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Thymidine phosphorylase (TP) (EC 2.4.2.4) (Gliostatin) (Platelet-derived endothelial cell growth factor) (PD-ECGF) (TdRPase)

 TYPH_HUMAN              Reviewed;         482 AA.
P19971; A8MW15; H9KVA0; Q13390; Q8WVB7;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 2.
22-NOV-2017, entry version 203.
RecName: Full=Thymidine phosphorylase;
Short=TP;
EC=2.4.2.4;
AltName: Full=Gliostatin;
AltName: Full=Platelet-derived endothelial cell growth factor;
Short=PD-ECGF;
AltName: Full=TdRPase;
Flags: Precursor;
Name=TYMP; Synonyms=ECGF1;
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
VARIANT LEU-471.
TISSUE=Placenta;
PubMed=2467210; DOI=10.1038/338557a0;
Ishikawa F., Miyazono K., Hellman U., Drexler H., Wernstedt C.,
Hagiwara K., Usuki K., Takaku F., Risau W., Heldin C.-H.;
"Identification of angiogenic activity and the cloning and expression
of platelet-derived endothelial cell growth factor.";
Nature 338:557-562(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1580101; DOI=10.1002/yea.320080106;
Finnis C., Goodey A., Courtney M., Sleep D.;
"Expression of recombinant platelet-derived endothelial cell growth
factor in the yeast Saccharomyces cerevisiae.";
Yeast 8:57-60(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Dermoid cancer;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
LEU-471.
TISSUE=Brain, and Lung;
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).
[6]
NUCLEOTIDE SEQUENCE OF 149-244, AND PROTEIN SEQUENCE OF 125-178 AND
236-244.
PubMed=1570012; DOI=10.1038/356668a0;
Furukawa T., Yoshimura A., Sumizawa T., Haraguchi M., Akiyama S.,
Fukui K., Yamada Y.;
"Angiogenic factor.";
Nature 356:668-668(1992).
[7]
PARTIAL PROTEIN SEQUENCE.
PubMed=1400349;
Asai K., Nakanishi K., Isobe I., Eksioglu Y.Z., Hirano A., Hama K.,
Miyamoto T., Kato T.;
"Neurotrophic action of gliostatin on cortical neurons. Identity of
gliostatin and platelet-derived endothelial cell growth factor.";
J. Biol. Chem. 267:20311-20316(1992).
[8]
FUNCTION.
PubMed=1590793; DOI=10.1016/S0006-291X(05)80025-7;
Usuki K., Saras J., Waltenberger J., Miyazono K., Pierce G.,
Thomason A., Heldin C.-H.;
"Platelet-derived endothelial cell growth factor has thymidine
phosphorylase activity.";
Biochem. Biophys. Res. Commun. 184:1311-1316(1992).
[9]
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).
[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 (2.11 ANGSTROMS) OF 12-482 IN COMPLEX WITH
INHIBITOR, AND SUBUNIT.
PubMed=14725767; DOI=10.1016/j.str.2003.11.018;
Norman R.A., Barry S.T., Bate M., Breed J., Colls J.G., Ernill R.J.,
Luke R.W., Minshull C.A., McAlister M.S., McCall E.J., McMiken H.H.,
Paterson D.S., Timms D., Tucker J.A., Pauptit R.A.;
"Crystal structure of human thymidine phosphorylase in complex with a
small molecule inhibitor.";
Structure 12:75-84(2004).
[12]
X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS), AND SUBUNIT.
PubMed=16803458; DOI=10.1042/BJ20060513;
El Omari K., Bronckaers A., Liekens S., Perez-Perez M.J.,
Balzarini J., Stammers D.K.;
"Structural basis for non-competitive product inhibition in human
thymidine phosphorylase: implications for drug design.";
Biochem. J. 399:199-204(2006).
[13]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) ALONE AND IN COMPLEX WITH
5-IODOURACIL, SUBSTRATE-BINDING SITES, AND MUTAGENESIS OF TYR-199.
