ID   GMPPA_HUMAN             Reviewed;         420 AA.
AC   Q96IJ6; A6NJ74; A8K3Q6; B3KMT4; Q53GI0; Q9NWC3; Q9Y5P5;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 171.
DE   RecName: Full=Mannose-1-phosphate guanyltransferase alpha;
DE   AltName: Full=GDP-mannose pyrophosphorylase A;
DE            Short=GMPP-alpha;
DE   AltName: Full=GTP-mannose-1-phosphate guanylyltransferase alpha;
GN   Name=GMPPA;
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).
RA   Matthijs G., Schollen E., Dierickx D.;
RT   "Human homolog of GDP-mannose pyrophosphorylase.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryo;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Kidney;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lymph;
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   [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   VARIANTS AAMR ASP-182; MET-334; PRO-334; PRO-390 AND THR-401, FUNCTION,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=24035193; DOI=10.1016/j.ajhg.2013.08.002;
RA   Koehler K., Malik M., Mahmood S., Giesselmann S., Beetz C., Hennings J.C.,
RA   Huebner A.K., Grahn A., Reunert J., Nurnberg G., Thiele H., Altmuller J.,
RA   Nurnberg P., Mumtaz R., Babovic-Vuksanovic D., Basel-Vanagaite L.,
RA   Borck G., Bramswig J., Muhlenberg R., Sarda P., Sikiric A.,
RA   Anyane-Yeboa K., Zeharia A., Ahmad A., Coubes C., Wada Y., Marquardt T.,
RA   Vanderschaeghe D., Van Schaftingen E., Kurth I., Huebner A., Hubner C.A.;
RT   "Mutations in GMPPA cause a glycosylation disorder characterized by
RT   intellectual disability and autonomic dysfunction.";
RL   Am. J. Hum. Genet. 93:727-734(2013).
CC   -!- FUNCTION: May serve as a regulatory subunit and allow allosteric
CC       feedback inhibition of GMPPB by GDP-mannose.
CC       {ECO:0000269|PubMed:24035193}.
CC   -!- SUBUNIT: Associates with GMPPB. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q96IJ6; P46379-2: BAG6; NbExp=3; IntAct=EBI-750953, EBI-10988864;
CC       Q96IJ6; P35070: BTC; NbExp=6; IntAct=EBI-750953, EBI-6590057;
CC       Q96IJ6; P02741: CRP; NbExp=3; IntAct=EBI-750953, EBI-1395983;
CC       Q96IJ6; Q96GG9: DCUN1D1; NbExp=3; IntAct=EBI-750953, EBI-740086;
CC       Q96IJ6; O14645: DNALI1; NbExp=3; IntAct=EBI-750953, EBI-395638;
CC       Q96IJ6; Q01658: DR1; NbExp=3; IntAct=EBI-750953, EBI-750300;
CC       Q96IJ6; Q9Y5P6: GMPPB; NbExp=8; IntAct=EBI-750953, EBI-750945;
CC       Q96IJ6; Q92917: GPKOW; NbExp=3; IntAct=EBI-750953, EBI-746309;
CC       Q96IJ6; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-750953, EBI-1054873;
CC       Q96IJ6; O14901: KLF11; NbExp=3; IntAct=EBI-750953, EBI-948266;
CC       Q96IJ6; A0A0S2Z4D7: NCK1; NbExp=3; IntAct=EBI-750953, EBI-16429340;
CC       Q96IJ6; Q13148: TARDBP; NbExp=6; IntAct=EBI-750953, EBI-372899;
CC       Q96IJ6; A0A0S2Z6P0: ZNF688; NbExp=3; IntAct=EBI-750953, EBI-16429989;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24035193}.
CC       Note=Myc-tagged GMPPA shows a diffuse cytoplasmic and nuclear pattern
CC       in transfected COS-7 cells.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96IJ6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96IJ6-2; Sequence=VSP_032741;
CC   -!- TISSUE SPECIFICITY: Expressed in fibroblasts (at protein level).
CC       {ECO:0000269|PubMed:24035193}.
