MPI_HUMAN
ID MPI_HUMAN Reviewed; 423 AA.
AC P34949; A8K8K9; Q96AB0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Mannose-6-phosphate isomerase;
DE EC=5.3.1.8;
DE AltName: Full=Phosphohexomutase;
DE AltName: Full=Phosphomannose isomerase;
DE Short=PMI;
GN Name=MPI; Synonyms=PMI1;
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 PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Placenta, and Testis;
RX PubMed=8307007; DOI=10.1111/j.1432-1033.1994.tb19954.x;
RA Proudfoot A.E.I., Turcatti G., Wells T.N.C., Payton M.A., Smith D.J.;
RT "Purification, cDNA cloning and heterologous expression of human
RT phosphomannose isomerase.";
RL Eur. J. Biochem. 219:415-423(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CDG1B THR-51; ASN-131;
RP GLN-152; SER-250 AND HIS-418.
RX PubMed=10980531;
RX DOI=10.1002/1098-1004(200009)16:3<247::aid-humu7>3.0.co;2-a;
RA Schollen E., Dorland L., de Koning T.J., Van Diggelen O.P.,
RA Huijmans J.G.M., Marquardt T., Babovic-Vuksanovic D., Patterson M.,
RA Imtiaz F., Winchester B., Adamowicz M., Pronicka E., Freeze H.,
RA Matthijs G.;
RT "Genomic organization of the human phosphomannose isomerase (MPI) gene and
RT mutation analysis in patients with congenital disorders of glycosylation
RT type Ib (CDG-Ib).";
RL Hum. Mutat. 16:247-252(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Blood, and Brain;
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 SER-102 AND SER-108, AND
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 CDG1B LEU-102 AND THR-138.
RX PubMed=9585601; DOI=10.1086/301873;
RA Jaeken J., Matthijs G., Saudubray J.-M., Dionisi-Vici C., Bertini E.,
RA de Lonlay P., Henri H., Carchon H., Schollen E., Van Schaftingen E.;
RT "Phosphomannose isomerase deficiency: a carbohydrate-deficient glycoprotein
RT syndrome with hepatic-intestinal presentation.";
RL Am. J. Hum. Genet. 62:1535-1539(1998).
RN [10]
RP VARIANT CDG1B GLN-219.
RX PubMed=9525984; DOI=10.1172/jci2350;
RA Niehues R., Hasilik M., Alton G., Koerner C., Schiebe-Sukumar M.,
RA Koch H.G., Zimmer K.-P., Wu R., Harms E., Reiter K., von Figura K.,
RA Freeze H.H., Harms H.K., Marquardt T.;
RT "Carbohydrate-deficient glycoprotein syndrome type Ib: phosphomannose
RT isomerase deficiency and mannose therapy.";
RL J. Clin. Invest. 101:1414-1420(1998).
RN [11]
RP VARIANTS CDG1B CYS-255 AND THR-398.
RX PubMed=11134235; DOI=10.1136/jmg.38.1.14;
RA de Lonlay P., Seta N., Barrot S., Chabrol B., Drouin V., Gabriel B.M.,
RA Journel H., Kretz M., Laurent J., Le Merrer M., Leroy A., Pedespan D.,
RA Sarda P., Villeneuve N., Schmitz J., van Schaftingen E., Matthijs G.,
RA Jaeken J., Koerner C., Munnich A., Saudubray J.-M., Cormier-Daire V.;
RT "A broad spectrum of clinical presentations in congenital disorders of
RT glycosylation I: a series of 26 cases.";
RL J. Med. Genet. 38:14-19(2001).
RN [12]
RP VARIANTS CDG1B THR-140 AND GLN-219.
RX PubMed=11350186; DOI=10.1006/mgme.2001.3161;
RA Westphal V., Kjaergaard S., Davis J.A., Peterson S.M., Skovby F.,
RA Freeze H.H.;
RT "Genetic and metabolic analysis of the first adult with congenital disorder
RT of glycosylation type Ib: long-term outcome and effects of mannose
RT supplementation.";
RL Mol. Genet. Metab. 73:77-85(2001).
RN [13]
RP VARIANT CDG1B CYS-129.
