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GDP-fucose protein O-fucosyltransferase 1 (EC 2.4.1.221) (Peptide-O-fucosyltransferase 1) (O-FucT-1)

 OFUT1_HUMAN             Reviewed;         388 AA.
Q9H488; A8K4R8; E1P5M4; Q14685; Q5W185; Q9BW76;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
22-NOV-2017, entry version 152.
RecName: Full=GDP-fucose protein O-fucosyltransferase 1;
EC=2.4.1.221 {ECO:0000269|PubMed:11524432};
AltName: Full=Peptide-O-fucosyltransferase 1;
Short=O-FucT-1;
Flags: Precursor;
Name=POFUT1; Synonyms=FUT12, KIAA0180;
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), FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
TISSUE=Heart;
PubMed=11524432; DOI=10.1074/jbc.M107849200;
Wang Y., Shao L., Shi S., Harris R.J., Spellman M.W., Stanley P.,
Haltiwanger R.S.;
"Modification of epidermal growth factor-like repeats with O-fucose:
molecular cloning and expression of a novel GDP-fucose protein O-
fucosyltransferase.";
J. Biol. Chem. 276:40338-40345(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=8724849; DOI=10.1093/dnares/3.1.17;
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. V.
The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 3:17-24(1996).
[3]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[8]
FUNCTION.
PubMed=8358148; DOI=10.1093/glycob/3.3.219;
Harris R.J., Spellman M.W.;
"O-linked fucose and other post-translational modifications unique to
EGF modules.";
Glycobiology 3:219-224(1993).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160.
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).
[10]
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).
[11]
INVOLVEMENT IN DDD2.
PubMed=23684010; DOI=10.1016/j.ajhg.2013.04.022;
Li M., Cheng R., Liang J., Yan H., Zhang H., Yang L., Li C., Jiao Q.,
Lu Z., He J., Ji J., Shen Z., Li C., Hao F., Yu H., Yao Z.;
"Mutations in POFUT1, encoding protein O-fucosyltransferase 1, cause
generalized Dowling-Degos disease.";
Am. J. Hum. Genet. 92:895-903(2013).
[12]
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).
[13] {ECO:0000244|PDB:5UX6, ECO:0000244|PDB:5UXH}
X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 24-384 IN COMPLEX WITH
GDP-FUCOSE, FUNCTION IN NOTCH SIGNALING, GLYCOSYLATION AT ASN-62,
DISULFIDE BONDS, AND MUTAGENESIS OF ARG-240; MET-262; SER-356 AND
ARG-366.
PubMed=28334865; DOI=10.1093/glycob/cwx020;
McMillan B.J., Zimmerman B., Egan E.D., Lofgren M., Xu X., Hesser A.,
Blacklow S.C.;
"Structure of human POFUT1, its requirement in ligand-independent
oncogenic Notch signaling, and functional effects of Dowling-Degos
mutations.";
Glycobiology 2017:1-10(2017).
-!- FUNCTION: Catalyzes the reaction that attaches fucose through an
O-glycosidic linkage to a conserved serine or threonine residue
found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains,
where C2 and C3 are the second and third conserved cysteines.
Specifically uses GDP-fucose as donor substrate and proper
disulfide pairing of the substrate EGF domains is required for
fucose transfer. Plays a crucial role in NOTCH signaling. Initial
fucosylation of NOTCH by POFUT1 generates a substrate for
FRINGE/RFNG, an acetylglucosaminyltransferase that can then extend
the fucosylation on the NOTCH EGF repeats. This extended
fucosylation is required for optimal ligand binding and canonical
NOTCH signaling induced by DLL1 or JAGGED1. Fucosylates AGRN and
determines its ability to cluster acetylcholine receptors (AChRs).
{ECO:0000269|PubMed:11524432, ECO:0000269|PubMed:28334865,
ECO:0000269|PubMed:8358148}.
-!- CATALYTIC ACTIVITY: Transfers an alpha-L-fucosyl residue from GDP-
beta-L-fucose to the serine hydroxy group of a protein acceptor.
{ECO:0000269|PubMed:11524432}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=6 uM for F7 EGF domain {ECO:0000269|PubMed:11524432};
KM=4 uM for GDP-fucose {ECO:0000269|PubMed:11524432};
Vmax=3 umol/min/mg enzyme {ECO:0000269|PubMed:11524432};
-!- PATHWAY: Protein modification; protein glycosylation.
