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Mannosyl-oligosaccharide alpha-1,2-mannosidase IA (EC 3.2.1.113) (Man(9)-alpha-mannosidase) (Mannosidase-1)

 MA1A1_DROME             Reviewed;         667 AA.
P53624; A4V480; M9PH54; P53625; Q9W2W6; Q9W2W7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
15-MAR-2004, sequence version 2.
12-SEP-2018, entry version 160.
RecName: Full=Mannosyl-oligosaccharide alpha-1,2-mannosidase IA {ECO:0000312|FlyBase:FBgn0259170};
EC=3.2.1.113 {ECO:0000250|UniProtKB:P32906};
AltName: Full=Man(9)-alpha-mannosidase;
AltName: Full=Mannosidase-1;
Name=alpha-Man-Ia {ECO:0000312|FlyBase:FBgn0259170};
Synonyms=alpha-man-1 {ECO:0000312|FlyBase:FBgn0259170},
mas-1 {ECO:0000312|FlyBase:FBgn0259170};
ORFNames=CG32684 {ECO:0000312|FlyBase:FBgn0259170};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS H AND K), TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
STRAIN=Berlin;
TISSUE=Head {ECO:0000303|PubMed:7729592}, and
Ovary {ECO:0000303|PubMed:7729592};
PubMed=7729592; DOI=10.1006/dbio.1995.1106;
Kerscher S., Albert S., Wucherpfennig D., Heisenberg M., Schneuwly S.;
"Molecular and genetic analysis of the Drosophila mas-1 (mannosidase-
1) gene which encodes a glycoprotein processing alpha 1,2-
mannosidase.";
Dev. Biol. 168:613-626(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W.,
Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
Celniker S.E.;
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Involved in the maturation of Asn-linked
oligosaccharides. Progressively trim alpha-1,2-linked mannose
residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).
{ECO:0000250|UniProtKB:Q2ULB2}.
-!- CATALYTIC ACTIVITY: Hydrolysis of the terminal (1->2)-linked
alpha-D-mannose residues in the oligo-mannose oligosaccharide
Man(9)(GlcNAc)(2). {ECO:0000250|UniProtKB:P32906}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000250|UniProtKB:Q2ULB2};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q2ULB2};
-!- PATHWAY: Protein modification; protein glycosylation.
{ECO:0000250|UniProtKB:Q2ULB2}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000250|UniProtKB:P39098}; Single-pass type II membrane
protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage; Named isoforms=2;
Name=H {ECO:0000312|FlyBase:FBgn0259170}; Synonyms=A
{ECO:0000303|PubMed:7729592}, J {ECO:0000312|FlyBase:FBgn0259170},
L {ECO:0000312|FlyBase:FBgn0259170}, M
{ECO:0000312|FlyBase:FBgn0259170}, N
{ECO:0000312|FlyBase:FBgn0259170}, O
{ECO:0000312|FlyBase:FBgn0259170};
IsoId=P53624-1; Sequence=Displayed;
Name=K {ECO:0000312|FlyBase:FBgn0259170}; Synonyms=B
{ECO:0000303|PubMed:7729592}, P {ECO:0000312|FlyBase:FBgn0259170};
IsoId=P53624-2, P53625-1;
Sequence=VSP_057904;
-!- TISSUE SPECIFICITY: Complex spatial distribution during
embryogenesis, including expression in lobula plate giant neurons.
Also expressed in adult wing and eyes.
{ECO:0000269|PubMed:7729592}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
during embryonic stages. {ECO:0000269|PubMed:7729592}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family.
{ECO:0000255|RuleBase:RU361193}.
-----------------------------------------------------------------------
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EMBL; X82640; CAA57962.1; -; mRNA.
EMBL; X82641; CAA57963.1; -; mRNA.
EMBL; AE014298; AAF46570.1; -; Genomic_DNA.
EMBL; AE014298; AAF46571.3; -; Genomic_DNA.
EMBL; AE014298; AAS65302.1; -; Genomic_DNA.
EMBL; AE014298; AAS65303.1; -; Genomic_DNA.
EMBL; AE014298; AAS65304.1; -; Genomic_DNA.
EMBL; AE014298; AAS65305.1; -; Genomic_DNA.
EMBL; AE014298; AAS65306.1; -; Genomic_DNA.
EMBL; AE014298; AGB95245.1; -; Genomic_DNA.
EMBL; BT011036; AAR30196.1; -; mRNA.
PIR; S60709; S60709.
RefSeq; NP_001259402.1; NM_001272473.2. [P53624-2]
RefSeq; NP_511105.2; NM_078550.4. [P53624-2]
RefSeq; NP_727407.1; NM_167223.3. [P53624-1]
RefSeq; NP_996395.1; NM_206672.3. [P53624-1]
RefSeq; NP_996396.1; NM_206673.3. [P53624-1]
RefSeq; NP_996397.1; NM_206674.3. [P53624-1]
RefSeq; NP_996398.1; NM_206675.3. [P53624-1]
RefSeq; NP_996399.1; NM_206676.3. [P53624-1]
UniGene; Dm.7316; -.
