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   24-JAN-2024, entry version 185.
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}, mas-1
GN   {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 Ovary
RC   {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)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan
CC         mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-(alpha-D-Man-
CC         (1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-
CC         beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-
CC         [protein] (N-glucan mannose isomer 5A1,2); Xref=Rhea:RHEA:56008,
CC         Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:139493;
CC         EC=3.2.1.113; 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         beta-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; 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   GlyCosmos; P53624; 1 site, No reported glycans.
DR   GlyGen; P53624; 1 site.
DR   PaxDb; 7227-FBpp0288908; -.
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   AGR; FB:FBgn0259170; -.
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; PESFGWD; -.
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 cell types or tissues.
DR   ExpressionAtlas; P53624; baseline and differential.
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: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: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   PANTHER; PTHR11742:SF6; MANNOSYL-OLIGOSACCHARIDE ALPHA-1,2-MANNOSIDASE IA-RELATED; 1.
DR   PANTHER; PTHR11742; MANNOSYL-OLIGOSACCHARIDE ALPHA-1,2-MANNOSIDASE-RELATED; 1.
DR   Pfam; PF01532; Glyco_hydro_47; 1.
DR   PRINTS; PR00747; GLYHDRLASE47.
DR   SUPFAM; SSF48225; Seven-hairpin glycosidases; 1.
DR   Genevisible; P53624; DM.
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
//