Reviewed, UniProtKB/Swiss-Prot P38888 (MNL1_YEAST)

Names and origin

Protein names

Recommended name:
    ER degradation-enhancing alpha-mannosidase-like protein 1

Gene names

Name:	MNL1
Synonyms:	HTM1
Ordered Locus Names:	YHR204W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	796 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Alpha-mannosidase-like protein involved in endoplasmic reticulum-associated degradation (ERAD). Delivers misfolded glycoproteins to proteasomes. It lacks mannosidase activity. Ref.2 Ref.3 Ref.4 Ref.5 Ref.6
Subcellular location	Endoplasmic reticulum lumen.
Miscellaneous	Present with 656 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the glycosyl hydrolase 47 family.

Ontologies

Keywords
Biological process	Unfolded protein response
Cellular component	Endoplasmic reticulum
Domain	Signal
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ER-associated protein catabolic process Ref.2 Ref.3 Inferred from mutant phenotype. Source: SGD response to unfolded protein Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum lumen Inferred from direct assay. Source: SGD membrane Inferred from electronic annotation. Source: InterPro
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro carbohydrate binding Ref.2 Inferred from mutant phenotype. Source: SGD mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PDI1	P17967	1	EBI-24256,EBI-13012

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 796	776	ER degradation-enhancing alpha-mannosidase-like protein 1		PRO_0000210324
Amino acid modifications
	Glycosylation	86	1	N-linked (GlcNAc...) Potential
	Glycosylation	517	1	N-linked (GlcNAc...) Potential
	Glycosylation	672	1	N-linked (GlcNAc...) Potential
	Glycosylation	762	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	P38888-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: D538E6F28D35BE80	FASTA	796	91,246
	10 20 30 40 50 60 MVCCLWVLLA LLLHLDHVAC EDDAYSFTSK ELKAYKQEVK ELFYFGFDNY LEHGYPYDEV 70 80 90 100 110 120 KPISCVPKKR NFEDPTDQGT NDILGNFTIT LIDSLTTIAI LEDRPQFLKA VRLVERTFPD 130 140 150 160 170 180 GNFDIDSTIQ VFEITIRVIG SLLSSHLYAT DPTKAVYLGD DYDGSLLRLA QNMADRLLPA 190 200 210 220 230 240 YLTSTGLPMP RRNIKRKWDV SEFPEFLETE NNVAAMASPM FEFTILSYLT GDPKYEKVTR 250 260 270 280 290 300 YAFDKTWSLR TGLDLLPMSF HPEKLTPYTP MTGIGASIDS LFEYALKGAI LFDDSELMEV 310 320 330 340 350 360 WNVAYEALKT NCKNDWFFAN VMADTGHLFV PWIDSLSAFF SGLQVLAGDL DDAIANHLMF 370 380 390 400 410 420 LKMWNTFGGI PERWNFSPPE FPPLSPLERS GAVALDNILP LEWYPLRPEF FESTYFLYRA 430 440 450 460 470 480 TKDPFYLNIG VHLLKDLKQR FKSNCGFAGF QNVITGELQD RMETFVLSET LKYLYLLFDE 490 500 510 520 530 540 ENELHNSASD VIFSTEAHPM WLPQEVRSNY KRNAKFNNSV YSSHLEICQK KDREQAGENT 550 560 570 580 590 600 LSQRIVGFAK SIFHKGPPDE EATDPIIDYT IDTELPGTCS IKPHHVIGDE FWYSPMLSNF 610 620 630 640 650 660 DRLFEIDSRF AATLIKPSHM HNYNAIELEP GFYNRWSNPQ FSTCLIPPTT EIFELLFDLP 670 680 690 700 710 720 GYHQLNPLML ENKTITFETF GGRSRLKIEK LQIYQIDYYG DLITASTFQD VSRKDIFSNA 730 740 750 760 770 780 CDAVASLYSP TYLYRVVAIN GRILPRHGSV QIKKHSPVLT SNGTREEDEF KMDGIGINDH 790 SQLMLECTPI INLFIV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII." 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. Science 265:2077-2082(1994) [PubMed: 8091229] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast." Jakob C.A., Bodmer D., Spirig U., Baettig P., Marcil A., Dignard D., Bergeron J.J.M., Thomas D.Y., Aebi M. EMBO Rep. 2:423-430(2001) [PubMed: 11375935] [Abstract] Cited for: FUNCTION.
[3]	"Mnl1p, an alpha -mannosidase-like protein in yeast Saccharomyces cerevisiae, is required for endoplasmic reticulum-associated degradation of glycoproteins." Nakatsukasa K., Nishikawa S., Hosokawa N., Nagata K., Endo T. J. Biol. Chem. 276:8635-8638(2001) [PubMed: 11254655] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[4]	"Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control." Vashist S., Ng D.T.W. J. Cell Biol. 165:41-52(2004) [PubMed: 15078901] [Abstract] Cited for: FUNCTION.
[5]	"Cystic fibrosis transmembrane conductance regulator degradation depends on the lectins Htm1p/EDEM and the Cdc48 protein complex in yeast." Gnann A., Riordan J.R., Wolf D.H. Mol. Biol. Cell 15:4125-4135(2004) [PubMed: 15215312] [Abstract] Cited for: FUNCTION.
[6]	"Single, context-specific glycans can target misfolded glycoproteins for ER-associated degradation." Spear E.D., Ng D.T.W. J. Cell Biol. 169:73-82(2005) [PubMed: 15809311] [Abstract] Cited for: FUNCTION.
[7]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U00030 Genomic DNA. Translation: AAB68370.1.
PIR	S46693.
RefSeq	NP_012074.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:1890N.
IntAct	P38888. 6 interactions.
STRING	P38888.
Protein family/group databases
CAZy	GH47. Glycoside Hydrolase Family 47.
Genome annotation databases
Ensembl	YHR204W; YHR204W; YHR204W; Saccharomyces cerevisiae. [Genome view]
GeneID	856611.
KEGG	sce:YHR204W.
NMPDR	fig|4932.3.peg.3245.
Organism-specific databases
CYGD	YHR204w.
SGD	S000001247. MNL1.
Phylogenomic databases
HOGENOM	P38888.
OMA	SSHLYAT
OrthoDB	EOG9WM6B4
Gene expression databases
ArrayExpress	P38888.
Genevestigator	P38888.
GermOnline	YHR204W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001382. Glyco_hydro_47. [Graphical view]
Gene3D	G3DSA:1.50.10.50. Glyco_hydro_47. 1 hit.
PANTHER	PTHR11742. Glyco_hydro_47. 1 hit.
Pfam	PF01532. Glyco_hydro_47. 1 hit. [Graphical view]
PRINTS	PR00747. GLYHDRLASE47.
ProtoNet	Search...
Other Resources
NextBio	982529.

Entry information

Entry name

MNL1_YEAST

Accession

Primary (citable) accession number: P38888

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	November 24, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)