ID W5MVK3_LEPOC Unreviewed; 1020 AA.
AC W5MVK3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN Name=MAN2B2 {ECO:0000313|Ensembl:ENSLOCP00000012412.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000012412.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000012412.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361199};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU361199};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792, ECO:0000256|RuleBase:RU361199}.
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DR EMBL; AHAT01001229; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MVK3; -.
DR STRING; 7918.ENSLOCP00000012412; -.
DR Ensembl; ENSLOCT00000012433.1; ENSLOCP00000012412.1; ENSLOCG00000010140.1.
DR eggNOG; KOG1959; Eukaryota.
DR GeneTree; ENSGT01030000234638; -.
DR HOGENOM; CLU_004690_3_0_1; -.
DR InParanoid; W5MVK3; -.
DR OMA; LWMILGS; -.
DR Proteomes; UP000018468; Linkage group LG4.
DR Bgee; ENSLOCG00000010140; Expressed in intestine and 13 other cell types or tissues.
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; cd10811; GH38N_AMII_Epman_like; 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:SF28; EPIDIDYMIS-SPECIFIC ALPHA-MANNOSIDASE; 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 Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361199};
KW Hydrolase {ECO:0000256|RuleBase:RU361199};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361199};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Signal {ECO:0000256|RuleBase:RU361199};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT CHAIN 17..1020
FT /note="Alpha-mannosidase"
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT /id="PRO_5017854179"
FT DOMAIN 357..442
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1020 AA; 117826 MW; D16417726447636B CRC64;
MFLFCVSLFF LRIVSASENH GMEKIQTFVI PHSHMDVGWV YTIQESMHAY AANVYTSVTE
ELTKERHRKF IAVEQEFFRL WWDSVATEQH KKQLWQLLKE GRLEFIIGGQ VMHDEAVTDL
EDQILQLTAT EEGHGFLYET FGVRPQFSWH VDPFGASATT PVVFALAGFN AHLISRIDYD
LKDDMQKNKK LQFVWRGSPS LGEKQEIFTH IMDQFSYCTP SHIPFSDRSG FYWNGVALFP
DPPKDGVYPN MSLPVSNNNL HSYAETMVNN IKQRAAWFRT KHVLWPWGCD KQFFNSSVQF
KNMDPLLAYI NQHSEEFGVT VQYATLGEYF EAVHKANLSW DVRDSQDFLP YSTDPFQAWT
GFYASRNVLK GAARRASSLL FAAESLFTRY RIMFPDGPIP KEWALQQLRA LRWAVSEGEV
QHHDGITGTE SPKVADMYID HLAQGMMAVQ ELMAAVFLLP KGGGAPFTYS QETASKDFSQ
DPEQHIIVYN PLAWNTTTFI NVTVTFPVAR VYDEDGKPVP AQIQKSPESV SVYDLYILVN
LSGLQYKKYV IKFSTSPCRK DSESWPTCFG RVVKFDRQKV KSSKITGRRL LPVMNRCYMV
MIDLDTNLLQ SIRDRTSQKT VKLTQDFAEY YVNGDVQQGP ISDNYIFTAR GSAVPVFKAV
GMEIVPGKLV TEIRQYFYRE ETDKNYRYAM YTRLYSVPEE YEGDLVCHRI EQSYKIGPLE
VNREAILRTV TDLRNNKTIF TDNNGFQMLK RQHKMFVNNT VARNYYPMVR TAYIEDNSMR
LVFLSERSHG VSSQDHGQVE VMLHRRLWNN QKWNLGYNLT LNDTSIVQPV LWMILGSKSM
TSSLYQRNSV ALEHRPVVML IDTPRKAWTA SEPKEQTGLP VQPVTLPVNL HLLSLSVPGW
RYSSNHTRHW RDVLQGKTRK ADPDFDRVLL RIMHLYEEGE DPVLSQPVTV NLKEVLRSLG
PVSSVEERSL TATWNLSELR RWKWRTTPKN VEELKNPSVT EDFTVTISPK EIRTFFVHFN
//
