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Protein ERGIC-53 (ER-Golgi intermediate compartment 53 kDa protein) (Gp58) (Intracellular mannose-specific lectin MR60) (Lectin mannose-binding 1)

 LMAN1_HUMAN             Reviewed;         510 AA.
P49257; Q12895; Q8N5I7; Q9UQG1; Q9UQG2; Q9UQG3; Q9UQG4; Q9UQG5;
Q9UQG6; Q9UQG7; Q9UQG8; Q9UQG9; Q9UQH0; Q9UQH1; Q9UQH2;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
13-AUG-2002, sequence version 2.
27-SEP-2017, entry version 180.
RecName: Full=Protein ERGIC-53;
AltName: Full=ER-Golgi intermediate compartment 53 kDa protein;
AltName: Full=Gp58;
AltName: Full=Intracellular mannose-specific lectin MR60;
AltName: Full=Lectin mannose-binding 1;
Flags: Precursor;
Name=LMAN1; Synonyms=ERGIC53, F5F8D;
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 PROTEIN SEQUENCE OF 31-59 AND 418-432.
TISSUE=Liver, and Placenta;
PubMed=8223692;
Schindler R., Itin C., Zerial M., Lottspeich F., Hauri H.-P.;
"ERGIC-53, a membrane protein of the ER-Golgi intermediate
compartment, carries an ER retention motif.";
Eur. J. Cell Biol. 61:1-9(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 31-41.
TISSUE=Peripheral blood;
PubMed=7876089; DOI=10.1074/jbc.270.8.3551;
Arar C., Carpentier V., Le Caer J.-P., Monsigny M., Legrand A.,
Roche A.-C.;
"ERGIC-53, a membrane protein of the endoplasmic reticulum-Golgi
intermediate compartment, is identical to MR60, an intracellular
mannose-specific lectin of myelomonocytic cells.";
J. Biol. Chem. 270:3551-3553(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-14; ALA-39 AND
LEU-410, AND INVOLVEMENT IN F5F8D1.
PubMed=10090935;
Nichols W.C., Terry V.H., Wheatley M.A., Yang A., Zivelin A.,
Ciavarella N., Stefanile C., Matsushita T., Saito H., de Bosch N.B.,
Ruiz-Saez A., Torres A., Thompson A.R., Feinstein D.I., White G.C.,
Negrier C., Vinciguerra C., Aktan M., Kaufman R.J., Ginsburg D.,
Seligsohn U.;
"ERGIC-53 gene structure and mutation analysis in 19 combined factors
V and VIII deficiency families.";
Blood 93:2261-2266(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-410.
TISSUE=Brain;
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).
[5]
PROTEIN SEQUENCE OF 31-44.
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]
SIMILARITY TO LEGUMINOUS LECTINS.
PubMed=8205612; DOI=10.1016/0092-8674(94)90047-7;
Fiedler K., Simons K.;
"A putative novel class of animal lectins in the secretory pathway
homologous to leguminous lectins.";
Cell 77:625-626(1994).
[7]
MASS SPECTROMETRY.
TISSUE=Mammary cancer;
PubMed=11840567;
DOI=10.1002/1615-9861(200202)2:2<212::AID-PROT212>3.0.CO;2-H;
Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A.,
Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J.,
Zvelebil M.J.;
"Cluster analysis of an extensive human breast cancer cell line
protein expression map database.";
Proteomics 2:212-223(2002).
[8]
FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MOTIF ER EXPORT,
AND DISULFIDE BOND.
PubMed=13130098; DOI=10.1242/jcs.00759;
Nufer O., Kappeler F., Guldbrandsen S., Hauri H.-P.;
"ER export of ERGIC-53 is controlled by cooperation of targeting
determinants in all three of its domains.";
J. Cell Sci. 116:4429-4440(2003).
[9]
INTERACTION WITH MCFD2, AND FUNCTION.
PubMed=12717434; DOI=10.1038/ng1153;
Zhang B., Cunningham M.A., Nichols W.C., Bernat J.A., Seligsohn U.,
Pipe S.W., McVey J.H., Schulte-Overberg U., de Bosch N.B.,
Ruiz-Saez A., White G.C., Tuddenham E.G., Kaufman R.J., Ginsburg D.;
"Bleeding due to disruption of a cargo-specific ER-to-Golgi transport
complex.";
Nat. Genet. 34:220-225(2003).
[10]
SUBCELLULAR LOCATION, SUBUNIT, AND INTERCHAIN DISULFIDE BONDS.
