ID CALX_HUMAN Reviewed; 592 AA. AC P27824; B2R5V8; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 2. DT 02-NOV-2010, entry version 127. 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]. RX MEDLINE=93252832; 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]. RC TISSUE=Lymph, and Placenta; RX MEDLINE=94183823; 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]. RC TISSUE=Keratinocyte; RX MEDLINE=94333293; 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]. 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]. RC TISSUE=Cerebellum; 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]. 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [8] RP PROTEIN SEQUENCE OF 62-77; 171-193; 200-205; 221-227; 401-415; 517-525 RP AND 574-582, AND MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (MAR-2005) to UniProtKB. RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 237-592. RX MEDLINE=92409534; 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 [10] RP PARTIAL PROTEIN SEQUENCE OF 275-286; 293-313; 383-398 AND 516-523. RC TISSUE=Keratinocyte; RX MEDLINE=93162043; 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 [11] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583, AND MASS RP SPECTROMETRY. RC TISSUE=Colon adenocarcinoma; RX PubMed=16083285; DOI=10.1021/pr050048h; RA Kim J.-E., Tannenbaum S.R., White F.M.; RT "Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; RL J. Proteome Res. 4:1339-1346(2005). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; SER-564 AND RP SER-583, AND MASS SPECTROMETRY. 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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-562 AND SER-583, AND RP MASS SPECTROMETRY. RC TISSUE=Cervix adenocarcinoma; RX PubMed=16565220; DOI=10.1073/pnas.0507066103; RA Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; RT "Phosphoproteome analysis of the human mitotic spindle."; RL Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa RT cells and high confident phosphopeptide identification by cross- RT validation of MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=19007248; DOI=10.1021/ac801708p; RA Wang B., Malik R., Nigg E.A., Korner R.; RT "Evaluation of the low-specificity protease elastase for large-scale RT phosphoproteome analysis."; RL Anal. Chem. 80:9526-9533(2008). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; SER-564 AND RP SER-583, AND MASS SPECTROMETRY. 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-583, AND MASS RP SPECTROMETRY. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using RT sequential IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554 AND SER-583, AND RP MASS SPECTROMETRY. 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; SER-564 AND RP SER-583, AND MASS SPECTROMETRY. 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 [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554 AND SER-564, AND RP MASS SPECTROMETRY. 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 [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583, AND MASS RP SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; SER-564 AND RP SER-583, AND MASS SPECTROMETRY. 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 [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554 AND SER-564, AND RP MASS SPECTROMETRY. 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 [27] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137, AND MASS SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., 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). 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. CC -!- INTERACTION: CC Q92597:NDRG1; NbExp=2; IntAct=EBI-355947, EBI-716486; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC type I membrane protein. Melanosome. Note=Identified by mass CC spectrometry in melanosome fractions from stage I to stage IV. CC -!