RX PubMed=12357336; DOI=10.1038/sj.ejhg.5200858;
RA Schollen E., Martens K., Geuzens E., Matthijs G.;
RT "DHPLC analysis as a platform for molecular diagnosis of congenital
RT disorders of glycosylation (CDG).";
RL Eur. J. Hum. Genet. 10:643-648(2002).
RN [14]
RP VARIANT CDG1B HIS-295.
RX PubMed=12414827; DOI=10.1136/jmg.39.11.849;
RA Vuillaumier-Barrot S., Le Bizec C., de Lonlay P., Barnier A., Mitchell G.,
RA Pelletier V., Prevost C., Saudubray J.-M., Durand G., Seta N.;
RT "Protein losing enteropathy-hepatic fibrosis syndrome in Saguenay-Lac St-
RT Jean, Quebec is a congenital disorder of glycosylation type Ib.";
RL J. Med. Genet. 39:849-851(2002).
CC -!- FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol-
CC phosphate-mannose required for a number of critical mannosyl transfer
CC reactions.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannose 6-phosphate = D-fructose 6-phosphate;
CC Xref=Rhea:RHEA:12356, ChEBI:CHEBI:58735, ChEBI:CHEBI:61527;
CC EC=5.3.1.8;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC step 1/2.
CC -!- INTERACTION:
CC P34949-2; P55212: CASP6; NbExp=3; IntAct=EBI-21823432, EBI-718729;
CC P34949-2; O00291: HIP1; NbExp=3; IntAct=EBI-21823432, EBI-473886;
CC P34949-2; P13473-2: LAMP2; NbExp=3; IntAct=EBI-21823432, EBI-21591415;
CC P34949-2; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-21823432, EBI-5280197;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P34949-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P34949-2; Sequence=VSP_013357;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues, but more abundant in
CC heart, brain and skeletal muscle.
CC -!- DISEASE: Congenital disorder of glycosylation 1B (CDG1B) [MIM:602579]:
CC A form of congenital disorder of glycosylation, a multisystem disorder
CC caused by a defect in glycoprotein biosynthesis and characterized by
CC under-glycosylated serum glycoproteins. Congenital disorders of
CC glycosylation result in a wide variety of clinical features, such as
CC defects in the nervous system development, psychomotor retardation,
CC dysmorphic features, hypotonia, coagulation disorders, and
CC immunodeficiency. The broad spectrum of features reflects the critical
CC role of N-glycoproteins during embryonic development, differentiation,
CC and maintenance of cell functions. CDG1B is clinically characterized by
CC protein-losing enteropathy. {ECO:0000269|PubMed:10980531,
CC ECO:0000269|PubMed:11134235, ECO:0000269|PubMed:11350186,
CC ECO:0000269|PubMed:12357336, ECO:0000269|PubMed:12414827,
CC ECO:0000269|PubMed:9525984, ECO:0000269|PubMed:9585601}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1 family.
CC {ECO:0000305}.
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DR EMBL; X76057; CAA53657.1; -; mRNA.
DR EMBL; AF227218; AAF37697.1; -; Genomic_DNA.
DR EMBL; AF227216; AAF37697.1; JOINED; Genomic_DNA.
DR EMBL; AF227217; AAF37697.1; JOINED; Genomic_DNA.
DR EMBL; AK292374; BAF85063.1; -; mRNA.
DR EMBL; CH471136; EAW99296.1; -; Genomic_DNA.
DR EMBL; BC017351; AAH17351.1; -; mRNA.
DR EMBL; BC046357; AAH46357.1; -; mRNA.
DR CCDS; CCDS10272.1; -. [P34949-1]
DR CCDS; CCDS73757.1; -. [P34949-2]
DR PIR; S41122; S41122.
DR RefSeq; NP_001276085.1; NM_001289156.1.
DR RefSeq; NP_001276086.1; NM_001289157.1. [P34949-2]
DR RefSeq; NP_002426.1; NM_002435.2. [P34949-1]
DR AlphaFoldDB; P34949; -.
DR SMR; P34949; -.
DR BioGRID; 110491; 41.
DR IntAct; P34949; 10.
