MANEL_MOUSE
ID MANEL_MOUSE Reviewed; 452 AA.
AC Q6P1J0; Q3UVP2;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Glycoprotein endo-alpha-1,2-mannosidase-like protein;
DE EC=3.2.1.-;
GN Name=Maneal; Synonyms=Gm50;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 323-452.
RC STRAIN=C57BL/6J;
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).
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 99 family. {ECO:0000305}.
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DR EMBL; AL606933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC065047; AAH65047.1; -; mRNA.
DR EMBL; AK137071; BAE23227.1; -; mRNA.
DR CCDS; CCDS18629.1; -.
DR RefSeq; NP_001007574.1; NM_001007573.3.
DR AlphaFoldDB; Q6P1J0; -.
DR SMR; Q6P1J0; -.
DR STRING; 10090.ENSMUSP00000066000; -.
DR CAZy; GH99; Glycoside Hydrolase Family 99.
DR PhosphoSitePlus; Q6P1J0; -.
DR MaxQB; Q6P1J0; -.
DR PaxDb; Q6P1J0; -.
DR PRIDE; Q6P1J0; -.
DR ProteomicsDB; 287308; -.
DR Antibodypedia; 54337; 25 antibodies from 10 providers.
DR Ensembl; ENSMUST00000064444; ENSMUSP00000066000; ENSMUSG00000042763.
DR GeneID; 215090; -.
DR KEGG; mmu:215090; -.
DR UCSC; uc008urg.1; mouse.
DR CTD; 149175; -.
DR MGI; MGI:2684896; Maneal.
DR VEuPathDB; HostDB:ENSMUSG00000042763; -.
DR eggNOG; ENOG502QPJV; Eukaryota.
DR GeneTree; ENSGT00390000016054; -.
DR HOGENOM; CLU_042710_1_1_1; -.
DR InParanoid; Q6P1J0; -.
DR OMA; VHWDHVM; -.
DR OrthoDB; 975667at2759; -.
DR PhylomeDB; Q6P1J0; -.
DR TreeFam; TF324051; -.
DR BioGRID-ORCS; 215090; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Maneal; mouse.
DR PRO; PR:Q6P1J0; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q6P1J0; protein.
DR Bgee; ENSMUSG00000042763; Expressed in retinal neural layer and 88 other tissues.
DR Genevisible; Q6P1J0; MM.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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:0004559; F:alpha-mannosidase activity; IBA:GO_Central.
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..452
FT /note="Glycoprotein endo-alpha-1,2-mannosidase-like
FT protein"
FT /id="PRO_0000282321"
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..452
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 40..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..77
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 452 AA; 51106 MW; 449940ACF3A3E783 CRC64;
MARRRRRACI ALFLVLLFAF GTLMGLRTLK APDGLPALGP GPELAPFERR PEGNPAPARA
PAAPAAPPPP PPRTAAPRAS LGPAEADPAP RQSLRVYSDL HAFYYSWYGS PRREGHYIHW
DHVMVPHWDP KISASYPRGR HSPPDDLGSS FYPELGPYSS RDPDVLREHM TQLKEAAIGV
LVLSWYPPGM ADDNGEPTDD LVPAILDTAH QYNIQVAFHI QPYKGRDDIT VHDNIKYIID
TYGSHGAFYR YKNSMGKSLP LFYIYDSYLT SPEAWAHLLT QNGPHSIRNT PYDGVFIALL
VEESHTHDIL AAGFDGMYTY FASNGFSFGS SHQNWKAVKN FCDTNNLMFI PSVGPGYIDT
SIRPWNNHNT RNRVNGKYYE TALQAALTVR PEIVSITSFN EWHEGTQIEK AVPKTTPTRL
YLDYLPHQSS LYLELTRRWA EHFIKEKEQW LM
