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5'-nucleotidase (5'-NT) (EC 3.1.3.5) (Ecto-5'-nucleotidase) (CD antigen CD73)

 5NTD_HUMAN              Reviewed;         574 AA.
P21589; B3KQI8; O75520; Q5W116;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 1.
12-SEP-2018, entry version 194.
RecName: Full=5'-nucleotidase;
Short=5'-NT;
EC=3.1.3.5;
AltName: Full=Ecto-5'-nucleotidase;
AltName: CD_antigen=CD73;
Flags: Precursor;
Name=NT5E; Synonyms=NT5, NTE;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
GPI-ANCHOR AT SER-549.
TISSUE=Placenta;
PubMed=2129526; DOI=10.1111/j.1432-1033.1990.tb19158.x;
Misumi Y., Ogata S., Ohkubo K., Hirose S., Ikehara Y.;
"Primary structure of human placental 5'-nucleotidase and
identification of the glycolipid anchor in the mature form.";
Eur. J. Biochem. 191:563-569(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-113.
TISSUE=Placenta;
PubMed=8566797; DOI=10.1016/0378-1119(95)00574-9;
Hansen K.R., Resta R., Webb C.F., Thompson L.F.;
"Isolation and characterization of the promoter of the human 5'-
nucleotidase (CD73)-encoding gene.";
Gene 167:307-312(1995).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 359-489, AND VARIANT ALA-376.
TISSUE=Leukocyte;
Zanoni L., Rosi F., Pagani R., Marinello E.;
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[6]
PROTEIN SEQUENCE OF 27-40.
TISSUE=Placenta;
PubMed=2173922; DOI=10.1016/0006-291X(90)91601-N;
Klemens M.R., Sherman W.R., Holmberg N.J., Ruedi J.M., Low M.G.,
Thompson L.F.;
"Characterization of soluble vs membrane-bound human placental 5'-
nucleotidase.";
Biochem. Biophys. Res. Commun. 172:1371-1377(1990).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-311; ASN-333 AND ASN-403.
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).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-333.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[9]
FUNCTION, AND SUBSTRATE SPECIFICITY.
PubMed=21933152; DOI=10.1042/BJ20111263;
Garavaglia S., Bruzzone S., Cassani C., Canella L., Allegrone G.,
Sturla L., Mannino E., Millo E., De Flora A., Rizzi M.;
"The high-resolution crystal structure of periplasmic Haemophilus
influenzae NAD nucleotidase reveals a novel enzymatic function of
human CD73 related to NAD metabolism.";
Biochem. J. 441:131-141(2012).
[10]
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).
[11]
X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 27-549 IN COMPLEXES WITH ATP
ANALOG AND ZINC IONS, SUBUNIT, GLYCOSYLATION AT ASN-311, AND DISULFIDE
BONDS.
PubMed=23142347; DOI=10.1016/j.str.2012.10.001;
Knapp K., Zebisch M., Pippel J., El-Tayeb A., Muller C.E., Strater N.;
"Crystal structure of the human ecto-5'-nucleotidase (CD73): insights
into the regulation of purinergic signaling.";
Structure 20:2161-2173(2012).
[12]
VARIANT CALJA TYR-358.
PubMed=21288095; DOI=10.1056/NEJMoa0912923;
St Hilaire C., Ziegler S.G., Markello T.C., Brusco A., Groden C.,
Gill F., Carlson-Donohoe H., Lederman R.J., Chen M.Y., Yang D.,
Siegenthaler M.P., Arduino C., Mancini C., Freudenthal B.,
Stanescu H.C., Zdebik A.A., Chaganti R.K., Nussbaum R.L., Kleta R.,
Gahl W.A., Boehm M.;
"NT5E mutations and arterial calcifications.";
N. Engl. J. Med. 364:432-442(2011).
[13]
CHARACTERIZATION OF VARIANT CALJA TYR-358.
PubMed=24887587; DOI=10.1371/journal.pone.0098568;
Fausther M., Lavoie E.G., Goree J.R., Baldini G., Dranoff J.A.;
"NT5E mutations that cause human disease are associated with
intracellular mistrafficking of NT5E protein.";
PLoS ONE 9:E98568-E98568(2014).
-!- FUNCTION: Hydrolyzes extracellular nucleotides into membrane
permeable nucleosides. Exhibits AMP-, NAD-, and NMN-nucleosidase
activities. {ECO:0000269|PubMed:21933152}.
-!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside
+ phosphate.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23142347}.
