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C-type mannose receptor 2 (C-type lectin domain family 13 member E) (Endocytic receptor 180) (Macrophage mannose receptor 2) (Urokinase-type plasminogen activator receptor-associated protein) (UPAR-associated protein) (Urokinase receptor-associated protein) (CD antigen CD280)

 MRC2_HUMAN              Reviewed;        1479 AA.
Q9UBG0; A6H8K4; D3DU08; Q7LGE7; Q9Y5P9;
07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
12-SEP-2018, entry version 140.
RecName: Full=C-type mannose receptor 2;
AltName: Full=C-type lectin domain family 13 member E;
AltName: Full=Endocytic receptor 180;
AltName: Full=Macrophage mannose receptor 2;
AltName: Full=Urokinase-type plasminogen activator receptor-associated protein;
Short=UPAR-associated protein;
Short=Urokinase receptor-associated protein;
AltName: CD_antigen=CD280;
Flags: Precursor;
Name=MRC2; Synonyms=CLEC13E, ENDO180, KIAA0709, UPARAP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 350-360,
IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND VARIANT HIS-1156.
PubMed=10636902; DOI=10.1074/jbc.275.3.1993;
Behrendt N., Jensen O.N., Engelholm L.H., Moertz E., Mann M.,
Danoe K.;
"A urokinase receptor-associated protein with specific collagen
binding properties.";
J. Biol. Chem. 275:1993-2002(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PHOSPHORYLATION, GLYCOSYLATION,
TISSUE SPECIFICITY, AND VARIANTS ILE-43 AND HIS-1156.
PubMed=10683150;
Sheikh H., Yarwood H., Ashworth A., Isacke C.M.;
"Endo180, an endocytic recycling glycoprotein related to the
macrophage mannose receptor is expressed on fibroblasts, endothelial
cells and macrophages and functions as a lectin receptor.";
J. Cell Sci. 113:1021-1032(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-1156.
TISSUE=Brain;
PubMed=9734811; DOI=10.1093/dnares/5.3.169;
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. X.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:169-176(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT HIS-1156.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-1156.
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).
[7]
TISSUE SPECIFICITY.
PubMed=8702911; DOI=10.1074/jbc.271.35.21323;
Wu K., Yuan J., Lasky L.A.;
"Characterization of a novel member of the macrophage mannose receptor
type C lectin family.";
J. Biol. Chem. 271:21323-21330(1996).
[8]
MUTAGENESIS OF TYR-1452; GLU-1464 AND 1468-LEU-VAL-1469.
PubMed=12068012; DOI=10.1074/jbc.M203631200;
Howard M.J., Isacke C.M.;
"The C-type lectin receptor Endo180 displays internalization and
recycling properties distinct from other members of the mannose
receptor family.";
J. Biol. Chem. 277:32320-32331(2002).
[9]
DOMAIN, AND MUTAGENESIS OF ASN-472.
PubMed=12399458; DOI=10.1074/jbc.M208985200;
East L., Rushton S., Taylor M.E., Isacke C.M.;
"Characterization of sugar binding by the mannose receptor family
member, Endo180.";
J. Biol. Chem. 277:50469-50475(2002).
[10]
FUNCTION, AND DOMAIN.
PubMed=12972549; DOI=10.1091/mbc.E02-12-0814;
Wienke D., MacFadyen J.R., Isacke C.M.;
"Identification and characterization of the endocytic transmembrane
glycoprotein Endo180 as a novel collagen receptor.";
Mol. Biol. Cell 14:3592-3604(2003).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69.
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).
[12]
GLYCOSYLATION AT ASN-69.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[13]
SUMOYLATION AT LYS-1142.
TISSUE=Cervix carcinoma;
PubMed=20388717; DOI=10.1074/jbc.M110.106955;
Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A.,
Eriksson J.E., Sistonen L.;
"In vivo identification of sumoylation sites by a signature tag and
cysteine-targeted affinity purification.";
J. Biol. Chem. 285:19324-19329(2010).
[14]
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: May play a role as endocytotic lectin receptor
displaying calcium-dependent lectin activity. Internalizes
glycosylated ligands from the extracellular space for release in
an endosomal compartment via clathrin-mediated endocytosis. May be
involved in plasminogen activation system controlling the
extracellular level of PLAUR/PLAU, and thus may regulate protease
activity at the cell surface. May contribute to cellular uptake,
remodeling and degradation of extracellular collagen matrices. May
play a role during cancer progression as well as in other chronic
tissue destructive diseases acting on collagen turnover. May
participate in remodeling of extracellular matrix cooperating with
the matrix metalloproteinases (MMPs).
