MA1A1_DROME
ID MA1A1_DROME Reviewed; 667 AA.
AC P53624; A4V480; M9PH54; P53625; Q9W2W6; Q9W2W7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Mannosyl-oligosaccharide alpha-1,2-mannosidase IA {ECO:0000312|FlyBase:FBgn0259170};
DE EC=3.2.1.113 {ECO:0000250|UniProtKB:P32906};
DE AltName: Full=Man(9)-alpha-mannosidase;
DE AltName: Full=Mannosidase-1;
GN Name=alpha-Man-Ia {ECO:0000312|FlyBase:FBgn0259170};
GN Synonyms=alpha-man-1 {ECO:0000312|FlyBase:FBgn0259170},
GN mas-1 {ECO:0000312|FlyBase:FBgn0259170};
GN ORFNames=CG32684 {ECO:0000312|FlyBase:FBgn0259170};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS H AND K), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Berlin;
RC TISSUE=Head {ECO:0000303|PubMed:7729592}, and
RC Ovary {ECO:0000303|PubMed:7729592};
RX PubMed=7729592; DOI=10.1006/dbio.1995.1106;
RA Kerscher S., Albert S., Wucherpfennig D., Heisenberg M., Schneuwly S.;
RT "Molecular and genetic analysis of the Drosophila mas-1 (mannosidase-1)
RT gene which encodes a glycoprotein processing alpha 1,2-mannosidase.";
RL Dev. Biol. 168:613-626(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the maturation of Asn-linked oligosaccharides.
CC Progressively trim alpha-1,2-linked mannose residues from
CC Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).
CC {ECO:0000250|UniProtKB:Q2ULB2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] (N-
CC glucan mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-
CC (alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-
CC Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-
CC asparaginyl-[protein] (N-glucan mannose isomer 5A1,2);
CC Xref=Rhea:RHEA:56008, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14367,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28563, ChEBI:CHEBI:59087,
CC ChEBI:CHEBI:139493; EC=3.2.1.113;
CC Evidence={ECO:0000250|UniProtKB:P32906};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer
CC 8A1,2,3B1,3) = 3 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-
CC (1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein]
CC (N-glucan mannose isomer 5A1,2); Xref=Rhea:RHEA:56028, Rhea:RHEA-
CC COMP:14358, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:60628;
CC EC=3.2.1.113; Evidence={ECO:0000250|UniProtKB:P32906};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q2ULB2};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q2ULB2};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q2ULB2}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P39098}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=H {ECO:0000312|FlyBase:FBgn0259170}; Synonyms=A
CC {ECO:0000303|PubMed:7729592}, J {ECO:0000312|FlyBase:FBgn0259170}, L
CC {ECO:0000312|FlyBase:FBgn0259170}, M {ECO:0000312|FlyBase:FBgn0259170},
CC N {ECO:0000312|FlyBase:FBgn0259170}, O
CC {ECO:0000312|FlyBase:FBgn0259170};
CC IsoId=P53624-1; Sequence=Displayed;
CC Name=K {ECO:0000312|FlyBase:FBgn0259170}; Synonyms=B
CC {ECO:0000303|PubMed:7729592}, P {ECO:0000312|FlyBase:FBgn0259170};
CC IsoId=P53624-2, P53625-1;
CC Sequence=VSP_057904;
CC -!- TISSUE SPECIFICITY: Complex spatial distribution during embryogenesis,
CC including expression in lobula plate giant neurons. Also expressed in
CC adult wing and eyes. {ECO:0000269|PubMed:7729592}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically during
CC embryonic stages. {ECO:0000269|PubMed:7729592}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family.
CC {ECO:0000255|RuleBase:RU361193}.
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DR EMBL; X82640; CAA57962.1; -; mRNA.
DR EMBL; X82641; CAA57963.1; -; mRNA.
DR EMBL; AE014298; AAF46570.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF46571.3; -; Genomic_DNA.
DR EMBL; AE014298; AAS65302.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65303.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65304.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65305.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65306.1; -; Genomic_DNA.
DR EMBL; AE014298; AGB95245.1; -; Genomic_DNA.
DR EMBL; BT011036; AAR30196.1; -; mRNA.
DR PIR; S60709; S60709.
DR RefSeq; NP_001259402.1; NM_001272473.2. [P53624-2]
DR RefSeq; NP_511105.2; NM_078550.4. [P53624-2]
DR RefSeq; NP_727407.1; NM_167223.3. [P53624-1]
DR RefSeq; NP_996395.1; NM_206672.3. [P53624-1]
DR RefSeq; NP_996396.1; NM_206673.3. [P53624-1]
DR RefSeq; NP_996397.1; NM_206674.3. [P53624-1]
DR RefSeq; NP_996398.1; NM_206675.3. [P53624-1]
DR RefSeq; NP_996399.1; NM_206676.3. [P53624-1]
DR AlphaFoldDB; P53624; -.
DR SMR; P53624; -.
DR BioGRID; 58390; 3.
DR IntAct; P53624; 2.
DR STRING; 7227.FBpp0288908; -.
DR BindingDB; P53624; -.
DR ChEMBL; CHEMBL1697673; -.
DR CAZy; GH47; Glycoside Hydrolase Family 47.
DR GlyGen; P53624; 1 site.
DR PRIDE; P53624; -.
DR DNASU; 31957; -.
