MNL1_SCHPO
ID MNL1_SCHPO Reviewed; 787 AA.
AC O94726;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=ER degradation-enhancing alpha-mannosidase-like protein 1;
DE Flags: Precursor;
GN Name=mnl1; ORFNames=SPAC23A1.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION.
RX PubMed=16079177; DOI=10.1091/mbc.e05-03-0246;
RA Movsichoff F., Castro O.A., Parodi A.J.;
RT "Characterization of Schizosaccharomyces pombe ER alpha-mannosidase: a
RT reevaluation of the role of the enzyme on ER-associated degradation.";
RL Mol. Biol. Cell 16:4714-4724(2005).
CC -!- FUNCTION: Alpha-mannosidase-like protein involved in endoplasmic
CC reticulum-associated degradation (ERAD). Delivers misfolded
CC glycoproteins to proteasomes. It lacks mannosidase activity.
CC {ECO:0000269|PubMed:16079177}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family. {ECO:0000305}.
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DR EMBL; CU329670; CAA16978.2; -; Genomic_DNA.
DR PIR; T38224; T38224.
DR RefSeq; NP_594434.1; NM_001019863.2.
DR AlphaFoldDB; O94726; -.
DR SMR; O94726; -.
DR BioGRID; 278466; 3.
DR STRING; 4896.SPAC23A1.04c.1; -.
DR CAZy; GH47; Glycoside Hydrolase Family 47.
DR MaxQB; O94726; -.
DR PaxDb; O94726; -.
DR EnsemblFungi; SPAC23A1.04c.1; SPAC23A1.04c.1:pep; SPAC23A1.04c.
DR GeneID; 2541981; -.
DR KEGG; spo:SPAC23A1.04c; -.
DR PomBase; SPAC23A1.04c; mnl1.
DR VEuPathDB; FungiDB:SPAC23A1.04c; -.
DR eggNOG; KOG2429; Eukaryota.
DR HOGENOM; CLU_003818_2_1_1; -.
DR InParanoid; O94726; -.
DR OMA; FARINLM; -.
DR PhylomeDB; O94726; -.
DR PRO; PR:O94726; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:PomBase.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:GOC.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; ISO:PomBase.
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; IBA:GO_Central.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR GO; GO:0097466; P:ubiquitin-dependent glycoprotein ERAD pathway; IMP:PomBase.
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 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Reference proteome; Signal;
KW Unfolded protein response.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..787
FT /note="ER degradation-enhancing alpha-mannosidase-like
FT protein 1"
FT /id="PRO_0000373874"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 693
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 756
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 787 AA; 89318 MW; D8CCD0FE784618EC CRC64;
MGSLHSIFCV CLILLCIFKE NSIVGAINSA RMVELRETSR RLFYHGYNNY MQFAFPNDEL
APLSCEGLGP DYENPNNIGV NDVRGDYLLT LVDVLDTLVV LGDREGFQDA VDKVIHHINF
ERDTKVQVFE ATIRILGGLL SSHIFASEEK YGFQIPLYKG ELLTLATELA ERLLPAFRTP
TGIPFARINL MKGVAYREVT ENCAAAASSL VLEFSMLTAL TGNNKFKASA ENAFFSVWKR
RSGIGLLGNS IDVLSGRWIY PVSGVGAGID SFYEYAFKSY IFLGDPRYLE VWQKSLESLR
HYTASLNEYY YQNVYSANGM VMSRWVDSLS AYFPGLLVLA GELELAKKMH LYYFSIYLKF
GQLPERYNLY TKSIELNGYP LRPEFAESTY YLYRATKDVF YLHVGELLLS NIENHLWTPC
GFAAVENLEK YTLSNRMESF FLSETLKYLF LLFDDDNPIH RSHHDFIFTT EGHLFPVTNQ
TRLSTSQRIY DGGEVCVAED YDRSKWPMLY SLIASRDDYD YVSHLVGIDN KAIPSYLIDP
SGVCKRPEYS DGFELLYGSA LVSPIKSVER VTNNVYISDI IGNKLKFVQK EGSNSLFLYT
AGAESINEND TVFLTDPDYE TFTRPDALYF DRTIAQLENP NSGQKTFGKF LQFDNDNSLP
SKVFKTVLLN NSMCQKPSDT LDKDTAYIAP LGNCSWVQQA KNTNKAGLLI LITDGEFINP
LENIHSQNSL FNWVKPYIPP TILLKNENNF VSKWANVSVR QSDFDAPSYF QGTPVSNLYL
CLKCINS
