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MANEA_XENLA
ID   MANEA_XENLA             Reviewed;         449 AA.
AC   Q6DE40;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Glycoprotein endo-alpha-1,2-mannosidase;
DE            EC=3.2.1.130 {ECO:0000250|UniProtKB:Q5SRI9};
GN   Name=manea;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-{alpha-Glc-(1->3)-alpha-Man-(1->2)-alpha-Man-(1->2)-
CC         alpha-Man-(1->3)-[alpha-Man-(1->2)-alpha-Man-(1->3)-[alpha-Man-
CC         (1->2)-alpha-Man-(1->6)]-alpha-Man-(1->6)]-beta-Man-(1->4)-beta-
CC         GlcNAc-(1->4)-beta-GlcNAc}-L-asparaginyl-[protein] = alpha-D-
CC         glucosyl-(1->3)-D-mannopyranose + N(4)-{alpha-D-Man-(1->2)-alpha-D-
CC         Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC         (1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC         beta-D-GlaNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] (N-glucan
CC         mannose isomer 8A1,2,3B1,2); Xref=Rhea:RHEA:54824, Rhea:RHEA-
CC         COMP:14010, Rhea:RHEA-COMP:14011, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:52996, ChEBI:CHEBI:59080, ChEBI:CHEBI:60627;
CC         EC=3.2.1.130; Evidence={ECO:0000250|UniProtKB:Q5SRI9};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q5SRI9}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:Q5SRI9}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 99 family. {ECO:0000305}.
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DR   EMBL; BC077304; AAH77304.1; -; mRNA.
DR   RefSeq; NP_001086682.1; NM_001093213.1.
DR   AlphaFoldDB; Q6DE40; -.
DR   SMR; Q6DE40; -.
DR   CAZy; GH99; Glycoside Hydrolase Family 99.
DR   DNASU; 446517; -.
DR   GeneID; 446517; -.
DR   KEGG; xla:446517; -.
DR   CTD; 446517; -.
DR   Xenbase; XB-GENE-985847; manea.L.
DR   OrthoDB; 975667at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 446517; Expressed in blastula and 19 other tissues.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004569; F:glycoprotein endo-alpha-1,2-mannosidase activity; IEA:UniProtKB-EC.
DR   CDD; cd11574; GH99; 1.
DR   InterPro; IPR026071; Glyco_Hydrolase_99.
DR   PANTHER; PTHR13572; PTHR13572; 1.
DR   Pfam; PF16317; Glyco_hydro_99; 1.
PE   2: Evidence at transcript level;
KW   Golgi apparatus; Hydrolase; Membrane; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..449
FT                   /note="Glycoprotein endo-alpha-1,2-mannosidase"
FT                   /id="PRO_0000282319"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..29
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..449
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          59..449
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   449 AA;  51862 MW;  1DBC0E54818AF9E4 CRC64;
     MIRFRRRTCI TLSIFIFLVC LIMAGLKHLR PENAAFGSPF GLGLFPGFHR ASVLEKIPDS
     ENHLKGNTVT ETNTLPAPKD KVYQLDMEEF PPPNYDLHIF YYTWYGNPQF DGKYIHWNHP
     LLKHWDAKIA NSFPLGKHNP PDDVGANFYP ELGPYSSRDP SVIDAHMKQI RSSSVGVISV
     SWYPPGISDD NGEPTDDFIP SILDKAHSYG LKVNFHIEPY RNRDDYSLRN NVVYIIDKYG
     SHPAFYKYKT DNGRTLPMFY IYDSYITTPG TWANLLTSSG SQSIRNTPYD GIFMALLVEE
     KHKHDILRGG FDGFYTYFAT NGFSYGSSHQ HWSSLKEFCN TNNLLFIPSV GPGYIDTSIR
     PWNFQNTRNR INGKYYETAI NAALLVRPKI ISITSFNEWH EGTQIEAAIP KKTAQMKYED
     YLPHKPNIYL ELTRKWSEKY MKEKEHWLV
 
 
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