ALG2_HUMAN
ID ALG2_HUMAN Reviewed; 416 AA.
AC Q9H553; A2A2Y0; Q8NBX2; Q8NC39;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Alpha-1,3/1,6-mannosyltransferase ALG2;
DE EC=2.4.1.132 {ECO:0000269|PubMed:12684507};
DE EC=2.4.1.257 {ECO:0000269|PubMed:12684507};
DE AltName: Full=Asparagine-linked glycosylation protein 2 homolog;
DE AltName: Full=GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase;
DE AltName: Full=GDP-Man:Man(1)GlcNAc(2)-PP-dolichol mannosyltransferase;
DE AltName: Full=GDP-Man:Man(2)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase;
GN Name=ALG2; ORFNames=UNQ666/PRO1298;
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 Takahashi T., Katoh R., Okutomi S., Suzuki Y., Mori H., Takizawa Y.,
RA Nishikawa Y.;
RT "Molecular cloning of the mammalian genes which complement the defect of
RT the yeast alg2 mutation.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic testis carcinoma;
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 FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND INVOLVEMENT IN CDG1I.
RX PubMed=12684507; DOI=10.1074/jbc.m302850200;
RA Thiel C., Schwarz M., Peng J., Grzmil M., Hasilik M., Braulke T.,
RA Kohlschuetter A., von Figura K., Lehle L., Koerner C.;
RT "A new type of congenital disorders of glycosylation (CDG-Ii) provides new
RT insights into the early steps of dolichol-linked oligosaccharide
RT biosynthesis.";
RL J. Biol. Chem. 278:22498-22505(2003).
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 INVOLVEMENT IN CMS14, VARIANT CMS14 GLY-68, AND CHARACTERIZATION OF VARIANT
RP CMS14 GLY-68.
RX PubMed=23404334; DOI=10.1093/brain/awt010;
RG WGS500 Consortium;
RA Cossins J., Belaya K., Hicks D., Salih M.A., Finlayson S., Carboni N.,
RA Liu W.W., Maxwell S., Zoltowska K., Farsani G.T., Laval S., Seidhamed M.Z.,
RA Donnelly P., Bentley D., McGowan S.J., Muller J., Palace J., Lochmuller H.,
RA Beeson D., Donnelly P., Bell J., Bentley D., McVean G., Ratcfliffe P.,
RA Taylor J., Wilkie A., Donnelly P., Broxholme J., Buck D., Cazier J.B.,
RA Cornall R., Gregory L., Knight J., Lunter G., McVean G., Taylor J.,
RA Tomlinson I., Wilkie A., Buck D., Allan C., Attar M., Green A., Gregory L.,
RA Humphray S., Kingsbury Z., Lamble S., Lonie L., Pagnamenta A., Piazza P.,
RA Polanco G., Trebes A., McVean G., Donnelly P., Cazier J.B., Broxholme J.,
RA Copley R., Fiddy S., Grocock R., Hatton E., Holmes C., Hughes L.,
RA Humburg P., Kanapin A., Lise S., Lunter G., Martin H., Murray L.,
RA McCarthy D., Rimmer A., Sahgal N., Wright B., Yau C.;
RT "Congenital myasthenic syndromes due to mutations in ALG2 and ALG14.";
RL Brain 136:944-956(2013).
CC -!- FUNCTION: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and
CC Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol
CC diphosphate. {ECO:0000269|PubMed:12684507}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-beta-D-
CC Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol +
CC GDP + H(+); Xref=Rhea:RHEA:29515, Rhea:RHEA-COMP:11044, Rhea:RHEA-
CC COMP:12624, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:58472, ChEBI:CHEBI:132510; EC=2.4.1.132;
CC Evidence={ECO:0000269|PubMed:12684507};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc-diphosphodolichol + GDP + H(+); Xref=Rhea:RHEA:29519,
CC Rhea:RHEA-COMP:12624, Rhea:RHEA-COMP:12626, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:132510,
CC ChEBI:CHEBI:132511; EC=2.4.1.257;
CC Evidence={ECO:0000269|PubMed:12684507};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:12684507}.
