ID   P90830_CAEEL            Unreviewed;       781 AA.
AC   P90830;
DT   01-MAY-1997, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1997, sequence version 1.
DT   02-SEP-2026, entry version 161.
DE   RecName: Full=alpha-1,2-Mannosidase {ECO:0000256|RuleBase:RU361193};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361193};
GN   ORFNames=CELE_F10C2.5 {ECO:0000313|EMBL:CAB04078.1}, F10C2.5
GN   {ECO:0000313|EMBL:CAB04078.1, ECO:0000313|WormBase:F10C2.5};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000313|EMBL:CAB04078.1, ECO:0000313|Proteomes:UP000001940};
RN   [1] {ECO:0000313|EMBL:CAB04078.1, ECO:0000313|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CAB04078.1,
RC   ECO:0000313|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RA   Sulson J.E., Waterston R.;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Involved in the endoplasmic reticulum-associated degradation
CC       (ERAD) pathway that targets misfolded glycoproteins for degradation in
CC       an N-glycan-dependent manner. May initiate ERAD by promoting the first
CC       mannose trimming step of ERAD substrates, from Man9GlcNAc2 to
CC       Man8GlcNAc2. Seems to recognize and bind to exposed hydrophobic regions
CC       in target proteins. {ECO:0000256|ARBA:ARBA00054385}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601382-2};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000256|ARBA:ARBA00004240}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family.
CC       {ECO:0000256|ARBA:ARBA00007658, ECO:0000256|RuleBase:RU361193}.
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DR   EMBL; BX284605; CAB04078.1; -; Genomic_DNA.
DR   PIR; T20699; T20699.
DR   RefSeq; NP_506018.1; NM_073617.6.
DR   AlphaFoldDB; P90830; -.
DR   SMR; P90830; -.
DR   FunCoup; P90830; 1573.
DR   STRING; 6239.F10C2.5.1; -.
DR   PaxDb; 6239-F10C2.5.1; -.
DR   PeptideAtlas; P90830; -.
DR   GeneID; 179653; -.
DR   KEGG; cel:CELE_F10C2.5; -.
DR   UCSC; F10C2.5; c. elegans.
DR   AGR; WB:WBGene00008646; -.
DR   CTD; 179653; -.
DR   WormBase; F10C2.5; CE09309; WBGene00008646; -.
DR   eggNOG; KOG2429; Eukaryota.
DR   HOGENOM; CLU_003818_5_4_1; -.
DR   InParanoid; P90830; -.
DR   OMA; MVESLMY; -.
DR   OrthoDB; 8118055at2759; -.
DR   PhylomeDB; P90830; -.
DR   PRO; PR:P90830; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00008646; Expressed in germ line (C elegans) and 4 other cell types or tissues.
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:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:1904380; P:endoplasmic reticulum mannose trimming; IEA:InterPro.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central.
DR   GO; GO:1904154; P:positive regulation of retrograde protein transport, ER to cytosol; IEA:UniProtKB-ARBA.
DR   GO; GO:0097466; P:ubiquitin-dependent glycoprotein ERAD pathway; IBA:GO_Central.
DR   FunFam; 1.50.10.10:FF:000015; alpha-1,2-Mannosidase; 1.
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; ER DEGRADATION-ENHANCING ALPHA-MANNOSIDASE-LIKE PROTEIN 2; 1.
DR   PANTHER; PTHR45679:SF6; ER DEGRADATION-ENHANCING ALPHA-MANNOSIDASE-LIKE PROTEIN 2; 1.
DR   Pfam; PF01532; Glyco_hydro_47; 1.
DR   PRINTS; PR00747; GLYHDRLASE47.
DR   SUPFAM; SSF48225; Seven-hairpin glycosidases; 1.
PE   1: Evidence at protein level;
KW   Calcium {ECO:0000256|PIRSR:PIRSR601382-2};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|RuleBase:RU361193};
KW   Hydrolase {ECO:0000256|RuleBase:RU361193};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601382-2};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:P90830};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..781
FT                   /note="alpha-1,2-Mannosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004161766"
FT   COILED          607..641
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        124
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   ACT_SITE        267
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   ACT_SITE        360
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   ACT_SITE        381
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   BINDING         485
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-2"
SQ   SEQUENCE   781 AA;  89050 MW;  D006B1CC85E86859 CRC64;
     MITRKAIFFL ALASIIQASD DSEAPDNKKS SIRFTPSVID SYREKVQKMF YHAYNGYLDH
     AFPLDELKPI TCVGQDTWGS FSLSLIDALD TLLVMGNTTE FRRAVSLVLE KARDDANVNV
     SVFETNIRVV GGLISAHMLA GRHKDLVVDW EGYPCDSPLL KLAVKMADRL MPAFNTETGM
     PYGTVNLKYG VHKDETPITC TAGVGTFLIE FGTLSRLTGD DKYEKVALKA LDALWSTRSP
     IGLVGNHINV QTGQWTATDS GIGAGVDSYF EYLAKGAYLF RRPSLMKQFH EHATSINKHV
     RKGEWFMWVS MAKGSVSLPI FQSLEAFWPG TLTMVGDVQD ASRIMLTYSE VIRKYGFPPE
     FYNIHNEEPG EKRAAFPLRP EMVESLMYLY RATKDETWLE LGAEMIDAIE SSARTKCGYA
     TINNVKEHSI EDRMESFFLA ETTKYLYLLF DPTNFIHSKG DQARILTSPK NLTCVIYGGG
     YIFNTEAHPV DPGMLDCCSV QAKRDQEVGV KQVNNGDEHE KMNRTEKGGE KYFENQYGKN
     ENLIEFEVDE KLKKESEKRK IELEAEKVKE NSHKAMLKVR EILVRAHQKD EAMQRNGETS
     DSARKLMDQL YKAYPNHTAE LENLNKEAII EFEELQHLED IRELVREIPI PEVFCEKCCV
     PLHEIVDSVV LRVLMADVYE YHFYPTRKTK FLHGPVCWLE ETPRIEDDYK NEPPSVNTEK
     WNSPLFTSDQ ASLNDFIGDD LETVRKFGFK TLLAPGYKKL DKLIAGQNIA LRRKKSWYYE
     V
//