GMPPA_HUMAN
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 03-AUG-2022, entry version 162.
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 intellectual disability syndrome
CC (AAMR) [MIM:615510]: An autosomal recessive disorder characterized by
CC onset of alacrima, achalasia, and intellectual disability at birth or
CC in early infancy. More variable features include hypotonia, gait
CC abnormalities, anisocoria, and visual or hearing deficits. The disorder
CC shows similarity to the triple A syndrome, but patients with AAMR do
CC not have adrenal insufficiency. {ECO:0000269|PubMed:24035193}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC 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 SMR; Q96IJ6; -.
DR BioGRID; 118967; 44.
DR IntAct; Q96IJ6; 23.
DR MINT; Q96IJ6; -.
DR STRING; 9606.ENSP00000350949; -.
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; Q96IJ6; -.
DR PeptideAtlas; Q96IJ6; -.
DR PRIDE; Q96IJ6; -.
DR ProteomicsDB; 76833; -. [Q96IJ6-1]
DR ProteomicsDB; 76834; -. [Q96IJ6-2]
DR Antibodypedia; 34335; 131 antibodies from 23 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 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; 806744at2759; -.
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; 10 hits in 1082 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 168 other tissues.
DR ExpressionAtlas; Q96IJ6; baseline and differential.
DR Genevisible; Q96IJ6; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
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