{ECO:0000269|PubMed:10683150, ECO:0000269|PubMed:12972549}.
-!- SUBUNIT: Interacts with C-terminal region of type I
collagen/COL1A1 (By similarity). Interacts directly with
PLAUR/UPAR and PLAU/pro-UPA to form a tri-molecular complex.
Interacts with collagen V. {ECO:0000250,
ECO:0000269|PubMed:10636902}.
-!- INTERACTION:
P02454:Col1a1 (xeno); NbExp=2; IntAct=EBI-1104992, EBI-915744;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: Ubiquitous with low expression in brain,
placenta, lung, kidney, pancreas, spleen, thymus and colon.
Expressed in endothelial cells, fibroblasts and macrophages.
Highly expressed in fetal lung and kidney.
{ECO:0000269|PubMed:10683150, ECO:0000269|PubMed:8702911}.
-!- DOMAIN: C-type lectin domains 3 to 8 are not required for calcium-
dependent binding of mannose, fucose and N-acetylglucosamine. C-
type lectin domain 2 is responsible for sugar-binding in a
calcium-dependent manner.
-!- DOMAIN: Fibronectin type-II domain mediates collagen-binding.
-!- DOMAIN: Ricin B-type lectin domain contacts with the second C-type
lectin domain. {ECO:0000250}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:10683150,
ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218}.
-!- SEQUENCE CAUTION:
Sequence=BAA31684.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=Endo180;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_251";
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EMBL; AF107292; AAF14192.1; -; mRNA.
EMBL; AF134838; AAD30280.1; -; mRNA.
EMBL; AB014609; BAA31684.2; ALT_INIT; mRNA.
EMBL; AC080038; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471109; EAW94341.1; -; Genomic_DNA.
EMBL; CH471109; EAW94342.1; -; Genomic_DNA.
EMBL; BC146647; AAI46648.1; -; mRNA.
EMBL; BC150212; AAI50213.1; -; mRNA.
EMBL; BC153884; AAI53885.1; -; mRNA.
CCDS; CCDS11634.1; -.
RefSeq; NP_006030.2; NM_006039.4.
UniGene; Hs.7835; -.
PDB; 5AO5; X-ray; 2.48 A; A/B=35-511.
PDB; 5AO6; X-ray; 3.36 A; A/B=35-511.
PDB; 5E4K; X-ray; 2.58 A; A=31-510.
PDB; 5E4L; X-ray; 2.44 A; A/B=31-510.
PDB; 5EW6; X-ray; 2.29 A; A=31-510.
PDBsum; 5AO5; -.
PDBsum; 5AO6; -.
PDBsum; 5E4K; -.
PDBsum; 5E4L; -.
PDBsum; 5EW6; -.
ProteinModelPortal; Q9UBG0; -.
SMR; Q9UBG0; -.
BioGrid; 115231; 29.
DIP; DIP-37631N; -.
IntAct; Q9UBG0; 15.
MINT; Q9UBG0; -.
STRING; 9606.ENSP00000307513; -.
GlyConnect; 764; -.
iPTMnet; Q9UBG0; -.
PhosphoSitePlus; Q9UBG0; -.
SwissPalm; Q9UBG0; -.
UniCarbKB; Q9UBG0; -.
BioMuta; MRC2; -.
DMDM; 317373394; -.
EPD; Q9UBG0; -.
MaxQB; Q9UBG0; -.
PaxDb; Q9UBG0; -.
PeptideAtlas; Q9UBG0; -.
PRIDE; Q9UBG0; -.
ProteomicsDB; 83964; -.
Ensembl; ENST00000303375; ENSP00000307513; ENSG00000011028.
GeneID; 9902; -.
KEGG; hsa:9902; -.
UCSC; uc002jad.5; human.
CTD; 9902; -.
DisGeNET; 9902; -.
EuPathDB; HostDB:ENSG00000011028.13; -.
GeneCards; MRC2; -.
H-InvDB; HIX0018596; -.
H-InvDB; HIX0027238; -.
HGNC; HGNC:16875; MRC2.