PubMed=19555658; DOI=10.1016/j.bbrc.2009.06.104;
Mitsiki E., Papageorgiou A.C., Iyer S., Thiyagarajan N., Prior S.H.,
Sleep D., Finnis C., Acharya K.R.;
"Structures of native human thymidine phosphorylase and in complex
with 5-iodouracil.";
Biochem. Biophys. Res. Commun. 386:666-670(2009).
[14]
VARIANTS MTDPS1 ARG-145; SER-153; ARG-222; ALA-289 AND 397-LEU-ALA-398
DEL.
PubMed=9924029; DOI=10.1126/science.283.5402.689;
Nishino I., Spinazzola A., Hirano M.;
"Thymidine phosphorylase gene mutations in MNGIE, a human
mitochondrial disorder.";
Science 283:689-692(1999).
[15]
VARIANT MTDPS1 GLN-44.
PubMed=12177387; DOI=10.1212/WNL.59.3.455;
Gamez J., Ferreiro C., Accarino M.L., Guarner L., Tadesse S.,
Marti R.A., Andreu A.L., Raguer N., Cervera C., Hirano M.;
"Phenotypic variability in a Spanish family with MNGIE.";
Neurology 59:455-457(2002).
-!- FUNCTION: May have a role in maintaining the integrity of the
blood vessels. Has growth promoting activity on endothelial cells,
angiogenic activity in vivo and chemotactic activity on
endothelial cells in vitro. {ECO:0000269|PubMed:1590793}.
-!- FUNCTION: Catalyzes the reversible phosphorolysis of thymidine.
The produced molecules are then utilized as carbon and energy
sources or in the rescue of pyrimidine bases for nucleotide
synthesis. {ECO:0000269|PubMed:1590793}.
-!- CATALYTIC ACTIVITY: Thymidine + phosphate = thymine + 2-deoxy-
alpha-D-ribose 1-phosphate.
-!- PATHWAY: Pyrimidine metabolism; dTMP biosynthesis via salvage
pathway; dTMP from thymine: step 1/2.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14725767,
ECO:0000269|PubMed:16803458, ECO:0000269|PubMed:19555658}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P19971-1; Sequence=Displayed;
Name=2;
IsoId=P19971-2; Sequence=VSP_045556;
Note=No experimental confirmation available.;
-!- DISEASE: Mitochondrial DNA depletion syndrome 1, MNGIE type
(MTDPS1) [MIM:603041]: A multisystem disease associated with
mitochondrial dysfunction. It is clinically characterized by onset
between the second and fifth decades of life, ptosis, progressive
external ophthalmoplegia, gastrointestinal dysmotility (often
pseudoobstruction), diffuse leukoencephalopathy, cachexia,
peripheral neuropathy, and myopathy. {ECO:0000269|PubMed:12177387,
ECO:0000269|PubMed:9924029}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
phosphorylase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TYMPID40397ch22q13.html";
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EMBL; M63193; AAA60043.1; -; mRNA.
EMBL; AK225269; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; U62317; AAB03344.2; -; Genomic_DNA.
EMBL; BC018160; AAH18160.1; -; mRNA.
EMBL; BC052211; AAH52211.1; -; mRNA.
CCDS; CCDS14096.1; -. [P19971-1]
CCDS; CCDS58811.1; -. [P19971-2]
PIR; S03904; S03904.
RefSeq; NP_001107227.1; NM_001113755.2. [P19971-1]
RefSeq; NP_001107228.1; NM_001113756.2. [P19971-1]
RefSeq; NP_001244917.1; NM_001257988.1. [P19971-1]
RefSeq; NP_001244918.1; NM_001257989.1. [P19971-2]
RefSeq; NP_001944.1; NM_001953.4. [P19971-1]
UniGene; Hs.180903; -.
UniGene; Hs.730607; -.
PDB; 1UOU; X-ray; 2.11 A; A=12-482.
PDB; 2J0F; X-ray; 2.31 A; A/B/C/D=1-482.
PDB; 2WK5; X-ray; 2.99 A; A/B/C/D=1-482.
PDB; 2WK6; X-ray; 2.50 A; A/B=1-482.