{ECO:0000269|PubMed:11524432}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum
{ECO:0000250|UniProtKB:Q6EV70}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H488-1; Sequence=Displayed;
Name=2;
IsoId=Q9H488-2; Sequence=VSP_001809;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in heart, brain, placenta,
lung, liver, skeletal muscle, kidney and pancreas.
{ECO:0000269|PubMed:11524432}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:19159218}.
-!- DISEASE: Dowling-Degos disease 2 (DDD2) [MIM:615327]: An autosomal
dominant genodermatosis. Affected individuals develop a
postpubertal reticulate hyperpigmentation that is progressive and
disfiguring, and small hyperkeratotic dark brown papules that
affect mainly the flexures and great skin folds. Patients usually
show no abnormalities of the hair or nails.
{ECO:0000269|PubMed:23684010}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the glycosyltransferase 65 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=Peptide-O-fucosyltransferase 1;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_609";
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EMBL; AF375884; AAL09576.1; -; mRNA.
EMBL; D80002; BAA11497.2; -; mRNA.
EMBL; AL121897; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK291033; BAF83722.1; -; mRNA.
EMBL; CH471077; EAW76383.1; -; Genomic_DNA.
EMBL; CH471077; EAW76384.1; -; Genomic_DNA.
EMBL; CH471077; EAW76385.1; -; Genomic_DNA.
EMBL; BC000582; AAH00582.1; -; mRNA.
CCDS; CCDS13198.1; -. [Q9H488-1]
CCDS; CCDS13199.1; -. [Q9H488-2]
RefSeq; NP_056167.1; NM_015352.1. [Q9H488-1]
RefSeq; NP_758436.1; NM_172236.1. [Q9H488-2]
UniGene; Hs.472409; -.
PDB; 5UX6; X-ray; 2.09 A; A/B=24-384.
PDB; 5UXH; X-ray; 2.41 A; A/B=24-384.
PDBsum; 5UX6; -.
PDBsum; 5UXH; -.
ProteinModelPortal; Q9H488; -.
SMR; Q9H488; -.
BioGrid; 117056; 10.
IntAct; Q9H488; 3.
STRING; 9606.ENSP00000364902; -.
CAZy; GT65; Glycosyltransferase Family 65.
iPTMnet; Q9H488; -.
PhosphoSitePlus; Q9H488; -.
SwissPalm; Q9H488; -.
BioMuta; POFUT1; -.
DMDM; 23396787; -.
EPD; Q9H488; -.
MaxQB; Q9H488; -.
PaxDb; Q9H488; -.
PeptideAtlas; Q9H488; -.
PRIDE; Q9H488; -.
Ensembl; ENST00000375730; ENSP00000364882; ENSG00000101346. [Q9H488-2]
Ensembl; ENST00000375749; ENSP00000364902; ENSG00000101346. [Q9H488-1]
GeneID; 23509; -.
KEGG; hsa:23509; -.
UCSC; uc002wxo.3; human. [Q9H488-1]
CTD; 23509; -.
DisGeNET; 23509; -.
EuPathDB; HostDB:ENSG00000101346.11; -.
GeneCards; POFUT1; -.
HGNC; HGNC:14988; POFUT1.
HPA; HPA054519; -.
HPA; HPA059935; -.
MalaCards; POFUT1; -.
MIM; 607491; gene.
MIM; 615327; phenotype.
neXtProt; NX_Q9H488; -.
OpenTargets; ENSG00000101346; -.
Orphanet; 79145; Dowling-Degos disease.
PharmGKB; PA33495; -.
eggNOG; KOG3849; Eukaryota.
eggNOG; ENOG410Y3JQ; LUCA.
GeneTree; ENSGT00390000015634; -.
HOGENOM; HOG000231651; -.
HOVERGEN; HBG059976; -.
InParanoid; Q9H488; -.
KO; K03691; -.
OMA; GQSNHFI; -.
OrthoDB; EOG091G048B; -.
PhylomeDB; Q9H488; -.
TreeFam; TF314805; -.
BRENDA; 2.4.1.221; 2681.