HPA; HPA041991; -.
MIM; 612264; gene.
neXtProt; NX_Q9UBG0; -.
OpenTargets; ENSG00000011028; -.
PharmGKB; PA134988161; -.
eggNOG; ENOG410IS43; Eukaryota.
eggNOG; ENOG410XQ89; LUCA.
GeneTree; ENSGT00720000108514; -.
HOGENOM; HOG000231191; -.
HOVERGEN; HBG053606; -.
InParanoid; Q9UBG0; -.
KO; K06560; -.
OMA; HEQTYIN; -.
OrthoDB; EOG091G0EGC; -.
PhylomeDB; Q9UBG0; -.
TreeFam; TF316663; -.
Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
ChiTaRS; MRC2; human.
GenomeRNAi; 9902; -.
PRO; PR:Q9UBG0; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000011028; Expressed in 239 organ(s), highest expression level in tendon of biceps brachii.
CleanEx; HS_MRC2; -.
ExpressionAtlas; Q9UBG0; baseline and differential.
Genevisible; Q9UBG0; HS.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0005518; F:collagen binding; IDA:UniProtKB.
GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
GO; GO:0030574; P:collagen catabolic process; IDA:UniProtKB.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
CDD; cd03590; CLECT_DC-SIGN_like; 1.
CDD; cd00062; FN2; 1.
CDD; cd00161; RICIN; 1.
Gene3D; 2.10.10.10; -; 1.
Gene3D; 3.10.100.10; -; 8.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR018378; C-type_lectin_CS.
InterPro; IPR033989; CD209-like_CTLD.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR000562; FN_type2_dom.
InterPro; IPR036943; FN_type2_sf.
InterPro; IPR013806; Kringle-like.
InterPro; IPR035992; Ricin_B-like_lectins.
InterPro; IPR000772; Ricin_B_lectin.
Pfam; PF00040; fn2; 1.
Pfam; PF00059; Lectin_C; 8.
SMART; SM00034; CLECT; 8.
SMART; SM00059; FN2; 1.
SMART; SM00458; RICIN; 1.
SUPFAM; SSF50370; SSF50370; 1.
SUPFAM; SSF56436; SSF56436; 8.
SUPFAM; SSF57440; SSF57440; 1.
PROSITE; PS00615; C_TYPE_LECTIN_1; 3.
PROSITE; PS50041; C_TYPE_LECTIN_2; 8.
PROSITE; PS00023; FN2_1; 1.
PROSITE; PS51092; FN2_2; 1.
PROSITE; PS50231; RICIN_B_LECTIN; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Direct protein sequencing;
Disulfide bond; Endocytosis; Glycoprotein; Isopeptide bond; Lectin;
Membrane; Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Repeat; Signal; Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 1479 C-type mannose receptor 2.
/FTId=PRO_0000046078.
TOPO_DOM 31 1414 Extracellular. {ECO:0000255}.
TRANSMEM 1415 1435 Helical. {ECO:0000255}.
TOPO_DOM 1436 1479 Cytoplasmic. {ECO:0000255}.
DOMAIN 41 167 Ricin B-type lectin.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
DOMAIN 182 230 Fibronectin type-II.
{ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 244 360 C-type lectin 1. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 389 505 C-type lectin 2. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 528 644 C-type lectin 3. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 678 809 C-type lectin 4. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 832 951 C-type lectin 5. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 979 1107 C-type lectin 6. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 1132 1243 C-type lectin 7. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 1273 1393 C-type lectin 8. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
CARBOHYD 69 69 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218}.
CARBOHYD 140 140 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 364 364 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 588 588 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 954 954 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1029 1029 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1350 1350 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 54 68 {ECO:0000250}.
DISULFID 93 112 {ECO:0000250}.
DISULFID 187 213 {ECO:0000250}.
DISULFID 201 228 {ECO:0000250}.
DISULFID 266 359 {ECO:0000250}.
DISULFID 335 351 {ECO:0000250}.
DISULFID 410 504 {ECO:0000250}.
DISULFID 481 496 {ECO:0000250}.
DISULFID 618 635 {ECO:0000250}.
DISULFID 704 808 {ECO:0000250}.
DISULFID 785 800 {ECO:0000250}.
DISULFID 853 950 {ECO:0000250}.
DISULFID 927 942 {ECO:0000250}.
DISULFID 1078 1098 {ECO:0000250}.
