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ER degradation-enhancing alpha-mannosidase-like protein 1 (EC 3.2.1.24)

 MNL1_YEAST              Reviewed;         796 AA.
P38888; D3DLF3;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
25-MAY-2022, entry version 166.
RecName: Full=ER degradation-enhancing alpha-mannosidase-like protein 1;
EC=3.2.1.24 {ECO:0000269|PubMed:19124653, ECO:0000269|PubMed:21700223};
Flags: Precursor;
Name=MNL1; Synonyms=HTM1; OrderedLocusNames=YHR204W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8091229; DOI=10.1126/science.8091229;
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
Waterston R., Wilson R., Vaudin M.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
VIII.";
Science 265:2077-2082(1994).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
G3 (Bethesda) 4:389-398(2014).
[3]
FUNCTION.
PubMed=11375935; DOI=10.1093/embo-reports/kve089;
Jakob C.A., Bodmer D., Spirig U., Baettig P., Marcil A., Dignard D.,
Bergeron J.J.M., Thomas D.Y., Aebi M.;
"Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation
in yeast.";
EMBO Rep. 2:423-430(2001).
[4]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11254655; DOI=10.1074/jbc.c100023200;
Nakatsukasa K., Nishikawa S., Hosokawa N., Nagata K., Endo T.;
"Mnl1p, an alpha -mannosidase-like protein in yeast Saccharomyces
cerevisiae, is required for endoplasmic reticulum-associated degradation of
glycoproteins.";
J. Biol. Chem. 276:8635-8638(2001).
[5]
FUNCTION.
PubMed=15078901; DOI=10.1083/jcb.200309132;
Vashist S., Ng D.T.W.;
"Misfolded proteins are sorted by a sequential checkpoint mechanism of ER
quality control.";
J. Cell Biol. 165:41-52(2004).
[6]
FUNCTION.
PubMed=15215312; DOI=10.1091/mbc.e04-01-0024;
Gnann A., Riordan J.R., Wolf D.H.;
"Cystic fibrosis transmembrane conductance regulator degradation depends on
the lectins Htm1p/EDEM and the Cdc48 protein complex in yeast.";
Mol. Biol. Cell 15:4125-4135(2004).
[7]
FUNCTION.
PubMed=15809311; DOI=10.1083/jcb.200411136;
Spear E.D., Ng D.T.W.;
"Single, context-specific glycans can target misfolded glycoproteins for
ER-associated degradation.";
J. Cell Biol. 169:73-82(2005).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[10]
FUNCTION, INTERACTION WITH PDI1, AND CATALYTIC ACTIVITY.
PubMed=19124653; DOI=10.1083/jcb.200809198;
Clerc S., Hirsch C., Oggier D.M., Deprez P., Jakob C., Sommer T., Aebi M.;
"Htm1 protein generates the N-glycan signal for glycoprotein degradation in
the endoplasmic reticulum.";
J. Cell Biol. 184:159-172(2009).
[11]
FUNCTION, INTERACTION WITH PDI1, AND CATALYTIC ACTIVITY.
PubMed=21700223; DOI=10.1016/j.molcel.2011.04.027;
Gauss R., Kanehara K., Carvalho P., Ng D.T., Aebi M.;
"A complex of Pdi1p and the mannosidase Htm1p initiates clearance of
unfolded glycoproteins from the endoplasmic reticulum.";
Mol. Cell 42:782-793(2011).
-!- FUNCTION: Alpha-1,2-specific exomannosidase involved in endoplasmic
reticulum-associated degradation (ERAD). Delivers misfolded
glycoproteins to proteasomes. Forms a complex with PDI1 to process
unfolded protein-bound Man8GlcNAc2 oligosaccharides to Man7GlcNAc2,
promoting degradation in unfolded protein response.
{ECO:0000269|PubMed:11254655, ECO:0000269|PubMed:11375935,
ECO:0000269|PubMed:15078901, ECO:0000269|PubMed:15215312,
ECO:0000269|PubMed:15809311, ECO:0000269|PubMed:19124653,
ECO:0000269|PubMed:21700223}.
-!- CATALYTIC ACTIVITY:
Reaction=Hydrolysis of terminal, non-reducing alpha-D-mannose residues
in alpha-D-mannosides.; EC=3.2.1.24;
Evidence={ECO:0000269|PubMed:19124653, ECO:0000269|PubMed:21700223};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000250|UniProtKB:P45700};
-!- PATHWAY: Protein modification; protein glycosylation.
