 200-205; 221-227; 401-415; 517-525 AND RP 574-582, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (MAR-2005) to UniProtKB. RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 237-592 (ISOFORM 1). RX PubMed=1326756; DOI=10.1073/pnas.89.18.8452; RA Galvin K., Krishna S., Ponchel F., Frohlich M., Cummings D.E., Carlson R., RA Wands J.R., Isselbacher K.J., Pillai S., Ozturk M.; RT "The major histocompatibility complex class I antigen-binding protein p88 RT is the product of the calnexin gene."; RL Proc. Natl. Acad. Sci. U.S.A. 89:8452-8456(1992). RN [11] RP PROTEIN SEQUENCE OF 275-286; 293-313; 383-398 AND 516-523. RC TISSUE=Keratinocyte; RX PubMed=1286667; DOI=10.1002/elps.11501301199; RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., RA Vandekerckhove J.; RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein RT database of normal human epidermal keratinocytes."; RL Electrophoresis 13:960-969(1992). RN [12] RP INTERACTION WITH HBV LARGE ENVELOPE PROTEIN ISOFORM L (MICROBIAL RP INFECTION). RX PubMed=9188622; DOI=10.1128/jvi.71.7.5487-5494.1997; RA Xu Z., Bruss V., Yen T.S.; RT "Formation of intracellular particles by hepatitis B virus large surface RT protein."; RL J. Virol. 71:5487-5494(1997). RN [13] RP INTERACTION WITH HBV LARGE ENVELOPE PROTEIN ISOFORM M (MICROBIAL RP INFECTION). RX PubMed=9420286; DOI=10.1128/jvi.72.1.778-782.1998; RA Werr M., Prange R.; RT "Role for calnexin and N-linked glycosylation in the assembly and secretion RT of hepatitis B virus middle envelope protein particles."; RL J. Virol. 72:778-782(1998). RN [14] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=12643545; DOI=10.1021/pr025562r; RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., RA Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., RA Appella E.; RT "Proteomic analysis of early melanosomes: identification of novel RT melanosomal proteins."; RL J. Proteome Res. 2:69-79(2003). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554 AND SER-583, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [16] RP INTERACTION WITH KCNH2. RX PubMed=16361248; DOI=10.1074/jbc.m511765200; RA Gong Q., Jones M.A., Zhou Z.; RT "Mechanisms of pharmacological rescue of trafficking-defective hERG mutant RT channels in human long QT syndrome."; RL J. Biol. Chem. 281:4069-4074(2006). RN [17] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554 AND SER-583, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554 AND SER-583, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554 AND SER-564, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [24] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [25] RP INTERACTION WITH PPIB. RX PubMed=20801878; DOI=10.1074/jbc.m110.160101; RA Kozlov G., Bastos-Aristizabal S., Maattanen P., Rosenauer A., Zheng F., RA Killikelly A., Trempe J.F., Thomas D.Y., Gehring K.; RT "Structural basis of cyclophilin B binding by the calnexin/calreticulin P- RT domain."; RL J. Biol. Chem. 285:35551-35557(2010). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; SER-564 AND SER-583, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [27] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [28] RP INTERACTION WITH ZNRF4, AND UBIQUITINATION. RX PubMed=21205830; DOI=10.1074/jbc.m110.197459; RA Neutzner A., Neutzner M., Benischke A.S., Ryu S.W., Frank S., Youle R.J., RA Karbowski M.; RT "A systematic search for endoplasmic reticulum (ER) membrane-associated RT RING finger proteins identifies Nixin/ZNRF4 as a regulator of calnexin RT stability and ER homeostasis."; RL J. Biol. Chem. 286:8633-8643(2011). