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Endoplasmin (94 kDa glucose-regulated protein) (GRP-94) (Heat shock protein 90 kDa beta member 1) (Tumor rejection antigen 1) (gp96 homolog)

 ENPL_HUMAN              Reviewed;         803 AA.
P14625; Q96A97;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
22-NOV-2017, entry version 211.
RecName: Full=Endoplasmin;
AltName: Full=94 kDa glucose-regulated protein;
Short=GRP-94;
AltName: Full=Heat shock protein 90 kDa beta member 1;
AltName: Full=Tumor rejection antigen 1;
AltName: Full=gp96 homolog;
Flags: Precursor;
Name=HSP90B1; Synonyms=GRP94, TRA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF
1-16.
TISSUE=Blood;
PubMed=2377606; DOI=10.1073/pnas.87.15.5658;
Maki R.G., Old L.J., Srivastava P.K.;
"Human homologue of murine tumor rejection antigen gp96: 5'-regulatory
and coding regions and relationship to stress-induced proteins.";
Proc. Natl. Acad. Sci. U.S.A. 87:5658-5662(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
TISSUE=Liver;
PubMed=2546060; DOI=10.1128/MCB.9.5.2153;
Chang S.C., Erwin A.E., Lee A.S.;
"Glucose-regulated protein (GRP94 and GRP78) genes share common
regulatory domains and are coordinately regulated by common trans-
acting factors.";
Mol. Cell. Biol. 9:2153-2162(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 22-803.
TISSUE=Liver;
Meng S., Tien P.;
"The association of heat shock protein gp96 with HBV-derived peptides
in vitro.";
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[5]
PROTEIN SEQUENCE OF 22-39.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[6]
COMPONENT OF A CHAPERONE COMPLEX.
PubMed=12475965; DOI=10.1091/mbc.E02-05-0311;
Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
"A subset of chaperones and folding enzymes form multiprotein
complexes in endoplasmic reticulum to bind nascent proteins.";
Mol. Biol. Cell 13:4456-4469(2002).
[7]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=12643545; DOI=10.1021/pr025562r;
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
Hearing V.J., Hunt D.F., Appella E.;
"Proteomic analysis of early melanosomes: identification of novel
melanosomal proteins.";
J. Proteome Res. 2:69-79(2003).
[8]
GLYCOSYLATION AT ASN-217 AND ASN-445.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
INTERACTION WITH CNPY3; TLR4 AND TLR9.
PubMed=20865800; DOI=10.1038/ncomms1070;
Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y.,
Hao B., Bona R., Han D., Li Z.;
"Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a
substrate-specific cochaperone.";
Nat. Commun. 1:79-79(2010).
[11]
ERRATUM.
Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y.,
Hao B., Bona R., Han D., Li Z.;
Nat. Commun. 3:653-653(2012).
[12]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-107.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[14]
FUNCTION, AND INTERACTION WITH OS9.
PubMed=18264092; DOI=10.1038/ncb1689;
Christianson J.C., Shaler T.A., Tyler R.E., Kopito R.R.;
"OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L
ubiquitin ligase complex for ERAD.";
Nat. Cell Biol. 10:272-282(2008).
[15]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-62; ASN-107; ASN-217 AND
ASN-445.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
INTERACTION WITH METTL23.
PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
"A newly uncovered group of distantly related lysine
methyltransferases preferentially interact with molecular chaperones
to regulate their activity.";
PLoS Genet. 9:E1003210-E1003210(2013).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-447 AND THR-786,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
PHOSPHORYLATION AT SER-306.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[23]
CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-21, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Molecular chaperone that functions in the processing and
transport of secreted proteins. When associated with CNPY3,
required for proper folding of Toll-like receptors (By
similarity). Functions in endoplasmic reticulum associated
degradation (ERAD). Has ATPase activity. {ECO:0000250,
ECO:0000269|PubMed:18264092}.
