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 16-SEP-2015, entry version 177. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=8486646; 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., RA Calderon J., Schreiber R.B., Gray P.W.; RT "Human, mouse, and rat calnexin cDNA cloning: identification of RT potential calcium binding motifs and gene localization to human RT 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., RA Celis J.E.; RT "The molecular chaperones HSP28, GRP78, endoplasmin, and calnexin RT exhibit strikingly different levels in quiescent keratinocytes as RT compared to their proliferating normal and transformed counterparts: RT cDNA cloning and 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 RP AND 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., RA Carlson R., Wands J.R., Isselbacher K.J., Pillai S., Ozturk M.; RT "The major histocompatibility complex class I antigen-binding protein RT p88 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 RT protein database of normal human epidermal keratinocytes."; RL Electrophoresis 13:960-969(1992). RN [12] 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., RA Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., RA Hearing V.J., Hunt D.F., Appella E.; RT "Proteomic analysis of early melanosomes: identification of novel RT melanosomal proteins."; RL J. Proteome Res. 2:69-79(2003). RN [13] 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [14] 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 RT mutant channels in human long QT syndrome."; RL J. Biol. Chem. 281:4069-4074(2006). RN [15] 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., RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., RA 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 [16] 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 [17] 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 RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [18] 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554, AND IDENTIFICATION RP BY 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 RT enrichment and fractionation of phosphopeptides with strong anion RT exchange chromatography."; RL Proteomics 8:1346-1361(2008). RN [20] 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564, AND IDENTIFICATION RP BY 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 [22] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., 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 [23] RP INTERACTION WITH PPIB. RX PubMed=20801878; DOI=10.1074/jbc.M110.160101; RA Kozlov G., Bastos-Aristizabal S., Maattanen P., Rosenauer A., RA Zheng F., Killikelly A., Trempe J.F., Thomas D.Y., Gehring K.; RT "Structural basis of cyclophilin B binding by the RT calnexin/calreticulin P-domain."; RL J. Biol. Chem. 285:35551-35557(2010). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; SER-564 AND RP SER-583, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [25] 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., RA Buerckstuemmer T., 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 [26] RP IDENTIFICATION IN A COMPLEX WITH DERL1; DERL2; DDOST; RPN1; RPN2; RP SELK; STT3A; VIMP AND VCP. RX PubMed=22016385; DOI=10.1074/jbc.M111.310920; RA Shchedrina V.A., Everley R.A., Zhang Y., Gygi S.P., Hatfield D.L., RA Gladyshev V.N.; RT "Selenoprotein K binds multiprotein complexes and is involved in the RT regulation of endoplasmic reticulum homeostasis."; RL J. Biol. Chem. 286:42937-42948(2011). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; THR-562 AND RP SER-583, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [28] RP PALMITOYLATION AT CYS-502 AND CYS-503 BY DHHC6, SUBCELLULAR LOCATION, RP AND INTERACTION WITH SSR1. RX PubMed=22314232; DOI=10.1038/emboj.2012.15; RA Lakkaraju A.K., Abrami L., Lemmin T., Blaskovic S., Kunz B., RA Kihara A., 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 [29] 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 [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; THR-562; SER-564 RP AND SER-583, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Calcium-binding protein that interacts with newly CC synthesized glycoproteins in the endoplasmic reticulum. It may act CC in assisting protein assembly and/or in the retention within the CC ER of unassembled protein subunits. It seems to play a major role CC in the quality control apparatus of the ER by the retention of CC incorrectly folded proteins. Associated with partial T-cell CC antigen receptor complexes that escape the ER of immature CC thymocytes, it may function as a signaling complex regulating CC thymocyte maturation. Additionally it may play a role in receptor- CC mediated endocytosis at the synapse. CC -!