GMPPB_HUMAN
ID GMPPB_HUMAN Reviewed; 360 AA.
AC Q9Y5P6; A8K6N5; Q9H7U3;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Mannose-1-phosphate guanyltransferase beta;
DE EC=2.7.7.13 {ECO:0000250|UniProtKB:P0C5I2};
DE AltName: Full=GDP-mannose pyrophosphorylase B;
DE AltName: Full=GTP-mannose-1-phosphate guanylyltransferase beta;
GN Name=GMPPB {ECO:0000312|HGNC:HGNC:22932};
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), AND VARIANT ARG-184.
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] (ISOFORMS 1 AND 2), AND VARIANT
RP ARG-184.
RC TISSUE=Placenta;
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 GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-184.
RC TISSUE=Brain, and 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 [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP SUBCELLULAR LOCATION, VARIANT MDDGA14 ASN-334, VARIANTS MDDGB14 LEU-32;
RP CYS-185 AND GLN-287, VARIANTS MDDGC14 SER-22; HIS-27 AND ILE-330,
RP CHARACTERIZATION OF VARIANT MDDGA14 ASN-334, CHARACTERIZATION OF VARIANTS
RP MDDGB14 LEU-32; CYS-185 AND GLN-287, AND CHARACTERIZATION OF VARIANTS
RP MDDGC14 SER-22; HIS-27 AND ILE-330.
RX PubMed=23768512; DOI=10.1016/j.ajhg.2013.05.009;
RG UK10K Consortium;
RA Carss K.J., Stevens E., Foley A.R., Cirak S., Riemersma M., Torelli S.,
RA Hoischen A., Willer T., van Scherpenzeel M., Moore S.A., Messina S.,
RA Bertini E., Boennemann C.G., Abdenur J.E., Grosmann C.M., Kesari A.,
RA Punetha J., Quinlivan R., Waddell L.B., Young H.K., Wraige E., Yau S.,
RA Brodd L., Feng L., Sewry C., MacArthur D.G., North K.N., Hoffman E.,
RA Stemple D.L., Hurles M.E., van Bokhoven H., Campbell K.P., Lefeber D.J.,
RA Lin Y.Y., Muntoni F.;
RT "Mutations in GDP-mannose pyrophosphorylase B cause congenital and limb-
RT girdle muscular dystrophies associated with hypoglycosylation of alpha-
RT dystroglycan.";
RL Am. J. Hum. Genet. 93:29-41(2013).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP VARIANTS MDDGC14 HIS-27; SER-32; CYS-132; THR-219; SER-241; MET-254;
RP GLN-287; TRP-287; ALA-318 AND ILE-330.
RX PubMed=26310427; DOI=10.1002/humu.22898;
RA Jensen B.S., Willer T., Saade D.N., Cox M.O., Mozaffar T., Scavina M.,
RA Stefans V.A., Winder T.L., Campbell K.P., Moore S.A., Mathews K.D.;
RT "GMPPB-associated dystroglycanopathy: Emerging common variants with
RT phenotype correlation.";
RL Hum. Mutat. 36:1159-1163(2015).
RN [10]
RP VARIANTS MDDGC14 TRP-293; LYS-322; ARG-340 AND HIS-357, AND
RP CHARACTERIZATION OF VARIANTS MDDGC14 TRP-293; LYS-322; ARG-340 AND HIS-357.
RX PubMed=28433477; DOI=10.1016/j.nmd.2017.03.004;
RA Luo S., Cai S., Maxwell S., Yue D., Zhu W., Qiao K., Zhu Z., Zhou L.,
RA Xi J., Lu J., Beeson D., Zhao C.;
RT "Novel mutations in the C-terminal region of GMPPB causing limb-girdle
RT muscular dystrophy overlapping with congenital syndrome.";
RL Neuromuscul. Disord. 27:557-564(2017).
RN [11]
RP VARIANTS MDDGC14 HIS-27 AND TRP-287.