PubMed=16257008; DOI=10.1016/j.jmb.2005.09.077;
Neve E.P., Lahtinen U., Pettersson R.F.;
"Oligomerization and intracellular localization of the glycoprotein
receptor ERGIC-53 is independent of disulfide bonds.";
J. Mol. Biol. 354:556-568(2005).
[11]
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).
[12]
INTERACTION WITH RAB3GAP1; RAB3GAP2 AND UBXN6, AND REGION.
PubMed=22337587; DOI=10.1074/mcp.M111.016444;
Haines D.S., Lee J.E., Beauparlant S.L., Kyle D.B., den Besten W.,
Sweredoski M.J., Graham R.L., Hess S., Deshaies R.J.;
"Protein interaction profiling of the p97 adaptor UBXD1 points to a
role for the complex in modulating ERGIC-53 trafficking.";
Mol. Cell. Proteomics 11:M111.016444-M111.016444(2012).
[13]
INTERACTION WITH TMEM115.
PubMed=24806965; DOI=10.1242/jcs.136754;
Ong Y.S., Tran T.H., Gounko N.V., Hong W.;
"TMEM115 is an integral membrane protein of the Golgi complex involved
in retrograde transport.";
J. Cell Sci. 127:2825-2839(2014).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, 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).
[15]
CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER GLY-30, 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).
[16]
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 32-277 IN COMPLEX WITH MCFD2
AND CALCIUM IONS, SUBUNIT, AND DISULFIDE BOND.
PubMed=20138881; DOI=10.1016/j.febslet.2010.02.009;
Wigren E., Bourhis J.M., Kursula I., Guy J.E., Lindqvist Y.;
"Crystal structure of the LMAN1-CRD/MCFD2 transport receptor complex
provides insight into combined deficiency of factor V and factor
VIII.";
FEBS Lett. 584:878-882(2010).
[17]
X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 31-285 IN COMPLEX WITH
CALCIUM IONS, SUBUNIT, AND DISULFIDE BOND.
PubMed=20142513; DOI=10.1073/pnas.0908526107;
Nishio M., Kamiya Y., Mizushima T., Wakatsuki S., Sasakawa H.,
Yamamoto K., Uchiyama S., Noda M., McKay A.R., Fukui K., Hauri H.P.,
Kato K.;
"Structural basis for the cooperative interplay between the two
causative gene products of combined factor V and factor VIII
deficiency.";
Proc. Natl. Acad. Sci. U.S.A. 107:4034-4039(2010).
[18]
VARIANT F5F8D1 SER-67, CHARACTERIZATION OF VARIANT F5F8D1 SER-67, AND
INTERACTION WITH MCFD2.
PubMed=19787799; DOI=10.1002/ajh.21532;
Yamada T., Fujimori Y., Suzuki A., Miyawaki Y., Takagi A., Murate T.,
Sano M., Matsushita T., Saito H., Kojima T.;
"A novel missense mutation causing abnormal LMAN1 in a Japanese
patient with combined deficiency of factor V and factor VIII.";
Am. J. Hematol. 84:738-742(2009).
-!- FUNCTION: Mannose-specific lectin. May recognize sugar residues of
glycoproteins, glycolipids, or glycosylphosphatidyl inositol
anchors and may be involved in the sorting or recycling of
proteins, lipids, or both. The LMAN1-MCFD2 complex forms a
specific cargo receptor for the ER-to-Golgi transport of selected
proteins. {ECO:0000269|PubMed:12717434,
ECO:0000269|PubMed:13130098}.
-!- SUBUNIT: Exists both as a covalent disulfide-linked homohexamer,
and a complex of three disulfide-linked dimers non-covalently kept
together. Interacts with MCFD2. May interact with TMEM115.
Interacts with RAB3GAP1 and RAB3GAP2 (PubMed:22337587). Interacts
with UBXN6 (PubMed:22337587). {ECO:0000269|PubMed:12717434,
ECO:0000269|PubMed:13130098, ECO:0000269|PubMed:16257008,
ECO:0000269|PubMed:19787799, ECO:0000269|PubMed:20138881,
ECO:0000269|PubMed:20142513, ECO:0000269|PubMed:22337587,
ECO:0000269|PubMed:24806965}.
-!- INTERACTION:
Q9BS26:ERP44; NbExp=3; IntAct=EBI-1057738, EBI-541644;
O15260:SURF4; NbExp=3; IntAct=EBI-1057738, EBI-1044848;
Q96GX1:TCTN2; NbExp=4; IntAct=EBI-1057738, EBI-11349465;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
compartment membrane; Single-pass type I membrane protein. Golgi
apparatus membrane; Single-pass membrane protein. Endoplasmic
reticulum membrane; Single-pass type I membrane protein.
