ID   GMDS_HUMAN              Reviewed;         372 AA.
AC   O60547; E9PI88; O75357; Q5T954; Q6FH09; Q9UGZ3; Q9UJK9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 207.
DE   RecName: Full=GDP-mannose 4,6 dehydratase {ECO:0000305};
DE            EC=4.2.1.47 {ECO:0000269|PubMed:9525924};
DE   AltName: Full=GDP-D-mannose dehydratase;
DE            Short=GMD;
GN   Name=GMDS {ECO:0000312|HGNC:HGNC:4369};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP   COFACTOR, ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RX   PubMed=9525924; DOI=10.1074/jbc.273.14.8193;
RA   Sullivan F.X., Kumar R., Kriz R., Stahl M., Xu G.-Y., Rouse J., Chang X.J.,
RA   Boodhoo A., Potvin B., Cumming D.A.;
RT   "Molecular cloning of human GDP-mannose 4,6-dehydratase and reconstitution
RT   of GDP-fucose biosynthesis in vitro.";
RL   J. Biol. Chem. 273:8193-8202(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
RC   TISSUE=Brain;
RX   PubMed=9603974; DOI=10.1074/jbc.273.23.14582;
RA   Ohyama C., Smith P.L., Angata K., Fukuda M.N., Lowe J.B., Fukuda M.;
RT   "Molecular cloning and expression of GDP-D-mannose-4,6-dehydratase, a key
RT   enzyme for fucose metabolism defective in Lec13 cells.";
RL   J. Biol. Chem. 273:14582-14587(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA   Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA   LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-323, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 23-372 IN COMPLEX WITH NADP, AND
RP   COFACTOR.
RA   Vedadi M., Walker J.R., Sharma S., Houston S., Wasney G., Loppnau P.,
RA   Oppermann U.;
RT   "Crystal structure and biophysical characterization of human GDP-D-mannose
RT   4,6-dehydratase.";
RL   Submitted (APR-2004) to the PDB data bank.
CC   -!- FUNCTION: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-
CC       deoxy-D-mannose. {ECO:0000269|PubMed:9525924,
CC       ECO:0000269|PubMed:9603974}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H2O;
CC         Xref=Rhea:RHEA:23820, ChEBI:CHEBI:15377, ChEBI:CHEBI:57527,
CC         ChEBI:CHEBI:57964; EC=4.2.1.47;
CC         Evidence={ECO:0000269|PubMed:9525924};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23821;
CC         Evidence={ECO:0000305|PubMed:9525924};
CC   -!- COFACTOR:
CC       Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000269|Ref.9};
CC   -!- ACTIVITY REGULATION: Inhibited by GDP-fucose.
CC       {ECO:0000269|PubMed:9525924}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=80 uM for GDP-mannose {ECO:0000269|PubMed:9525924};
CC         Vmax=0.11 umol/min/mg enzyme {ECO:0000269|PubMed:9525924};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via
CC       de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 1/2.
CC       {ECO:0000305|PubMed:9525924}.
CC   -!- INTERACTION:
CC       O60547; O60547: GMDS; NbExp=6; IntAct=EBI-746373, EBI-746373;
CC       O60547; O43448: KCNAB3; NbExp=3; IntAct=EBI-746373, EBI-12050557;
CC       O60547; Q96HA8: NTAQ1; NbExp=6; IntAct=EBI-746373, EBI-741158;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O60547-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O60547-2; Sequence=VSP_047324;
CC   -!- TISSUE SPECIFICITY: Highly expressed in pancreas and small intestine.
CC       Expressed in thymus, protstate, colon, heart, placenta, liver and
CC       kidney. Expressed at low levels in spleen, testis, brain and lung.
CC       {ECO:0000269|PubMed:9525924}.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. GDP-mannose 4,6-dehydratase subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC24501.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF042377; AAC13553.1; -; mRNA.
DR   EMBL; AF040260; AAC24501.1; ALT_INIT; mRNA.
DR   EMBL; CR541929; CAG46727.1; -; mRNA.
DR   EMBL; CR541947; CAG46745.1; -; mRNA.
DR   EMBL; AL033517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL034344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL035693; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL137179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL158139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL354670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL451141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL591048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC000117; AAH00117.1; -; mRNA.