RX PubMed=28478914; DOI=10.1016/j.nmd.2017.04.006;
RA Balcin H., Palmio J., Penttilae S., Nennesmo I., Lindfors M., Solders G.,
RA Udd B.;
RT "Late-onset limb-girdle muscular dystrophy caused by GMPPB mutations.";
RL Neuromuscul. Disord. 27:627-630(2017).
CC -!- FUNCTION: Catalyzes the formation of GDP-mannose, an essential
CC precursor of glycan moieties of glycoproteins and glycolipids.
CC {ECO:0000250|UniProtKB:P0C5I2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-
CC alpha-D-mannose; Xref=Rhea:RHEA:15229, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57527,
CC ChEBI:CHEBI:58409; EC=2.7.7.13;
CC Evidence={ECO:0000250|UniProtKB:P0C5I2};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP
CC route): step 1/1. {ECO:0000250|UniProtKB:P0C5I2}.
CC -!- SUBUNIT: Associates with GMPPA. {ECO:0000250|UniProtKB:P0C5I2}.
CC -!- INTERACTION:
CC Q9Y5P6; Q7L190: DPPA4; NbExp=3; IntAct=EBI-750945, EBI-710457;
CC Q9Y5P6; Q8IVS8: GLYCTK; NbExp=5; IntAct=EBI-750945, EBI-748515;
CC Q9Y5P6; Q96IJ6: GMPPA; NbExp=8; IntAct=EBI-750945, EBI-750953;
CC Q9Y5P6; O15160: POLR1C; NbExp=3; IntAct=EBI-750945, EBI-1055079;
CC Q9Y5P6; Q86UY0: TXNDC5; NbExp=3; IntAct=EBI-750945, EBI-2825190;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23768512}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y5P6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y5P6-2; Sequence=VSP_028619;
CC -!- DISEASE: Muscular dystrophy-dystroglycanopathy congenital with brain
CC and eye anomalies A14 (MDDGA14) [MIM:615350]: An autosomal recessive
CC disorder characterized by congenital muscular dystrophy associated with
CC brain anomalies, eye malformations, and profound intellectual
CC disability. The disorder includes a severe form designated as Walker-
CC Warburg syndrome and a less severe phenotype known as muscle-eye-brain
CC disease. MDDGA14 features include increased muscle tone, microcephaly,
CC cleft palate, feeding difficulties, severe muscle weakness,
CC sensorineural hearing loss, cerebellar hypoplasia, ataxia, and retinal
CC dysfunction. {ECO:0000269|PubMed:23768512}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- DISEASE: Muscular dystrophy-dystroglycanopathy congenital with impaired
CC intellectual development B14 (MDDGB14) [MIM:615351]: A congenital
CC muscular dystrophy characterized by severe muscle weakness apparent in
CC infancy and intellectual disability. Some patients may have additional
CC features, such as microcephaly, cardiac dysfunction, seizures, or
CC cerebellar hypoplasia. {ECO:0000269|PubMed:23768512}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Muscular dystrophy-dystroglycanopathy limb-girdle C14
CC (MDDGC14) [MIM:615352]: An autosomal recessive form of muscular
CC dystrophy characterized by mild proximal muscle weakness with onset in
CC early childhood. Some patients may have additional features, such as
CC mild intellectual disability or seizures. {ECO:0000269|PubMed:23768512,
CC ECO:0000269|PubMed:26310427, ECO:0000269|PubMed:28433477,
CC ECO:0000269|PubMed:28478914}. 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}.
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DR EMBL; AF135421; AAD38516.1; -; mRNA.
DR EMBL; AK024319; BAB14882.1; -; mRNA.
DR EMBL; AK291700; BAF84389.1; -; mRNA.
DR EMBL; AC099668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001141; AAH01141.1; -; mRNA.
DR EMBL; BC008033; AAH08033.1; -; mRNA.
