Full text data of GANAB
GANAB
(G2AN, KIAA0088)
[Confidence: high (present in two of the MS resources)]
Neutral alpha-glucosidase AB; 3.2.1.84 (Alpha-glucosidase 2; Glucosidase II subunit alpha; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Neutral alpha-glucosidase AB; 3.2.1.84 (Alpha-glucosidase 2; Glucosidase II subunit alpha; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00011454
IPI00011454 Splice isoform 2 of Q14697 Neutral alpha-glucosidase AB precursor Splice isoform 2 of Q14697 Neutral alpha-glucosidase AB precursor membrane n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a 4 n/a 1 ER lumen and Golgi splice isoforms 1, 2 and 3 found at its expected molecular weight found at molecular weight
IPI00011454 Splice isoform 2 of Q14697 Neutral alpha-glucosidase AB precursor Splice isoform 2 of Q14697 Neutral alpha-glucosidase AB precursor membrane n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a 4 n/a 1 ER lumen and Golgi splice isoforms 1, 2 and 3 found at its expected molecular weight found at molecular weight
UniProt
Q14697
ID GANAB_HUMAN Reviewed; 944 AA.
AC Q14697; A6NC20; Q8WTS9; Q9P0X0;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 3.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Neutral alpha-glucosidase AB;
DE EC=3.2.1.84;
DE AltName: Full=Alpha-glucosidase 2;
DE AltName: Full=Glucosidase II subunit alpha;
DE Flags: Precursor;
GN Name=GANAB; Synonyms=G2AN, KIAA0088;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Stuerzenhofecker B., Nguyenvan P., Soeling H.D.;
RT "Sequence and analysis of the endoplasmic reticulum protein
RT glucosidase II.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, MUTAGENESIS OF
RP ASP-542, INTERACTION WITH PRKCSH, SUBCELLULAR LOCATION, AND
RP ALTERNATIVE SPLICING.
RX PubMed=10929008; DOI=10.1093/glycob/10.8.815;
RA Pelletier M.F., Marcil A., Sevigny G., Jakob C.A., Tessier D.C.,
RA Chevet E., Menard R., Bergeron J.J.M., Thomas D.Y.;
RT "The heterodimeric structure of glucosidase II is required for its
RT activity, solubility, and localization in vivo.";
RL Glycobiology 10:815-827(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-944 (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
RA Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III.
RT The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 457-944 (ISOFORMS 1/2).
RC TISSUE=Lymph, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 915-929, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [7]
RP GLYCOSYLATION, AND TISSUE SPECIFICITY.
RX PubMed=3881423;
RA Martiniuk F., Ellenbogen A., Hirschhorn R.;
RT "Identity of neutral alpha-glucosidase AB and the glycoprotein
RT processing enzyme glucosidase II. Biochemical and genetic studies.";
RL J. Biol. Chem. 260:1238-1242(1985).
RN [8]
RP INTERACTION WITH PRKCSH.
RX PubMed=8910335; DOI=10.1074/jbc.271.44.27509;
RA Trombetta E.S., Simons J.F., Helenius A.;
RT "Endoplasmic reticulum glucosidase II is composed of a catalytic
RT subunit, conserved from yeast to mammals, and a tightly bound
RT noncatalytic HDEL-containing subunit.";
RL J. Biol. Chem. 271:27509-27516(1996).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [10]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Cleaves sequentially the 2 innermost alpha-1,3-linked
CC glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide
CC precursor of immature glycoproteins.
CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal (1->3)-alpha-D-
CC glucosidic links in (1->3)-alpha-D-glucans.
CC -!- PATHWAY: Glycan metabolism; N-glycan metabolism.
CC -!- SUBUNIT: Heterodimer of a catalytic alpha subunit (GANAB) and a
CC beta subunit (PRKCSH). Binds glycosylated PTPRC (By similarity).