DR EnsemblMetazoa; FBtr0299632; FBpp0288907; FBgn0259170. [P53624-1]
DR EnsemblMetazoa; FBtr0300511; FBpp0289738; FBgn0259170. [P53624-1]
DR EnsemblMetazoa; FBtr0300512; FBpp0289739; FBgn0259170. [P53624-2]
DR EnsemblMetazoa; FBtr0300513; FBpp0289740; FBgn0259170. [P53624-1]
DR EnsemblMetazoa; FBtr0300514; FBpp0289741; FBgn0259170. [P53624-1]
DR EnsemblMetazoa; FBtr0300515; FBpp0289742; FBgn0259170. [P53624-1]
DR EnsemblMetazoa; FBtr0300516; FBpp0289743; FBgn0259170. [P53624-1]
DR EnsemblMetazoa; FBtr0331759; FBpp0304147; FBgn0259170. [P53624-2]
DR GeneID; 31957; -.
DR KEGG; dme:Dmel_CG42275; -.
DR CTD; 31957; -.
DR FlyBase; FBgn0259170; alpha-Man-Ia.
DR VEuPathDB; VectorBase:FBgn0259170; -.
DR eggNOG; KOG2204; Eukaryota.
DR GeneTree; ENSGT00940000167910; -.
DR HOGENOM; CLU_003818_3_2_1; -.
DR InParanoid; P53624; -.
DR OMA; LIKMYLY; -.
DR PhylomeDB; P53624; -.
DR Reactome; R-DME-964827; Progressive trimming of alpha-1,2-linked mannose residues from Man9/8/7GlcNAc2 to produce Man5GlcNAc2.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 31957; 1 hit in 3 CRISPR screens.
DR ChiTaRS; alpha-Man-Ia; fly.
DR GenomeRNAi; 31957; -.
DR PRO; PR:P53624; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0259170; Expressed in cleaving embryo and 23 other tissues.
DR ExpressionAtlas; P53624; baseline and differential.
DR Genevisible; P53624; DM.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IDA:FlyBase.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0035010; P:encapsulation of foreign target; IMP:FlyBase.
DR GO; GO:0006491; P:N-glycan processing; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0072347; P:response to anesthetic; IMP:FlyBase.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR001382; Glyco_hydro_47.
DR InterPro; IPR036026; Seven-hairpin_glycosidases.
DR Pfam; PF01532; Glyco_hydro_47; 1.
DR PRINTS; PR00747; GLYHDRLASE47.
DR SUPFAM; SSF48225; SSF48225; 1.
PE 2: Evidence at transcript level;
KW Alternative promoter usage; Calcium; Disulfide bond; Glycoprotein;
KW Glycosidase; Golgi apparatus; Hydrolase; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..667
FT /note="Mannosyl-oligosaccharide alpha-1,2-mannosidase IA"
FT /id="PRO_0000210316"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..667
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 154..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 529
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P31723"
FT BINDING 640
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32906"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 483..515
FT /evidence="ECO:0000250|UniProtKB:P32906"
FT VAR_SEQ 1..206
FT /note="MYRISPIGRKSNFHSREKCLIGLVLVTLCFLCFGGIFLLPDNFGSDRVLRVY
FT KHFRKAGPEIFIPAPPLAAHAPHRSEDPHFIGDRQRLEQKIRAELGDMLDEPPAAGGGE
FT PGQFQVLAQQAQAPAPVAALADQPLDQDEGHAAIPVLAAPVQGDNAASQASSHPQSSAQ
FT QHNQQQPQLPLGGGGNDQAPDTLDATLEERRQKVKE -> MCPKTSKTTPLLLIGGICF
FT VIVLVGITGITLINNINLSNIIRLNEKVASDSVSNNENQIKELNYVNNHPRNVYLKLNA
FT SSRDDEDDEQMQKEQEQLELPKISAVIGGSKPKVEDNQVKESSEVISPSTSTFSMRSSA
FT GELTSTSAPLSSIVSVTAPPMPFGGVKYNQSSGLIDYEKRNQVVK (in isoform
FT K)"
FT /id="VSP_057904"
FT CONFLICT 21
FT /note="I -> T (in Ref. 1; CAA57962)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="D -> E (in Ref. 1; CAA57962)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 667 AA; 74966 MW; D707F491E4AE47F2 CRC64;
MYRISPIGRK SNFHSREKCL IGLVLVTLCF LCFGGIFLLP DNFGSDRVLR VYKHFRKAGP
EIFIPAPPLA AHAPHRSEDP HFIGDRQRLE QKIRAELGDM LDEPPAAGGG EPGQFQVLAQ
QAQAPAPVAA LADQPLDQDE GHAAIPVLAA PVQGDNAASQ ASSHPQSSAQ QHNQQQPQLP
LGGGGNDQAP DTLDATLEER RQKVKEMMEH AWHNYKLYAW GKNELRPLSQ RPHSASIFGS
YDLGATIVDG LDTLYIMGLE KEYREGRDWI ERKFSLDNIS AELSVFETNI RFVGGMLTLY
AFTGDPLYKE KAQHVADKLL PAFQTPTGIP YALVNTKTGV AKNYGWASGG SSILSEFGTL
HLEFAYLSDI TGNPLYRERV QTIRQVLKEI EKPKGLYPNF LNPKTGKWGQ LHMSLGALGD
SYYEYLLKAW LQSGQTDEEA REMFDEAMLA ILDKMVRTSP GGLTYVSDLK FDRLEHKMDH
LACFSGGLFA LGAATRQNDY TDKYMEVGKG ITNTCHESYI RAPTQLGPEA FRFSEAVEAR
ALRSQEKYYI LRPETFESYF VLWRLTHDQK YRDWGWEAVL ALEKHCRTAH GYCGLRNVYQ
QEPQKDDVQQ SFFLAETLKY LYLLFSDDSV LPLDEWVFNT EAHPLPIKGA NAYYRQAPVT
LPVSNAS