PDBsum; 1UOU; -.
PDBsum; 2J0F; -.
PDBsum; 2WK5; -.
PDBsum; 2WK6; -.
ProteinModelPortal; P19971; -.
SMR; P19971; -.
BioGrid; 108219; 23.
IntAct; P19971; 2.
STRING; 9606.ENSP00000252029; -.
BindingDB; P19971; -.
ChEMBL; CHEMBL3106; -.
DrugBank; DB01101; Capecitabine.
DrugBank; DB00369; Cidofovir.
DrugBank; DB00322; Floxuridine.
DrugBank; DB00544; Fluorouracil.
DrugBank; DB09343; Tipiracil.
DrugBank; DB00432; Trifluridine.
iPTMnet; P19971; -.
PhosphoSitePlus; P19971; -.
SwissPalm; P19971; -.
BioMuta; TYMP; -.
DMDM; 67477361; -.
OGP; P19971; -.
MaxQB; P19971; -.
PaxDb; P19971; -.
PeptideAtlas; P19971; -.
PRIDE; P19971; -.
DNASU; 1890; -.
Ensembl; ENST00000252029; ENSP00000252029; ENSG00000025708. [P19971-1]
Ensembl; ENST00000395678; ENSP00000379036; ENSG00000025708. [P19971-1]
Ensembl; ENST00000395680; ENSP00000379037; ENSG00000025708. [P19971-1]
Ensembl; ENST00000395681; ENSP00000379038; ENSG00000025708. [P19971-2]
GeneID; 1890; -.
KEGG; hsa:1890; -.
UCSC; uc003bmb.7; human. [P19971-1]
CTD; 1890; -.
DisGeNET; 1890; -.
EuPathDB; HostDB:ENSG00000025708.13; -.
GeneCards; TYMP; -.
GeneReviews; TYMP; -.
HGNC; HGNC:3148; TYMP.
HPA; CAB002518; -.
HPA; HPA000530; -.
HPA; HPA001072; -.
MalaCards; TYMP; -.
MIM; 131222; gene.
MIM; 603041; phenotype.
neXtProt; NX_P19971; -.
OpenTargets; ENSG00000025708; -.
Orphanet; 298; Mitochondrial neurogastrointestinal encephalomyopathy.
PharmGKB; PA162407502; -.
eggNOG; ENOG410IIV8; Eukaryota.
eggNOG; COG0213; LUCA.
GeneTree; ENSGT00390000009250; -.
HOGENOM; HOG000047313; -.
HOVERGEN; HBG000082; -.
InParanoid; P19971; -.
KO; K00758; -.
OMA; VHSIGGV; -.
OrthoDB; EOG091G08UG; -.
PhylomeDB; P19971; -.
TreeFam; TF332198; -.
BioCyc; MetaCyc:HS00442-MONOMER; -.
BRENDA; 2.4.2.4; 2681.
Reactome; R-HSA-73614; Pyrimidine salvage.
Reactome; R-HSA-73621; Pyrimidine catabolism.
SABIO-RK; P19971; -.
UniPathway; UPA00578; UER00638.
EvolutionaryTrace; P19971; -.
GeneWiki; ECGF1; -.
GenomeRNAi; 1890; -.
PRO; PR:P19971; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000025708; -.
CleanEx; HS_TYMP; -.
ExpressionAtlas; P19971; baseline and differential.
Genevisible; P19971; HS.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0004645; F:phosphorylase activity; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:InterPro.
GO; GO:0009032; F:thymidine phosphorylase activity; IDA:CAFA.
GO; GO:0016763; F:transferase activity, transferring pentosyl groups; EXP:Reactome.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
GO; GO:0000002; P:mitochondrial genome maintenance; IMP:CAFA.
GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
GO; GO:0046135; P:pyrimidine nucleoside catabolic process; TAS:Reactome.
GO; GO:0006213; P:pyrimidine nucleoside metabolic process; IDA:CAFA.
GO; GO:0043097; P:pyrimidine nucleoside salvage; TAS:Reactome.
GO; GO:1905333; P:regulation of gastric motility; IMP:CAFA.