DR CCDS; CCDS2802.1; -. [Q9Y5P6-2]
DR CCDS; CCDS2803.1; -. [Q9Y5P6-1]
DR RefSeq; NP_037466.2; NM_013334.3. [Q9Y5P6-2]
DR RefSeq; NP_068806.1; NM_021971.2. [Q9Y5P6-1]
DR PDB; 7D72; EM; 3.40 A; E/F/G/H/I/J/K/L=1-360.
DR PDB; 7D73; EM; 3.00 A; E/F/G/H/I/J/K/L=1-360.
DR PDB; 7D74; EM; 3.10 A; E/F/G/H/I/J/K/L=1-360.
DR PDBsum; 7D72; -.
DR PDBsum; 7D73; -.
DR PDBsum; 7D74; -.
DR AlphaFoldDB; Q9Y5P6; -.
DR SMR; Q9Y5P6; -.
DR BioGRID; 118966; 64.
DR IntAct; Q9Y5P6; 12.
DR STRING; 9606.ENSP00000309092; -.
DR GlyGen; Q9Y5P6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y5P6; -.
DR MetOSite; Q9Y5P6; -.
DR PhosphoSitePlus; Q9Y5P6; -.
DR BioMuta; GMPPB; -.
DR DMDM; 160013885; -.
DR EPD; Q9Y5P6; -.
DR jPOST; Q9Y5P6; -.
DR MassIVE; Q9Y5P6; -.
DR MaxQB; Q9Y5P6; -.
DR PeptideAtlas; Q9Y5P6; -.
DR PRIDE; Q9Y5P6; -.
DR ProteomicsDB; 86466; -. [Q9Y5P6-1]
DR ProteomicsDB; 86467; -. [Q9Y5P6-2]
DR Antibodypedia; 1597; 172 antibodies from 24 providers.
DR DNASU; 29925; -.
DR Ensembl; ENST00000308375.10; ENSP00000309092.6; ENSG00000173540.14. [Q9Y5P6-2]
DR Ensembl; ENST00000308388.7; ENSP00000311130.6; ENSG00000173540.14. [Q9Y5P6-1]
DR Ensembl; ENST00000480687.5; ENSP00000418565.1; ENSG00000173540.14. [Q9Y5P6-1]
DR GeneID; 29925; -.
DR KEGG; hsa:29925; -.
DR MANE-Select; ENST00000308388.7; ENSP00000311130.6; NM_021971.4; NP_068806.2.
DR UCSC; uc003cxk.3; human. [Q9Y5P6-1]
DR CTD; 29925; -.
DR DisGeNET; 29925; -.
DR GeneCards; GMPPB; -.
DR GeneReviews; GMPPB; -.
DR HGNC; HGNC:22932; GMPPB.
DR HPA; ENSG00000173540; Low tissue specificity.
DR MalaCards; GMPPB; -.
DR MIM; 615320; gene.
DR MIM; 615350; phenotype.
DR MIM; 615351; phenotype.
DR MIM; 615352; phenotype.
DR neXtProt; NX_Q9Y5P6; -.
DR OpenTargets; ENSG00000173540; -.
DR Orphanet; 370959; Congenital muscular dystrophy with cerebellar involvement.
DR Orphanet; 370968; Congenital muscular dystrophy with intellectual disability.
DR Orphanet; 353327; Congenital myasthenic syndromes with glycosylation defect.
DR Orphanet; 363623; GMPPB-related limb-girdle muscular dystrophy R19.
DR Orphanet; 588; Muscle-eye-brain disease.
DR PharmGKB; PA134875590; -.
DR VEuPathDB; HostDB:ENSG00000173540; -.
DR eggNOG; KOG1322; Eukaryota.
DR GeneTree; ENSGT00940000158909; -.
DR HOGENOM; CLU_029499_0_0_1; -.
DR InParanoid; Q9Y5P6; -.
DR OMA; PFLTHQL; -.
DR OrthoDB; 806744at2759; -.
DR PhylomeDB; Q9Y5P6; -.
DR TreeFam; TF300718; -.
DR BRENDA; 2.7.7.13; 2681.
DR PathwayCommons; Q9Y5P6; -.