CC   -!- DISEASE: Alacrima, achalasia, and impaired intellectual development
CC       syndrome (AAMR) [MIM:615510]: An autosomal recessive disorder
CC       characterized by onset of alacrima, achalasia, and intellectual
CC       disability at birth or in early infancy. More variable features include
CC       hypotonia, gait abnormalities, anisocoria, and visual or hearing
CC       deficits. The disorder shows similarity to the triple A syndrome, but
CC       patients with AAMR do not have adrenal insufficiency.
CC       {ECO:0000269|PubMed:24035193}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000305}.
CC   -!- CAUTION: GMPPA is a close homolog of GMPPB, that has been shown to
CC       catalyze the formation of GDP-mannose, an essential precursor of glycan
CC       moieties of glycoproteins and glycolipids. However, lymphocytes from
CC       AAMR patients, that exhibit very low GMPPA protein levels, have
CC       unchanged GDP-mannose pyrophosphorylase activity and higher GDP-mannose
CC       levels than those from healthy controls. Affected individuals and
CC       control subjects show similar N-glycosylation profiles, both for
CC       transferrin glycosylation and for N-glycans derived from either total
CC       serum protein or immunoglobulin G. These observations led to the
CC       hypothesis that GMPPA might serve as a regulatory subunit and allow
CC       allosteric feedback inhibition of GMPPB by GDP-mannose. Alignment of
CC       GMPPAs and GMPPBs from various species shows that GMPPAs are
CC       characterized by a 2 amino acid-insertion (residues 11-12) in a highly
CC       conserved motif that borders the catalytic pocket and binds the
CC       nucleotide substrate in homologous enzymes. This insertion might
CC       inactivate the ancestral catalytic site, converting it to an allosteric
CC       site (PubMed:24035193). {ECO:0000305|PubMed:24035193}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD38517.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF135422; AAD38517.1; ALT_FRAME; mRNA.
DR   EMBL; AK000999; BAA91460.1; -; mRNA.
DR   EMBL; AK022578; BAG51096.1; -; mRNA.
DR   EMBL; AK290671; BAF83360.1; -; mRNA.
DR   EMBL; AK222951; BAD96671.1; -; mRNA.
DR   EMBL; AC053503; AAY15053.1; -; Genomic_DNA.
DR   EMBL; CH471063; EAW70755.1; -; Genomic_DNA.
DR   EMBL; CH471063; EAW70759.1; -; Genomic_DNA.
DR   EMBL; BC007456; AAH07456.1; -; mRNA.
DR   CCDS; CCDS2441.1; -. [Q96IJ6-1]
DR   RefSeq; NP_037467.2; NM_013335.3. [Q96IJ6-1]
DR   RefSeq; NP_995319.1; NM_205847.2. [Q96IJ6-1]
DR   RefSeq; XP_005246543.1; XM_005246486.3.
DR   RefSeq; XP_016859398.1; XM_017003909.1.
DR   RefSeq; XP_016859399.1; XM_017003910.1.
DR   RefSeq; XP_016859400.1; XM_017003911.1.
DR   PDB; 7D72; EM; 3.40 A; A/B/C/D=1-420.
DR   PDB; 7D73; EM; 3.00 A; A/B/C/D=1-420.
DR   PDB; 7D74; EM; 3.10 A; A/B/C/D=1-420.
DR   PDBsum; 7D72; -.
DR   PDBsum; 7D73; -.
DR   PDBsum; 7D74; -.
DR   AlphaFoldDB; Q96IJ6; -.
DR   EMDB; EMD-30599; -.
DR   EMDB; EMD-30600; -.
DR   EMDB; EMD-30601; -.
DR   SMR; Q96IJ6; -.
DR   BioGRID; 118967; 52.
DR   IntAct; Q96IJ6; 24.
DR   MINT; Q96IJ6; -.
DR   STRING; 9606.ENSP00000350949; -.
DR   GlyGen; Q96IJ6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q96IJ6; -.
DR   PhosphoSitePlus; Q96IJ6; -.
DR   BioMuta; GMPPA; -.
DR   DMDM; 74732065; -.
DR   EPD; Q96IJ6; -.
DR   jPOST; Q96IJ6; -.
DR   MassIVE; Q96IJ6; -.
DR   MaxQB; Q96IJ6; -.
DR   PaxDb; 9606-ENSP00000350949; -.
DR   PeptideAtlas; Q96IJ6; -.