{ECO:0000250|UniProtKB:P32906}.
-!- SUBUNIT: Interacts with PDI1. {ECO:0000269|PubMed:19124653,
ECO:0000269|PubMed:21700223}.
-!- INTERACTION:
P38888; P17967: PDI1; NbExp=4; IntAct=EBI-24256, EBI-13012;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
{ECO:0000269|PubMed:11254655, ECO:0000269|PubMed:14562095}.
-!- MISCELLANEOUS: Present with 656 molecules/cell in log phase SD medium.
{ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family. {ECO:0000305}.
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EMBL; U00030; AAB68370.1; -; Genomic_DNA.
EMBL; BK006934; DAA06897.1; -; Genomic_DNA.
PIR; S46693; S46693.
RefSeq; NP_012074.3; NM_001179335.3.
AlphaFoldDB; P38888; -.
SMR; P38888; -.
BioGRID; 36638; 37.
ComplexPortal; CPX-1283; HTM1-PDI1 exomannosidase complex.
DIP; DIP-1890N; -.
IntAct; P38888; 3.
MINT; P38888; -.
STRING; 4932.YHR204W; -.
CAZy; GH47; Glycoside Hydrolase Family 47.
MaxQB; P38888; -.
PaxDb; P38888; -.
PRIDE; P38888; -.
EnsemblFungi; YHR204W_mRNA; YHR204W; YHR204W.
GeneID; 856611; -.
KEGG; sce:YHR204W; -.
SGD; S000001247; MNL1.
VEuPathDB; FungiDB:YHR204W; -.
eggNOG; KOG2429; Eukaryota.
GeneTree; ENSGT00940000157717; -.
HOGENOM; CLU_003818_5_3_1; -.
InParanoid; P38888; -.
OMA; EIDYRYN; -.
UniPathway; UPA00378; -.
PRO; PR:P38888; -.
Proteomes; UP000002311; Chromosome VIII.
RNAct; P38888; protein.
GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:SGD.
GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:GOC.
GO; GO:0106055; C:mannosyl-oligosaccharide 1,2-alpha-mannosidase complex; IPI:ComplexPortal.
GO; GO:0016020; C:membrane; IEA:InterPro.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0030246; F:carbohydrate binding; IMP:SGD.
GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IDA:SGD.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:1904380; P:endoplasmic reticulum mannose trimming; IDA:ComplexPortal.
GO; GO:1904382; P:mannose trimming involved in glycoprotein ERAD pathway; IDA:SGD.
GO; GO:1900103; P:positive regulation of endoplasmic reticulum unfolded protein response; IDA:ComplexPortal.
GO; GO:0036508; P:protein alpha-1,2-demannosylation; IDA:SGD.
GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
GO; GO:0097466; P:ubiquitin-dependent glycoprotein ERAD pathway; IMP:SGD.
Gene3D; 1.50.10.10; -; 1.
InterPro; IPR012341; 6hp_glycosidase-like_sf.
InterPro; IPR044674; EDEM1/2/3.
InterPro; IPR001382; Glyco_hydro_47.
InterPro; IPR036026; Seven-hairpin_glycosidases.
PANTHER; PTHR45679; PTHR45679; 1.
Pfam; PF01532; Glyco_hydro_47; 1.
PRINTS; PR00747; GLYHDRLASE47.
SUPFAM; SSF48225; SSF48225; 1.
1: Evidence at protein level;
Endoplasmic reticulum; Glycoprotein; Glycosidase; Hydrolase; Metal-binding;
Reference proteome; Signal; Unfolded protein response.