-!- SUBUNIT: Homodimer; disulfide-linked. Component of an EIF2 complex
at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2,
HSP90B1 and HSPA5 (By similarity). Part of a large chaperone
multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU,
PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts
of ERP29, but not, or at very low levels, CALR nor CANX. Interacts
with AIMP1; regulates its retention in the endoplasmic reticulum.
Interacts with OS9. Interacts with CNPY3. This interaction is
disrupted in the presence of ATP (By similarity). Interacts with
TLR4 and TLR9, but not with TLR3. Interacts with MZB1 in a
calcium-dependent manner (By similarity). Interacts with METTL23.
{ECO:0000250, ECO:0000269|PubMed:18264092,
ECO:0000269|PubMed:20865800, ECO:0000269|PubMed:23349634}.
-!- INTERACTION:
P04626:ERBB2; NbExp=2; IntAct=EBI-359129, EBI-641062;
Q00597:FANCC; NbExp=4; IntAct=EBI-359129, EBI-81625;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Melanosome.
Note=Identified by mass spectrometry in melanosome fractions from
stage I to stage IV.
-!- SIMILARITY: Belongs to the heat shock protein 90 family.
{ECO:0000305}.
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EMBL; X15187; CAA33261.1; -; mRNA.
EMBL; M33716; AAA68201.1; -; Genomic_DNA.
EMBL; BC066656; AAH66656.1; -; mRNA.
EMBL; M26596; AAA58621.1; -; Genomic_DNA.
EMBL; AY040226; AAK74072.1; -; mRNA.
CCDS; CCDS9094.1; -.
PIR; A35954; A35954.
RefSeq; NP_003290.1; NM_003299.2.
UniGene; Hs.192374; -.
PDB; 4NH9; X-ray; 2.77 A; A=69-337.
PDBsum; 4NH9; -.
ProteinModelPortal; P14625; -.
SMR; P14625; -.
BioGrid; 113036; 159.
CORUM; P14625; -.
DIP; DIP-36060N; -.
IntAct; P14625; 78.
MINT; MINT-210408; -.
STRING; 9606.ENSP00000299767; -.
BindingDB; P14625; -.
ChEMBL; CHEMBL1075323; -.
DrugBank; DB02935; 1-Methoxy-2-(2-Methoxyethoxy)Ethane.
DrugBank; DB02103; 2-Chlorodideoxyadenosine.
DrugBank; DB03719; N-Ethyl-5'-Carboxamido Adenosine.
DrugBank; DB03758; Radicicol.
DrugBank; DB00615; Rifabutin.
GuidetoPHARMACOLOGY; 2904; -.
iPTMnet; P14625; -.
PhosphoSitePlus; P14625; -.
SwissPalm; P14625; -.
DMDM; 119360; -.
DOSAC-COBS-2DPAGE; P14625; -.
OGP; P14625; -.
REPRODUCTION-2DPAGE; IPI00027230; -.
EPD; P14625; -.
PaxDb; P14625; -.
PeptideAtlas; P14625; -.
PRIDE; P14625; -.
TopDownProteomics; P14625; -.
DNASU; 7184; -.
Ensembl; ENST00000299767; ENSP00000299767; ENSG00000166598.
GeneID; 7184; -.
KEGG; hsa:7184; -.
CTD; 7184; -.
DisGeNET; 7184; -.
EuPathDB; HostDB:ENSG00000166598.12; -.
GeneCards; HSP90B1; -.
H-InvDB; HIX0056796; -.
HGNC; HGNC:12028; HSP90B1.
HPA; CAB005224; -.
HPA; HPA003901; -.
HPA; HPA008424; -.
MIM; 191175; gene.
neXtProt; NX_P14625; -.
OpenTargets; ENSG00000166598; -.
PharmGKB; PA36705; -.
eggNOG; KOG0020; Eukaryota.
eggNOG; COG0326; LUCA.
GeneTree; ENSGT00900000140978; -.
HOGENOM; HOG000031988; -.