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; THR-562 AND SER-583, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [30] RP PALMITOYLATION AT CYS-502 AND CYS-503 BY DHHC6, SUBCELLULAR LOCATION, AND RP INTERACTION WITH SSR1. RX PubMed=22314232; DOI=10.1038/emboj.2012.15; RA Lakkaraju A.K., Abrami L., Lemmin T., Blaskovic S., Kunz B., Kihara A., RA Dal Peraro M., van der Goot F.G.; RT "Palmitoylated calnexin is a key component of the ribosome-translocon RT complex."; RL EMBO J. 31:1823-1835(2012). RN [31] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; THR-562; SER-564 AND RP SER-583, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [32] RP INTERACTION WITH SERPINA2P AND SERPINA1, AND SUBCELLULAR LOCATION. RX PubMed=23826168; DOI=10.1371/journal.pone.0066889; RA Marques P.I., Ferreira Z., Martins M., Figueiredo J., Silva D.I., RA Castro P., Morales-Hojas R., Simoes-Correia J., Seixas S.; RT "SERPINA2 is a novel gene with a divergent function from SERPINA1."; RL PLoS ONE 8:E66889-E66889(2013). RN [33] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; THR-562; SER-564 AND RP SER-583, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [34] RP INTERACTION WITH DNM1L. RX PubMed=24196833; DOI=10.1091/mbc.e13-09-0525; RA Shen Q., Yamano K., Head B.P., Kawajiri S., Cheung J.T., Wang C., Cho J.H., RA Hattori N., Youle R.J., van der Bliek A.M.; RT "Mutations in Fis1 disrupt orderly disposal of defective mitochondria."; RL Mol. Biol. Cell 25:145-159(2014). RN [35] RP CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-20, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [36] RP INTERACTION WITH SMIM22. RX PubMed=29765154; DOI=10.1038/s41388-018-0281-5; RA Polycarpou-Schwarz M., Gross M., Mestdagh P., Schott J., Grund S.E., RA Hildenbrand C., Rom J., Aulmann S., Sinn H.P., Vandesompele J., RA Diederichs S.; RT "The cancer-associated microprotein CASIMO1 controls cell proliferation and RT interacts with squalene epoxidase modulating lipid droplet formation."; RL Oncogene 37:4750-4768(2018). RN [37] RP INTERACTION WITH TMX2. RX PubMed=31735293; DOI=10.1016/j.ajhg.2019.10.009; RA Vandervore L.V., Schot R., Milanese C., Smits D.J., Kasteleijn E., RA Fry A.E., Pilz D.T., Brock S., Boerklue-Yuecel E., Post M., RA Bahi-Buisson N., Sanchez-Soler M.J., van Slegtenhorst M., Keren B., RA Afenjar A., Coury S.A., Tan W.H., Oegema R., de Vries L.S., Fawcett K.A., RA Nikkels P.G.J., Bertoli-Avella A., Al Hashem A., Alwabel A.A., RA Tlili-Graiess K., Efthymiou S., Zafar F., Rana N., Bibi F., Houlden H., RA Maroofian R., Person R.E., Crunk A., Savatt J.M., Turner L., Doosti M., RA Karimiani E.G., Saadi N.W., Akhondian J., Lequin M.H., Kayserili H., RA van der Spek P.J., Jansen A.C., Kros J.M., Verdijk R.M., Milosevic N.J., RA Fornerod M., Mastroberardino P.G., Mancini G.M.S.; RT "TMX2 is a crucial regulator of cellular redox state, and its dysfunction RT causes severe brain developmental abnormalities."; RL Am. J. Hum. Genet. 105:1126-1147(2019). RN [38] RP INTERACTION WITH CHRNA7. 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). RN [39] RP INTERACTION WITH RETREG2 AND RETREG3. RX PubMed=34338405; DOI=10.15252/embr.202052289; RA Reggio A., Buonomo V., Berkane R., Bhaskara R.M., Tellechea M., Peluso I., RA Polishchuk E., Di Lorenzo G., Cirillo C., Esposito M., Hussain A., RA Huebner A.K., Huebner C.A., Settembre C., Hummer G., Grumati P., Stolz A.; RT "Role of FAM134 paralogues in endoplasmic reticulum remodeling, ER-phagy, RT and Collagen quality control."; RL EMBO Rep. 22:e52289-e52289(2021). 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 -!