DR   ProteomicsDB; 76833; -. [Q96IJ6-1]
DR   ProteomicsDB; 76834; -. [Q96IJ6-2]
DR   Pumba; Q96IJ6; -.
DR   Antibodypedia; 34335; 140 antibodies from 24 providers.
DR   DNASU; 29926; -.
DR   Ensembl; ENST00000313597.10; ENSP00000315925.6; ENSG00000144591.20. [Q96IJ6-1]
DR   Ensembl; ENST00000341142.8; ENSP00000340760.3; ENSG00000144591.20. [Q96IJ6-1]
DR   Ensembl; ENST00000358215.8; ENSP00000350949.3; ENSG00000144591.20. [Q96IJ6-1]
DR   Ensembl; ENST00000373908.5; ENSP00000363016.1; ENSG00000144591.20. [Q96IJ6-1]
DR   Ensembl; ENST00000373917.7; ENSP00000363027.3; ENSG00000144591.20. [Q96IJ6-2]
DR   Ensembl; ENST00000622191.2; ENSP00000478700.2; ENSG00000144591.20. [Q96IJ6-1]
DR   Ensembl; ENST00000683946.1; ENSP00000506941.1; ENSG00000144591.20. [Q96IJ6-1]
DR   GeneID; 29926; -.
DR   KEGG; hsa:29926; -.
DR   MANE-Select; ENST00000313597.10; ENSP00000315925.6; NM_013335.4; NP_037467.2.
DR   UCSC; uc002vlr.4; human. [Q96IJ6-1]
DR   AGR; HGNC:22923; -.
DR   CTD; 29926; -.
DR   DisGeNET; 29926; -.
DR   GeneCards; GMPPA; -.
DR   HGNC; HGNC:22923; GMPPA.
DR   HPA; ENSG00000144591; Low tissue specificity.
DR   MalaCards; GMPPA; -.
DR   MIM; 615495; gene.
DR   MIM; 615510; phenotype.
DR   neXtProt; NX_Q96IJ6; -.
DR   OpenTargets; ENSG00000144591; -.
DR   Orphanet; 869; Triple A syndrome.
DR   PharmGKB; PA134925506; -.
DR   VEuPathDB; HostDB:ENSG00000144591; -.
DR   eggNOG; KOG1460; Eukaryota.
DR   GeneTree; ENSGT00940000157018; -.
DR   HOGENOM; CLU_029499_3_0_1; -.
DR   InParanoid; Q96IJ6; -.
DR   OMA; MPVPNWW; -.
DR   OrthoDB; 5486038at2759; -.
DR   PhylomeDB; Q96IJ6; -.
DR   TreeFam; TF300832; -.
DR   PathwayCommons; Q96IJ6; -.
DR   Reactome; R-HSA-446205; Synthesis of GDP-mannose.
DR   SignaLink; Q96IJ6; -.
DR   BioGRID-ORCS; 29926; 11 hits in 1162 CRISPR screens.
DR   ChiTaRS; GMPPA; human.
DR   GenomeRNAi; 29926; -.
DR   Pharos; Q96IJ6; Tbio.
DR   PRO; PR:Q96IJ6; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q96IJ6; Protein.
DR   Bgee; ENSG00000144591; Expressed in body of pancreas and 170 other cell types or tissues.
DR   ExpressionAtlas; Q96IJ6; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd06428; M1P_guanylylT_A_like_N; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR018357; Hexapep_transf_CS.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR22572:SF104; MANNOSE-1-PHOSPHATE GUANYLTRANSFERASE ALPHA; 1.
DR   PANTHER; PTHR22572; SUGAR-1-PHOSPHATE GUANYL TRANSFERASE; 1.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
DR   Genevisible; Q96IJ6; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Disease variant;
KW   Intellectual disability; Reference proteome.