DR MINT; P34949; -.
DR STRING; 9606.ENSP00000318318; -.
DR BindingDB; P34949; -.
DR ChEMBL; CHEMBL2758; -.
DR DrugCentral; P34949; -.
DR iPTMnet; P34949; -.
DR MetOSite; P34949; -.
DR PhosphoSitePlus; P34949; -.
DR BioMuta; MPI; -.
DR DMDM; 462567; -.
DR OGP; P34949; -.
DR EPD; P34949; -.
DR jPOST; P34949; -.
DR MassIVE; P34949; -.
DR MaxQB; P34949; -.
DR PaxDb; P34949; -.
DR PeptideAtlas; P34949; -.
DR PRIDE; P34949; -.
DR ProteomicsDB; 54959; -. [P34949-1]
DR ProteomicsDB; 54960; -. [P34949-2]
DR Antibodypedia; 2008; 414 antibodies from 32 providers.
DR DNASU; 4351; -.
DR Ensembl; ENST00000323744.10; ENSP00000318192.6; ENSG00000178802.18. [P34949-2]
DR Ensembl; ENST00000352410.9; ENSP00000318318.6; ENSG00000178802.18. [P34949-1]
DR GeneID; 4351; -.
DR KEGG; hsa:4351; -.
DR MANE-Select; ENST00000352410.9; ENSP00000318318.6; NM_002435.3; NP_002426.1.
DR UCSC; uc002azc.3; human. [P34949-1]
DR CTD; 4351; -.
DR DisGeNET; 4351; -.
DR GeneCards; MPI; -.
DR GeneReviews; MPI; -.
DR HGNC; HGNC:7216; MPI.
DR HPA; ENSG00000178802; Low tissue specificity.
DR MalaCards; MPI; -.
DR MIM; 154550; gene.
DR MIM; 602579; phenotype.
DR neXtProt; NX_P34949; -.
DR OpenTargets; ENSG00000178802; -.
DR Orphanet; 79319; MPI-CDG.
DR PharmGKB; PA30922; -.
DR VEuPathDB; HostDB:ENSG00000178802; -.
DR eggNOG; KOG2757; Eukaryota.
DR GeneTree; ENSGT00390000016075; -.
DR HOGENOM; CLU_026967_2_0_1; -.
DR InParanoid; P34949; -.
DR OMA; DIGLFCG; -.
DR OrthoDB; 1043197at2759; -.
DR PhylomeDB; P34949; -.
DR TreeFam; TF312831; -.
DR PathwayCommons; P34949; -.
DR Reactome; R-HSA-4043916; Defective MPI causes MPI-CDG.
DR Reactome; R-HSA-446205; Synthesis of GDP-mannose.
DR SignaLink; P34949; -.
DR UniPathway; UPA00126; UER00423.
DR BioGRID-ORCS; 4351; 62 hits in 1082 CRISPR screens.
DR GenomeRNAi; 4351; -.
DR Pharos; P34949; Tchem.
DR PRO; PR:P34949; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P34949; protein.
DR Bgee; ENSG00000178802; Expressed in apex of heart and 168 other tissues.
DR ExpressionAtlas; P34949; baseline and differential.
DR Genevisible; P34949; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IBA:GO_Central.
DR GO; GO:0061611; P:mannose to fructose-6-phosphate metabolic process; IEA:Ensembl.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR001250; Man6P_Isoase-1.
DR InterPro; IPR016305; Mannose-6-P_Isomerase.
DR InterPro; IPR018050; Pmannose_isomerase-type1_CS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR10309; PTHR10309; 1.
DR Pfam; PF01238; PMI_typeI; 1.
DR PIRSF; PIRSF001480; Mannose-6-phosphate_isomerase; 1.
DR PRINTS; PR00714; MAN6PISMRASE.
DR SUPFAM; SSF51182; SSF51182; 1.
DR TIGRFAMs; TIGR00218; manA; 1.
DR PROSITE; PS00965; PMI_I_1; 1.