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:13130098}.
-!- DOMAIN: The FF ER export motif at the C-terminus is not sufficient
to support endoplasmic reticulum exit, and needs assistance of
Gln-501 for proper recognition of COPII coat components.
-!- PTM: The N-terminal may be partly blocked.
-!- MASS SPECTROMETRY: Mass=54222.91; Method=MALDI; Range=31-510;
Evidence={ECO:0000269|PubMed:11840567};
-!- DISEASE: Factor V and factor VIII combined deficiency 1 (F5F8D1)
[MIM:227300]: A blood coagulation disorder characterized by
bleeding symptoms similar to those in hemophilia or
parahemophilia, that are caused by single deficiency of FV or
FVIII, respectively. The most common symptoms are epistaxis,
menorrhagia, and excessive bleeding during or after trauma. Plasma
levels of coagulation factors V and VIII are in the range of 5 to
30% of normal. {ECO:0000269|PubMed:10090935,
ECO:0000269|PubMed:19787799}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
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EMBL; X71661; CAA50653.1; -; mRNA.
EMBL; U09716; AAA95960.1; -; mRNA.
EMBL; AF081866; AAD32479.1; -; Genomic_DNA.
EMBL; AF081865; AAD32479.1; JOINED; Genomic_DNA.
EMBL; AF081867; AAD32480.1; -; Genomic_DNA.
EMBL; AF081869; AAD32481.1; -; Genomic_DNA.
EMBL; AF081868; AAD32481.1; JOINED; Genomic_DNA.
EMBL; AF081871; AAD32482.1; -; Genomic_DNA.
EMBL; AF081870; AAD32482.1; JOINED; Genomic_DNA.
EMBL; AF081873; AAD32483.1; -; Genomic_DNA.
EMBL; AF081872; AAD32483.1; JOINED; Genomic_DNA.
EMBL; AF081875; AAD32484.1; -; Genomic_DNA.
EMBL; AF081874; AAD32484.1; JOINED; Genomic_DNA.
EMBL; AF081877; AAD32485.1; -; Genomic_DNA.
EMBL; AF081876; AAD32485.1; JOINED; Genomic_DNA.
EMBL; AF081879; AAD32486.1; -; Genomic_DNA.
EMBL; AF081878; AAD32486.1; JOINED; Genomic_DNA.
EMBL; AF081880; AAD32487.1; -; Genomic_DNA.
EMBL; AF081882; AAD32488.1; -; Genomic_DNA.
EMBL; AF081881; AAD32488.1; JOINED; Genomic_DNA.
EMBL; AF081884; AAD32489.1; -; Genomic_DNA.
EMBL; AF081883; AAD32489.1; JOINED; Genomic_DNA.
EMBL; AF081885; AAD32490.1; -; Genomic_DNA.
EMBL; BC032330; AAH32330.1; -; mRNA.
CCDS; CCDS11974.1; -.
PIR; S42626; S42626.
RefSeq; NP_005561.1; NM_005570.3.
UniGene; Hs.465295; -.
PDB; 3A4U; X-ray; 1.84 A; A=31-285.
PDB; 3LCP; X-ray; 2.45 A; A/B=32-277.
PDB; 3WHT; X-ray; 1.80 A; A=31-269.
PDB; 3WHU; X-ray; 2.60 A; A=31-269.
PDB; 3WNX; X-ray; 2.75 A; A=31-269.
PDB; 4GKX; X-ray; 2.70 A; A/B/C/D/E/F=31-270.
PDB; 4GKY; X-ray; 2.42 A; A=31-270.
PDB; 4YGB; X-ray; 1.60 A; A/C=31-269.
PDB; 4YGC; X-ray; 2.40 A; A/C/E/G=31-269.
PDB; 4YGD; X-ray; 2.51 A; A/C/E/G=31-269.
PDB; 4YGE; X-ray; 3.05 A; A/C/E=31-269.
PDBsum; 3A4U; -.
PDBsum; 3LCP; -.
PDBsum; 3WHT; -.
PDBsum; 3WHU; -.
PDBsum; 3WNX; -.
PDBsum; 4GKX; -.
PDBsum; 4GKY; -.
PDBsum; 4YGB; -.
PDBsum; 4YGC; -.
PDBsum; 4YGD; -.
PDBsum; 4YGE; -.
ProteinModelPortal; P49257; -.
SMR; P49257; -.
BioGrid; 110185; 69.
DIP; DIP-42188N; -.