DR Reactome; R-HSA-446205; Synthesis of GDP-mannose.
DR SignaLink; Q9Y5P6; -.
DR UniPathway; UPA00126; UER00930.
DR BioGRID-ORCS; 29925; 690 hits in 1085 CRISPR screens.
DR ChiTaRS; GMPPB; human.
DR GeneWiki; GMPPB; -.
DR GenomeRNAi; 29925; -.
DR Pharos; Q9Y5P6; Tbio.
DR PRO; PR:Q9Y5P6; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9Y5P6; protein.
DR Bgee; ENSG00000173540; Expressed in body of pancreas and 107 other tissues.
DR ExpressionAtlas; Q9Y5P6; baseline and differential.
DR Genevisible; Q9Y5P6; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase activity; IBA:GO_Central.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR CDD; cd06425; M1P_guanylylT_B_like_N; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR045233; GMPPB_N.
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; Congenital muscular dystrophy;
KW Cytoplasm; Disease variant; Dystroglycanopathy; GTP-binding;
KW Limb-girdle muscular dystrophy; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..360
FT /note="Mannose-1-phosphate guanyltransferase beta"
FT /id="PRO_0000307162"
FT VAR_SEQ 317
FT /note="W -> WVSLWAGLGGERGGECACLPDKAYPLLE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028619"
FT VARIANT 22
FT /note="P -> S (in MDDGC14; causes protein aggregation;
FT dbSNP:rs397509424)"
FT /evidence="ECO:0000269|PubMed:23768512,
FT ECO:0000269|PubMed:26310427, ECO:0000269|PubMed:28478914"
FT /id="VAR_070142"
FT VARIANT 27
FT /note="D -> H (in MDDGC14; the protein remains distributed
FT in the cytoplasm and has no discernable changes compared to
FT wild-type; dbSNP:rs142336618)"
FT /evidence="ECO:0000269|PubMed:23768512"
FT /id="VAR_070143"
FT VARIANT 32
FT /note="P -> L (in MDDGB14; causes protein aggregation;
FT dbSNP:rs397509426)"
FT /evidence="ECO:0000269|PubMed:23768512"
FT /id="VAR_070144"
FT VARIANT 32
FT /note="P -> S (in MDDGC14)"
FT /evidence="ECO:0000269|PubMed:26310427"
FT /id="VAR_079761"
FT VARIANT 126
FT /note="H -> D (in dbSNP:rs34345884)"
FT /id="VAR_035372"
FT VARIANT 132
FT /note="S -> C (in MDDGC14; dbSNP:rs145535498)"
FT /evidence="ECO:0000269|PubMed:26310427"
FT /id="VAR_079762"
FT VARIANT 184
FT /note="Q -> R (in dbSNP:rs1466685)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1"
FT /id="VAR_035373"
FT VARIANT 185
FT /note="R -> C (in MDDGB14; the protein remains distributed
FT in the cytoplasm and has no discernable changes compared to
FT wild-type; dbSNP:rs397509425)"
FT /evidence="ECO:0000269|PubMed:23768512"
FT /id="VAR_070145"
FT VARIANT 219
FT /note="I -> T (in MDDGC14; dbSNP:rs761714818)"
FT /evidence="ECO:0000269|PubMed:26310427"
FT /id="VAR_079763"
FT VARIANT 241
FT /note="P -> S (in MDDGC14)"
FT /evidence="ECO:0000269|PubMed:26310427"
FT /id="VAR_079764"
FT VARIANT 254
FT /note="V -> M (in MDDGC14; dbSNP:rs875989850)"
FT /evidence="ECO:0000269|PubMed:26310427"
FT /id="VAR_079765"
FT VARIANT 287
FT /note="R -> Q (in MDDGB14 and MDDGC14; dbSNP:rs202160208)"
FT /evidence="ECO:0000269|PubMed:23768512,
FT ECO:0000269|PubMed:26310427"
FT /id="VAR_070146"
FT VARIANT 287
FT /note="R -> W (in MDDGC14; dbSNP:rs142908436)"
FT /evidence="ECO:0000269|PubMed:26310427,
FT ECO:0000269|PubMed:28478914"
FT /id="VAR_079766"
FT VARIANT 293
FT /note="R -> W (in MDDGC14; slight reduction in protein
FT abundance; dbSNP:rs756682220)"
FT /evidence="ECO:0000269|PubMed:28433477"
FT /id="VAR_079767"
FT VARIANT 318
FT /note="V -> A (in MDDGC14; dbSNP:rs559784211)"
FT /evidence="ECO:0000269|PubMed:26310427"
FT /id="VAR_079768"
FT VARIANT 322