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P21589-1; Sequence=Displayed;
Name=2;
IsoId=P21589-2; Sequence=VSP_043076;
Note=No experimental confirmation available.;
-!- DISEASE: Calcification of joints and arteries (CALJA)
[MIM:211800]: A condition characterized by adult-onset
calcification of the lower extremity arteries, including the
iliac, femoral and tibial arteries, and hand and foot capsule
joints. Age of onset has been reported as early as the second
decade of life, usually involving intense joint pain or
calcification in the hands. {ECO:0000269|PubMed:21288095,
ECO:0000269|PubMed:24887587}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/NT5EID44492ch6q14.html";
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EMBL; X55740; CAA39271.1; -; mRNA.
EMBL; AK075008; BAG52050.1; -; mRNA.
EMBL; AL135903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL589666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U21730; AAA96950.1; -; Genomic_DNA.
EMBL; AF069067; AAC98672.1; -; Genomic_DNA.
CCDS; CCDS5002.1; -. [P21589-1]
CCDS; CCDS56439.1; -. [P21589-2]
PIR; S11032; S11032.
RefSeq; NP_001191742.1; NM_001204813.1. [P21589-2]
RefSeq; NP_002517.1; NM_002526.3. [P21589-1]
UniGene; Hs.153952; -.
PDB; 4H1S; X-ray; 2.20 A; A/B=27-549.
PDB; 4H1Y; X-ray; 1.58 A; P=27-549.
PDB; 4H2B; X-ray; 1.70 A; A=27-549.
PDB; 4H2F; X-ray; 1.85 A; A=27-549.
PDB; 4H2G; X-ray; 1.55 A; A=27-549.
PDB; 4H2I; X-ray; 2.00 A; A=27-549.
PDBsum; 4H1S; -.
PDBsum; 4H1Y; -.
PDBsum; 4H2B; -.
PDBsum; 4H2F; -.
PDBsum; 4H2G; -.
PDBsum; 4H2I; -.
ProteinModelPortal; P21589; -.
SMR; P21589; -.
BioGrid; 110962; 49.
DIP; DIP-59992N; -.
IntAct; P21589; 4.
STRING; 9606.ENSP00000257770; -.
BindingDB; P21589; -.
ChEMBL; CHEMBL5957; -.
DrugBank; DB00987; Cytarabine.
DrugBank; DB00806; Pentoxifylline.
GuidetoPHARMACOLOGY; 1232; -.
DEPOD; P21589; -.
iPTMnet; P21589; -.
PhosphoSitePlus; P21589; -.
SwissPalm; P21589; -.
BioMuta; NT5E; -.
DMDM; 112825; -.
EPD; P21589; -.
MaxQB; P21589; -.
PaxDb; P21589; -.
PeptideAtlas; P21589; -.
PRIDE; P21589; -.
ProteomicsDB; 53883; -.
ProteomicsDB; 53884; -. [P21589-2]
DNASU; 4907; -.
Ensembl; ENST00000257770; ENSP00000257770; ENSG00000135318. [P21589-1]
Ensembl; ENST00000369651; ENSP00000358665; ENSG00000135318. [P21589-2]
GeneID; 4907; -.
KEGG; hsa:4907; -.
UCSC; uc003pko.5; human. [P21589-1]
CTD; 4907; -.
DisGeNET; 4907; -.
EuPathDB; HostDB:ENSG00000135318.11; -.
GeneCards; NT5E; -.
HGNC; HGNC:8021; NT5E.
HPA; HPA017357; -.
MalaCards; NT5E; -.
MIM; 129190; gene.
MIM; 211800; phenotype.
neXtProt; NX_P21589; -.
OpenTargets; ENSG00000135318; -.
Orphanet; 289601; Hereditary arterial and articular multiple calcification syndrome.
PharmGKB; PA31804; -.
eggNOG; KOG4419; Eukaryota.
eggNOG; COG0737; LUCA.
GeneTree; ENSGT00530000063775; -.
HOGENOM; HOG000247215; -.
HOVERGEN; HBG000026; -.
KO; K19970; -.
OMA; CRFQECN; -.
OrthoDB; EOG091G08IK; -.
PhylomeDB; P21589; -.
TreeFam; TF323589; -.
BioCyc; MetaCyc:HS05981-MONOMER; -.
Reactome; R-HSA-196807; Nicotinate metabolism.
Reactome; R-HSA-73621; Pyrimidine catabolism.
Reactome; R-HSA-74259; Purine catabolism.
SIGNOR; P21589; -.
ChiTaRS; NT5E; human.
GeneWiki; NT5E; -.
GenomeRNAi; 4907; -.
PRO; PR:P21589; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000135318; Expressed in 220 organ(s), highest expression level in endometrium.