- SUBUNIT: Interacts with MAPK3/ERK1 (By similarity). Interacts with CC KCNH2 (PubMed:16361248). Associates with ribosomes (By similarity). CC Interacts with SGIP1; involved in negative regulation of endocytosis CC (By similarity). The palmitoylated form interacts with the ribosome- CC translocon complex component SSR1, promoting efficient folding of CC glycoproteins (PubMed:22314232). Interacts with SERPINA2P/SERPINA2 and CC with the S and Z variants of SERPINA1 (PubMed:23826168). Interacts with CC PPIB (PubMed:20801878). Interacts with ZNRF4 (PubMed:21205830). CC Interacts with SMIM22 (PubMed:29765154). Interacts with TMX2 CC (PubMed:31735293). Interacts with TMEM35A/NACHO (By similarity). CC Interacts with CHRNA7 (PubMed:32783947). Interacts with reticulophagy CC regulators RETREG2 and RETREG3 (PubMed:34338405). Interacts with DNM1L; CC may form part of a larger protein complex at the ER-mitochondrial CC interface during mitochondrial fission (PubMed:24196833). CC {ECO:0000250|UniProtKB:P35564, ECO:0000250|UniProtKB:P35565, CC ECO:0000269|PubMed:16361248, ECO:0000269|PubMed:20801878, CC ECO:0000269|PubMed:21205830, ECO:0000269|PubMed:22314232, CC ECO:0000269|PubMed:23826168, ECO:0000269|PubMed:29765154, CC ECO:0000269|PubMed:31735293, ECO:0000269|PubMed:32783947, CC ECO:0000269|PubMed:34338405}. CC -!- SUBUNIT: (Microbial infection) Interacts with HBV large envelope CC protein, isoform L. {ECO:0000269|PubMed:9188622}. CC -!- SUBUNIT: (Microbial infection) Interacts with HBV large envelope CC protein, isoform M; this association may be essential for isoform M CC proper secretion. {ECO:0000269|PubMed:9188622}. CC -!- INTERACTION: CC P27824; O95477: ABCA1; NbExp=8; IntAct=EBI-355947, EBI-784112; CC P27824; P13569: CFTR; NbExp=13; IntAct=EBI-355947, EBI-349854; CC P27824; Q7LFX5: CHST15; NbExp=2; IntAct=EBI-355947, EBI-11123530; CC P27824; Q9UHC6-1: CNTNAP2; NbExp=2; IntAct=EBI-355947, EBI-16594440; CC P27824; Q92597: NDRG1; NbExp=2; IntAct=EBI-355947, EBI-716486; CC P27824; P41143: OPRD1; NbExp=2; IntAct=EBI-355947, EBI-2624456; CC P27824; P30050: RPL12; NbExp=3; IntAct=EBI-355947, EBI-352743; CC P27824; P61619: SEC61A1; NbExp=4; IntAct=EBI-355947, EBI-358919; CC P27824; P43307: SSR1; NbExp=6; IntAct=EBI-355947, EBI-714168; CC P27824; P11607: ATP2A2; Xeno; NbExp=2; IntAct=EBI-355947, EBI-8004986; CC P27824; P04578: env; Xeno; NbExp=3; IntAct=EBI-355947, EBI-6163496; CC P27824-2; P05067: APP; NbExp=3; IntAct=EBI-25890990, EBI-77613; CC P27824-2; P04271: S100B; NbExp=3; IntAct=EBI-25890990, EBI-458391; CC P27824-2; P43405-2: SYK; NbExp=3; IntAct=EBI-25890990, EBI-25892332; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:22314232}; Single-pass type I membrane protein CC {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:22314232}. CC Melanosome {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}. CC Note=Identified by mass spectrometry in melanosome fractions from stage CC I to stage IV (PubMed:12643545, PubMed:17081065). The palmitoylated CC form preferentially localizes to the perinuclear rough ER CC (PubMed:22314232). {ECO:0000269|PubMed:12643545, CC ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:22314232}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P27824-1; Sequence=Displayed; CC Name=2; CC IsoId=P27824-2; Sequence=VSP_055516; CC Name=3; CC IsoId=P27824-3; Sequence=VSP_055515; CC -!- PTM: Phosphorylated at Ser-564 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. {ECO:0000269|PubMed:22314232}. CC -!