- SUBUNIT: Interacts with MAPK3/ERK1. Interacts with KCNH2. CC Associates with ribosomes. Interacts with SGIP1; involved in CC negative regulation of endocytosis (By similarity). The CC palmitoylated form interacts with the ribosome-translocon complex CC component SSR1, promoting efficient folding of glycoproteins. CC Interacts with SERPINA2P/SERPINA2 and with the S and Z variants of CC SERPINA1. Part of a complex which includes CANX, DERL1, DERL2, CC DDOST/OST48, RPN1, RPN2, SELK, STT3A, VCP AND VIMP. Interacts with CC PPIB. {ECO:0000250, ECO:0000269|PubMed:16361248, CC ECO:0000269|PubMed:20801878, ECO:0000269|PubMed:22016385, CC ECO:0000269|PubMed:22314232, ECO:0000269|PubMed:23826168}. CC -!- INTERACTION: CC P11607:ATP2A2 (xeno); NbExp=2; IntAct=EBI-355947, EBI-8004986; CC P13569:CFTR; NbExp=3; IntAct=EBI-355947, EBI-349854; CC Q92597:NDRG1; NbExp=2; IntAct=EBI-355947, EBI-716486; CC P41143:OPRD1; NbExp=2; IntAct=EBI-355947, EBI-2624456; CC P30050:RPL12; NbExp=3; IntAct=EBI-355947, EBI-352743; CC P61619:SEC61A1; NbExp=3; IntAct=EBI-355947, EBI-358919; CC P43307:SSR1; NbExp=5; IntAct=EBI-355947, EBI-714168; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC type I membrane protein. Endoplasmic reticulum. Melanosome. CC Note=Identified by mass spectrometry in melanosome fractions from CC stage I to stage IV. The palmitoylated form preferentially CC localizes to the perinuclear rough ER. 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 Note=No experimental confirmation available.; CC Name=3; CC IsoId=P27824-3; Sequence=VSP_055515; CC Note=No experimental confirmation available.; CC -!- PTM: Phosphorylated at Ser-564 by MAPK3/ERK1. phosphorylation by CC MAPK3/ERK1 increases its association with ribosomes (By CC similarity). {ECO:0000250}. CC -!- PTM: Palmitoylation by DHHC6 leads to the preferential CC localization to the perinuclear rough ER. It mediates the CC association of calnexin with the ribosome-translocon complex (RTC) CC which is required for efficient folding of glycosylated proteins. CC {ECO:0000269|PubMed:22314232}. CC -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Calnexin entry; CC URL="http://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 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_011534665.1. [P27824-1] DR UniGene; Hs.567968; -. DR ProteinModelPortal; P27824; -. DR SMR; P27824; 60-457. DR BioGrid; 107271; 145. DR DIP; DIP-457N; -. DR IntAct; P27824; 68. DR MINT; MINT-5000964; -. DR STRING; 9606.ENSP00000247461; -. DR BindingDB; P27824; -. DR ChEMBL; CHEMBL2719; -. DR DrugBank; DB00025; Antihemophilic Factor. DR DrugBank; DB00031; Tenecteplase. DR PhosphoSite; P27824; -. DR BioMuta; CANX; -. DR DMDM; 543920; -. DR MaxQB; P27824; -. DR PaxDb; P27824; -. DR PeptideAtlas; P27824; -. DR PRIDE; P27824; -. DR DNASU; 821; -. DR Ensembl; ENST00000247461; ENSP00000247461; ENSG00000127022. [P27824-1] DR Ensembl; ENST00000452673; ENSP00000391646; ENSG00000127022. [P27824-1] DR Ensembl; ENST00000504734; ENSP00000424063; ENSG00000127022. [P27824-1] DR GeneID; 821; -. DR KEGG; hsa:821; -. DR UCSC; uc003mkk.3; human. [P27824-1] DR UCSC; uc011dgp.2; human. DR CTD; 821; -. DR GeneCards; GC05P179678; -. DR HGNC; HGNC:1473; CANX. DR HPA; CAB004738; -. DR HPA; HPA009433; -. DR HPA; HPA009696; -. DR MIM; 114217; gene. DR neXtProt; NX_P27824; -. DR PharmGKB; PA26055; -. DR eggNOG; NOG305105; -. DR GeneTree; ENSGT00430000030841; -. DR HOGENOM; HOG000192436; -. DR HOVERGEN; HBG005407; -. DR InParanoid; P27824; -. DR KO; K08054; -. DR OMA; VDDWASD; -. DR OrthoDB; EOG77126Z; -. DR PhylomeDB; P27824; -. DR TreeFam; TF300618; -. 