ID   MAND_DICDI              Reviewed;        1222 AA.
AC   Q54YC4;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Alpha-mannosidase D;
DE            EC=3.2.1.24;
DE   Flags: Precursor;
GN   Name=manD; ORFNames=DDB_G0278653;
OS   Dictyostelium discoideum (Social amoeba).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAFI02000023; EAL68499.1; -; Genomic_DNA.
DR   RefSeq; XP_642278.1; XM_637186.1.
DR   AlphaFoldDB; Q54YC4; -.
DR   SMR; Q54YC4; -.
DR   STRING; 44689.Q54YC4; -.
DR   GlyCosmos; Q54YC4; 14 sites, No reported glycans.
DR   PaxDb; 44689-DDB0231614; -.
DR   EnsemblProtists; EAL68499; EAL68499; DDB_G0278653.
DR   GeneID; 8621485; -.
DR   KEGG; ddi:DDB_G0278653; -.
DR   dictyBase; DDB_G0278653; manD.
DR   eggNOG; KOG1958; Eukaryota.
DR   HOGENOM; CLU_268576_0_0_1; -.
DR   InParanoid; Q54YC4; -.
DR   OMA; GPHPSIC; -.
DR   PhylomeDB; Q54YC4; -.
DR   Reactome; R-DDI-8853383; Lysosomal oligosaccharide catabolism.
DR   PRO; PR:Q54YC4; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   CDD; cd00451; GH38N_AMII_euk; 1.
DR   Gene3D; 2.60.40.1360; -; 1.
DR   Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR   Gene3D; 1.20.1270.50; Glycoside hydrolase family 38, central domain; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR011682; Glyco_hydro_38_C.
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   PANTHER; PTHR11607; ALPHA-MANNOSIDASE; 1.
DR   PANTHER; PTHR11607:SF39; ALPHA-MANNOSIDASE D-RELATED; 1.
DR   Pfam; PF09261; Alpha-mann_mid; 1.
DR   Pfam; PF07748; Glyco_hydro_38C; 1.
DR   Pfam; PF01074; Glyco_hydro_38N; 1.
DR   SMART; SM00872; Alpha-mann_mid; 1.
DR   SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 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..1222
FT                   /note="Alpha-mannosidase D"
FT                   /id="PRO_0000327843"
FT   TOPO_DOM        22..1170
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1171..1191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1192..1222
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          493..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1202..1222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        185
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         185
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         453
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        175
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        492
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        496
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        547
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        551
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        566
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        613
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        665
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        768
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        785
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        952
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        981
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1069
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1084
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1222 AA;  141190 MW;  FDA5A919C2C65880 CRC64;
     MESSKFVKII WVFGIWILVF TFLIIYNNYD YKSTFGINKF EKRSLKTINQ INNKENGDDK
     KLSVFLIPHS HCDGGWLQDY DGYYYNIVQY ILSGVVNELN LDKEKKFNWV EIGFFSRWWN
     DQNEIQKEIV RNLINNKQLS FISGGWVQND EATATIDDVI TQMTQGHQWL KDTLNYTVEY
     AWQIDPFGYS SSTPTIFSSM GIKGLVINRV SNDVKSYMKS VKEMEFIWKG SESLGEQSQM
     LVSTLNIHYD YPKHIDPKKD FSLNDRIKGF TKYLNDLSKT RESNILMIPL GDDFRYSNAK
     TEFSVSKEWV KALQDNKEYY NIKEIKYATL DEYFIALEDS FLRNNKFGKS RKQNVYTETF
     SDGDDEVSAL SLYNKDFFPY STGNLEYWTG YYTTRPLLKR LIRESSLLQK SSDILYTLAI
     GENSNNQIDI NNLQTLSNQL NENRNTIALV QHHDIVTGTS RSFVLNDNFQ RLQKSRISNY
     NIISNSLEYL LNKSNNKTNN NNNNNNKNNN NNNNNNNNNN NNLKNTNSIS TTGSSSSSGS
     GSSNNNNNTV NKSEPFNFEN AIDLSNESNN QYSLVFHNTL GWEVNQHVSF RIKVNKNDNQ
     LLESIQLVEA ISNKTIQIQI IPIQDDSNCQ SIENNYIVFA IINLPPLGLN TYYLSIANSE
     DSKSNFTYLS KPKLLKKGNE INFNNNRFKV EFESNGLISK ITDKNSNEIK TIEQTFHQYS
     TKKSGPYIFN VKGGKKHGFL ENPDKFIYHD GPLVSQLTML YGVDDYCNVT SIVVQRIYKN
     NNEINNSNSK SLITENYIET GYSINGDMNR ETTINYKVKD LENDDIFYTD NGLESRKRIY
     NHDRSVNQNY YPVLGYIKLK ETSENNNHQY TVYVDRSVGA TSPSDGEMEI MIHRTMDTDD
     WKGVNWPSKD IGRSDAKLYF NMDLVNNQLQ NEKRISLHIT NQPIMFVKKH NNQTGYLLKY
     SPLSNQLPSN IHLQSLLTLK NNTVGLRLFN IHEVDSNTQS TTDTDKSTLF NELEISNFIE
     TGLSFLKLTK NNLIDKFSTR INKKFPIKCG ESEYSFINEK PSSIIFSNNG TNNIIDGENK
     GENNKTIETI QIKPHEIKSF TFNFNFQLDQ IIPNNNNNNN KYAINKELNN EYIEQSIENQ
     RYEYDFSFFP IKPTFYDDRG KYNRPNHLAL ILSLSIGIPA GILIIVIALV VTYKKRKNRK
     TLTSSNSSSN LIQQEDQTDY SP
//