- PTM: Ubiquitinated, leading to proteasomal degradation. Probably CC ubiquitinated by ZNRF4. {ECO:0000269|PubMed:21205830}. CC -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Calnexin entry; CC URL="https://en.wikipedia.org/wiki/Calnexin"; 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; L10284; AAA36125.1; -; mRNA. DR EMBL; L18887; AAA21013.1; -; mRNA. DR EMBL; M94859; AAA21749.1; -; mRNA. DR EMBL; M98452; AAA35696.1; -; mRNA. DR EMBL; AK294702; BAG57859.1; -; mRNA. DR EMBL; AK304420; BAG65250.1; -; mRNA. DR EMBL; AK312334; BAG35255.1; -; mRNA. DR EMBL; AC113426; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC136604; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471165; EAW53802.1; -; Genomic_DNA. DR EMBL; CH471165; EAW53803.1; -; Genomic_DNA. DR EMBL; CH471165; EAW53805.1; -; Genomic_DNA. DR EMBL; BC003552; AAH03552.1; -; mRNA. DR EMBL; BC042843; AAH42843.1; -; mRNA. DR EMBL; AJ271880; CAB72137.1; -; mRNA. DR CCDS; CCDS4447.1; -. [P27824-1] DR CCDS; CCDS93840.1; -. [P27824-3] DR PIR; A46164; A46164. DR PIR; A46673; A46673. DR PIR; I53260; I53260. DR RefSeq; NP_001019820.1; NM_001024649.1. [P27824-1] DR RefSeq; NP_001737.1; NM_001746.3. [P27824-1] DR RefSeq; XP_011532967.1; XM_011534665.2. [P27824-1] DR AlphaFoldDB; P27824; -. DR SMR; P27824; -. DR BioGRID; 107271; 1268. DR CORUM; P27824; -. DR DIP; DIP-457N; -. DR IntAct; P27824; 586. DR MINT; P27824; -. DR STRING; 9606.ENSP00000247461; -. DR BindingDB; P27824; -. DR ChEMBL; CHEMBL2719; -. DR DrugBank; DB00025; Antihemophilic factor, human recombinant. DR DrugBank; DB11093; Calcium citrate. DR DrugBank; DB11348; Calcium Phosphate. DR DrugBank; DB14481; Calcium phosphate dihydrate. DR DrugBank; DB06245; Lanoteplase. DR DrugBank; DB13998; Lonoctocog alfa. DR DrugBank; DB13999; Moroctocog alfa. DR DrugBank; DB00031; Tenecteplase. DR TCDB; 8.A.165.1.1; the calnexin (calnexin) family. DR GlyCosmos; P27824; 3 sites, 2 glycans. DR GlyGen; P27824; 7 sites, 4 O-linked glycans (7 sites). DR iPTMnet; P27824; -. DR PhosphoSitePlus; P27824; -. DR SwissPalm; P27824; -. DR BioMuta; CANX; -. DR DMDM; 543920; -. DR EPD; P27824; -. DR jPOST; P27824; -. DR MassIVE; P27824; -. DR MaxQB; P27824; -. DR PaxDb; P27824; -. DR PeptideAtlas; P27824; -. DR PRIDE; P27824; -. DR ProteomicsDB; 54425; -. [P27824-1] DR ProteomicsDB; 5850; -. DR TopDownProteomics; P27824-1; -. [P27824-1] DR ABCD; P27824; 1 sequenced antibody. DR Antibodypedia; 2421; 1166 antibodies from 46 providers. DR DNASU; 821; -. DR Ensembl; ENST00000247461.9; ENSP00000247461.4; ENSG00000127022.16. [P27824-1] DR Ensembl; ENST00000452673.6; ENSP00000391646.2; ENSG00000127022.16. [P27824-1] DR Ensembl; ENST00000502296.6; ENSP00000424745.2; ENSG00000127022.16. [P27824-1] DR Ensembl; ENST00000504734.5; ENSP00000424063.1; ENSG00000127022.16. [P27824-1] DR Ensembl; ENST00000506654.6; ENSP00000426555.2; ENSG00000127022.16. [P27824-3] DR Ensembl; ENST00000509563.2; ENSP00000421434.2; ENSG00000127022.16. [P27824-1] DR Ensembl; ENST00000513246.6; ENSP00000421813.2; ENSG00000127022.16. [P27824-1] DR Ensembl; ENST00000638425.1; ENSP00000492372.1; ENSG00000283777.2. [P27824-1] DR Ensembl; ENST00000638706.2; ENSP00000492868.1; ENSG00000283777.2. [P27824-1] DR Ensembl; ENST00000639938.1; ENSP00000491760.1; ENSG00000283777.2. [P27824-1] DR Ensembl; ENST00000680006.1; ENSP00000505129.1; ENSG00000127022.16. [P27824-3] DR Ensembl; ENST00000680013.1; ENSP00000506078.1; ENSG00000127022.16. [P27824-1] DR Ensembl; ENST00000680042.1; ENSP00000505960.1; ENSG00000127022.16. [P27824-1] DR Ensembl; ENST00000680092.1; ENSP00000505202.1; ENSG00000127022.16. [P27824-1] DR Ensembl; ENST00000680618.1; ENSP00000506583.1; ENSG00000127022.16. [P27824-1] DR Ensembl; ENST00000680827.1; ENSP00000506051.1; ENSG00000127022.16. [P27824-3] DR Ensembl; ENST00000681072.1; ENSP00000505526.1; ENSG00000127022.16. [P27824-1] DR Ensembl; ENST00000681168.1; ENSP00000506021.1; ENSG00000127022.16. [P27824-1] DR