Reactome; R-HSA-1912399; Pre-NOTCH Processing in the Endoplasmic Reticulum.
SignaLink; Q9H488; -.
SIGNOR; Q9H488; -.
UniPathway; UPA00378; -.
ChiTaRS; POFUT1; human.
GenomeRNAi; 23509; -.
PRO; PR:Q9H488; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000101346; -.
CleanEx; HS_POFUT1; -.
Genevisible; Q9H488; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0008417; F:fucosyltransferase activity; IDA:UniProtKB.
GO; GO:0046922; F:peptide-O-fucosyltransferase activity; IDA:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:0009790; P:embryo development; NAS:UniProtKB.
GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0007399; P:nervous system development; IEA:Ensembl.
GO; GO:0007219; P:Notch signaling pathway; NAS:UniProtKB.
GO; GO:0016266; P:O-glycan processing; TAS:UniProtKB.
GO; GO:0036066; P:protein O-linked fucosylation; IDA:UniProtKB.
GO; GO:0006493; P:protein O-linked glycosylation; IDA:UniProtKB.
GO; GO:0008593; P:regulation of Notch signaling pathway; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
InterPro; IPR019378; GDP-Fuc_O-FucTrfase.
Pfam; PF10250; O-FucT; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Carbohydrate metabolism;
Complete proteome; Disulfide bond; Endoplasmic reticulum;
Fucose metabolism; Glycoprotein; Glycosyltransferase; Manganese;
Notch signaling pathway; Polymorphism; Reference proteome; Signal;
Transferase.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 388 GDP-fucose protein O-fucosyltransferase
1.
/FTId=PRO_0000012148.
REGION 43 46 Substrate binding. {ECO:0000244|PDB:5UXH,
ECO:0000269|PubMed:28334865}.
REGION 238 240 Substrate binding. {ECO:0000244|PDB:5UXH,
ECO:0000269|PubMed:28334865}.
REGION 357 358 Substrate binding. {ECO:0000244|PDB:5UXH,
ECO:0000269|PubMed:28334865}.
MOTIF 385 388 Prevents secretion from ER.
{ECO:0000255}.
BINDING 340 340 Substrate. {ECO:0000244|PDB:5UXH,
ECO:0000269|PubMed:28334865}.
CARBOHYD 62 62 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5UX6,
ECO:0000269|PubMed:28334865}.
CARBOHYD 160 160 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 38 40 {ECO:0000244|PDB:5UX6,
ECO:0000244|PDB:5UXH,
ECO:0000269|PubMed:28334865}.
DISULFID 126 140 {ECO:0000244|PDB:5UX6,
ECO:0000244|PDB:5UXH,
ECO:0000269|PubMed:28334865}.
DISULFID 249 283 {ECO:0000244|PDB:5UX6,
ECO:0000244|PDB:5UXH,
ECO:0000269|PubMed:28334865}.
DISULFID 267 354 {ECO:0000244|PDB:5UX6,
ECO:0000244|PDB:5UXH,
ECO:0000269|PubMed:28334865}.
VAR_SEQ 182 388 FSPKEHPVLALPGAPAQFPVLEEHRPLQKYMVWSDEMVKTG
EAQIHAHLVRPYVGIHLRIGSDWKNACAMLKDGTAGSHFMA
SPQCVGYSRSTAAPLTMTMCLPDLKEIQRAVKLWVRSLDAQ
SVYVATDSESYVPELQQLFKGKVKVVSLKPEVAQVDLYILG
QADHFIGNCVSSFTAFVKRERDLQGRPSSFFGMDRPPKLRD
EF -> RENHSCVTLLFPR (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_001809.
VARIANT 322 322 L -> F (in dbSNP:rs17268666).
/FTId=VAR_049231.
VARIANT 348 348 D -> N (in dbSNP:rs35259534).
/FTId=VAR_049232.
MUTAGEN 240 240 R->A,C: Strongly impaired ability to
activate NOTCH signaling.
{ECO:0000269|PubMed:28334865}.
MUTAGEN 262 262 M->T: No effect on ability to activate
NOTCH signaling.
{ECO:0000269|PubMed:28334865}.
MUTAGEN 356 356 S->F: Abolishes ability to activate NOTCH
signaling. {ECO:0000269|PubMed:28334865}.
