EDEM1_MOUSE
ID EDEM1_MOUSE Reviewed; 652 AA.
AC Q925U4; Q8CFM1;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=ER degradation-enhancing alpha-mannosidase-like protein 1;
GN Name=Edem1; Synonyms=Edem;
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 [MRNA], AND FUNCTION.
RX PubMed=11375934; DOI=10.1093/embo-reports/kve084;
RA Hosokawa N., Wada I., Hasegawa K., Yorihuzi T., Tremblay L.O.,
RA Herscovics A., Nagata K.;
RT "A novel ER alpha-mannosidase-like protein accelerates ER-associated
RT degradation.";
RL EMBO Rep. 2:415-422(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Mammary gland;
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 [4]
RP INTERACTION WITH DNAJC10.
RX PubMed=18653895; DOI=10.1126/science.1159293;
RA Ushioda R., Hoseki J., Araki K., Jansen G., Thomas D.Y., Nagata K.;
RT "ERdj5 is required as a disulfide reductase for degradation of misfolded
RT proteins in the ER.";
RL Science 321:569-572(2008).
RN [5]
RP INTERACTION WITH DNAJC10.
RX PubMed=21329881; DOI=10.1016/j.molcel.2011.01.021;
RA Hagiwara M., Maegawa K., Suzuki M., Ushioda R., Araki K., Matsumoto Y.,
RA Hoseki J., Nagata K., Inaba K.;
RT "Structural basis of an ERAD pathway mediated by the ER-resident protein
RT disulfide reductase ERdj5.";
RL Mol. Cell 41:432-444(2011).
CC -!- FUNCTION: Extracts misfolded glycoproteins, but not glycoproteins
CC undergoing productive folding, from the calnexin cycle. It is directly
CC involved in endoplasmic reticulum-associated degradation (ERAD) and
CC targets misfolded glycoproteins for degradation in an N-glycan-
CC independent manner, probably by forming a complex with SEL1L. It has
CC low mannosidase activity, catalyzing mannose trimming from Man8GlcNAc2
CC to Man7GlcNAc2. {ECO:0000250|UniProtKB:Q92611,
CC ECO:0000269|PubMed:11375934}.
CC -!- SUBUNIT: Interacts with DERL2 and DERL3. Binds to SEL1L (By
CC similarity). Interacts with DNAJC10. {ECO:0000250,
CC ECO:0000269|PubMed:18653895, ECO:0000269|PubMed:21329881}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family. {ECO:0000305}.
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DR EMBL; AB042828; BAB55676.1; -; mRNA.
DR EMBL; AK082920; BAC38688.1; -; mRNA.
DR EMBL; BC023237; AAH23237.2; -; mRNA.
DR CCDS; CCDS20402.1; -.
DR RefSeq; NP_619618.1; NM_138677.2.
DR AlphaFoldDB; Q925U4; -.
DR SMR; Q925U4; -.
DR BioGRID; 228670; 4.
DR IntAct; Q925U4; 8.
DR STRING; 10090.ENSMUSP00000086565; -.
DR CAZy; GH47; Glycoside Hydrolase Family 47.
DR GlyGen; Q925U4; 4 sites.
DR iPTMnet; Q925U4; -.
DR PhosphoSitePlus; Q925U4; -.
DR EPD; Q925U4; -.
DR jPOST; Q925U4; -.
DR MaxQB; Q925U4; -.
DR PaxDb; Q925U4; -.
DR PRIDE; Q925U4; -.
DR ProteomicsDB; 277715; -.
DR Antibodypedia; 25261; 102 antibodies from 27 providers.
DR DNASU; 192193; -.
DR Ensembl; ENSMUST00000089162; ENSMUSP00000086565; ENSMUSG00000030104.
DR GeneID; 192193; -.
DR KEGG; mmu:192193; -.
DR UCSC; uc009ddq.1; mouse.
DR CTD; 9695; -.
DR MGI; MGI:2180139; Edem1.