CC -!- INTERACTION:
CC Q9H553; P54253: ATXN1; NbExp=3; IntAct=EBI-25806804, EBI-930964;
CC Q9H553; P42858: HTT; NbExp=3; IntAct=EBI-25806804, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H553-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H553-2; Sequence=VSP_013188, VSP_013189;
CC -!- DISEASE: Congenital disorder of glycosylation 1I (CDG1I) [MIM:607906]:
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. {ECO:0000269|PubMed:12684507}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Myasthenic syndrome, congenital, 14 (CMS14) [MIM:616228]: A
CC form of congenital myasthenic syndrome, a group of disorders
CC characterized by failure of neuromuscular transmission, including pre-
CC synaptic, synaptic, and post-synaptic disorders that are not of
CC autoimmune origin. Clinical features are easy fatigability and muscle
CC weakness. CMS14 is an autosomal recessive form characterized by onset
CC of limb-girdle muscle weakness in early childhood. The disorder is
CC slowly progressive, and some patients may become wheelchair-bound.
CC {ECO:0000269|PubMed:23404334}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR EMBL; AB161356; BAD11905.1; -; mRNA.
DR EMBL; AY358697; AAQ89060.1; -; mRNA.
DR EMBL; AK027417; BAB55099.1; -; mRNA.
DR EMBL; AK074704; BAC11150.1; -; mRNA.
DR EMBL; AK074988; BAC11337.1; -; mRNA.
DR EMBL; AK075172; BAC11449.1; -; mRNA.
DR EMBL; AL137067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017876; AAH17876.1; -; mRNA.
DR CCDS; CCDS6739.1; -. [Q9H553-1]
DR RefSeq; NP_149078.1; NM_033087.3. [Q9H553-1]
DR AlphaFoldDB; Q9H553; -.
DR SMR; Q9H553; -.
DR BioGRID; 124493; 33.
DR IntAct; Q9H553; 5.
DR STRING; 9606.ENSP00000417764; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR iPTMnet; Q9H553; -.
DR PhosphoSitePlus; Q9H553; -.
DR BioMuta; ALG2; -.
DR DMDM; 46395991; -.
DR EPD; Q9H553; -.
DR jPOST; Q9H553; -.
DR MassIVE; Q9H553; -.
DR MaxQB; Q9H553; -.
DR PaxDb; Q9H553; -.
DR PeptideAtlas; Q9H553; -.
DR PRIDE; Q9H553; -.
DR ProteomicsDB; 80891; -. [Q9H553-1]
DR ProteomicsDB; 80892; -. [Q9H553-2]
DR Antibodypedia; 29048; 265 antibodies from 23 providers.
DR DNASU; 85365; -.
DR Ensembl; ENST00000319033.7; ENSP00000326609.6; ENSG00000119523.10. [Q9H553-2]
DR Ensembl; ENST00000476832.2; ENSP00000417764.1; ENSG00000119523.10. [Q9H553-1]
DR GeneID; 85365; -.
DR KEGG; hsa:85365; -.
DR MANE-Select; ENST00000476832.2; ENSP00000417764.1; NM_033087.4; NP_149078.1.
DR UCSC; uc004azf.4; human. [Q9H553-1]
DR CTD; 85365; -.
DR DisGeNET; 85365; -.
DR GeneCards; ALG2; -.
DR GeneReviews; ALG2; -.
DR HGNC; HGNC:23159; ALG2.
DR HPA; ENSG00000119523; Low tissue specificity.
DR MalaCards; ALG2; -.
DR MIM; 607905; gene.
DR MIM; 607906; phenotype.
DR MIM; 616228; phenotype.
DR neXtProt; NX_Q9H553; -.
DR OpenTargets; ENSG00000119523; -.
DR Orphanet; 79326; ALG2-CDG.