FT /note="N -> K (in MDDGC14; no change in protein abundance;
FT dbSNP:rs781114909)"
FT /evidence="ECO:0000269|PubMed:28433477"
FT /id="VAR_079769"
FT VARIANT 330
FT /note="V -> I (in MDDGC14; causes protein aggregation;
FT dbSNP:rs199922550)"
FT /evidence="ECO:0000269|PubMed:23768512,
FT ECO:0000269|PubMed:26310427"
FT /id="VAR_070147"
FT VARIANT 334
FT /note="D -> N (in MDDGA14; causes protein aggregation;
FT dbSNP:rs397509422)"
FT /evidence="ECO:0000269|PubMed:23768512"
FT /id="VAR_070148"
FT VARIANT 340
FT /note="G -> R (in MDDGC14; slight reduction in protein
FT abundance; shows an increased propensity to form punctate
FT aggregates; dbSNP:rs1064796834)"
FT /evidence="ECO:0000269|PubMed:28433477"
FT /id="VAR_079770"
FT VARIANT 357
FT /note="R -> H (in MDDGC14; no change in protein abundance;
FT shows an increased propensity to form punctate aggregates;
FT dbSNP:rs771861177)"
FT /evidence="ECO:0000269|PubMed:28433477"
FT /id="VAR_079771"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:7D73"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:7D73"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:7D74"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:7D73"
FT HELIX 33..40
FT /evidence="ECO:0007829|PDB:7D73"
FT TURN 41..45
FT /evidence="ECO:0007829|PDB:7D73"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:7D73"
FT HELIX 57..71
FT /evidence="ECO:0007829|PDB:7D73"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:7D73"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:7D73"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:7D73"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:7D73"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:7D73"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:7D73"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:7D74"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:7D73"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:7D73"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:7D72"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:7D74"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:7D72"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:7D73"
FT STRAND 169..178
FT /evidence="ECO:0007829|PDB:7D73"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:7D73"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:7D73"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:7D73"
FT HELIX 197..203
FT /evidence="ECO:0007829|PDB:7D73"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:7D73"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:7D74"
FT HELIX 222..239
FT /evidence="ECO:0007829|PDB:7D73"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:7D74"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:7D73"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:7D73"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:7D73"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:7D73"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:7D73"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:7D73"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:7D73"
SQ SEQUENCE 360 AA; 39834 MW; 8212C77BBB2EF960 CRC64;
MKALILVGGY GTRLRPLTLS TPKPLVDFCN KPILLHQVEA LAAAGVDHVI LAVSYMSQVL
EKEMKAQEQR LGIRISMSHE EEPLGTAGPL ALARDLLSET ADPFFVLNSD VICDFPFQAM
VQFHRHHGQE GSILVTKVEE PSKYGVVVCE ADTGRIHRFV EKPQVFVSNK INAGMYILSP
AVLQRIQLQP TSIEKEVFPI MAKEGQLYAM ELQGFWMDIG QPKDFLTGMC LFLQSLRQKQ
PERLCSGPGI VGNVLVDPSA RIGQNCSIGP NVSLGPGVVV EDGVCIRRCT VLRDARIRSH
SWLESCIVGW RCRVGQWVRM ENVTVLGEDV IVNDELYLNG ASVLPHKSIG ESVPEPRIIM