CC -!- INTERACTION:
CC P78545:ELF3; NbExp=1; IntAct=EBI-348004, EBI-1057285;
CC P48634:PRRC2A; NbExp=1; IntAct=EBI-348004, EBI-347545;
CC Q9Y4K3:TRAF6; NbExp=1; IntAct=EBI-348004, EBI-359276;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum (By similarity). Golgi
CC apparatus (By similarity). Melanosome. Note=Identified by mass
CC spectrometry in melanosome fractions from stage I to stage IV.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q14697-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14697-2; Sequence=VSP_010674;
CC Name=3;
CC IsoId=Q14697-3; Sequence=VSP_039976, VSP_039977;
CC Note=May be produced at very low levels due to a premature stop
CC codon in the mRNA, leading to nonsense-mediated mRNA decay;
CC -!- TISSUE SPECIFICITY: Detected in placenta.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH65266.1; Type=Erroneous translation; Note=Wrong choice of CDS;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AJ000332; CAA04006.1; -; mRNA.
DR EMBL; AF144074; AAF66685.1; -; mRNA.
DR EMBL; AP001458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D42041; BAA07642.1; -; mRNA.
DR EMBL; BC017433; AAH17433.2; -; mRNA.
DR EMBL; BC017435; AAH17435.2; -; mRNA.
DR EMBL; BC065266; AAH65266.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001265121.1; NM_001278192.1.
DR RefSeq; NP_001265122.1; NM_001278193.1.
DR RefSeq; NP_001265123.1; NM_001278194.1.
DR RefSeq; NP_938148.1; NM_198334.2.
DR RefSeq; NP_938149.2; NM_198335.3.
DR UniGene; Hs.595071; -.
DR ProteinModelPortal; Q14697; -.
DR SMR; Q14697; 249-911.
DR IntAct; Q14697; 17.
DR MINT; MINT-5001279; -.
DR STRING; 9606.ENSP00000340466; -.
DR BindingDB; Q14697; -.
DR ChEMBL; CHEMBL2519; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR PhosphoSite; Q14697; -.
DR DMDM; 54037162; -.
DR REPRODUCTION-2DPAGE; IPI00383581; -.
DR PaxDb; Q14697; -.
DR PRIDE; Q14697; -.
DR DNASU; 23193; -.
DR Ensembl; ENST00000346178; ENSP00000340466; ENSG00000089597.
DR Ensembl; ENST00000356638; ENSP00000349053; ENSG00000089597.
DR Ensembl; ENST00000526210; ENSP00000433799; ENSG00000089597.
DR Ensembl; ENST00000532402; ENSP00000432181; ENSG00000089597.
DR Ensembl; ENST00000534613; ENSP00000434921; ENSG00000089597.
DR GeneID; 23193; -.
DR KEGG; hsa:23193; -.
DR UCSC; uc001nub.4; human.
DR CTD; 23193; -.
DR GeneCards; GC11M062430; -.
DR HGNC; HGNC:4138; GANAB.
DR HPA; HPA026874; -.
DR MIM; 104160; gene.
DR neXtProt; NX_Q14697; -.
DR PharmGKB; PA28551; -.
DR eggNOG; COG1501; -.
DR HOVERGEN; HBG051683; -.
DR KO; K05546; -.
DR OMA; AIDDQLY; -.
DR OrthoDB; EOG7VQJDS; -.
DR BRENDA; 3.2.1.84; 2681.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_17015; Metabolism of proteins.
DR UniPathway; UPA00957; -.
DR ChiTaRS; GANAB; human.
DR GeneWiki; GANAB; -.
DR GenomeRNAi; 23193; -.
DR NextBio; 44685; -.
DR PRO; PR:Q14697; -.
DR ArrayExpress; Q14697; -.
DR Bgee; Q14697; -.
DR CleanEx; HS_GANAB; -.
DR Genevestigator; Q14697; -.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0017177; C:glucosidase II complex; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0033919; F:glucan 1,3-alpha-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR GO; GO:0006457; P:protein folding; TAS:Reactome.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
DR InterPro; IPR011013; Gal_mutarotase_SF_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 2.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
DR PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Direct protein sequencing;
KW Endoplasmic reticulum; Glycoprotein; Glycosidase; Golgi apparatus;
KW Hydrolase; Polymorphism; Reference proteome; Signal.