Ensembl; ENST00000681476.1; ENSP00000506003.1; ENSG00000127022.16. [P27824-1] DR Ensembl; ENST00000681674.1; ENSP00000505013.1; ENSG00000127022.16. [P27824-1] DR Ensembl; ENST00000681712.1; ENSP00000506061.1; ENSG00000127022.16. [P27824-1] DR Ensembl; ENST00000681733.1; ENSP00000506568.1; ENSG00000127022.16. [P27824-1] DR Ensembl; ENST00000681903.1; ENSP00000506509.1; ENSG00000127022.16. [P27824-1] DR GeneID; 821; -. DR KEGG; hsa:821; -. DR MANE-Select; ENST00000247461.9; ENSP00000247461.4; NM_001746.4; NP_001737.1. DR UCSC; uc003mkk.4; human. [P27824-1] DR AGR; HGNC:1473; -. DR CTD; 821; -. DR DisGeNET; 821; -. DR GeneCards; CANX; -. DR HGNC; HGNC:1473; CANX. DR HPA; ENSG00000127022; Low tissue specificity. DR MIM; 114217; gene. DR neXtProt; NX_P27824; -. DR OpenTargets; ENSG00000127022; -. DR PharmGKB; PA26055; -. DR VEuPathDB; HostDB:ENSG00000127022; -. DR eggNOG; KOG0675; Eukaryota. DR GeneTree; ENSGT00950000182915; -. DR HOGENOM; CLU_018224_2_0_1; -. DR InParanoid; P27824; -. DR OMA; SGCGKWE; -. DR OrthoDB; 5489154at2759; -. DR PhylomeDB; P27824; -. DR TreeFam; TF300618; -. DR PathwayCommons; P27824; -. DR Reactome; R-HSA-168316; Assembly of Viral Components at the Budding Site. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-8984722; Interleukin-35 Signalling. DR Reactome; R-HSA-901042; Calnexin/calreticulin cycle. DR Reactome; R-HSA-9020956; Interleukin-27 signaling. DR Reactome; R-HSA-9683686; Maturation of spike protein. DR Reactome; R-HSA-9694548; Maturation of spike protein. DR Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC. DR SignaLink; P27824; -. DR BioGRID-ORCS; 821; 18 hits in 1165 CRISPR screens. DR ChiTaRS; CANX; human. DR GeneWiki; Calnexin; -. DR GenomeRNAi; 821; -. DR Pharos; P27824; Tbio. DR PRO; PR:P27824; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; P27824; protein. DR Bgee; ENSG00000127022; Expressed in stromal cell of endometrium and 112 other tissues. DR ExpressionAtlas; P27824; baseline and differential. DR Genevisible; P27824; HS. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0032839; C:dendrite cytoplasm; IEA:Ensembl. DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:AgBase. DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0098553; C:lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IDA:MGI. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl. DR GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl. DR GO; GO:0048787; C:presynaptic active zone membrane; IEA:Ensembl. DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl. DR GO; GO:0005840; C:ribosome; IEA:Ensembl. DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0034185; F:apolipoprotein binding; IEA:Ensembl. 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; IEA:Ensembl. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0051082; F:unfolded protein binding; TAS:Reactome. DR GO; GO:0007568; P:aging; IEA:Ensembl. DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISS:UniProtKB. DR GO; GO:0006457; P:protein folding; IBA:GO_Central. DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; TAS:ParkinsonsUK-UCL. DR GO; GO:0009306; P:protein secretion; TAS:ProtInc. DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISS:UniProtKB. DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central. DR GO; GO:0019082; P:viral protein processing; TAS:Reactome. 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. