GMDS_HUMAN
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 03-AUG-2022, entry version 198.
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; 52.
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 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; O60547; -.
DR PeptideAtlas; O60547; -.
DR PRIDE; O60547; -.
DR ProteomicsDB; 20728; -.
DR ProteomicsDB; 49465; -. [O60547-1]
DR Antibodypedia; 24246; 214 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 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; TDCLYLG; -.
DR OrthoDB; 877551at2759; -.
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; 15 hits in 1084 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 182 other tissues.
DR Genevisible; O60547; HS.
DR GO; GO:0005737; C:cytoplasm; IC:UniProtKB.
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 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 PANTHER; PTHR43715; PTHR43715; 1.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01472; gmd; 1.
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