ELM; P49257; -.
IntAct; P49257; 20.
MINT; MINT-4999949; -.
STRING; 9606.ENSP00000251047; -.
DrugBank; DB00025; Antihemophilic Factor (Recombinant).
iPTMnet; P49257; -.
PhosphoSitePlus; P49257; -.
SwissPalm; P49257; -.
BioMuta; LMAN1; -.
DMDM; 22261801; -.
EPD; P49257; -.
MaxQB; P49257; -.
PaxDb; P49257; -.
PeptideAtlas; P49257; -.
PRIDE; P49257; -.
DNASU; 3998; -.
Ensembl; ENST00000251047; ENSP00000251047; ENSG00000074695.
GeneID; 3998; -.
KEGG; hsa:3998; -.
UCSC; uc002lhz.4; human.
CTD; 3998; -.
DisGeNET; 3998; -.
EuPathDB; HostDB:ENSG00000074695.5; -.
GeneCards; LMAN1; -.
HGNC; HGNC:6631; LMAN1.
HPA; CAB037163; -.
HPA; HPA002320; -.
MalaCards; LMAN1; -.
MIM; 227300; phenotype.
MIM; 601567; gene.
neXtProt; NX_P49257; -.
OpenTargets; ENSG00000074695; -.
Orphanet; 35909; Combined deficiency of factor V and factor VIII.
PharmGKB; PA30399; -.
eggNOG; KOG3838; Eukaryota.
eggNOG; ENOG410ZFRX; LUCA.
GeneTree; ENSGT00530000062977; -.
HOVERGEN; HBG052332; -.
InParanoid; P49257; -.
KO; K10080; -.
OMA; NMIIPAQ; -.
OrthoDB; EOG091G08WZ; -.
PhylomeDB; P49257; -.
TreeFam; TF313311; -.
Reactome; R-HSA-204005; COPII (Coat Protein 2) Mediated Vesicle Transport.
Reactome; R-HSA-5694530; Cargo concentration in the ER.
Reactome; R-HSA-948021; Transport to the Golgi and subsequent modification.
ChiTaRS; LMAN1; human.
EvolutionaryTrace; P49257; -.
GeneWiki; LMAN1; -.
GenomeRNAi; 3998; -.
PRO; PR:P49257; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000074695; -.
ExpressionAtlas; P49257; baseline and differential.
Genevisible; P49257; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; TAS:ProtInc.
GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0030017; C:sarcomere; IEA:Ensembl.
GO; GO:0005537; F:mannose binding; TAS:ProtInc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc.
GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome.
GO; GO:0007029; P:endoplasmic reticulum organization; IEA:Ensembl.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
GO; GO:0010638; P:positive regulation of organelle organization; IMP:UniProtKB.
GO; GO:0006457; P:protein folding; TAS:ProtInc.
GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
InterPro; IPR013320; ConA-like_dom.
InterPro; IPR005052; Lectin_leg.
InterPro; IPR033085; LMAN1.
PANTHER; PTHR12223:SF34; PTHR12223:SF34; 1.
Pfam; PF03388; Lectin_leg-like; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS51328; L_LECTIN_LIKE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Endoplasmic reticulum; ER-Golgi transport;
Golgi apparatus; Lectin; Membrane; Metal-binding; Phosphoprotein;
Polymorphism; Protein transport; Reference proteome; Signal;
Transmembrane; Transmembrane helix; Transport.
SIGNAL 1 30 {ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:12665801,
ECO:0000269|PubMed:7876089,
ECO:0000269|PubMed:8223692}.
CHAIN 31 510 Protein ERGIC-53.
/FTId=PRO_0000017660.
TOPO_DOM 31 477 Lumenal. {ECO:0000255}.
TRANSMEM 478 498 Helical. {ECO:0000255}.
TOPO_DOM 499 510 Cytoplasmic. {ECO:0000255}.
DOMAIN 44 267 L-type lectin-like. {ECO:0000255|PROSITE-
ProRule:PRU00658}.
REGION 251 253 Carbohydrate binding.
{ECO:0000255|PROSITE-ProRule:PRU00658}.
REGION 499 510 Mediates interaction with RAB3GAP1,
RAB3GAP2 and UBXN6.
{ECO:0000269|PubMed:22337587}.
MOTIF 509 510 ER export motif.
METAL 152 152 Calcium.
METAL 154 154 Calcium; via carbonyl oxygen.
METAL 156 156 Calcium.
METAL 181 181 Calcium.
BINDING 88 88 Carbohydrate. {ECO:0000255|PROSITE-
ProRule:PRU00658}.