DR Orphanet; 353327; Congenital myasthenic syndromes with glycosylation defect.
DR PharmGKB; PA134956849; -.
DR VEuPathDB; HostDB:ENSG00000119523; -.
DR eggNOG; KOG0853; Eukaryota.
DR GeneTree; ENSGT00550000075033; -.
DR HOGENOM; CLU_030619_1_0_1; -.
DR InParanoid; Q9H553; -.
DR OMA; TIFTSHC; -.
DR PhylomeDB; Q9H553; -.
DR TreeFam; TF106000; -.
DR BRENDA; 2.4.1.132; 2681.
DR BRENDA; 2.4.1.257; 2681.
DR PathwayCommons; Q9H553; -.
DR Reactome; R-HSA-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
DR Reactome; R-HSA-4549349; Defective ALG2 causes CDG-1i.
DR SignaLink; Q9H553; -.
DR SIGNOR; Q9H553; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 85365; 761 hits in 1095 CRISPR screens.
DR ChiTaRS; ALG2; human.
DR GeneWiki; ALG2; -.
DR GenomeRNAi; 85365; -.
DR Pharos; Q9H553; Tbio.
DR PRO; PR:Q9H553; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9H553; protein.
DR Bgee; ENSG00000119523; Expressed in epithelial cell of pancreas and 184 other tissues.
DR ExpressionAtlas; Q9H553; baseline and differential.
DR Genevisible; Q9H553; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0000033; F:alpha-1,3-mannosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IMP:UniProtKB.
DR GO; GO:0004378; F:GDP-Man:Man1GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102704; F:GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IGI:GO_Central.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IGI:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; IDA:UniProtKB.
DR InterPro; IPR027054; ALG2.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR PANTHER; PTHR45918; PTHR45918; 1.
DR Pfam; PF13439; Glyco_transf_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Congenital disorder of glycosylation;
KW Congenital myasthenic syndrome; Disease variant; Glycosyltransferase;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..416
FT /note="Alpha-1,3/1,6-mannosyltransferase ALG2"
FT /id="PRO_0000080260"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..91
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_013188"
FT VAR_SEQ 92..116
FT /note="VRMVFLALYVLFLADEEFDVVVCDQ -> MPLLKLVHGSPLVFGEKFKLFTL
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_013189"
FT VARIANT 11
FT /note="S -> P (in dbSNP:rs11545137)"
FT /id="VAR_049351"
FT VARIANT 68
FT /note="V -> G (in CMS14; shows severely reduced expression
FT of the mutant protein; dbSNP:rs730882051)"
FT /evidence="ECO:0000269|PubMed:23404334"
FT /id="VAR_073332"
FT VARIANT 367
FT /note="V -> A (in dbSNP:rs35626507)"
FT /id="VAR_049352"
FT CONFLICT 178
FT /note="Q -> R (in Ref. 2; BAC11449)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 416 AA; 47092 MW; 778DB1FD069E7F29 CRC64;
MAEEQGRERD SVPKPSVLFL HPDLGVGGAE RLVLDAALAL QARGCSVKIW TAHYDPGHCF
AESRELPVRC AGDWLPRGLG WGGRGAAVCA YVRMVFLALY VLFLADEEFD VVVCDQVSAC
IPVFRLARRR KKILFYCHFP DLLLTKRDSF LKRLYRAPID WIEEYTTGMA DCILVNSQFT
AAVFKETFKS LSHIDPDVLY PSLNVTSFDS VVPEKLDDLV PKGKKFLLLS INRYERKKNL
TLALEALVQL RGRLTSQDWE RVHLIVAGGY DERVLENVEH YQELKKMVQQ SDLGQYVTFL
RSFSDKQKIS LLHSCTCVLY TPSNEHFGIV PLEAMYMQCP VIAVNSGGPL ESIDHSVTGF
LCEPDPVHFS EAIEKFIREP SLKATMGLAG RARVKEKFSP EAFTEQLYRY VTKLLV