MUTAGEN 366 366 R->W: Strongly impaired ability to
activate NOTCH signaling.
{ECO:0000269|PubMed:28334865}.
STRAND 34 37 {ECO:0000244|PDB:5UX6}.
STRAND 41 43 {ECO:0000244|PDB:5UX6}.
HELIX 44 61 {ECO:0000244|PDB:5UX6}.
STRAND 64 67 {ECO:0000244|PDB:5UX6}.
STRAND 70 72 {ECO:0000244|PDB:5UX6}.
STRAND 83 85 {ECO:0000244|PDB:5UX6}.
HELIX 87 90 {ECO:0000244|PDB:5UX6}.
STRAND 91 93 {ECO:0000244|PDB:5UXH}.
HELIX 94 98 {ECO:0000244|PDB:5UX6}.
STRAND 102 104 {ECO:0000244|PDB:5UX6}.
HELIX 105 111 {ECO:0000244|PDB:5UX6}.
HELIX 113 116 {ECO:0000244|PDB:5UX6}.
HELIX 119 121 {ECO:0000244|PDB:5UX6}.
STRAND 123 127 {ECO:0000244|PDB:5UX6}.
HELIX 128 132 {ECO:0000244|PDB:5UX6}.
STRAND 134 136 {ECO:0000244|PDB:5UX6}.
STRAND 142 145 {ECO:0000244|PDB:5UX6}.
HELIX 148 153 {ECO:0000244|PDB:5UX6}.
TURN 154 156 {ECO:0000244|PDB:5UX6}.
STRAND 161 165 {ECO:0000244|PDB:5UX6}.
HELIX 172 174 {ECO:0000244|PDB:5UX6}.
HELIX 175 181 {ECO:0000244|PDB:5UX6}.
TURN 184 186 {ECO:0000244|PDB:5UX6}.
STRAND 188 194 {ECO:0000244|PDB:5UX6}.
HELIX 203 211 {ECO:0000244|PDB:5UX6}.
HELIX 216 229 {ECO:0000244|PDB:5UX6}.
STRAND 232 239 {ECO:0000244|PDB:5UX6}.
HELIX 243 253 {ECO:0000244|PDB:5UX6}.
TURN 262 264 {ECO:0000244|PDB:5UX6}.
HELIX 265 268 {ECO:0000244|PDB:5UX6}.
HELIX 272 274 {ECO:0000244|PDB:5UX6}.
HELIX 280 283 {ECO:0000244|PDB:5UX6}.
HELIX 287 301 {ECO:0000244|PDB:5UX6}.
STRAND 304 312 {ECO:0000244|PDB:5UX6}.
HELIX 316 322 {ECO:0000244|PDB:5UX6}.
TURN 323 325 {ECO:0000244|PDB:5UX6}.
STRAND 326 330 {ECO:0000244|PDB:5UX6}.
HELIX 337 345 {ECO:0000244|PDB:5UX6}.
STRAND 347 352 {ECO:0000244|PDB:5UX6}.
HELIX 357 369 {ECO:0000244|PDB:5UX6}.
STRAND 373 375 {ECO:0000244|PDB:5UX6}.
STRAND 378 380 {ECO:0000244|PDB:5UX6}.
SEQUENCE 388 AA; 43956 MW; 3FACCCA434D02415 CRC64;
MGAAAWARPL SVSFLLLLLP LPGMPAGSWD PAGYLLYCPC MGRFGNQADH FLGSLAFAKL
LNRTLAVPPW IEYQHHKPPF TNLHVSYQKY FKLEPLQAYH RVISLEDFME KLAPTHWPPE
KRVAYCFEVA AQRSPDKKTC PMKEGNPFGP FWDQFHVSFN KSELFTGISF SASYREQWSQ
RFSPKEHPVL ALPGAPAQFP VLEEHRPLQK YMVWSDEMVK TGEAQIHAHL VRPYVGIHLR
IGSDWKNACA MLKDGTAGSH FMASPQCVGY SRSTAAPLTM TMCLPDLKEI QRAVKLWVRS
LDAQSVYVAT DSESYVPELQ QLFKGKVKVV SLKPEVAQVD LYILGQADHF IGNCVSSFTA
FVKRERDLQG RPSSFFGMDR PPKLRDEF


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