MANE_DICDI
ID MANE_DICDI Reviewed; 1123 AA.
AC Q1ZXI8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Alpha-mannosidase E;
DE EC=3.2.1.24;
DE Flags: Precursor;
GN Name=manE; ORFNames=DDB_G0278651;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-mannose residues
CC in alpha-D-mannosides.; EC=3.2.1.24;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
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DR EMBL; AAFI02000023; EAS66899.1; -; Genomic_DNA.
DR RefSeq; XP_001134583.1; XM_001134583.1.
DR AlphaFoldDB; Q1ZXI8; -.
DR SMR; Q1ZXI8; -.
DR STRING; 44689.DDB0231615; -.
DR PaxDb; Q1ZXI8; -.
DR EnsemblProtists; EAS66899; EAS66899; DDB_G0278651.
DR GeneID; 8621484; -.
DR KEGG; ddi:DDB_G0278651; -.
DR dictyBase; DDB_G0278651; manE.
DR eggNOG; KOG1958; Eukaryota.
DR HOGENOM; CLU_268576_0_0_1; -.
DR InParanoid; Q1ZXI8; -.
DR OMA; GEMEIMQ; -.
DR PhylomeDB; Q1ZXI8; -.
DR Reactome; R-DDI-8853383; Lysosomal oligosaccharide catabolism.
DR PRO; PR:Q1ZXI8; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0004559; F:alpha-mannosidase activity; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR Gene3D; 1.20.1270.50; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.20.110.10; -; 2.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR015341; Glyco_hydro_38_cen.
DR InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR InterPro; IPR000602; Glyco_hydro_38_N.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR InterPro; IPR013780; Glyco_hydro_b.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF01074; Glyco_hydro_38N; 2.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR SUPFAM; SSF88688; SSF88688; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Glycosidase; Hydrolase; Membrane; Metal-binding;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Zinc.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1123
FT /note="Alpha-mannosidase E"
FT /id="PRO_0000327844"
FT TOPO_DOM 22..1072
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1073..1093
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1094..1123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 150
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 675
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 858
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 887
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 975
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 990
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1123 AA; 129935 MW; 7EAB06BD0CC3966C CRC64;
MNKTKLIKII FVIGVWILLS TFIINIYNEN FEIVNYNNNS QSLKKIFQLN GDLKDEKLSI
FLIPHSHCDS GWLQDYDWYY NHVVQYILSG IVNELNLDKE KKFNWVEIGG WVQNDEATAT
IDDVITQMTQ GHQWLKDTLN YTIEYAWQID PFGYSSSTPT IFSSMGIKGL IINRVSDDVK
SYMKSAKEME FIWKGSESLG EQSQMLVSTL NVHYDYPKHI DPKKDFSLEE RVKGFTKYIK
DLSNTRESSI LMIPLGDDFR YSNAKNEFSV SKEWLKVIQD NKEKYNIKEI KYATIDEYFI
ALEDEFMNKL GKTVEENLKT GFSSTLSLYN KDFFPYSTGD LEYWTGYYTT RPLLKRLIRE
SSLLQKSSDI LYTLAIGENS NNQIDINNLQ TLSNQLNENR NTIALVQHHD IVTGTSRSFV
LNDNFQRLQK SRISNYNIIS NSLEYLLNKD NNNNENTDST NEPFNFENVI DLSNEINNQY
SLVFHNTLGW EVNQHVSFRI KVNKNDNQLL ESIQLVEAIS NKTIQIQIIP IQDDSNCQSI
ENNYIVFAII NLPPLGLNTY YLSISSNEDS KPNTILSKPK LLKKGNEINF NNNRFKVEFE
SNGLISKITD KNSNEIKTIE QTFHQYSTKK SGPYIFNVKG GKKHGFLENP DKFIYHDGPL
VSQLTMLYGV DDGCNVTSIV VQRIYKNNEI DNSNSKSLIT ENYIETGYSI NGDMNRETTI
NYKVKDLEND DIFYTDNGLE SRKRIYNHDR TVNQNYYPVL GYIKLKETSE NNNHQYTVYV
DRSVGATSPS DGEMEIMIHR TMDTDDWKGV NWPSKDIGRS DAKLYFNMDL VNNQLQNEKR
ISLHITNQPI MFVKKHNNQT GYLLKYSPLS NQLPSNIHLQ SLLTLKNNTV GLRLFNIHEV
DSNTQSTTDT DKSTLFNELE ISNFIETGLS FLKLTKNNLI DKYSTRINKK FPVKCGESEY
SFINEKPSSI IFSNNGTNNI IDGENKGENN KTIETIQIKP HEIKSFTFNF NFQLDQIIPN
NNNYAINKEL NNEYIEQSIE NQRYEYDFSF FPIKPTFYDD RGKYNRPNHL ALILSLSIGT
PAGILIIVIA LVVIYKKRKN RKTLTSSYSL LNLILKDRAD SSP
