MA2B1_MACFA
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 03-AUG-2022, entry version 75.
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.XP_005588178.1; -.
DR CAZy; GH38; Glycoside Hydrolase Family 38.
DR PRIDE; Q60HE9; -.
DR GeneID; 102137710; -.
DR CTD; 4125; -.
DR eggNOG; KOG1959; Eukaryota.
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 Gene3D; 1.20.1270.50; -; 2.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.20.110.10; -; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR041147; GH38_C.
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 Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF17677; Glyco_hydro38C2; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 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 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
