MA2B1_FELCA
ID MA2B1_FELCA Reviewed; 1007 AA.
AC O46432;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 106.
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; Synonyms=MANB;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND DISEASE.
RX PubMed=9396732; DOI=10.1042/bj3280863;
RA Berg T., Tollersrud O.-K., Walkley S.U., Siegel D., Nilssen O.;
RT "Purification of feline lysosomal alpha-mannosidase, determination of its
RT cDNA sequence and identification of a mutation causing alpha-mannosidosis
RT in Persian cats.";
RL Biochem. J. 328:863-870(1997).
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.
CC -!- PTM: Processed into 3 peptides of 72 kDa, 41 kDa and 12 kDa.
CC -!- DISEASE: Note=Defects in MAN2B1 are the cause of lysosomal alpha-
CC mannosidosis (AM). AM is a lysosomal storage disease characterized by
CC accumulation of unbranched oligosaccharide chains.
CC {ECO:0000269|PubMed:9396732}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
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DR EMBL; AF010191; AAB97672.1; -; mRNA.
DR EMBL; AF010192; AAB97733.1; -; Genomic_DNA.
DR PIR; T42219; T42219.
DR RefSeq; NP_001009222.1; NM_001009222.1.
DR AlphaFoldDB; O46432; -.
DR SMR; O46432; -.
DR STRING; 9685.ENSFCAP00000020308; -.
DR CAZy; GH38; Glycoside Hydrolase Family 38.
DR GeneID; 493697; -.
DR KEGG; fca:493697; -.
DR CTD; 4125; -.
DR eggNOG; KOG1959; Eukaryota.
DR InParanoid; O46432; -.
DR OrthoDB; 201312at2759; -.
DR Proteomes; UP000011712; Unplaced.
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 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..1007
FT /note="Lysosomal alpha-mannosidase"
FT /id="PRO_0000012068"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 448
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 643
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 649
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 690
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 764
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 927
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 56..360
FT /evidence="ECO:0000250"
FT DISULFID 269..274
FT /evidence="ECO:0000250"
FT DISULFID 414..474
FT /evidence="ECO:0000250"
FT DISULFID 495..503
FT /evidence="ECO:0000250"
SQ SEQUENCE 1007 AA; 113230 MW; C064A8168F5DC20A CRC64;
MGADARPLGV RAGGGGRGAA RPGTSSRALP PPLPPLSFLL LLLAAPGARA AGYETCPMVH
PDMLNVHLVA HTHDDVGWLK TVDQYFYGIH NDVQHAGVQY ILDSVISSLL VEPTRRFIYV
EIAFFSRWWH QQTNATQEVV RDLVRQGRLE FANGGWVMND EAATHYGAII DQMTLGLRFL
EDTFGKDGRP RVAWHIDPFG HSREQASLFA QMGFDGLFFG RLDYQDKRVR EENLGLEQVW
RASASLKPPA ADLFTSVLPN IYNPPEKLCW DTLCADKPFV EDRRSPEYNA EELVNYFLQL
ATAQGQHFRT NHTIMTMGSD FQYENANMWF RNLDRLIQLV NAQQQANGSR VNVLYSTPAC
YLWELNKANL TWSVKQDDFF PYADGPHQFW SGYFSSRPAL KRYERLSYNF LQVCNQLEAL
AGPAANVGPY GSGDSAPLNQ AMAVLQHHDA VSGTSKQHVA DDYARQLAAG WDPCEVLLSN
ALARLSGSKE DFTYCRNLNV SVCPLSQTAK NFQVTIYNPL GRKIDWMVRL PVSKHGFVVR
DPNGTVVPSD VVILPSSDGQ ELLFPASVPA LGFSIYSVSQ VPGQRPHAHK PQPRSQRPWS
RVLAIQNEHI RARFDPDTGL LVEMENLDQN LLLPVRQAFY WYNASVGNNL STQVSGAYIF
RPNQEKPLMV SHWAQTRLVK TPLVQEVHQN FSAWCSQVVR LYRGQRHLEL EWTVGPIPVG
DGWGKEIISR FDTVLETKGL FYTDSNGREI LERRRDYRPT WKLNQTETVA GNYYPVNSRI
YIRDGNMQLT VLTDRSQGGS SLRDGSMELM VHRRLLKDDG RGVGEALLED GLGRWVRGRH
LVLLDKVRTA ATGHRLQAEK EVLTPQVVLA PGGGAPYHLK VAPRKQFSGL RRELPPSVHL
LTLARWDQKT LLLRLEHQFA VGEDSGNLSS PVTLDLTDLF SAFTITYLQE TTLVANQLRA
SASRLKWTPN TGPTPLPSPS RLDPATITLQ PMEIRTFLAS VQWEEHG