CleanEx; HS_NT5E; -.
ExpressionAtlas; P21589; baseline and differential.
Genevisible; P21589; HS.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; HDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0008253; F:5'-nucleotidase activity; IDA:CACAO.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0046086; P:adenosine biosynthetic process; IEA:Ensembl.
GO; GO:0006196; P:AMP catabolic process; IEA:Ensembl.
GO; GO:0006259; P:DNA metabolic process; TAS:ProtInc.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:CACAO.
GO; GO:0019674; P:NAD metabolic process; TAS:Reactome.
GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
GO; GO:0006195; P:purine nucleotide catabolic process; TAS:Reactome.
GO; GO:0046135; P:pyrimidine nucleoside catabolic process; TAS:Reactome.
Gene3D; 3.60.21.10; -; 1.
Gene3D; 3.90.780.10; -; 1.
InterPro; IPR008334; 5'-Nucleotdase_C.
InterPro; IPR036907; 5'-Nucleotdase_C_sf.
InterPro; IPR006146; 5'-Nucleotdase_CS.
InterPro; IPR006179; 5_nucleotidase/apyrase.
InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
InterPro; IPR029052; Metallo-depent_PP-like.
PANTHER; PTHR11575; PTHR11575; 1.
Pfam; PF02872; 5_nucleotid_C; 1.
Pfam; PF00149; Metallophos; 1.
PRINTS; PR01607; APYRASEFAMLY.
SUPFAM; SSF55816; SSF55816; 1.
PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
Metal-binding; Nucleotide-binding; Polymorphism; Reference proteome;
Signal; Zinc.
SIGNAL 1 26 {ECO:0000269|PubMed:2173922}.
CHAIN 27 549 5'-nucleotidase.
{ECO:0000269|PubMed:2129526}.
/FTId=PRO_0000000015.
PROPEP 550 574 Removed in mature form.
/FTId=PRO_0000000016.
REGION 500 506 Substrate binding.
METAL 36 36 Zinc 1.
METAL 38 38 Zinc 1.
METAL 85 85 Zinc 1.
METAL 85 85 Zinc 2.
METAL 117 117 Zinc 2.
METAL 220 220 Zinc 2.
METAL 243 243 Zinc 2.
BINDING 245 245 Substrate.
BINDING 354 354 Substrate.
BINDING 390 390 Substrate.
BINDING 395 395 Substrate.
BINDING 417 417 Substrate.
SITE 118 118 Transition state stabilizer.
SITE 121 121 Transition state stabilizer.
{ECO:0000305}.
LIPID 549 549 GPI-anchor amidated serine.
{ECO:0000269|PubMed:2129526}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 311 311 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:23142347}.
CARBOHYD 333 333 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 403 403 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 51 57 {ECO:0000269|PubMed:23142347}.
DISULFID 353 358 {ECO:0000269|PubMed:23142347}.
DISULFID 365 387 {ECO:0000269|PubMed:23142347}.
DISULFID 476 479 {ECO:0000269|PubMed:23142347}.
VAR_SEQ 404 453 Missing (in isoform 2).
{ECO:0000303|PubMed:16303743}.
/FTId=VSP_043076.
VARIANT 358 358 C -> Y (in CALJA; absence from the
plasma-membrane; exhibits no catalytic
AMPase activity; dbSNP:rs387906620).
{ECO:0000269|PubMed:21288095,
ECO:0000269|PubMed:24887587}.
/FTId=VAR_065185.
VARIANT 376 376 T -> A (in dbSNP:rs2229523).
{ECO:0000269|Ref.5}.
/FTId=VAR_022091.
VARIANT 379 379 M -> T (in dbSNP:rs2229524).
/FTId=VAR_048103.
STRAND 27 34 {ECO:0000244|PDB:4H2G}.
STRAND 48 50 {ECO:0000244|PDB:4H2G}.
HELIX 54 56 {ECO:0000244|PDB:4H2G}.
HELIX 61 74 {ECO:0000244|PDB:4H2G}.
STRAND 76 82 {ECO:0000244|PDB:4H2G}.
STRAND 87 90 {ECO:0000244|PDB:4H2G}.
HELIX 91 96 {ECO:0000244|PDB:4H2G}.
HELIX 99 108 {ECO:0000244|PDB:4H2G}.
STRAND 111 114 {ECO:0000244|PDB:4H2G}.
HELIX 117 120 {ECO:0000244|PDB:4H2G}.
HELIX 123 128 {ECO:0000244|PDB:4H2G}.
TURN 129 134 {ECO:0000244|PDB:4H2G}.