FT SIGNAL 1 28 Potential.
FT CHAIN 29 944 Neutral alpha-glucosidase AB.
FT /FTId=PRO_0000018571.
FT ACT_SITE 542 542 Nucleophile.
FT ACT_SITE 545 545 By similarity.
FT ACT_SITE 618 618 Proton donor (By similarity).
FT CARBOHYD 97 97 N-linked (GlcNAc...).
FT VAR_SEQ 49 52 RQRS -> CCWC (in isoform 3).
FT /FTId=VSP_039976.
FT VAR_SEQ 53 944 Missing (in isoform 3).
FT /FTId=VSP_039977.
FT VAR_SEQ 187 187 S -> SFSDKVNLTLGSIWDKIKNLFSR (in isoform
FT 2).
FT /FTId=VSP_010674.
FT VARIANT 154 154 R -> W (in dbSNP:rs2276296).
FT /FTId=VAR_024529.
FT VARIANT 173 173 R -> Q (in dbSNP:rs2276295).
FT /FTId=VAR_022086.
FT VARIANT 309 309 R -> C (in dbSNP:rs1063445).
FT /FTId=VAR_050272.
FT MUTAGEN 542 542 D->N: Loss of activity.
FT CONFLICT 400 400 R -> C (in Ref. 5; AAH65266).
FT CONFLICT 461 461 R -> W (in Ref. 5; AAH65266).
FT CONFLICT 850 850 H -> Y (in Ref. 1; CAA04006 and 4;
FT BAA07642).
SQ SEQUENCE 944 AA; 106874 MW; 9E3426FE9A016BF1 CRC64;
MAAVAAVAAR RRRSWASLVL AFLGVCLGIT LAVDRSNFKT CEESSFCKRQ RSIRPGLSPY
RALLDSLQLG PDSLTVHLIH EVTKVLLVLE LQGLQKNMTR FRIDELEPRR PRYRVPDVLV
ADPPIARLSV SGRDENSVEL TMAEGPYKII LTARPFRLDL LEDRSLLLSV NARGLLEFEH
QRAPRVSQGS KDPAEGDGAQ PEETPRDGDK PEETQGKAEK DEPGAWEETF KTHSDSKPYG
PMSVGLDFSL PGMEHVYGIP EHADNLRLKV TEGGEPYRLY NLDVFQYELY NPMALYGSVP
VLLAHNPHRD LGIFWLNAAE TWVDISSNTA GKTLFGKMMD YLQGSGETPQ TDVRWMSETG
IIDVFLLLGP SISDVFRQYA SLTGTQALPP LFSLGYHQSR WNYRDEADVL EVDQGFDDHN
LPCDVIWLDI EHADGKRYFT WDPSRFPQPR TMLERLASKR RKLVAIVDPH IKVDSGYRVH
EELRNLGLYV KTRDGSDYEG WCWPGSAGYP DFTNPTMRAW WANMFSYDNY EGSAPNLFVW
NDMNEPSVFN GPEVTMLKDA QHYGGWEHRD VHNIYGLYVH MATADGLRQR SGGMERPFVL
ARAFFAGSQR FGAVWTGDNT AEWDHLKISI PMCLSLGLVG LSFCGADVGG FFKNPEPELL
VRWYQMGAYQ PFFRAHAHLD TGRREPWLLP SQHNDIIRDA LGQRYSLLPF WYTLLYQAHR
EGIPVMRPLW VQYPQDVTTF NIDDQYLLGD ALLVHPVSDS GAHGVQVYLP GQGEVWYDIQ
SYQKHHGPQT LYLPVTLSSI PVFQRGGTIV PRWMRVRRSS ECMKDDPITL FVALSPQGTA
QGELFLDDGH TFNYQTRQEF LLRRFSFSGN TLVSSSADPE GHFETPIWIE RVVIIGAGKP
AAVVLQTKGS PESRLSFQHD PETSVLVLRK PGINVASDWS IHLR
//
ID GANAB_HUMAN Reviewed; 944 AA.