HOVERGEN; HBG007374; -.
InParanoid; P14625; -.
KO; K09487; -.
OMA; SDHEIFL; -.
OrthoDB; EOG091G0270; -.
PhylomeDB; P14625; -.
TreeFam; TF105969; -.
Reactome; R-HSA-1679131; Trafficking and processing of endosomal TLR.
Reactome; R-HSA-3000480; Scavenging by Class A Receptors.
Reactome; R-HSA-381183; ATF6 (ATF6-alpha) activates chaperone genes.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
ChiTaRS; HSP90B1; human.
GeneWiki; HSP90B1; -.
GenomeRNAi; 7184; -.
PMAP-CutDB; P14625; -.
PRO; PR:P14625; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000166598; -.
CleanEx; HS_HSP90B1; -.
ExpressionAtlas; P14625; baseline and differential.
Genevisible; P14625; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IEA:Ensembl.
GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; TAS:UniProtKB.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IDA:MGI.
GO; GO:0019903; F:protein phosphatase binding; IDA:MGI.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
GO; GO:0031247; P:actin rod assembly; IDA:MGI.
GO; GO:0036500; P:ATF6-mediated unfolded protein response; TAS:Reactome.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0071318; P:cellular response to ATP; IDA:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0034975; P:protein folding in endoplasmic reticulum; TAS:ParkinsonsUK-UCL.
GO; GO:0015031; P:protein transport; NAS:UniProtKB.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IDA:MGI.
GO; GO:0034976; P:response to endoplasmic reticulum stress; TAS:ParkinsonsUK-UCL.
GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL.
GO; GO:0051208; P:sequestering of calcium ion; NAS:UniProtKB.
GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:UniProtKB.
CDD; cd00075; HATPase_c; 1.
Gene3D; 3.30.565.10; -; 1.
HAMAP; MF_00505; HSP90; 1.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR019805; Heat_shock_protein_90_CS.
InterPro; IPR037196; HSP90_C.
InterPro; IPR001404; Hsp90_fam.
InterPro; IPR020575; Hsp90_N.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
PANTHER; PTHR11528; PTHR11528; 1.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF00183; HSP90; 1.
PIRSF; PIRSF002583; Hsp90; 1.
PRINTS; PR00775; HEATSHOCK90.
SMART; SM00387; HATPase_c; 1.
SUPFAM; SSF110942; SSF110942; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF55874; SSF55874; 2.
PROSITE; PS00014; ER_TARGET; 1.
PROSITE; PS00298; HSP90; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Calcium; Chaperone;
Complete proteome; Direct protein sequencing; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Nucleotide-binding;
Phosphoprotein; Reference proteome; Signal.
SIGNAL 1 21 {ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:12665801}.
CHAIN 22 803 Endoplasmin.
/FTId=PRO_0000013598.
MOTIF 800 803 Prevents secretion from ER.
BINDING 107 107 ATP. {ECO:0000250}.
BINDING 149 149 ATP. {ECO:0000250}.
BINDING 162 162 ATP. {ECO:0000250}.
BINDING 168 168 ATP. {ECO:0000250}.
BINDING 199 199 ATP; via amide nitrogen. {ECO:0000250}.
BINDING 448 448 ATP. {ECO:0000250}.
MOD_RES 64 64 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 172 172 Phosphoserine.
{ECO:0000250|UniProtKB:Q66HD0}.
MOD_RES 306 306 Phosphoserine; by FAM20C.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:26091039}.
MOD_RES 403 403 Phosphoserine.
{ECO:0000250|UniProtKB:Q66HD0}.
MOD_RES 404 404 N6-succinyllysine.
{ECO:0000250|UniProtKB:P08113}.
MOD_RES 447 447 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 479 479 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08113}.
MOD_RES 633 633 N6-succinyllysine.
{ECO:0000250|UniProtKB:P08113}.
MOD_RES 786 786 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 62 62 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 107 107 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:19159218}.
CARBOHYD 217 217 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19159218}.
