ID   MA2B1_MACFA             Reviewed;        1012 AA.
AC   Q60HE9;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Lysosomal alpha-mannosidase;
DE            Short=Laman;
DE            EC=3.2.1.24;
DE   AltName: Full=Lysosomal acid alpha-mannosidase;
DE   AltName: Full=Mannosidase alpha class 2B member 1;
DE   AltName: Full=Mannosidase alpha-B;
DE   Flags: Precursor;
GN   Name=MAN2B1; ORFNames=QmoA-10471;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Medulla oblongata;
RA   Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
RT   "Isolation and characterization of cDNA for macaque neurological disease
RT   genes.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Necessary for the catabolism of N-linked carbohydrates
CC       released during glycoprotein turnover. {ECO:0000250}.
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: Lysosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
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DR   EMBL; AB125178; BAD51966.1; -; mRNA.
DR   RefSeq; NP_001306452.1; NM_001319523.1.
DR   AlphaFoldDB; Q60HE9; -.
DR   SMR; Q60HE9; -.
DR   STRING; 9541.ENSMFAP00000022654; -.
DR   CAZy; GH38; Glycoside Hydrolase Family 38.
DR   GlyCosmos; Q60HE9; 9 sites, No reported glycans.
DR   eggNOG; KOG1959; Eukaryota.
DR   OrthoDB; 5474711at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IEA:UniProtKB-EC.
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; cd10810; GH38N_AMII_LAM_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; 2.
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   InterPro; IPR048534; Man2a1-like_dom.
DR   PANTHER; PTHR11607; ALPHA-MANNOSIDASE; 1.
DR   PANTHER; PTHR11607:SF3; LYSOSOMAL 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   Pfam; PF21260; Laman-like_dom; 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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Lysosome;
KW   Metal-binding; Reference proteome; Signal; Zinc.
FT   SIGNAL          1..50
FT                   /evidence="ECO:0000250"
FT   CHAIN           51..1012
FT                   /note="Lysosomal alpha-mannosidase"
FT                   /id="PRO_0000012075"
FT   ACT_SITE        197
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         447
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        368
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        498
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        646
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        652
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        693
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        767
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        833
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        931
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        990
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        56..359
FT                   /evidence="ECO:0000250"
FT   DISULFID        269..274
FT                   /evidence="ECO:0000250"
FT   DISULFID        413..473
FT                   /evidence="ECO:0000250"
FT   DISULFID        494..502
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1012 AA;  113922 MW;  87FA3277FFBF1326 CRC64;
     MGAYAPAAGV SARGCLDAAG PWTISRALRP PLPPLCFFLL LLLAAPCARA GGYETCPTVQ
     PNILNVHLVP HTHDDVGWLK TVDQYFYGIK NDIQHAGVQY ILDSVISALL ADPTRRFIYV
     EIAFFSRWWH QQTNAMREVV RDLVRQGRLE FANGGWVMND EAATHYGAIV DQMTLGLRFL
     EDTFGSDGRP RVAWHIDPFG HSREQASLFA QMGFDGFFFG RLDYQDKRVR MQKLEMEQVW
     RASASLKPPT ADLFTGVLPN GYNPPMNLCW DVLCVDQPVV EDPRSPEYNA KELVDYFLNV
     ATAQGRHYRT NHIVMTMGSD FQYENANMWF KNLDKLIRLV NAQQAKGSSV HVLYSTPACY
     LWELNKANLT WSVKHDDFFP YADGPHQFWT GYFSSRPALK RYERLSYNFL QVCNQLEALV
     GLAANVGPYG SGDSAPLNKA MAVLQHHDAV SGTSRQHVAD DYARQLAAGW VSCEVLLSNA
     LARLRGFKDH LTFCRQLNIS ICPLSQTAAR FQVIVYNPLG RKVNWMVRLP VSEGVFVVKD
     PNGRTVPSDV VIYPSSDSQA HPPELLFSAS LPALGFSTYS VAQVPRWKPQ ARAPQPIPRR
     SWSPALTIEN EHIRATFDPD TGLLMEIMNM NQRLLLPVRQ TFFWYNASIG DNESDQASGA
     YIFRPNQQKP LPVSRWAQIR LVKTPLVQEV HQNFSAWCSQ VVRLYPGRRH LELEWSVGPI
     PVGDTWGKEV ISRFDTPLET KGRFYTDSNG REILERRRDY RPTWKLNQTE PVAGNYYPVN
     TRIYITDGKM QLTVLTDRSQ GGSSLRDGSL ELMVHRRLLK DDERGVSEPL MENGSGAWVR
     GRHLVLLDTA QAAAAGHRLL AEQEVLAPQV VLAPGGGAAY NLGAPPRTQF SGLRRELPPS
     VHLLTLASWG PEMLLLRLEH QFAVGEDSGR NLSAPVTLNL RDLFSTFTIT RLQETTLVAN
     QLREAASRLK WTTNTGPTPH QTPYQLDPAN ITLEPMEIRT FLASVQWKEV DG
//