DISULFID 1220 1234 {ECO:0000250}.
DISULFID 1369 1384 {ECO:0000250}.
CROSSLNK 1142 1142 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
VARIANT 43 43 V -> I (in dbSNP:rs2014055).
{ECO:0000269|PubMed:10683150}.
/FTId=VAR_025304.
VARIANT 1156 1156 R -> H (in dbSNP:rs2429387).
{ECO:0000269|PubMed:10636902,
ECO:0000269|PubMed:10683150,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9734811,
ECO:0000269|Ref.5}.
/FTId=VAR_025305.
MUTAGEN 472 472 N->D: Reduced sugar-binding activity.
{ECO:0000269|PubMed:12399458}.
MUTAGEN 1452 1452 Y->A: No alteration of distribution and
trafficking.
{ECO:0000269|PubMed:12068012}.
MUTAGEN 1464 1464 E->A: Increased cell surface
distribution.
{ECO:0000269|PubMed:12068012}.
MUTAGEN 1468 1469 LV->AA: Reduction of endocytotic
activity; distribution almost restricted
to the cell surface.
{ECO:0000269|PubMed:12068012}.
STRAND 46 48 {ECO:0000244|PDB:5EW6}.
TURN 49 52 {ECO:0000244|PDB:5EW6}.
STRAND 53 58 {ECO:0000244|PDB:5EW6}.
STRAND 61 67 {ECO:0000244|PDB:5EW6}.
HELIX 73 75 {ECO:0000244|PDB:5EW6}.
STRAND 77 80 {ECO:0000244|PDB:5EW6}.
TURN 81 83 {ECO:0000244|PDB:5EW6}.
STRAND 84 87 {ECO:0000244|PDB:5EW6}.
TURN 88 91 {ECO:0000244|PDB:5EW6}.
STRAND 92 96 {ECO:0000244|PDB:5EW6}.
STRAND 108 110 {ECO:0000244|PDB:5EW6}.
STRAND 116 118 {ECO:0000244|PDB:5AO5}.
TURN 123 125 {ECO:0000244|PDB:5EW6}.
HELIX 126 134 {ECO:0000244|PDB:5EW6}.
HELIX 138 141 {ECO:0000244|PDB:5E4L}.
STRAND 158 160 {ECO:0000244|PDB:5EW6}.
TURN 161 163 {ECO:0000244|PDB:5EW6}.
TURN 180 184 {ECO:0000244|PDB:5EW6}.
STRAND 189 193 {ECO:0000244|PDB:5EW6}.
STRAND 196 200 {ECO:0000244|PDB:5EW6}.
STRAND 212 218 {ECO:0000244|PDB:5EW6}.
HELIX 219 222 {ECO:0000244|PDB:5EW6}.
STRAND 225 227 {ECO:0000244|PDB:5EW6}.
TURN 236 238 {ECO:0000244|PDB:5EW6}.
STRAND 240 242 {ECO:0000244|PDB:5AO5}.
TURN 243 245 {ECO:0000244|PDB:5EW6}.
STRAND 248 257 {ECO:0000244|PDB:5EW6}.
HELIX 259 267 {ECO:0000244|PDB:5EW6}.
TURN 268 270 {ECO:0000244|PDB:5EW6}.
HELIX 279 288 {ECO:0000244|PDB:5EW6}.
TURN 289 291 {ECO:0000244|PDB:5EW6}.
STRAND 295 301 {ECO:0000244|PDB:5EW6}.
STRAND 303 305 {ECO:0000244|PDB:5AO5}.
STRAND 309 311 {ECO:0000244|PDB:5EW6}.
STRAND 330 332 {ECO:0000244|PDB:5EW6}.
STRAND 335 339 {ECO:0000244|PDB:5EW6}.
TURN 340 343 {ECO:0000244|PDB:5EW6}.
STRAND 344 349 {ECO:0000244|PDB:5EW6}.
STRAND 355 361 {ECO:0000244|PDB:5EW6}.
STRAND 387 389 {ECO:0000244|PDB:5EW6}.
STRAND 392 401 {ECO:0000244|PDB:5EW6}.
HELIX 403 412 {ECO:0000244|PDB:5EW6}.
HELIX 423 432 {ECO:0000244|PDB:5EW6}.
TURN 433 436 {ECO:0000244|PDB:5EW6}.