SIGNAL 1..20
/evidence="ECO:0000255"
CHAIN 21..796
/note="ER degradation-enhancing alpha-mannosidase-like
protein 1"
/id="PRO_0000210324"
ACT_SITE 372
/note="Proton donor"
/evidence="ECO:0000250|UniProtKB:P31723"
METAL 495
/note="Calcium"
/evidence="ECO:0000250|UniProtKB:P32906"
CARBOHYD 86
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 517
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 672
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 762
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
SEQUENCE 796 AA; 91246 MW; D538E6F28D35BE80 CRC64;
MVCCLWVLLA LLLHLDHVAC EDDAYSFTSK ELKAYKQEVK ELFYFGFDNY LEHGYPYDEV
KPISCVPKKR NFEDPTDQGT NDILGNFTIT LIDSLTTIAI LEDRPQFLKA VRLVERTFPD
GNFDIDSTIQ VFEITIRVIG SLLSSHLYAT DPTKAVYLGD DYDGSLLRLA QNMADRLLPA
YLTSTGLPMP RRNIKRKWDV SEFPEFLETE NNVAAMASPM FEFTILSYLT GDPKYEKVTR
YAFDKTWSLR TGLDLLPMSF HPEKLTPYTP MTGIGASIDS LFEYALKGAI LFDDSELMEV
WNVAYEALKT NCKNDWFFAN VMADTGHLFV PWIDSLSAFF SGLQVLAGDL DDAIANHLMF
LKMWNTFGGI PERWNFSPPE FPPLSPLERS GAVALDNILP LEWYPLRPEF FESTYFLYRA
TKDPFYLNIG VHLLKDLKQR FKSNCGFAGF QNVITGELQD RMETFVLSET LKYLYLLFDE
ENELHNSASD VIFSTEAHPM WLPQEVRSNY KRNAKFNNSV YSSHLEICQK KDREQAGENT
LSQRIVGFAK SIFHKGPPDE EATDPIIDYT IDTELPGTCS IKPHHVIGDE FWYSPMLSNF
DRLFEIDSRF AATLIKPSHM HNYNAIELEP GFYNRWSNPQ FSTCLIPPTT EIFELLFDLP
GYHQLNPLML ENKTITFETF GGRSRLKIEK LQIYQIDYYG DLITASTFQD VSRKDIFSNA
CDAVASLYSP TYLYRVVAIN GRILPRHGSV QIKKHSPVLT SNGTREEDEF KMDGIGINDH
SQLMLECTPI INLFIV


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EDEM3 EDEM1 Gene ER degradation enhancer, mannosidase alpha-like 1
Pathways :
WP1654: gamma-Hexachlorocyclohexane degradation
WP1665: Limonene and pinene degradation
WP210: Cytoplasmic Ribosomal Proteins
WP1566: Citrate cycle (TCA cycle)
WP1650: Fluorobenzoate degradation
WP1614: 1- and 2-Methylnaphthalene degradation
WP1531: Vitamin D synthesis
WP1673: Naphthalene and anthracene degradation
WP1613: 1,4-Dichlorobenzene degradation
WP2199: Seed Development
WP1655: Geraniol degradation
WP1003: Ovarian Infertility Genes
WP1615: 3-Chloroacrylic acid degradation
WP1693: Purine metabolism
WP2218: sGC
WP427: Synthesis and Degradation of Ketone Bodies
WP931: G Protein Signaling Pathways
WP1369: TNF-alpha NF-kB Signaling Pathway
WP183: Proteasome Degradation
WP273: Ovarian Infertility Genes
WP559: Glutamate degradation VII
WP1438: Influenza A virus infection
WP1659: Glycine, serine and threonine metabolism
WP1892: Protein folding
WP301: Tryptophan Degradation

Related Genes :

Bibliography :
[35500441] In vitro mannosidase activity of EDEM3 against asparagine-linked oligomannose-type glycans.
[35008544] EDEM1 Regulates Amyloid Precursor Protein (APP) Metabolism and Amyloid-β Production.
[34332121] Affinity Proteomics and Deglycoproteomics Uncover Novel EDEM2 Endogenous Substrates and an Integrative ERAD Network.
[32083795] Cleavage and degradation of EDEM1 promotes coxsackievirus B3 replication via ATF6a-mediated unfolded protein response signalling.
[30021839] EDEM1's mannosidase-like domain binds ERAD client proteins in a redox-sensitive manner and possesses catalytic activity.
[26205822] ERManI (Endoplasmic Reticulum Class I α-Mannosidase) Is Required for HIV-1 Envelope Glycoprotein Degradation via Endoplasmic Reticulum-associated Protein Degradation Pathway.
[16449189] Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation.
[15911611] Energetics of substrate binding and catalysis by class 1 (glycosylhydrolase family 47) alpha-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control.
[15713668] Mechanism of class 1 (glycosylhydrolase family 47) {alpha}-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control.
[11375934] A novel ER alpha-mannosidase-like protein accelerates ER-associated degradation.