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-901042; Calnexin/calreticulin cycle. DR Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC. DR ChiTaRS; CANX; human. DR GeneWiki; Calnexin; -. DR GenomeRNAi; 821; -. DR NextBio; 3360; -. DR PRO; PR:P27824; -. DR Proteomes; UP000005640; Chromosome 5. DR Bgee; P27824; -. DR CleanEx; HS_CANX; -. 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:0044233; C:ER-mitochondrion membrane contact site; IDA:MGI. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0043209; C:myelin sheath; IEA:Ensembl. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0043234; C:protein 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:0005509; F:calcium ion binding; TAS:ProtInc. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0007568; P:aging; IEA:Ensembl. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome. DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:Ensembl. DR GO; GO:0072583; P:clathrin-mediated endocytosis; ISS:UniProtKB. DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome. DR GO; GO:0006457; P:protein folding; TAS:Reactome. DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; TAS:ParkinsonsUK-UCL. DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome. DR GO; GO:0009306; P:protein secretion; TAS:ProtInc. DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISS:UniProtKB. DR Gene3D; 2.10.250.10; -; 1. DR Gene3D; 2.60.120.200; -; 1. DR InterPro; IPR001580; Calret/calnex. DR InterPro; IPR018124; Calret/calnex_CS. DR InterPro; IPR009033; Calreticulin/calnexin_P_dom. DR InterPro; IPR013320; ConA-like_dom. 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; Alternative splicing; Calcium; Chaperone; KW Complete proteome; Direct protein sequencing; Disulfide bond; KW Endoplasmic reticulum; Lectin; Lipoprotein; Membrane; Metal-binding; KW Palmitate; Phosphoprotein; Reference proteome; Repeat; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 20 {ECO:0000255}. FT CHAIN 21 592 Calnexin. FT /FTId=PRO_0000004198. FT TOPO_DOM 21 481 Lumenal. {ECO:0000255}. FT TRANSMEM 482 502 Helical. {ECO:0000255}. FT TOPO_DOM 503 592 Cytoplasmic. {ECO:0000255}. FT REPEAT 278 290 1-1. FT REPEAT 295 307 1-2. FT REPEAT 314 326 1-3. FT REPEAT 333 345 1-4. FT REPEAT 348 358 2-1. FT REPEAT 367 377 2-2. FT REPEAT 381 391 2-3. FT REPEAT 395 405 2-4. FT REGION 276 409 P domain (Extended arm). {ECO:0000250}. FT REGION 278 345 4 X approximate repeats. FT REGION 326 359 Interaction with PPIB. {ECO:0000250}. FT REGION 348 405 4 X approximate repeats. FT REGION 503 592 Sufficient to mediate interaction with FT SGIP1. {ECO:0000250}. FT METAL 74 74 Calcium; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 117 117 Calcium; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 436 436 Calcium. {ECO:0000250}. FT BINDING 164 164 Carbohydrate. {ECO:0000250}. FT BINDING 166 166 Carbohydrate. {ECO:0000250}. FT BINDING 185 185 Carbohydrate. {ECO:0000250}. FT BINDING 216 216 Carbohydrate. {ECO:0000250}. FT MOD_RES 137 137 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 554 554 Phosphoserine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:18088087, FT ECO:0000244|PubMed:18318008, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:18691976, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 562 562 Phosphothreonine. FT {ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 564 564 Phosphoserine; by MAPK3. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 583 583 Phosphoserine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:18088087, FT ECO:0000244|PubMed:18691976, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:24275569}. FT LIPID 502 502 S-palmitoyl cysteine. FT {ECO:0000269|PubMed:22314232}. FT LIPID 503 503 S-palmitoyl cysteine. FT {ECO:0000269|PubMed:22314232}. FT DISULFID 160 194 {ECO:0000250}. FT DISULFID 360 366 {ECO:0000250}. FT VAR_SEQ 1 108 Missing (in isoform 3). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_055515. FT VAR_SEQ 1 1 M -> MADRRTPTPFAGCRLPRQRRARDASQVSAPGTRRIM FT (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_055516. FT CONFLICT 179 179 F -> L (in Ref. 2; AAA21749). FT {ECO:0000305}. FT CONFLICT 431 433 SDI -> LTF (in Ref. 10; AAA35696). FT {ECO:0000305}. FT CONFLICT 480 480 R -> L (in Ref. 10; AAA35696). FT {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 //