STRAND 439 445 {ECO:0000244|PDB:5EW6}.
STRAND 447 449 {ECO:0000244|PDB:5EW6}.
STRAND 452 455 {ECO:0000244|PDB:5E4L}.
TURN 474 476 {ECO:0000244|PDB:5EW6}.
STRAND 478 485 {ECO:0000244|PDB:5EW6}.
TURN 486 489 {ECO:0000244|PDB:5EW6}.
STRAND 490 495 {ECO:0000244|PDB:5EW6}.
STRAND 500 507 {ECO:0000244|PDB:5EW6}.
SEQUENCE 1479 AA; 166674 MW; AAAA5286F91DF7E7 CRC64;
MGPGRPAPAP WPRHLLRCVL LLGCLHLGRP GAPGDAALPE PNVFLIFSHG LQGCLEAQGG
QVRVTPACNT SLPAQRWKWV SRNRLFNLGT MQCLGTGWPG TNTTASLGMY ECDREALNLR
WHCRTLGDQL SLLLGARTSN ISKPGTLERG DQTRSGQWRI YGSEEDLCAL PYHEVYTIQG
NSHGKPCTIP FKYDNQWFHG CTSTGREDGH LWCATTQDYG KDERWGFCPI KSNDCETFWD
KDQLTDSCYQ FNFQSTLSWR EAWASCEQQG ADLLSITEIH EQTYINGLLT GYSSTLWIGL
NDLDTSGGWQ WSDNSPLKYL NWESDQPDNP SEENCGVIRT ESSGGWQNRD CSIALPYVCK
KKPNATAEPT PPDRWANVKV ECEPSWQPFQ GHCYRLQAEK RSWQESKKAC LRGGGDLVSI
HSMAELEFIT KQIKQEVEEL WIGLNDLKLQ MNFEWSDGSL VSFTHWHPFE PNNFRDSLED
CVTIWGPEGR WNDSPCNQSL PSICKKAGQL SQGAAEEDHG CRKGWTWHSP SCYWLGEDQV
TYSEARRLCT DHGSQLVTIT NRFEQAFVSS LIYNWEGEYF WTALQDLNST GSFFWLSGDE
VMYTHWNRDQ PGYSRGGCVA LATGSAMGLW EVKNCTSFRA RYICRQSLGT PVTPELPGPD
PTPSLTGSCP QGWASDTKLR YCYKVFSSER LQDKKSWVQA QGACQELGAQ LLSLASYEEE
HFVANMLNKI FGESEPEIHE QHWFWIGLNR RDPRGGQSWR WSDGVGFSYH NFDRSRHDDD
DIRGCAVLDL ASLQWVAMQC DTQLDWICKI PRGTDVREPD DSPQGRREWL RFQEAEYKFF
EHHSTWAQAQ RICTWFQAEL TSVHSQAELD FLSHNLQKFS RAQEQHWWIG LHTSESDGRF
RWTDGSIINF ISWAPGKPRP VGKDKKCVYM TASREDWGDQ RCLTALPYIC KRSNVTKETQ
PPDLPTTALG GCPSDWIQFL NKCFQVQGQE PQSRVKWSEA QFSCEQQEAQ LVTITNPLEQ
AFITASLPNV TFDLWIGLHA SQRDFQWVEQ EPLMYANWAP GEPSGPSPAP SGNKPTSCAV
VLHSPSAHFT GRWDDRSCTE ETHGFICQKG TDPSLSPSPA ALPPAPGTEL SYLNGTFRLL
QKPLRWHDAL LLCESRNASL AYVPDPYTQA FLTQAARGLR TPLWIGLAGE EGSRRYSWVS
EEPLNYVGWQ DGEPQQPGGC TYVDVDGAWR TTSCDTKLQG AVCGVSSGPP PPRRISYHGS
CPQGLADSAW IPFREHCYSF HMELLLGHKE ARQRCQRAGG AVLSILDEME NVFVWEHLQS
YEGQSRGAWL GMNFNPKGGT LVWQDNTAVN YSNWGPPGLG PSMLSHNSCY WIQSNSGLWR
PGACTNITMG VVCKLPRAEQ SSFSPSALPE NPAALVVVLM AVLLLLALLT AALILYRRRQ
SIERGAFEGA RYSRSSSSPT EATEKNILVS DMEMNEQQE


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