GO; GO:0031641; P:regulation of myelination; IMP:CAFA.
GO; GO:0051969; P:regulation of transmission of nerve impulse; IMP:CAFA.
Gene3D; 3.40.1030.10; -; 1.
InterPro; IPR000312; Glycosyl_Trfase_fam3.
InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom.
InterPro; IPR036320; Glycosyl_Trfase_fam3_N_dom)sf.
InterPro; IPR035902; Nuc_phospho_transferase.
InterPro; IPR036566; PYNP-like_C_sf.
InterPro; IPR013102; PYNP_C.
InterPro; IPR018090; Pyrmidine_PPas_bac/euk.
InterPro; IPR017872; Pyrmidine_PPase_CS.
InterPro; IPR000053; Thymidine/pyrmidine_PPase.
PANTHER; PTHR10515; PTHR10515; 1.
Pfam; PF02885; Glycos_trans_3N; 1.
Pfam; PF00591; Glycos_transf_3; 1.
Pfam; PF07831; PYNP_C; 1.
PIRSF; PIRSF000478; TP_PyNP; 1.
SMART; SM00941; PYNP_C; 1.
SUPFAM; SSF47648; SSF47648; 1.
SUPFAM; SSF52418; SSF52418; 1.
SUPFAM; SSF54680; SSF54680; 1.
TIGRFAMs; TIGR02644; Y_phosphoryl; 1.
PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Angiogenesis; Chemotaxis;
Complete proteome; Developmental protein; Differentiation;
Direct protein sequencing; Disease mutation; Glycosyltransferase;
Growth factor; Phosphoprotein; Polymorphism;
Primary mitochondrial disease; Progressive external ophthalmoplegia;
Reference proteome; Repeat; Transferase.
PROPEP 1 10
/FTId=PRO_0000035874.
CHAIN 11 482 Thymidine phosphorylase.
/FTId=PRO_0000035875.
REPEAT 265 279 R-V-A-A-A-L-X(5,6)-L-G-R.
REPEAT 329 342 R-V-A-A-A-L-X(5,6)-L-G-R.
REPEAT 393 401 R-A-L-X-X-A-L-V-L.
REPEAT 453 461 R-A-L-X-X-A-L-V-L.
BINDING 116 116 Substrate.
BINDING 202 202 Substrate.
BINDING 217 217 Substrate.
BINDING 221 221 Substrate.
MOD_RES 6 6 Phosphothreonine.
{ECO:0000250|UniProtKB:Q5FVR2}.
VAR_SEQ 386 386 D -> DAPLPA (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_045556.
VARIANT 44 44 R -> Q (in MTDPS1; dbSNP:rs28931613).
{ECO:0000269|PubMed:12177387}.
/FTId=VAR_016777.
VARIANT 145 145 G -> R (in MTDPS1; dbSNP:rs121913037).
{ECO:0000269|PubMed:9924029}.
/FTId=VAR_007643.
VARIANT 153 153 G -> S (in MTDPS1; dbSNP:rs121913038).
{ECO:0000269|PubMed:9924029}.
/FTId=VAR_007644.
VARIANT 222 222 K -> R (in MTDPS1; dbSNP:rs149977726).
{ECO:0000269|PubMed:9924029}.
/FTId=VAR_007645.
VARIANT 289 289 E -> A (in MTDPS1; dbSNP:rs121913036).
{ECO:0000269|PubMed:9924029}.
/FTId=VAR_007646.
VARIANT 397 398 Missing (in MTDPS1).
{ECO:0000269|PubMed:9924029}.
/FTId=VAR_007647.
VARIANT 471 471 S -> L (in dbSNP:rs11479).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2467210}.
/FTId=VAR_007648.
MUTAGEN 199 199 Y->A: Abolishes catalytic activity.
{ECO:0000269|PubMed:19555658}.
MUTAGEN 199 199 Y->F: Reduced catalytic activity.
{ECO:0000269|PubMed:19555658}.
MUTAGEN 199 199 Y->L: Reduced catalytic activity.