AC Q14697; A6NC20; Q8WTS9; Q9P0X0;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 3.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Neutral alpha-glucosidase AB;
DE EC=3.2.1.84;
DE AltName: Full=Alpha-glucosidase 2;
DE AltName: Full=Glucosidase II subunit alpha;
DE Flags: Precursor;
GN Name=GANAB; Synonyms=G2AN, KIAA0088;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Stuerzenhofecker B., Nguyenvan P., Soeling H.D.;
RT "Sequence and analysis of the endoplasmic reticulum protein
RT glucosidase II.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, MUTAGENESIS OF
RP ASP-542, INTERACTION WITH PRKCSH, SUBCELLULAR LOCATION, AND
RP ALTERNATIVE SPLICING.
RX PubMed=10929008; DOI=10.1093/glycob/10.8.815;
RA Pelletier M.F., Marcil A., Sevigny G., Jakob C.A., Tessier D.C.,
RA Chevet E., Menard R., Bergeron J.J.M., Thomas D.Y.;
RT "The heterodimeric structure of glucosidase II is required for its
RT activity, solubility, and localization in vivo.";
RL Glycobiology 10:815-827(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-944 (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
RA Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III.
RT The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 457-944 (ISOFORMS 1/2).
RC TISSUE=Lymph, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 915-929, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [7]
RP GLYCOSYLATION, AND TISSUE SPECIFICITY.
RX PubMed=3881423;
RA Martiniuk F., Ellenbogen A., Hirschhorn R.;
RT "Identity of neutral alpha-glucosidase AB and the glycoprotein
RT processing enzyme glucosidase II. Biochemical and genetic studies.";
RL J. Biol. Chem. 260:1238-1242(1985).
RN [8]
RP INTERACTION WITH PRKCSH.
RX PubMed=8910335; DOI=10.1074/jbc.271.44.27509;
RA Trombetta E.S., Simons J.F., Helenius A.;
RT "Endoplasmic reticulum glucosidase II is composed of a catalytic
RT subunit, conserved from yeast to mammals, and a tightly bound
RT noncatalytic HDEL-containing subunit.";
RL J. Biol. Chem. 271:27509-27516(1996).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [10]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Cleaves sequentially the 2 innermost alpha-1,3-linked
CC glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide
CC precursor of immature glycoproteins.
CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal (1->3)-alpha-D-
CC glucosidic links in (1->3)-alpha-D-glucans.
CC -!- PATHWAY: Glycan metabolism; N-glycan metabolism.
CC -!- SUBUNIT: Heterodimer of a catalytic alpha subunit (GANAB) and a
CC beta subunit (PRKCSH). Binds glycosylated PTPRC (By similarity).
CC -!- INTERACTION:
CC P78545:ELF3; NbExp=1; IntAct=EBI-348004, EBI-1057285;
CC P48634:PRRC2A; NbExp=1; IntAct=EBI-348004, EBI-347545;
CC Q9Y4K3:TRAF6; NbExp=1; IntAct=EBI-348004, EBI-359276;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum (By similarity). Golgi
CC apparatus (By similarity). Melanosome. Note=Identified by mass
CC spectrometry in melanosome fractions from stage I to stage IV.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q14697-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14697-2; Sequence=VSP_010674;
CC Name=3;
CC IsoId=Q14697-3; Sequence=VSP_039976, VSP_039977;
CC Note=May be produced at very low levels due to a premature stop
CC codon in the mRNA, leading to nonsense-mediated mRNA decay;
CC -!- TISSUE SPECIFICITY: Detected in placenta.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH65266.1; Type=Erroneous translation; Note=Wrong choice of CDS;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AJ000332; CAA04006.1; -; mRNA.
DR EMBL; AF144074; AAF66685.1; -; mRNA.
DR EMBL; AP001458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D42041; BAA07642.1; -; mRNA.
DR EMBL; BC017433; AAH17433.2; -; mRNA.
DR EMBL; BC017435; AAH17435.2; -; mRNA.
DR EMBL; BC065266; AAH65266.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001265121.1; NM_001278192.1.
DR RefSeq; NP_001265122.1; NM_001278193.1.
DR RefSeq; NP_001265123.1; NM_001278194.1.