CARBOHYD 445 445 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19159218}.
CARBOHYD 481 481 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 502 502 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 138 138 Interchain. {ECO:0000250}.
CONFLICT 188 188 T -> S (in Ref. 4; AAK74072).
{ECO:0000305}.
CONFLICT 419 419 T -> P (in Ref. 4; AAK74072).
{ECO:0000305}.
CONFLICT 803 803 L -> F (in Ref. 4; AAK74072).
{ECO:0000305}.
HELIX 80 92 {ECO:0000244|PDB:4NH9}.
HELIX 99 118 {ECO:0000244|PDB:4NH9}.
TURN 119 121 {ECO:0000244|PDB:4NH9}.
TURN 123 128 {ECO:0000244|PDB:4NH9}.
STRAND 134 139 {ECO:0000244|PDB:4NH9}.
TURN 140 143 {ECO:0000244|PDB:4NH9}.
STRAND 144 149 {ECO:0000244|PDB:4NH9}.
HELIX 156 160 {ECO:0000244|PDB:4NH9}.
HELIX 175 184 {ECO:0000244|PDB:4NH9}.
HELIX 189 194 {ECO:0000244|PDB:4NH9}.
HELIX 198 204 {ECO:0000244|PDB:4NH9}.
STRAND 206 214 {ECO:0000244|PDB:4NH9}.
STRAND 221 225 {ECO:0000244|PDB:4NH9}.
STRAND 230 234 {ECO:0000244|PDB:4NH9}.
STRAND 241 251 {ECO:0000244|PDB:4NH9}.
HELIX 256 259 {ECO:0000244|PDB:4NH9}.
HELIX 261 271 {ECO:0000244|PDB:4NH9}.
STRAND 279 284 {ECO:0000244|PDB:4NH9}.
STRAND 331 335 {ECO:0000244|PDB:4NH9}.
SEQUENCE 803 AA; 92469 MW; 9BF6705A7A2ED0D0 CRC64;
MRALWVLGLC CVLLTFGSVR ADDEVDVDGT VEEDLGKSRE GSRTDDEVVQ REEEAIQLDG
LNASQIRELR EKSEKFAFQA EVNRMMKLII NSLYKNKEIF LRELISNASD ALDKIRLISL
TDENALSGNE ELTVKIKCDK EKNLLHVTDT GVGMTREELV KNLGTIAKSG TSEFLNKMTE
AQEDGQSTSE LIGQFGVGFY SAFLVADKVI VTSKHNNDTQ HIWESDSNEF SVIADPRGNT
LGRGTTITLV LKEEASDYLE LDTIKNLVKK YSQFINFPIY VWSSKTETVE EPMEEEEAAK
EEKEESDDEA AVEEEEEEKK PKTKKVEKTV WDWELMNDIK PIWQRPSKEV EEDEYKAFYK
SFSKESDDPM AYIHFTAEGE VTFKSILFVP TSAPRGLFDE YGSKKSDYIK LYVRRVFITD
DFHDMMPKYL NFVKGVVDSD DLPLNVSRET LQQHKLLKVI RKKLVRKTLD MIKKIADDKY
NDTFWKEFGT NIKLGVIEDH SNRTRLAKLL RFQSSHHPTD ITSLDQYVER MKEKQDKIYF
MAGSSRKEAE SSPFVERLLK KGYEVIYLTE PVDEYCIQAL PEFDGKRFQN VAKEGVKFDE
SEKTKESREA VEKEFEPLLN WMKDKALKDK IEKAVVSQRL TESPCALVAS QYGWSGNMER
IMKAQAYQTG KDISTNYYAS QKKTFEINPR HPLIRDMLRR IKEDEDDKTV LDLAVVLFET
ATLRSGYLLP DTKAYGDRIE RMLRLSLNID PDAKVEEEPE EEPEETAEDT TEDTEQDEDE
EMDVGTDEEE ETAKESTAEK DEL


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