DR   CCDS; CCDS4474.1; -. [O60547-1]
DR   CCDS; CCDS58994.1; -. [O60547-2]
DR   RefSeq; NP_001240775.1; NM_001253846.1. [O60547-2]
DR   RefSeq; NP_001491.1; NM_001500.3. [O60547-1]
DR   PDB; 1T2A; X-ray; 1.84 A; A/B/C/D=23-372.
DR   PDB; 5IN4; X-ray; 1.60 A; A/B/C/D=23-372.
DR   PDB; 5IN5; X-ray; 1.90 A; A/B/C/D=23-372.
DR   PDB; 6GPJ; X-ray; 1.94 A; A/B/C/D=23-372.
DR   PDB; 6GPK; X-ray; 1.47 A; A/B/C/D=23-372.
DR   PDB; 6GPL; X-ray; 1.76 A; B/C/D/E=23-372.
DR   PDB; 6Q94; X-ray; 2.80 A; A/B/C/D/E/F/G/H=23-372.
DR   PDBsum; 1T2A; -.
DR   PDBsum; 5IN4; -.
DR   PDBsum; 5IN5; -.
DR   PDBsum; 6GPJ; -.
DR   PDBsum; 6GPK; -.
DR   PDBsum; 6GPL; -.
DR   PDBsum; 6Q94; -.
DR   AlphaFoldDB; O60547; -.
DR   SMR; O60547; -.
DR   BioGRID; 109024; 67.
DR   IntAct; O60547; 19.
DR   STRING; 9606.ENSP00000370194; -.
DR   ChEMBL; CHEMBL4105807; -.
DR   DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR   DrugBank; DB02547; Guanosine-5'-Diphosphate-Rhamnose.
DR   GlyGen; O60547; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O60547; -.
DR   MetOSite; O60547; -.
DR   PhosphoSitePlus; O60547; -.
DR   BioMuta; GMDS; -.
DR   EPD; O60547; -.
DR   jPOST; O60547; -.
DR   MassIVE; O60547; -.
DR   MaxQB; O60547; -.
DR   PaxDb; 9606-ENSP00000370194; -.
DR   PeptideAtlas; O60547; -.
DR   ProteomicsDB; 20728; -.
DR   ProteomicsDB; 49465; -. [O60547-1]
DR   Pumba; O60547; -.
DR   Antibodypedia; 24246; 240 antibodies from 29 providers.
DR   DNASU; 2762; -.
DR   Ensembl; ENST00000380815.5; ENSP00000370194.4; ENSG00000112699.11. [O60547-1]
DR   Ensembl; ENST00000530927.5; ENSP00000436726.1; ENSG00000112699.11. [O60547-2]
DR   GeneID; 2762; -.
DR   KEGG; hsa:2762; -.
DR   MANE-Select; ENST00000380815.5; ENSP00000370194.4; NM_001500.4; NP_001491.1.
DR   UCSC; uc003mtq.4; human. [O60547-1]
DR   AGR; HGNC:4369; -.
DR   CTD; 2762; -.
DR   DisGeNET; 2762; -.
DR   GeneCards; GMDS; -.
DR   HGNC; HGNC:4369; GMDS.
DR   HPA; ENSG00000112699; Tissue enhanced (intestine, salivary gland, stomach).
DR   MIM; 602884; gene.
DR   neXtProt; NX_O60547; -.
DR   OpenTargets; ENSG00000112699; -.
DR   PharmGKB; PA28754; -.
DR   VEuPathDB; HostDB:ENSG00000112699; -.
DR   eggNOG; KOG1372; Eukaryota.
DR   GeneTree; ENSGT00440000033640; -.
DR   HOGENOM; CLU_007383_14_0_1; -.
DR   InParanoid; O60547; -.
DR   OMA; HWQTVNY; -.
DR   OrthoDB; 5484740at2759; -.
DR   PhylomeDB; O60547; -.
DR   TreeFam; TF300682; -.
DR   BRENDA; 4.2.1.47; 2681.
DR   PathwayCommons; O60547; -.
DR   Reactome; R-HSA-6787639; GDP-fucose biosynthesis.
DR   SignaLink; O60547; -.
DR   UniPathway; UPA00128; UER00190.
DR   BioGRID-ORCS; 2762; 16 hits in 1165 CRISPR screens.
DR   ChiTaRS; GMDS; human.
DR   EvolutionaryTrace; O60547; -.
DR   GeneWiki; GMDS_(gene); -.
