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MANEA_MOUSE
ID   MANEA_MOUSE             Reviewed;         462 AA.
AC   Q6NXH2; Q8C0N9;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Glycoprotein endo-alpha-1,2-mannosidase;
DE            Short=Endo-alpha mannosidase;
DE            Short=Endomannosidase;
DE            Short=mEndo;
DE            EC=3.2.1.130 {ECO:0000250|UniProtKB:Q5GF25};
GN   Name=Manea;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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:Q5GF25};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q5GF25}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:Q5GF25}.
CC   -!- PTM: Undergoes proteolytic cleavage in the C-terminal region.
CC       {ECO:0000250|UniProtKB:Q5GF25}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 99 family. {ECO:0000305}.
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DR   EMBL; AK030141; BAC26805.1; -; mRNA.
DR   EMBL; AL805949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC067076; AAH67076.1; -; mRNA.
DR   CCDS; CCDS18012.1; -.
DR   RefSeq; NP_766453.2; NM_172865.2.
DR   RefSeq; XP_006537962.1; XM_006537899.3.
DR   AlphaFoldDB; Q6NXH2; -.
DR   SMR; Q6NXH2; -.
DR   STRING; 10090.ENSMUSP00000038671; -.
DR   CAZy; GH99; Glycoside Hydrolase Family 99.
DR   PhosphoSitePlus; Q6NXH2; -.
DR   EPD; Q6NXH2; -.
DR   MaxQB; Q6NXH2; -.
DR   PaxDb; Q6NXH2; -.
DR   PeptideAtlas; Q6NXH2; -.
DR   PRIDE; Q6NXH2; -.
DR   ProteomicsDB; 295777; -.
DR   Antibodypedia; 2637; 60 antibodies from 19 providers.
DR   Ensembl; ENSMUST00000041374; ENSMUSP00000038671; ENSMUSG00000040520.
DR   GeneID; 242362; -.
DR   KEGG; mmu:242362; -.
DR   UCSC; uc008sej.1; mouse.
DR   CTD; 79694; -.
DR   MGI; MGI:2444484; Manea.
DR   VEuPathDB; HostDB:ENSMUSG00000040520; -.
DR   eggNOG; ENOG502QPJV; Eukaryota.
DR   GeneTree; ENSGT00390000016054; -.
DR   HOGENOM; CLU_042710_1_1_1; -.
DR   InParanoid; Q6NXH2; -.
DR   OMA; ASYNNWP; -.
DR   OrthoDB; 975667at2759; -.
DR   PhylomeDB; Q6NXH2; -.
DR   TreeFam; TF324051; -.
DR   Reactome; R-MMU-964739; N-glycan trimming and elongation in the cis-Golgi.
DR   BioGRID-ORCS; 242362; 2 hits in 73 CRISPR screens.
DR   ChiTaRS; Manea; mouse.
DR   PRO; PR:Q6NXH2; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q6NXH2; protein.
DR   Bgee; ENSMUSG00000040520; Expressed in olfactory epithelium and 216 other tissues.
DR   ExpressionAtlas; Q6NXH2; baseline and differential.
DR   Genevisible; Q6NXH2; MM.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004559; F:alpha-mannosidase activity; ISO:MGI.
DR   GO; GO:0004569; F:glycoprotein endo-alpha-1,2-mannosidase activity; ISO:MGI.
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_0000282316"
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:0000250"
FT   CONFLICT        294
FT                   /note="P -> L (in Ref. 1; BAC26805)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   462 AA;  53183 MW;  01262CFE7DD9FC5F CRC64;
     MAKFRRRTCI LLSLFILFIF SLMMGLKMLW PNAASFGPPF GLDLLPELHP LNAHSGNKAD
     FQRSDRINME TNTKALKGAG MTVLPAKASE VNLEELPPLN YFLHAFYYSW YGNPQFDGKY
     IHWNHPVLEH WDPRIAKNYP QGQHSPPDDI GSSFYPELGS YSSRDPSVIE THMKQMRSAS
     IGVLALSWYP PDSRDDNGEA TDHLVPTILD KAHKYNLKVT FHIEPYSNRD DQNMHQNIKY
     IIDKYGNHPA FYRYKTRTGH SLPMFYVYDS YITKPTIWAN LLTPSGSQSV RSSPYDGLFI
     ALLVEEKHKN DILQSGFDGI YTYFATNGFT YGSSHQNWNN LKSFCEKNNL MFIPSVGPGY
     IDTSIRPWNT QNTRNRVNGK YYEVGLSAAL QTHPSLISIT SFNEWHEGTQ IEKAVPKRTA
     NTIYLDYRPH KPSLYLELTR KWSEKFSKER MTYALDQQQP AS
 
 
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