DR RefSeq; NP_938148.1; NM_198334.2.
DR RefSeq; NP_938149.2; NM_198335.3.
DR UniGene; Hs.595071; -.
DR ProteinModelPortal; Q14697; -.
DR SMR; Q14697; 249-911.
DR IntAct; Q14697; 17.
DR MINT; MINT-5001279; -.
DR STRING; 9606.ENSP00000340466; -.
DR BindingDB; Q14697; -.
DR ChEMBL; CHEMBL2519; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR PhosphoSite; Q14697; -.
DR DMDM; 54037162; -.
DR REPRODUCTION-2DPAGE; IPI00383581; -.
DR PaxDb; Q14697; -.
DR PRIDE; Q14697; -.
DR DNASU; 23193; -.
DR Ensembl; ENST00000346178; ENSP00000340466; ENSG00000089597.
DR Ensembl; ENST00000356638; ENSP00000349053; ENSG00000089597.
DR Ensembl; ENST00000526210; ENSP00000433799; ENSG00000089597.
DR Ensembl; ENST00000532402; ENSP00000432181; ENSG00000089597.
DR Ensembl; ENST00000534613; ENSP00000434921; ENSG00000089597.
DR GeneID; 23193; -.
DR KEGG; hsa:23193; -.
DR UCSC; uc001nub.4; human.
DR CTD; 23193; -.
DR GeneCards; GC11M062430; -.
DR HGNC; HGNC:4138; GANAB.
DR HPA; HPA026874; -.
DR MIM; 104160; gene.
DR neXtProt; NX_Q14697; -.
DR PharmGKB; PA28551; -.
DR eggNOG; COG1501; -.
DR HOVERGEN; HBG051683; -.
DR KO; K05546; -.
DR OMA; AIDDQLY; -.
DR OrthoDB; EOG7VQJDS; -.
DR BRENDA; 3.2.1.84; 2681.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_17015; Metabolism of proteins.
DR UniPathway; UPA00957; -.
DR ChiTaRS; GANAB; human.
DR GeneWiki; GANAB; -.
DR GenomeRNAi; 23193; -.
DR NextBio; 44685; -.
DR PRO; PR:Q14697; -.
DR ArrayExpress; Q14697; -.
DR Bgee; Q14697; -.
DR CleanEx; HS_GANAB; -.
DR Genevestigator; Q14697; -.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0017177; C:glucosidase II complex; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0033919; F:glucan 1,3-alpha-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR GO; GO:0006457; P:protein folding; TAS:Reactome.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
DR InterPro; IPR011013; Gal_mutarotase_SF_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 2.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
DR PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Direct protein sequencing;
KW Endoplasmic reticulum; Glycoprotein; Glycosidase; Golgi apparatus;
KW Hydrolase; Polymorphism; Reference proteome; Signal.
FT SIGNAL 1 28 Potential.
FT CHAIN 29 944 Neutral alpha-glucosidase AB.
FT /FTId=PRO_0000018571.
FT ACT_SITE 542 542 Nucleophile.
FT ACT_SITE 545 545 By similarity.
FT ACT_SITE 618 618 Proton donor (By similarity).
FT CARBOHYD 97 97 N-linked (GlcNAc...).
FT VAR_SEQ 49 52 RQRS -> CCWC (in isoform 3).
FT /FTId=VSP_039976.
FT VAR_SEQ 53 944 Missing (in isoform 3).
FT /FTId=VSP_039977.
FT VAR_SEQ 187 187 S -> SFSDKVNLTLGSIWDKIKNLFSR (in isoform
FT 2).
FT /FTId=VSP_010674.
FT VARIANT 154 154 R -> W (in dbSNP:rs2276296).
FT /FTId=VAR_024529.
FT VARIANT 173 173 R -> Q (in dbSNP:rs2276295).
FT /FTId=VAR_022086.
FT VARIANT 309 309 R -> C (in dbSNP:rs1063445).
FT /FTId=VAR_050272.
FT MUTAGEN 542 542 D->N: Loss of activity.
FT CONFLICT 400 400 R -> C (in Ref. 5; AAH65266).