STRAND 142 146 {ECO:0000244|PDB:4H2G}.
HELIX 150 154 {ECO:0000244|PDB:4H2G}.
TURN 155 157 {ECO:0000244|PDB:4H2F}.
STRAND 158 166 {ECO:0000244|PDB:4H2G}.
STRAND 169 177 {ECO:0000244|PDB:4H2G}.
HELIX 181 184 {ECO:0000244|PDB:4H2G}.
STRAND 189 193 {ECO:0000244|PDB:4H2G}.
HELIX 196 209 {ECO:0000244|PDB:4H2G}.
STRAND 215 221 {ECO:0000244|PDB:4H2G}.
HELIX 223 232 {ECO:0000244|PDB:4H2G}.
STRAND 238 240 {ECO:0000244|PDB:4H2G}.
STRAND 250 252 {ECO:0000244|PDB:4H2G}.
STRAND 254 256 {ECO:0000244|PDB:4H2G}.
STRAND 263 268 {ECO:0000244|PDB:4H2G}.
STRAND 274 278 {ECO:0000244|PDB:4H2G}.
STRAND 285 294 {ECO:0000244|PDB:4H2G}.
STRAND 300 305 {ECO:0000244|PDB:4H2G}.
HELIX 318 335 {ECO:0000244|PDB:4H2G}.
STRAND 337 344 {ECO:0000244|PDB:4H2G}.
HELIX 350 353 {ECO:0000244|PDB:4H2G}.
HELIX 359 371 {ECO:0000244|PDB:4H2G}.
HELIX 379 381 {ECO:0000244|PDB:4H2F}.
STRAND 386 390 {ECO:0000244|PDB:4H2G}.
HELIX 391 393 {ECO:0000244|PDB:4H2G}.
TURN 401 404 {ECO:0000244|PDB:4H2G}.
STRAND 405 407 {ECO:0000244|PDB:4H2G}.
HELIX 408 414 {ECO:0000244|PDB:4H2G}.
STRAND 420 427 {ECO:0000244|PDB:4H2G}.
HELIX 428 439 {ECO:0000244|PDB:4H2G}.
TURN 440 443 {ECO:0000244|PDB:4H2G}.
STRAND 450 459 {ECO:0000244|PDB:4H2G}.
STRAND 469 475 {ECO:0000244|PDB:4H2G}.
STRAND 477 481 {ECO:0000244|PDB:4H2G}.
STRAND 484 486 {ECO:0000244|PDB:4H2G}.
STRAND 492 498 {ECO:0000244|PDB:4H2G}.
HELIX 499 502 {ECO:0000244|PDB:4H2G}.
HELIX 505 507 {ECO:0000244|PDB:4H2G}.
HELIX 509 514 {ECO:0000244|PDB:4H2G}.
STRAND 516 523 {ECO:0000244|PDB:4H2G}.
HELIX 524 535 {ECO:0000244|PDB:4H2G}.
STRAND 536 538 {ECO:0000244|PDB:4H2G}.
STRAND 544 548 {ECO:0000244|PDB:4H2G}.
SEQUENCE 574 AA; 63368 MW; A99AF170AB7EAECE CRC64;
MCPRAARAPA TLLLALGAVL WPAAGAWELT ILHTNDVHSR LEQTSEDSSK CVNASRCMGG
VARLFTKVQQ IRRAEPNVLL LDAGDQYQGT IWFTVYKGAE VAHFMNALRY DAMALGNHEF
DNGVEGLIEP LLKEAKFPIL SANIKAKGPL ASQISGLYLP YKVLPVGDEV VGIVGYTSKE
TPFLSNPGTN LVFEDEITAL QPEVDKLKTL NVNKIIALGH SGFEMDKLIA QKVRGVDVVV
GGHSNTFLYT GNPPSKEVPA GKYPFIVTSD DGRKVPVVQA YAFGKYLGYL KIEFDERGNV
ISSHGNPILL NSSIPEDPSI KADINKWRIK LDNYSTQELG KTIVYLDGSS QSCRFRECNM
GNLICDAMIN NNLRHTDEMF WNHVSMCILN GGGIRSPIDE RNNGTITWEN LAAVLPFGGT
FDLVQLKGST LKKAFEHSVH RYGQSTGEFL QVGGIHVVYD LSRKPGDRVV KLDVLCTKCR
VPSYDPLKMD EVYKVILPNF LANGGDGFQM IKDELLRHDS GDQDINVVST YISKMKVIYP
AVEGRIKFST GSHCHGSFSL IFLSLWAVIF VLYQ


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