ID   A0A922E3Q4_CARIL        Unreviewed;       561 AA.
AC   A0A922E3Q4;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   27-NOV-2024, entry version 9.
DE   RecName: Full=mannosyl-oligosaccharide 1,2-alpha-mannosidase {ECO:0000256|ARBA:ARBA00012238};
DE            EC=3.2.1.113 {ECO:0000256|ARBA:ARBA00012238};
GN   ORFNames=I3842_09G122100 {ECO:0000313|EMBL:KAG6695939.1};
OS   Carya illinoinensis (Pecan).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fagales; Juglandaceae; Carya.
OX   NCBI_TaxID=32201 {ECO:0000313|EMBL:KAG6695939.1, ECO:0000313|Proteomes:UP000811246};
RN   [1] {ECO:0000313|EMBL:KAG6695939.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAG6695939.1};
RA   Lovell J.T., Bentley N., Bhattarai G., Jenkins J.W., Sreedasyam A.,
RA   Alarcon Y., Bock C., Boston L., Carlson J., Cervantes K., Clermont K.,
RA   Krom N., Kubenka K., Mamidi S., Mattison C., Monteros M., Pisani C.,
RA   Plott C., Rajasekar S., Rhein H.S., Rohla C., Song M., Hilaire R.S.,
RA   Shu S., Wells L., Wang X., Webber J., Heerema R.J., Klein P., Conner P.,
RA   Grauke L., Grimwood J., Schmutz J., Randall J.J.;
RL   Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-
CC         (1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-
CC         alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-
CC         GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,3)
CC         + 3 H2O = N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-
CC         (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC         beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer
CC         5A1,2) + 3 beta-D-mannose; Xref=Rhea:RHEA:56028, Rhea:RHEA-
CC         COMP:14358, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:60628;
CC         EC=3.2.1.113; Evidence={ECO:0000256|ARBA:ARBA00034217};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-
CC         (1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC         alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-
CC         GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan
CC         mannose isomer 9A1,2,3B1,2,3) + 4 H2O = N(4)-(alpha-D-Man-(1->3)-
CC         [alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-
CC         Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-
CC         [protein] (N-glucan mannose isomer 5A1,2) + 4 beta-D-mannose;
CC         Xref=Rhea:RHEA:56008, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14367,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:28563, ChEBI:CHEBI:59087,
CC         ChEBI:CHEBI:139493; EC=3.2.1.113;
CC         Evidence={ECO:0000256|ARBA:ARBA00034437};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAG6695939.1}.
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DR   EMBL; CM031833; KAG6695939.1; -; Genomic_DNA.
DR   Proteomes; UP000811246; Chromosome 9.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:TreeGrafter.
DR   GO; GO:0005768; C:endosome; IEA:TreeGrafter.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005802; C:trans-Golgi network; IEA:TreeGrafter.
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:1904382; P:mannose trimming involved in glycoprotein ERAD pathway; IEA:TreeGrafter.
DR   InterPro; IPR001382; Glyco_hydro_47.
DR   InterPro; IPR050749; Glycosyl_Hydrolase_47.
DR   PANTHER; PTHR11742:SF55; ENDOPLASMIC RETICULUM MANNOSYL-OLIGOSACCHARIDE 1,2-ALPHA-MANNOSIDASE; 1.
DR   PANTHER; PTHR11742; MANNOSYL-OLIGOSACCHARIDE ALPHA-1,2-MANNOSIDASE-RELATED; 1.
DR   Pfam; PF01532; Glyco_hydro_47; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601382-3}.
FT   REGION          87..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..116
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        213
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   ACT_SITE        357
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   ACT_SITE        485
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   ACT_SITE        526
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   DISULFID        428..471
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-3"
SQ   SEQUENCE   561 AA;  62561 MW;  8EB792CA92B0D8D3 CRC64;
     MSSKSLPYSM KDVDYDNAKF RHRSFFKVIT QTLFTSKVRR DCQSCSTGKF LALVLLFGLL
     YLMFTHTSPA HSATENEENL ITKGGSRLGM FWRKPPRLPP RLPPEEKGSD SSFSHEHEKL
     NAPSNWISRQ QSVKKAFIHA WSGYKRYAMG SDELMPLIQR GVDGLGGLGA TIVDALDTAM
     IMGVDEAVSE AGSWIEAHLL DRITHKGQVN LFETTIRVMG GLLSAYHLST HEEGINMTHT
     GPKPVIYLET ARNLADRLLS AFTFSQTPIP FSDVVLRDSS AHAAPDGLSS TSEVSTLQLE
     FNYLSAVSGD PKYSIEAMKV LEHMKTLPKV EGLVPIYISP RTGEFSGENI RLGSRGDSYY
     EYLLKVWLQQ GITRDSNLTY LYDMYQEAMK GVRHLLVQKS IPNGLVFVGE LPFGSKGAFS
     PKMDHLVCFL PGVLALGATK GITKEKAMRD NLLNFEDLEN LKLAEDLAKT CFEMYSVTST
     GLAPEIAYFH TAEFTEGGLD GGNKSSKYVH DIIIKPADRH NLLRPETVES LFVLFRITED
     PKYGFFPFSF SFFVYALASL V
//