ID L5LAF8_MYODS Unreviewed; 856 AA.
AC L5LAF8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=alpha-1,2-Mannosidase {ECO:0000256|RuleBase:RU361193};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361193};
GN ORFNames=MDA_GLEAN10017488 {ECO:0000313|EMBL:ELK23314.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK23314.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR601382-2};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family.
CC {ECO:0000256|ARBA:ARBA00007658, ECO:0000256|RuleBase:RU361193}.
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DR EMBL; KB113703; ELK23314.1; -; Genomic_DNA.
DR AlphaFoldDB; L5LAF8; -.
DR eggNOG; KOG2430; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
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 CDD; cd02126; PA_EDEM3_like; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR044674; EDEM1/2/3.
DR InterPro; IPR037322; EDEM3_PA.
DR InterPro; IPR001382; Glyco_hydro_47.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR036026; Seven-hairpin_glycosidases.
DR PANTHER; PTHR45679; ER DEGRADATION-ENHANCING ALPHA-MANNOSIDASE-LIKE PROTEIN 2; 1.
DR PANTHER; PTHR45679:SF2; ER DEGRADATION-ENHANCING ALPHA-MANNOSIDASE-LIKE PROTEIN 3; 1.
DR Pfam; PF01532; Glyco_hydro_47; 1.
DR Pfam; PF02225; PA; 1.
DR PRINTS; PR00747; GLYHDRLASE47.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF48225; Seven-hairpin glycosidases; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR601382-2};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycosidase {ECO:0000256|RuleBase:RU361193};
KW Hydrolase {ECO:0000256|RuleBase:RU361193};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601382-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556}.
FT DOMAIN 610..696
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT REGION 714..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..810
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 69
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 216
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 310
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 328
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT BINDING 414
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-2"
SQ SEQUENCE 856 AA; 96000 MW; 63A4FA548A791F31 CRC64;
MPLTCRGRIR GEEPSRGDVD DALGKFSLTL IDSLDTLVVL NKTKEFEDAV KKVLRDVNLD
NDVVVSVFET NIRVLGGLLG GHSLAIMLKE KGEYMQWYND ELLQMAKQLG YKLLPAFNTT
SGLPYPRINL KFGIRKPEAR TGTETDTCTA CAGTLILEFA ALSRFTGATI FEEYARKALD
FLWEKRQRSS NLVGVTINIH TGDWVRKDSG VGAGIDSYYE YLLKAYVLLG DDSFLERFNT
HYDAIMRYIS QPPLLLDVHI HKPMLNARTW MDALLAFFPG LQVLKGDIRP AIETHEMLYQ
VIKKHNFLPE AFTTDFRVHW AQHPLRPEFA ESTYFLYKAT GDPYYLEVGK TLIENLNKYA
RVPCGFAAMK DVRTGSHEDR MDSFFLAEMF KYLYLLFADK EDIIFDIEDY IFTTEAHLLP
LWLSTTNQSV SKKSTTSEYI ELDDSNFDWT CPNTQILFPN DPLYAQSIRE PLKNVVDKSC
PRGVIRVEES FRSGSRPPLR ARDFMATNPE HLEILKKMGV SLIHLKDGRV QLVQHAIQAA
SSIDAEDGLR FMQEMIELSS QQQKEQQLPP RAVQIVSHPF FGRVVLTAGP AQFGLDLSKH
KETRGFVASS KPYNGCSELT NPEAVMGKIA LLVRGQCMFA EKARNIQNAG AIGGIVIDDN
EGSSSDTAPL FQMAGDGKDT DDIKIPMLFL FSKEGSIILD AIREYEEVEV LLSDKAKDRD
PETENESQNQ SAEQTTPGSQ EVDLVAGASP EDSPLNSHPE ASSPAAADSA AASASPSQQN
SDPTENHGPP GFDGECTYLD EDEEQSETEE DSSPNVSWGK EAQPMHPILA NWNEDMEAIE
MMEKEMKKRE MMKGEL
//