{ECO:0000269|PubMed:19555658}.
CONFLICT 195 195 D -> E (in Ref. 5; AAH18160).
{ECO:0000305}.
HELIX 36 44 {ECO:0000244|PDB:1UOU}.
HELIX 51 63 {ECO:0000244|PDB:1UOU}.
HELIX 68 81 {ECO:0000244|PDB:1UOU}.
HELIX 85 96 {ECO:0000244|PDB:1UOU}.
HELIX 106 111 {ECO:0000244|PDB:1UOU}.
STRAND 112 118 {ECO:0000244|PDB:1UOU}.
HELIX 125 134 {ECO:0000244|PDB:1UOU}.
TURN 135 137 {ECO:0000244|PDB:1UOU}.
STRAND 139 143 {ECO:0000244|PDB:1UOU}.
HELIX 154 158 {ECO:0000244|PDB:1UOU}.
HELIX 170 180 {ECO:0000244|PDB:1UOU}.
STRAND 181 185 {ECO:0000244|PDB:1UOU}.
STRAND 189 192 {ECO:0000244|PDB:1UOU}.
HELIX 193 204 {ECO:0000244|PDB:1UOU}.
HELIX 211 224 {ECO:0000244|PDB:1UOU}.
STRAND 228 236 {ECO:0000244|PDB:1UOU}.
STRAND 240 244 {ECO:0000244|PDB:2J0F}.
HELIX 245 261 {ECO:0000244|PDB:1UOU}.
STRAND 266 272 {ECO:0000244|PDB:1UOU}.
STRAND 280 283 {ECO:0000244|PDB:1UOU}.
HELIX 284 294 {ECO:0000244|PDB:1UOU}.
HELIX 300 316 {ECO:0000244|PDB:1UOU}.
STRAND 319 322 {ECO:0000244|PDB:2J0F}.
HELIX 323 335 {ECO:0000244|PDB:1UOU}.
HELIX 338 349 {ECO:0000244|PDB:1UOU}.
HELIX 354 362 {ECO:0000244|PDB:1UOU}.
HELIX 365 371 {ECO:0000244|PDB:1UOU}.
STRAND 376 382 {ECO:0000244|PDB:1UOU}.
STRAND 387 392 {ECO:0000244|PDB:1UOU}.
HELIX 394 405 {ECO:0000244|PDB:1UOU}.
STRAND 409 412 {ECO:0000244|PDB:2WK5}.
STRAND 420 423 {ECO:0000244|PDB:1UOU}.
STRAND 436 446 {ECO:0000244|PDB:1UOU}.
HELIX 449 458 {ECO:0000244|PDB:1UOU}.
STRAND 459 464 {ECO:0000244|PDB:1UOU}.
STRAND 475 477 {ECO:0000244|PDB:1UOU}.
SEQUENCE 482 AA; 49955 MW; 0652FA0B8F3BDE28 CRC64;
MAALMTPGTG APPAPGDFSG EGSQGLPDPS PEPKQLPELI RMKRDGGRLS EADIRGFVAA
VVNGSAQGAQ IGAMLMAIRL RGMDLEETSV LTQALAQSGQ QLEWPEAWRQ QLVDKHSTGG
VGDKVSLVLA PALAACGCKV PMISGRGLGH TGGTLDKLES IPGFNVIQSP EQMQVLLDQA
GCCIVGQSEQ LVPADGILYA ARDVTATVDS LPLITASILS KKLVEGLSAL VVDVKFGGAA
VFPNQEQARE LAKTLVGVGA SLGLRVAAAL TAMDKPLGRC VGHALEVEEA LLCMDGAGPP
DLRDLVTTLG GALLWLSGHA GTQAQGAARV AAALDDGSAL GRFERMLAAQ GVDPGLARAL
CSGSPAERRQ LLPRAREQEE LLAPADGTVE LVRALPLALV LHELGAGRSR AGEPLRLGVG
AELLVDVGQR LRRGTPWLRV HRDGPALSGP QSRALQEALV LSDRAPFAAP SPFAELVLPP
QQ


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