ID   MANF_DICDI              Reviewed;         994 AA.
AC   Q54KN4;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Alpha-mannosidase F;
DE            EC=3.2.1.24;
DE   Flags: Precursor;
GN   Name=manF; ORFNames=DDB_G0287231;
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: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
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DR   EMBL; AAFI02000099; EAL63817.1; -; Genomic_DNA.
DR   RefSeq; XP_637323.1; XM_632231.1.
DR   AlphaFoldDB; Q54KN4; -.
DR   SMR; Q54KN4; -.
DR   GlyCosmos; Q54KN4; 5 sites, No reported glycans.
DR   PaxDb; 44689-DDB0231616; -.
DR   EnsemblProtists; EAL63817; EAL63817; DDB_G0287231.
DR   GeneID; 8626020; -.
DR   KEGG; ddi:DDB_G0287231; -.
DR   dictyBase; DDB_G0287231; manF.
DR   eggNOG; KOG1958; Eukaryota.
DR   HOGENOM; CLU_004690_2_0_1; -.
DR   InParanoid; Q54KN4; -.
DR   OMA; WHNENKV; -.
DR   PhylomeDB; Q54KN4; -.
DR   Reactome; R-DDI-8853383; Lysosomal oligosaccharide catabolism.
DR   PRO; PR:Q54KN4; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   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   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   PANTHER; PTHR11607; ALPHA-MANNOSIDASE; 1.
DR   PANTHER; PTHR11607:SF68; ALPHA-MANNOSIDASE F; 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; Metal-binding; Reference proteome;
KW   Secreted; Signal; Zinc.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..994
FT                   /note="Alpha-mannosidase F"
FT                   /id="PRO_0000327845"
FT   ACT_SITE        151
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         35
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         37
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         392
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        247
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        381
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        554
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        712
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        932
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   994 AA;  114357 MW;  CB2E2F98BFF05CCB CRC64;
     MKNFYYFILI LLFFNEVCYS LKDGEIKLHL IPHSHCDSGW TSTMNEYYMG QVKSIISSMV
     QSLNVESNPP RKFVWSEIGF LEQWWDDMPI EIKNDFIKHV KNDRIEFVNG GWVMNDEACA
     SLESVIRQLS NGHKFIREKF GKQPESGWQI DPFGHSSLTP TLQAQFGYKH VVLNRIHYEL
     KKKFKEEKNL QFKWRGSPEG VGPKSDILAH VFDDFYTSPP HMSFDGYNFL AYGLPRLTME
     MIELARNRSV FYKSPHVLIP MGGDFAFKNA YKSFEQMDQL VASINGQHAN GESNVICQYS
     TLADFFSDTI NWHNENKVSF NYYDSDFFPY ADDSNTYWTG YYTSRPLLKG YERHVSSKLR
     SAEILSALQN DEKYYPNQLL NASKQVSILQ HHDAISGTSK KHVVQDYFSR LQKADILVSE
     QSEKLLASAL SQHSPTKLDI IDIGGSLNFP KNNDAISFIL FNQLSWSKEE LISIKVQSVG
     DHGESLNSPT NNACPYVLAQ EDFLNEIEID CSPRSDFKSD QSDDHKEFIQ IDFPAKLKPF
     SSKLYYLKRK SNPNKSNWVL PKTNHFNSIE NSIYTANLDE NYLIKSLKSK SSRHGGGANQ
     ITEINQQLLT YSDIGGAYIF RTNKQVFQPP RQVYSTFTYI GKFYQEAQSI LQDTHQISNR
     NGYYYYYGNN QQQQQQQQTI STFNYNSIKL INTGNEMIDK KINFNFHIRG INGTTTINRF
     TTDIDNNREL YSDNGLEMMH RKSISSQSVE VGRETQSYYP TINSVYIESQ STGKRFVCNN
     DRSRGVSSQG QGCLEMALHR SLTYEDGKGL EIPAIDESSI NARFECYLDE VPSNSQQSNG
     GGGGDDIRKQ SINYQHKFQI YQGQDSSYMS SKSFMLKPLP EFIHILSMER SGPRSIKLRI
     HNIENNNQSP ITFDLNGLFS FIKSIKSIKE YNLSLINRFV DNNIDNIISS HRSIVGKNLF
     PIKDTPTRFN PINTKQTKIT LYPSEIKAIE ITYH
//