MAND_DICDI
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 03-AUG-2022, entry version 109.
DE RecName: Full=Alpha-mannosidase D;
DE EC=3.2.1.24;
DE Flags: Precursor;
GN Name=manD; ORFNames=DDB_G0278653;
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; EAL68499.1; -; Genomic_DNA.
DR RefSeq; XP_642278.1; XM_637186.1.
DR AlphaFoldDB; Q54YC4; -.
DR SMR; Q54YC4; -.
DR STRING; 44689.DDB0231614; -.
DR PaxDb; Q54YC4; -.
DR PRIDE; Q54YC4; -.
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; HRQGYDC; -.
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: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; -; 1.
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; 1.
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..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
