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
//