DR   GenomeRNAi; 2762; -.
DR   Pharos; O60547; Tbio.
DR   PRO; PR:O60547; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; O60547; Protein.
DR   Bgee; ENSG00000112699; Expressed in parotid gland and 184 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0008446; F:GDP-mannose 4,6-dehydratase activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0070401; F:NADP+ binding; IDA:UniProtKB.
DR   GO; GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0019673; P:GDP-mannose metabolic process; IDA:UniProtKB.
DR   GO; GO:0007219; P:Notch signaling pathway; ISS:UniProtKB.
DR   CDD; cd05260; GDP_MD_SDR_e; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR   HAMAP; MF_00955; GDP_Man_dehydratase; 1.
DR   InterPro; IPR006368; GDP_Man_deHydtase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01472; gmd; 1.
DR   PANTHER; PTHR43715:SF1; GDP-MANNOSE 4,6 DEHYDRATASE; 1.
DR   PANTHER; PTHR43715; GDP-MANNOSE 4,6-DEHYDRATASE; 1.
DR   Pfam; PF16363; GDP_Man_Dehyd; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   Genevisible; O60547; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Lyase; NADP;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   CHAIN           2..372
FT                   /note="GDP-mannose 4,6 dehydratase"
FT                   /id="PRO_0000201705"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        155
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        157
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        179
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         30..35
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|Ref.9"
FT   BINDING         55..58
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|Ref.9"
FT   BINDING         86..87
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|Ref.9"
FT   BINDING         108..112
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|Ref.9"
FT   BINDING         123
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|Ref.9"
FT   BINDING         183
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|Ref.9"
FT   BINDING         209
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|Ref.9"
FT   BINDING         214
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|Ref.9"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   MOD_RES         323
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..34
FT                   /note="MAHAPARCPSARGSGDGEMGKPRNVALITGITGQ -> MCKM (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9603974"
FT                   /id="VSP_047324"
FT   CONFLICT        156
FT                   /note="S -> N (in Ref. 3; CAG46745)"
FT                   /evidence="ECO:0000305"
FT   STRAND          25..29
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   TURN            30..32
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   HELIX           34..45
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   STRAND          49..54
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   TURN            63..65
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   TURN            72..75
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   STRAND          78..84
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   HELIX           90..100
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   STRAND          103..107
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   HELIX           114..117
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   HELIX           121..128
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   HELIX           130..141
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   TURN            145..147
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   STRAND          149..155
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   HELIX           156..159
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   STRAND          163..167
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   HELIX           178..197
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   STRAND          200..206
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   HELIX           219..231
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   STRAND          238..241
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   STRAND          246..248
FT                   /evidence="ECO:0007829|PDB:5IN4"
FT   HELIX           252..264
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   STRAND          265..267
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   STRAND          271..273
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   STRAND          278..280
FT                   /evidence="ECO:0007829|PDB:5IN4"
FT   HELIX           281..290
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   TURN            291..293
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   STRAND          296..300
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   HELIX           302..304
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   STRAND          306..309
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   TURN            310..312
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   STRAND          315..319
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   HELIX           321..323
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   HELIX           337..343
FT                   /evidence="ECO:0007829|PDB:6GPK"
FT   HELIX           351..368
FT                   /evidence="ECO:0007829|PDB:6GPK"
SQ   SEQUENCE   372 AA;  41950 MW;  B1BAC441736D4C2B CRC64;
     MAHAPARCPS ARGSGDGEMG KPRNVALITG ITGQDGSYLA EFLLEKGYEV HGIVRRSSSF
     NTGRIEHLYK NPQAHIEGNM KLHYGDLTDS TCLVKIINEV KPTEIYNLGA QSHVKISFDL
     AEYTADVDGV GTLRLLDAVK TCGLINSVKF YQASTSELYG KVQEIPQKET TPFYPRSPYG
     AAKLYAYWIV VNFREAYNLF AVNGILFNHE SPRRGANFVT RKISRSVAKI YLGQLECFSL
     GNLDAKRDWG HAKDYVEAMW LMLQNDEPED FVIATGEVHS VREFVEKSFL HIGKTIVWEG
     KNENEVGRCK ETGKVHVTVD LKYYRPTEVD FLQGDCTKAK QKLNWKPRVA FDELVREMVH
     ADVELMRTNP NA
//