DR VEuPathDB; HostDB:ENSMUSG00000030104; -.
DR eggNOG; KOG2429; Eukaryota.
DR GeneTree; ENSGT00940000157717; -.
DR HOGENOM; CLU_003818_5_6_1; -.
DR InParanoid; Q925U4; -.
DR OMA; NWTFVKD; -.
DR OrthoDB; 434316at2759; -.
DR PhylomeDB; Q925U4; -.
DR TreeFam; TF300807; -.
DR BioGRID-ORCS; 192193; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Edem1; mouse.
DR PRO; PR:Q925U4; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q925U4; protein.
DR Bgee; ENSMUSG00000030104; Expressed in lacrimal gland and 235 other tissues.
DR ExpressionAtlas; Q925U4; baseline and differential.
DR Genevisible; Q925U4; MM.
DR GO; GO:0016235; C:aggresome; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IMP:ParkinsonsUK-UCL.
DR GO; GO:0051787; F:misfolded protein binding; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1904380; P:endoplasmic reticulum mannose trimming; IBA:GO_Central.
DR GO; GO:1904382; P:mannose trimming involved in glycoprotein ERAD pathway; ISO:MGI.
DR GO; GO:1904154; P:positive regulation of retrograde protein transport, ER to cytosol; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045047; P:protein targeting to ER; ISO:MGI.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR GO; GO:0036510; P:trimming of terminal mannose on C branch; IMP:ParkinsonsUK-UCL.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:MGI.
DR GO; GO:0097466; P:ubiquitin-dependent glycoprotein ERAD pathway; ISO:MGI.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR044674; EDEM1/2/3.
DR InterPro; IPR001382; Glyco_hydro_47.
DR InterPro; IPR036026; Seven-hairpin_glycosidases.
DR PANTHER; PTHR45679; PTHR45679; 1.
DR Pfam; PF01532; Glyco_hydro_47; 1.
DR PRINTS; PR00747; GLYHDRLASE47.
DR SUPFAM; SSF48225; SSF48225; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix;
KW Unfolded protein response.
FT CHAIN 1..652
FT /note="ER degradation-enhancing alpha-mannosidase-like
FT protein 1"
FT /id="PRO_0000210322"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..652
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 50..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 652 AA; 73701 MW; 3BFC9A874B0E537E CRC64;
MQWRALVLGL VLLRLGLHAV LWLVFGLGPS MGFYQRFPLS FGFQRLRDPD GSGPVGPPGG
PAWLHRPRRG TEGRLETPPE PGPTPGPGVC GPAHWGYALG GGGCGPDEYE RRYSGAFPPQ
LRAQMRDLAR GMFVFGYDNY MAHAFPQDEL NPIYCRGRGP DRGDPSNLNI NDVLGNYSLT
LVDALDTLAI MGNSSEFQKA VKLVINTVSF DKDSTVQVFE ATIRVLGSLL SAHRIITDSK
QPFGDMTIED YDNELLYMAH DLAVRLLPAF ENTKTGIPYP RVNLKTGVPP DSNNETCTAG
AGSLLVEFGI LSRLLGDSTF EWVARRAVKA LWNLRSNDTG LLGNVVNIQT GHWVGKQSGL
GAGLDSFYEY LLKSYILFGE KEDLEMFNAA YQSIQSYLRR GREACNEGEG DPPLYVNVNM
FSGQLMNTWI DSLQAFFPGL QVLIGDVEDA ICLHAFYYAI WKRYGALPER YNWQLQAPDV
LFYPLRPELV ESTYLLYQAT KNPFYLHVGM DILQSLEKYT KVKCGYATLH HVIDKSKEDR
MESFFLSETC KYLYLLFDEE NPVHKSGTRY MFTTEGHIIS VDKRLRELPW KEFFSEDGER
DQEEKFVHRP KSQELRVINS SSNCNRVPDE RRYSLPLKSI YMRQIDQMVG LI
