MANEA_RAT
ID MANEA_RAT Reviewed; 462 AA.
AC Q5GF25; O35390;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Glycoprotein endo-alpha-1,2-mannosidase;
DE Short=Endo-alpha mannosidase;
DE Short=Endomannosidase;
DE Short=rEndo;
DE EC=3.2.1.130 {ECO:0000269|PubMed:15677381};
DE AltName: Full=Endo-alpha-D-mannosidase;
DE Short=Enman;
GN Name=Manea;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 245-253; 277-291 AND
RP 381-400, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=9361017; DOI=10.1074/jbc.272.46.29356;
RA Spiro M.J., Bhoyroo V.D., Spiro R.G.;
RT "Molecular cloning and expression of rat liver endo-alpha-mannosidase, an
RT N-linked oligosaccharide processing enzyme.";
RL J. Biol. Chem. 272:29356-29363(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, PTM, SUBCELLULAR LOCATION,
RP AND TOPOLOGY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=15677381; DOI=10.1093/glycob/cwi045;
RA Hamilton S.R., Li H., Wischnewski H., Prasad A., Kerley-Hamilton J.S.,
RA Mitchell T., Walling A.J., Davidson R.C., Wildt S., Gerngross T.U.;
RT "Intact alpha-1,2-endomannosidase is a typical type II membrane protein.";
RL Glycobiology 15:615-624(2005).
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:0000269|PubMed:15677381};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:15677381}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:15677381}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the liver and kidney.
CC {ECO:0000269|PubMed:9361017}.
CC -!- PTM: Undergoes proteolytic cleavage in the C-terminal region.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 99 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB86925.1; Type=Miscellaneous discrepancy; Note=Cloning artifact. The sequence differs from that shown at the N-terminus (1-54).; Evidence={ECO:0000305};
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DR EMBL; AF023657; AAB86925.1; ALT_SEQ; mRNA.
DR EMBL; AY599499; AAT44962.1; -; mRNA.
DR RefSeq; NP_542963.2; NM_080785.2.
DR RefSeq; XP_006238022.1; XM_006237960.2.
DR RefSeq; XP_006238023.1; XM_006237961.2.
DR AlphaFoldDB; Q5GF25; -.
DR SMR; Q5GF25; -.
DR STRING; 10116.ENSRNOP00000011576; -.
DR CAZy; GH99; Glycoside Hydrolase Family 99.
DR PaxDb; Q5GF25; -.
DR PRIDE; Q5GF25; -.
DR Ensembl; ENSRNOT00000011576; ENSRNOP00000011576; ENSRNOG00000008626.
DR GeneID; 140808; -.
DR KEGG; rno:140808; -.
DR UCSC; RGD:620327; rat.
DR CTD; 79694; -.
DR RGD; 620327; Manea.
DR eggNOG; ENOG502QPJV; Eukaryota.
DR GeneTree; ENSGT00390000016054; -.
DR HOGENOM; CLU_042710_1_1_1; -.
DR InParanoid; Q5GF25; -.
DR OMA; ASYNNWP; -.
DR OrthoDB; 975667at2759; -.
DR PhylomeDB; Q5GF25; -.
DR TreeFam; TF324051; -.
DR BRENDA; 3.2.1.130; 5301.
DR Reactome; R-RNO-964739; N-glycan trimming and elongation in the cis-Golgi.
DR PRO; PR:Q5GF25; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000008626; Expressed in duodenum and 20 other tissues.
DR Genevisible; Q5GF25; RN.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004559; F:alpha-mannosidase activity; IDA:RGD.
DR GO; GO:0004569; F:glycoprotein endo-alpha-1,2-mannosidase activity; ISO:RGD.
DR CDD; cd11574; GH99; 1.
DR InterPro; IPR026071; Glyco_Hydrolase_99.
DR PANTHER; PTHR13572; PTHR13572; 1.
DR Pfam; PF16317; Glyco_hydro_99; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Golgi apparatus; Hydrolase; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..462
FT /note="Glycoprotein endo-alpha-1,2-mannosidase"
FT /id="PRO_0000282318"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..462
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 60..462
FT /note="Catalytic"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 53416 MW; 0D8F1C3EB29C0785 CRC64;
MAKFRRRTCI ILSLFIVFIF SLMMGLKMLW PNAASFGPPF GLDLLPELRP PNTHLENKAD
FQRSDRIDME TNTKDLKGAG VTVHPPRASE VNLEELPPLN YFVHAFYYSW YGNPQFDGKY
VHWNHPVLEH WDPRIAKNYP QGRHSPPDDI GSSFYPELGS YSSRDPSVIE THMKQMRSAS
IGVLALSWYP PDASDENGEA TDYLVPTILD KAHKYNLKVT FHIEPYSNRD DQNMHQNVKY
IIDKYGNHPA FYRYKTRMGH SLPMFYIYDS YITKPKTWAN LLTPSGSQSV RGSPYDGLFI
ALLVEEKHKY DILQSGFDGI YTYFATNGFT YGSSHQNWNK LKSFCEKNNM IFIPSVGPGY
IDTSIRPWNT QNTRNRINGK YYEVGLSAAL QTQPSLISIT SFNEWHEGTQ IEKAVPKRTA
NTVYLDYRPH KPSLYLEITR KWSEKYSKER MTYALDQQLP AS