ProteinModelPortal; P53624; -.
SMR; P53624; -.
BioGrid; 58390; 2.
IntAct; P53624; 2.
BindingDB; P53624; -.
ChEMBL; CHEMBL1697673; -.
CAZy; GH47; Glycoside Hydrolase Family 47.
PRIDE; P53624; -.
EnsemblMetazoa; FBtr0299632; FBpp0288907; FBgn0259170. [P53624-1]
EnsemblMetazoa; FBtr0300511; FBpp0289738; FBgn0259170. [P53624-1]
EnsemblMetazoa; FBtr0300512; FBpp0289739; FBgn0259170. [P53624-2]
EnsemblMetazoa; FBtr0300513; FBpp0289740; FBgn0259170. [P53624-1]
EnsemblMetazoa; FBtr0300514; FBpp0289741; FBgn0259170. [P53624-1]
EnsemblMetazoa; FBtr0300515; FBpp0289742; FBgn0259170. [P53624-1]
EnsemblMetazoa; FBtr0300516; FBpp0289743; FBgn0259170. [P53624-1]
EnsemblMetazoa; FBtr0331759; FBpp0304147; FBgn0259170. [P53624-2]
GeneID; 31957; -.
KEGG; dme:Dmel_CG42275; -.
CTD; 31957; -.
FlyBase; FBgn0259170; alpha-Man-Ia.
GeneTree; ENSGT00390000016529; -.
InParanoid; P53624; -.
KO; K01230; -.
OMA; QYGWGHN; -.
OrthoDB; EOG091G04C8; -.
PhylomeDB; P53624; -.
Reactome; R-DME-964827; Progressive trimming of alpha-1,2-linked mannose residues from Man9/8/7GlcNAc2 to produce Man5GlcNAc2.
UniPathway; UPA00378; -.
ChiTaRS; alpha-Man-Ia; fly.
GenomeRNAi; 31957; -.
PRO; PR:P53624; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0259170; Expressed in 28 organ(s), highest expression level in embryo.
ExpressionAtlas; P53624; baseline and differential.
Genevisible; P53624; DM.
GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IDA:FlyBase.
GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
GO; GO:0035010; P:encapsulation of foreign target; IMP:FlyBase.
GO; GO:0006491; P:N-glycan processing; IBA:GO_Central.
GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
GO; GO:0072347; P:response to anesthetic; IMP:FlyBase.
Gene3D; 1.50.10.10; -; 1.
InterPro; IPR012341; 6hp_glycosidase-like_sf.
InterPro; IPR001382; Glyco_hydro_47.
InterPro; IPR036026; Seven-hairpin_glycosidases.
Pfam; PF01532; Glyco_hydro_47; 1.
PRINTS; PR00747; GLYHDRLASE47.
SUPFAM; SSF48225; SSF48225; 1.
2: Evidence at transcript level;
Alternative promoter usage; Calcium; Complete proteome;
Disulfide bond; Glycoprotein; Glycosidase; Golgi apparatus; Hydrolase;
Membrane; Metal-binding; Reference proteome; Signal-anchor;
Transmembrane; Transmembrane helix.
CHAIN 1 667 Mannosyl-oligosaccharide alpha-1,2-
mannosidase IA.
/FTId=PRO_0000210316.
TOPO_DOM 1 18 Cytoplasmic. {ECO:0000255}.
TRANSMEM 19 39 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 40 667 Lumenal. {ECO:0000255}.
ACT_SITE 529 529 Proton donor.
{ECO:0000250|UniProtKB:P31723}.
METAL 640 640 Calcium. {ECO:0000250|UniProtKB:P32906}.
CARBOHYD 278 278 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 483 515 {ECO:0000250|UniProtKB:P32906}.
VAR_SEQ 1 206 MYRISPIGRKSNFHSREKCLIGLVLVTLCFLCFGGIFLLPD
NFGSDRVLRVYKHFRKAGPEIFIPAPPLAAHAPHRSEDPHF
IGDRQRLEQKIRAELGDMLDEPPAAGGGEPGQFQVLAQQAQ
APAPVAALADQPLDQDEGHAAIPVLAAPVQGDNAASQASSH
PQSSAQQHNQQQPQLPLGGGGNDQAPDTLDATLEERRQKVK
E -> MCPKTSKTTPLLLIGGICFVIVLVGITGITLINNIN
LSNIIRLNEKVASDSVSNNENQIKELNYVNNHPRNVYLKLN
ASSRDDEDDEQMQKEQEQLELPKISAVIGGSKPKVEDNQVK
ESSEVISPSTSTFSMRSSAGELTSTSAPLSSIVSVTAPPMP
FGGVKYNQSSGLIDYEKRNQVVK (in isoform K).
/FTId=VSP_057904.
CONFLICT 21 21 I -> T (in Ref. 1; CAA57962).
{ECO:0000305}.
CONFLICT 568 568 D -> E (in Ref. 1; CAA57962).
{ECO:0000305}.
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


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