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Calcium; Chaperone; KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; KW Host-virus interaction; Lectin; Lipoprotein; Membrane; Metal-binding; KW Palmitate; Phosphoprotein; Reference proteome; Repeat; Signal; KW Transmembrane; Transmembrane helix; Ubl conjugation. FT SIGNAL 1..20 FT /evidence="ECO:0000255, ECO:0007744|PubMed:25944712" FT CHAIN 21..592 FT /note="Calnexin" FT /id="PRO_0000004198" FT TOPO_DOM 21..481 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 482..502 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 503..592 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 278..290 FT /note="1-1" FT REPEAT 295..307 FT /note="1-2" FT REPEAT 314..326 FT /note="1-3" FT REPEAT 333..345 FT /note="1-4" FT REPEAT 348..358 FT /note="2-1" FT REPEAT 367..377 FT /note="2-2" FT REPEAT 381..391 FT /note="2-3" FT REPEAT 395..405 FT /note="2-4" FT REGION 260..345 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 276..409 FT /note="P domain (Extended arm)" FT /evidence="ECO:0000250" FT REGION 278..345 FT /note="4 X approximate repeats" FT REGION 326..359 FT /note="Interaction with PPIB" FT /evidence="ECO:0000250" FT REGION 348..405 FT /note="4 X approximate repeats" FT REGION 503..592 FT /note="Sufficient to mediate interaction with SGIP1" FT /evidence="ECO:0000250" FT REGION 511..592 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 274..326 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 327..345 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 525..546 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 547..585 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 74 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 117 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 164 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 166 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 185 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 192 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 425 FT /ligand="an alpha-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22390" FT /evidence="ECO:0000250|UniProtKB:P14211" FT BINDING 436 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT MOD_RES 137 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 554 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 562 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 564 FT /note="Phosphoserine; by MAPK3" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 583 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT LIPID 502 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:22314232" FT LIPID 503 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:22314232" FT DISULFID 160..194 FT /evidence="ECO:0000250" FT DISULFID 360..366 FT /evidence="ECO:0000250" FT VAR_SEQ 1..108 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055515" FT VAR_SEQ 1 FT /note="M -> MADRRTPTPFAGCRLPRQRRARDASQVSAPGTRRIM (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055516" FT CONFLICT 179 FT /note="F -> L (in Ref. 2; AAA21749)" FT /evidence="ECO:0000305" FT CONFLICT 431..433 FT /note="SDI -> LTF (in Ref. 10; AAA35696)" FT /evidence="ECO:0000305" FT CONFLICT 480 FT /note="R -> L (in Ref. 10; AAA35696)" FT /evidence="ECO:0000305" SQ SEQUENCE 592 AA; 67568 MW; EDE094D9B82261EE CRC64; MEGKWLLCML LVLGTAIVEA HDGHDDDVID IEDDLDDVIE EVEDSKPDTT APPSSPKVTY KAPVPTGEVY FADSFDRGTL SGWILSKAKK DDTDDEIAKY DGKWEVEEMK ESKLPGDKGL VLMSRAKHHA ISAKLNKPFL FDTKPLIVQY EVNFQNGIEC GGAYVKLLSK TPELNLDQFH DKTPYTIMFG PDKCGEDYKL HFIFRHKNPK TGIYEEKHAK RPDADLKTYF TDKKTHLYTL ILNPDNSFEI LVDQSVVNSG NLLNDMTPPV NPSREIEDPE DRKPEDWDER PKIPDPEAVK PDDWDEDAPA KIPDEEATKP EGWLDDEPEY VPDPDAEKPE DWDEDMDGEW EAPQIANPRC ESAPGCGVWQ RPVIDNPNYK GKWKPPMIDN PSYQGIWKPR KIPNPDFFED LEPFRMTPFS AIGLELWSMT SDIFFDNFII CADRRIVDDW ANDGWGLKKA ADGAAEPGVV GQMIEAAEER PWLWVVYILT VALPVFLVIL FCCSGKKQTS GMEYKKTDAP QPDVKEEEEE KEEEKDKGDE EEEGEEKLEE KQKSDAEEDG GTVSQEEEDR KPKAEEDEIL NRSPRNRKPR RE //