BINDING 121 121 Carbohydrate. {ECO:0000255|PROSITE-
ProRule:PRU00658}.
BINDING 156 156 Carbohydrate. {ECO:0000255|PROSITE-
ProRule:PRU00658}.
BINDING 178 178 Carbohydrate. {ECO:0000255|PROSITE-
ProRule:PRU00658}.
SITE 501 501 Required for ER export.
MOD_RES 425 425 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
DISULFID 190 230
DISULFID 466 466 Interchain.
DISULFID 475 475 Interchain.
VARIANT 14 14 R -> Q (in dbSNP:rs1043302).
{ECO:0000269|PubMed:10090935}.
/FTId=VAR_013703.
VARIANT 39 39 V -> A (in dbSNP:rs33926449).
{ECO:0000269|PubMed:10090935}.
/FTId=VAR_013704.
VARIANT 67 67 W -> S (in F5F8D1; loss of interaction
with MCFD2 and ability to bind D-
mannose). {ECO:0000269|PubMed:19787799}.
/FTId=VAR_071969.
VARIANT 355 355 I -> T (in dbSNP:rs3737392).
/FTId=VAR_049770.
VARIANT 410 410 M -> L (in dbSNP:rs2298711).
{ECO:0000269|PubMed:10090935,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_013705.
CONFLICT 153 153 S -> T (in Ref. 1; CAA50653).
{ECO:0000305}.
STRAND 43 46 {ECO:0000244|PDB:4YGB}.
HELIX 48 50 {ECO:0000244|PDB:4YGB}.
STRAND 52 56 {ECO:0000244|PDB:4YGB}.
STRAND 67 71 {ECO:0000244|PDB:4YGB}.
STRAND 80 83 {ECO:0000244|PDB:4YGB}.
STRAND 85 88 {ECO:0000244|PDB:3WHU}.
STRAND 90 97 {ECO:0000244|PDB:4YGB}.
STRAND 102 113 {ECO:0000244|PDB:4YGB}.
STRAND 115 118 {ECO:0000244|PDB:4YGB}.
STRAND 122 128 {ECO:0000244|PDB:4YGB}.
STRAND 134 137 {ECO:0000244|PDB:3A4U}.
STRAND 146 152 {ECO:0000244|PDB:4YGB}.
STRAND 158 160 {ECO:0000244|PDB:4GKY}.
STRAND 164 170 {ECO:0000244|PDB:4YGB}.
HELIX 178 180 {ECO:0000244|PDB:3A4U}.
HELIX 183 185 {ECO:0000244|PDB:3A4U}.
STRAND 186 191 {ECO:0000244|PDB:4YGB}.
STRAND 201 208 {ECO:0000244|PDB:4YGB}.
STRAND 211 217 {ECO:0000244|PDB:4YGB}.
STRAND 219 222 {ECO:0000244|PDB:3WHT}.
STRAND 228 235 {ECO:0000244|PDB:4YGB}.
STRAND 240 249 {ECO:0000244|PDB:4YGB}.
STRAND 251 253 {ECO:0000244|PDB:4GKY}.
STRAND 256 268 {ECO:0000244|PDB:4YGB}.
SEQUENCE 510 AA; 57549 MW; B87EF117C0CD386C CRC64;
MAGSRQRGLR ARVRPLFCAL LLSLGRFVRG DGVGGDPAVA LPHRRFEYKY SFKGPHLVQS
DGTVPFWAHA GNAIPSSDQI RVAPSLKSQR GSVWTKTKAA FENWEVEVTF RVTGRGRIGA
DGLAIWYAEN QGLEGPVFGS ADLWNGVGIF FDSFDNDGKK NNPAIVIIGN NGQIHYDHQN
DGASQALASC QRDFRNKPYP VRAKITYYQN TLTVMINNGF TPDKNDYEFC AKVENMIIPA
QGHFGISAAT GGLADDHDVL SFLTFQLTEP GKEPPTPDKE ISEKEKEKYQ EEFEHFQQEL
DKKKEEFQKG HPDLQGQPAE EIFESVGDRE LRQVFEGQNR IHLEIKQLNR QLDMILDEQR
RYVSSLTEEI SKRGAGMPGQ HGQITQQELD TVVKTQHEIL RQVNEMKNSM SETVRLVSGM
QHPGSAGGVY ETTQHFIDIK EHLHIVKRDI DNLVQRNMPS NEKPKCPELP PFPSCLSTVH
FIIFVVVQTV LFIGYIMYRS QQEAAAKKFF


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