FT CONFLICT 461 461 R -> W (in Ref. 5; AAH65266).
FT CONFLICT 850 850 H -> Y (in Ref. 1; CAA04006 and 4;
FT BAA07642).
SQ SEQUENCE 944 AA; 106874 MW; 9E3426FE9A016BF1 CRC64;
MAAVAAVAAR RRRSWASLVL AFLGVCLGIT LAVDRSNFKT CEESSFCKRQ RSIRPGLSPY
RALLDSLQLG PDSLTVHLIH EVTKVLLVLE LQGLQKNMTR FRIDELEPRR PRYRVPDVLV
ADPPIARLSV SGRDENSVEL TMAEGPYKII LTARPFRLDL LEDRSLLLSV NARGLLEFEH
QRAPRVSQGS KDPAEGDGAQ PEETPRDGDK PEETQGKAEK DEPGAWEETF KTHSDSKPYG
PMSVGLDFSL PGMEHVYGIP EHADNLRLKV TEGGEPYRLY NLDVFQYELY NPMALYGSVP
VLLAHNPHRD LGIFWLNAAE TWVDISSNTA GKTLFGKMMD YLQGSGETPQ TDVRWMSETG
IIDVFLLLGP SISDVFRQYA SLTGTQALPP LFSLGYHQSR WNYRDEADVL EVDQGFDDHN
LPCDVIWLDI EHADGKRYFT WDPSRFPQPR TMLERLASKR RKLVAIVDPH IKVDSGYRVH
EELRNLGLYV KTRDGSDYEG WCWPGSAGYP DFTNPTMRAW WANMFSYDNY EGSAPNLFVW
NDMNEPSVFN GPEVTMLKDA QHYGGWEHRD VHNIYGLYVH MATADGLRQR SGGMERPFVL
ARAFFAGSQR FGAVWTGDNT AEWDHLKISI PMCLSLGLVG LSFCGADVGG FFKNPEPELL
VRWYQMGAYQ PFFRAHAHLD TGRREPWLLP SQHNDIIRDA LGQRYSLLPF WYTLLYQAHR
EGIPVMRPLW VQYPQDVTTF NIDDQYLLGD ALLVHPVSDS GAHGVQVYLP GQGEVWYDIQ
SYQKHHGPQT LYLPVTLSSI PVFQRGGTIV PRWMRVRRSS ECMKDDPITL FVALSPQGTA
QGELFLDDGH TFNYQTRQEF LLRRFSFSGN TLVSSSADPE GHFETPIWIE RVVIIGAGKP
AAVVLQTKGS PESRLSFQHD PETSVLVLRK PGINVASDWS IHLR
//
MIM
104160
*RECORD*
*FIELD* NO
104160
*FIELD* TI
*104160 GLUCOSIDASE, ALPHA, NEUTRAL AB; GANAB
;;ALPHA-GLUCOSIDASE, NEUTRAL, AB FORM;;
read moreGLUCOSIDASE II, ALPHA SUBUNIT
*FIELD* TX
CLONING
Human tissues contain 2 isozymes of neutral alpha-glucosidase designated
AB (GANAB) and C (GANC; 104180). Initially distinguished on the basis of
differences in electrophoretic mobility in starch gel, the two have been
shown to have other differences including those of substrate
specificity. Since the AB form of mouse is not different
electrophoretically from that in man, Martiniuk et al. (1982, 1983) used
rocket immunoelectrophoresis to distinguish the enzymes from the 2
species.
Trombetta et al. (1996) isolated enzymatically active glucosidase II
from rat liver and found that it was composed of 2 subunits, alpha and
beta (177060). Based on peptide sequences of the purified enzyme, they
identified the corresponding human cDNAs in existing sequence databases.
Trombetta et al. (1996) reported that the available sequence of the
alpha subunit of human glucosidase II predicts a 912-amino acid
polypeptide with homology to the catalytic domains of several other
glucosidases, but without significant homology to human glucosidase I.
They found that the alpha subunit of human glucosidase II is a
functional homolog of a gene found on S. cerevisiae chromosome II.
