ID   MANEA_PONAB             Reviewed;         462 AA.
AC   Q5RD93;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Glycoprotein endo-alpha-1,2-mannosidase;
DE            Short=Endo-alpha mannosidase;
DE            Short=Endomannosidase;
DE            EC=3.2.1.130 {ECO:0000250|UniProtKB:Q5SRI9};
GN   Name=MANEA;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-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   -!- PTM: Undergoes proteolytic cleavage in the C-terminal region.
CC       {ECO:0000250|UniProtKB:Q5SRI9}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 99 family. {ECO:0000305}.
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DR   EMBL; CR858023; CAH90264.1; -; mRNA.
DR   RefSeq; NP_001127260.1; NM_001133788.1.
DR   AlphaFoldDB; Q5RD93; -.
DR   SMR; Q5RD93; -.
DR   STRING; 9601.ENSPPYP00000018864; -.
DR   CAZy; GH99; Glycoside Hydrolase Family 99.
DR   GeneID; 100174316; -.
DR   KEGG; pon:100174316; -.
DR   CTD; 79694; -.
DR   eggNOG; ENOG502QPJV; Eukaryota.
DR   InParanoid; Q5RD93; -.
DR   OrthoDB; 975667at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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..462
FT                   /note="Glycoprotein endo-alpha-1,2-mannosidase"
FT                   /id="PRO_0000282317"
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..462
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          60..462
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   462 AA;  53537 MW;  8E9DDE909C6ADD7B CRC64;
     MAKFRRGTCI ILALFILFIF SLMMGLKMLR PNTATFGAPF GLDLLPELHQ RTVHLGKSFD
     FQKSDRINSE TNTKNLKSVE ITMKPSKASE LNLDELPPLN NYLHVFYYSW YGNPQFDGKY
     IHWNHPVLEH WDPRIAKNYP QGRHNPPDDI GSSFYPELGS YSSRDPSVIE THMRQMRSAS
     IGVLALSWYP PDVNDENGEP TDNLVPTILD KAHKYNLKVT FHIEPYSNRD DQNMYKNVKY
     IIDKYGNHPA FYRYKTKTGN ALPMFYVYDS YITKPEKWAN LLTTSGSWSI RNSPYDGLFI
     ALLVEEKHKY DILQSGFDGI YTYFATNGFT YGSSHQNWAS LKLFCDKYNL IFIPSVGPGY
     IDTSIRPWNT QNTRNRINGK YYEIALSAAL QTHPSLISIT SFNEWHEGTQ IEKAVPKRTS
     NTVYLDYRPH KPGLYLELTR KWSEKYSKER ATYALDHQLP VS