DR PROSITE; PS00966; PMI_I_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Congenital disorder of glycosylation;
KW Cytoplasm; Direct protein sequencing; Disease variant; Isomerase;
KW Metal-binding; Phosphoprotein; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..423
FT /note="Mannose-6-phosphate isomerase"
FT /id="PRO_0000194235"
FT ACT_SITE 295
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 163..224
FT /note="KVPEFQFLIGDEAATHLKQTMSHDSQAVASSLQSCFSHLMKSEKKVVVEQLN
FT LLVKRISQQA -> T (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013357"
FT VARIANT 51
FT /note="M -> T (in CDG1B; dbSNP:rs764835081)"
FT /evidence="ECO:0000269|PubMed:10980531"
FT /id="VAR_022516"
FT VARIANT 102
FT /note="S -> L (in CDG1B; dbSNP:rs104894494)"
FT /evidence="ECO:0000269|PubMed:9585601"
FT /id="VAR_012338"
FT VARIANT 129
FT /note="Y -> C (in CDG1B; dbSNP:rs887249336)"
FT /evidence="ECO:0000269|PubMed:12357336"
FT /id="VAR_022517"
FT VARIANT 131
FT /note="D -> N (in CDG1B; dbSNP:rs566620411)"
FT /evidence="ECO:0000269|PubMed:10980531"
FT /id="VAR_022518"
FT VARIANT 138
FT /note="M -> T (in CDG1B; dbSNP:rs104894495)"
FT /evidence="ECO:0000269|PubMed:9585601"
FT /id="VAR_012339"
FT VARIANT 140
FT /note="I -> T (in CDG1B; dbSNP:rs773678732)"
FT /evidence="ECO:0000269|PubMed:11350186"
FT /id="VAR_012345"
FT VARIANT 152
FT /note="R -> Q (in CDG1B; dbSNP:rs766458792)"
FT /evidence="ECO:0000269|PubMed:10980531"
FT /id="VAR_022519"
FT VARIANT 219
FT /note="R -> Q (in CDG1B; dbSNP:rs104894489)"
FT /evidence="ECO:0000269|PubMed:11350186,
FT ECO:0000269|PubMed:9525984"
FT /id="VAR_012340"
FT VARIANT 250
FT /note="G -> S (in CDG1B; dbSNP:rs748090636)"
FT /evidence="ECO:0000269|PubMed:10980531"
FT /id="VAR_022520"
FT VARIANT 255
FT /note="Y -> C (in CDG1B)"
FT /evidence="ECO:0000269|PubMed:11134235"
FT /id="VAR_022521"
FT VARIANT 295
FT /note="R -> H (in CDG1B; dbSNP:rs28928906)"
FT /evidence="ECO:0000269|PubMed:12414827"
FT /id="VAR_022522"
FT VARIANT 398
FT /note="I -> T (in CDG1B; dbSNP:rs369326210)"
FT /evidence="ECO:0000269|PubMed:11134235"
FT /id="VAR_022523"
FT VARIANT 418
FT /note="R -> H (in CDG1B; dbSNP:rs863225087)"
FT /evidence="ECO:0000269|PubMed:10980531"
FT /id="VAR_022524"
SQ SEQUENCE 423 AA; 46656 MW; 1612DD966B86D3AC CRC64;
MAAPRVFPLS CAVQQYAWGK MGSNSEVARL LASSDPLAQI AEDKPYAELW MGTHPRGDAK
ILDNRISQKT LSQWIAENQD SLGSKVKDTF NGNLPFLFKV LSVETPLSIQ AHPNKELAEK
LHLQAPQHYP DANHKPEMAI ALTPFQGLCG FRPVEEIVTF LKKVPEFQFL IGDEAATHLK
QTMSHDSQAV ASSLQSCFSH LMKSEKKVVV EQLNLLVKRI SQQAAAGNNM EDIFGELLLQ
LHQQYPGDIG CFAIYFLNLL TLKPGEAMFL EANVPHAYLK GDCVECMACS DNTVRAGLTP
KFIDVPTLCE MLSYTPSSSK DRLFLPTRSQ EDPYLSIYDP PVPDFTIMKT EVPGSVTEYK
VLALDSASIL LMVQGTVIAS TPTTQTPIPL QRGGVLFIGA NESVSLKLTE PKDLLIFRAC
CLL