MAPPING
Martiniuk et al. (1982, 1983) assigned the GANAB gene to 11q13-qter by
study of mouse-man hybrid cells.
*FIELD* RF
1. Martiniuk, F.; Smith, M.; Desnick, R.; Astrin, K.; Mitra, J.; Hirschhorn,
R.: Assignment of the gene for neutral alpha-glucosidase AB to chromosome
11. (Abstract) Am. J. Hum. Genet. 34: 173A only, 1982.
2. Martiniuk, F.; Smith, M.; Ellenbogen, A.; Desnick, R. J.; Astrin,
K.; Mitra, J.; Hirschhorn, R.: Assignment of the gene for neutral
alpha-glucosidase AB to chromosome 11. Cytogenet. Cell Genet. 35:
110-116, 1983.
3. Trombetta, E. S.; Simons, J. F.; Helenius, A.: Endoplasmic reticulum
glucosidase II is composed of a catalytic subunit, conserved from
yeast to mammals, and a tightly bound noncatalytic HDEL-containing
subunit. J. Biol. Chem. 271: 27509-27516, 1996.
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
carol: 06/14/2005
carol: 6/14/2005
jason: 6/16/1994
supermim: 3/16/1992
carol: 8/23/1990
supermim: 3/20/1990
ddp: 10/26/1989
marie: 3/25/1988
*RECORD*
*FIELD* NO
104160
*FIELD* TI
*104160 GLUCOSIDASE, ALPHA, NEUTRAL AB; GANAB
;;ALPHA-GLUCOSIDASE, NEUTRAL, AB FORM;;
read moreGLUCOSIDASE II, ALPHA SUBUNIT
*FIELD* TX
CLONING
Human tissues contain 2 isozymes of neutral alpha-glucosidase designated
AB (GANAB) and C (GANC; 104180). Initially distinguished on the basis of
differences in electrophoretic mobility in starch gel, the two have been
shown to have other differences including those of substrate
specificity. Since the AB form of mouse is not different
electrophoretically from that in man, Martiniuk et al. (1982, 1983) used
rocket immunoelectrophoresis to distinguish the enzymes from the 2
species.
Trombetta et al. (1996) isolated enzymatically active glucosidase II
from rat liver and found that it was composed of 2 subunits, alpha and
beta (177060). Based on peptide sequences of the purified enzyme, they
identified the corresponding human cDNAs in existing sequence databases.
Trombetta et al. (1996) reported that the available sequence of the
alpha subunit of human glucosidase II predicts a 912-amino acid
polypeptide with homology to the catalytic domains of several other
glucosidases, but without significant homology to human glucosidase I.
They found that the alpha subunit of human glucosidase II is a
functional homolog of a gene found on S. cerevisiae chromosome II.
MAPPING
Martiniuk et al. (1982, 1983) assigned the GANAB gene to 11q13-qter by
study of mouse-man hybrid cells.
*FIELD* RF
1. Martiniuk, F.; Smith, M.; Desnick, R.; Astrin, K.; Mitra, J.; Hirschhorn,
R.: Assignment of the gene for neutral alpha-glucosidase AB to chromosome
11. (Abstract) Am. J. Hum. Genet. 34: 173A only, 1982.
2. Martiniuk, F.; Smith, M.; Ellenbogen, A.; Desnick, R. J.; Astrin,
K.; Mitra, J.; Hirschhorn, R.: Assignment of the gene for neutral
alpha-glucosidase AB to chromosome 11. Cytogenet. Cell Genet. 35:
110-116, 1983.
3. Trombetta, E. S.; Simons, J. F.; Helenius, A.: Endoplasmic reticulum
glucosidase II is composed of a catalytic subunit, conserved from
yeast to mammals, and a tightly bound noncatalytic HDEL-containing
subunit. J. Biol. Chem. 271: 27509-27516, 1996.
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
carol: 06/14/2005
carol: 6/14/2005
jason: 6/16/1994
supermim: 3/16/1992
carol: 8/23/1990
supermim: 3/20/1990
ddp: 10/26/1989
marie: 3/25/1988