- SIMILARITY: Belongs to the calreticulin family. 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; AK312334; BAG35255.1; -; mRNA. DR EMBL; CH471165; EAW53802.1; -; Genomic_DNA. DR EMBL; BC003552; AAH03552.1; -; mRNA. DR EMBL; BC042843; AAH42843.1; -; mRNA. DR EMBL; AJ271880; CAB72137.1; -; mRNA. DR IPI; IPI00941747; -. DR PIR; A46164; A46164. DR PIR; A46673; A46673. DR PIR; I53260; I53260. DR RefSeq; NP_001019820.1; -. DR RefSeq; NP_001737.1; -. DR UniGene; Hs.567968; -. DR ProteinModelPortal; P27824; -. DR SMR; P27824; 60-457. DR DIP; DIP-457N; -. DR IntAct; P27824; 21. DR MINT; MINT-5000964; -. DR STRING; P27824; -. DR PhosphoSite; P27824; -. DR Aarhus/Ghent-2DPAGE; 9702; IEF. DR PeptideAtlas; P27824; -. DR PRIDE; P27824; -. DR Ensembl; ENST00000247461; ENSP00000247461; ENSG00000127022. DR Ensembl; ENST00000415618; ENSP00000394817; ENSG00000127022. DR Ensembl; ENST00000452673; ENSP00000391646; ENSG00000127022. DR GeneID; 821; -. DR KEGG; hsa:821; -. DR UCSC; uc003mkk.1; human. DR CTD; 821; -. DR GeneCards; GC05P179058; -. DR H-InvDB; HIX0005484; -. DR HGNC; HGNC:1473; CANX. DR HPA; CAB004738; -. DR HPA; HPA009433; -. DR HPA; HPA009696; -. DR MIM; 114217; gene. DR PharmGKB; PA26055; -. DR eggNOG; prNOG10502; -. DR HOVERGEN; HBG005407; -. DR InParanoid; P27824; -. DR PhylomeDB; P27824; -. DR DrugBank; DB00009; Alteplase. DR DrugBank; DB00029; Anistreplase. DR DrugBank; DB00025; Antihemophilic Factor. DR DrugBank; DB00015; Reteplase. DR DrugBank; DB00031; Tenecteplase. DR NextBio; 3360; -. DR ArrayExpress; P27824; -. DR Bgee; P27824; -. DR CleanEx; HS_CANX; -. DR Genevestigator; P27824; -. DR GermOnline; ENSG00000127022; Homo sapiens. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc. DR GO; GO:0005529; F:sugar binding; IEA:UniProtKB-KW. DR GO; GO:0051082; F:unfolded protein binding; NAS:UniProtKB. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR GO; GO:0009306; P:protein secretion; TAS:ProtInc. DR InterPro; IPR001580; Calret/calnex. DR InterPro; IPR018124; Calret/calnex_CS. DR InterPro; IPR009033; Calreticulin/calnexin_P. DR InterPro; IPR008985; ConA-like_lec_gl. DR InterPro; IPR013320; ConA-like_subgrp. DR Gene3D; G3DSA:2.10.250.10; Calreticulin/calnexin_P; 2. DR Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 1. DR PANTHER; PTHR11073; Calret/calnex; 1. DR Pfam; PF00262; Calreticulin; 1. DR PRINTS; PR00626; CALRETICULIN. DR SUPFAM; SSF63887; Calret_calnex_P; 1. DR SUPFAM; SSF49899; ConA_like_lec_gl; 2. 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; Complete proteome; KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; KW Lectin; Membrane; Metal-binding; Phosphoprotein; Repeat; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 20 Potential. FT CHAIN 21 592 Calnexin. FT /FTId=PRO_0000004198. FT TOPO_DOM 21 481 Lumenal (Potential). FT TRANSMEM 482 502 Helical; (Potential). FT TOPO_DOM 503 592 Cytoplasmic (Potential). 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) (By similarity). FT REGION 278 345 4 X approximate repeats. FT REGION 348 405 4 X approximate repeats. FT METAL 74 74 Calcium; via carbonyl oxygen (By FT similarity). FT METAL 117 117 Calcium; via carbonyl oxygen (By FT similarity). FT METAL 436 436 Calcium (By similarity). FT BINDING 164 164 Carbohydrate (By similarity). FT BINDING 166 166 Carbohydrate (By similarity). FT BINDING 185 185 Carbohydrate (By similarity). FT BINDING 216 216 Carbohydrate (By similarity). FT MOD_RES 137 137 N6-acetyllysine. FT MOD_RES 554 554 Phosphoserine. FT MOD_RES 562 562 Phosphothreonine. FT MOD_RES 564 564 Phosphoserine. FT MOD_RES 583 583 Phosphoserine. FT DISULFID 160 194 By similarity. FT DISULFID 360 366 By similarity. FT CONFLICT 179 179 F -> L (in Ref. 2; AAA21749). FT CONFLICT 431 433 SDI -> LTF (in Ref. 9; AAA35696). FT CONFLICT 480 480 R -> L (in Ref. 9; AAA35696). 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 //