FT   CHAIN           1..420
FT                   /note="Mannose-1-phosphate guanyltransferase alpha"
FT                   /id="PRO_0000327872"
FT   VAR_SEQ         285
FT                   /note="G -> GTQPAPIPNLWLPPQPSEPGFLTSSPELKPQSLPLPDQIRFGIFAPR
FT                   ASLLLLG (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_032741"
FT   VARIANT         21
FT                   /note="S -> F (in dbSNP:rs34218609)"
FT                   /id="VAR_042434"
FT   VARIANT         156
FT                   /note="V -> A (in dbSNP:rs13396066)"
FT                   /id="VAR_042435"
FT   VARIANT         182
FT                   /note="G -> D (in AAMR; drastically reduced protein
FT                   expression; dbSNP:rs397518462)"
FT                   /evidence="ECO:0000269|PubMed:24035193"
FT                   /id="VAR_070203"
FT   VARIANT         334
FT                   /note="T -> M (in AAMR; dbSNP:rs774778439)"
FT                   /evidence="ECO:0000269|PubMed:24035193"
FT                   /id="VAR_070204"
FT   VARIANT         334
FT                   /note="T -> P (in AAMR; drastically reduced protein
FT                   expression; dbSNP:rs397518461)"
FT                   /evidence="ECO:0000269|PubMed:24035193"
FT                   /id="VAR_070205"
FT   VARIANT         390
FT                   /note="R -> P (in AAMR; drastically reduced protein
FT                   expression; dbSNP:rs1467274040)"
FT                   /evidence="ECO:0000269|PubMed:24035193"
FT                   /id="VAR_070206"
FT   VARIANT         401
FT                   /note="N -> T (in AAMR; drastically reduced protein
FT                   expression)"
FT                   /evidence="ECO:0000269|PubMed:24035193"
FT                   /id="VAR_070207"
FT   CONFLICT        57
FT                   /note="G -> C (in Ref. 3; BAD96671)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        67
FT                   /note="Q -> H (in Ref. 2; BAF83360)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        118
FT                   /note="C -> Y (in Ref. 2; BAA91460)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        339
FT                   /note="S -> C (in Ref. 1; AAD38517)"
FT                   /evidence="ECO:0000305"
FT   STRAND          2..7
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   TURN            11..14
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   HELIX           15..17
FT                   /evidence="ECO:0007829|PDB:7D74"
FT   STRAND          22..24
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   HELIX           26..28
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   STRAND          29..31
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   HELIX           36..46
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   STRAND          50..57
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   HELIX           63..76
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   STRAND          80..84
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   HELIX           90..97
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   HELIX           99..102
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   STRAND          108..119
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   HELIX           123..133
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   STRAND          136..143
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   HELIX           148..151
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   STRAND          154..158
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   TURN            159..162
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   STRAND          163..170
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   STRAND          177..186
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   TURN            188..190
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   HELIX           191..201
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   HELIX           222..225
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   TURN            226..229
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   TURN            231..234
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   STRAND          236..240
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   STRAND          245..247
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   HELIX           251..268
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   TURN            270..272
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   STRAND          285..289
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   STRAND          305..307
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   STRAND          318..321
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   STRAND          335..341
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   STRAND          352..354
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   STRAND          362..366
FT                   /evidence="ECO:0007829|PDB:7D72"
FT   STRAND          374..380
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   STRAND          385..387
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   STRAND          398..401
FT                   /evidence="ECO:0007829|PDB:7D73"
FT   STRAND          414..416
FT                   /evidence="ECO:0007829|PDB:7D73"
SQ   SEQUENCE   420 AA;  46291 MW;  741B77ABA198D4BC CRC64;
     MLKAVILIGG PQKGTRFRPL SFEVPKPLFP VAGVPMIQHH IEACAQVPGM QEILLIGFYQ
     PDEPLTQFLE AAQQEFNLPV RYLQEFAPLG TGGGLYHFRD QILAGSPEAF FVLNADVCSD
     FPLSAMLEAH RRQRHPFLLL GTTANRTQSL NYGCIVENPQ THEVLHYVEK PSTFISDIIN
     CGIYLFSPEA LKPLRDVFQR NQQDGQLEDS PGLWPGAGTI RLEQDVFSAL AGQGQIYVHL
     TDGIWSQIKS AGSALYASRL YLSRYQDTHP ERLAKHTPGG PWIRGNVYIH PTAKVAPSAV
     LGPNVSIGKG VTVGEGVRLR ESIVLHGATL QEHTCVLHSI VGWGSTVGRW ARVEGTPSDP
     NPNDPRARMD SESLFKDGKL LPAITILGCR VRIPAEVLIL NSIVLPHKEL SRSFTNQIIL
//