ID D2HFM3_AILME Unreviewed; 932 AA.
AC D2HFM3;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=alpha-1,2-Mannosidase {ECO:0000256|RuleBase:RU361193};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361193};
DE Flags: Fragment;
GN ORFNames=PANDA_009702 {ECO:0000313|EMBL:EFB29458.1};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|EMBL:EFB29458.1};
RN [1] {ECO:0000313|EMBL:EFB29458.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
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; GL192792; EFB29458.1; -; Genomic_DNA.
DR RefSeq; XP_002920894.1; XM_002920848.3.
DR AlphaFoldDB; D2HFM3; -.
DR STRING; 9646.ENSAMEP00000014207; -.
DR GeneID; 100478666; -.
DR KEGG; aml:100478666; -.
DR CTD; 80267; -.
DR eggNOG; KOG2430; Eukaryota.
DR InParanoid; D2HFM3; -.
DR OMA; NYVCANP; -.
DR OrthoDB; 942598at2759; -.
DR TreeFam; TF300807; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601382-2};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 688..774
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT REGION 791..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 147
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 294
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 388
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 406
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT BINDING 492
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-2"
FT NON_TER 932
FT /evidence="ECO:0000313|EMBL:EFB29458.1"
SQ SEQUENCE 932 AA; 104431 MW; 942D87438CC72FA4 CRC64;
MSEAGGGRGC GSSVPQRAPW SLVAATAAFC LVSATSVWTA GAAPMSREER QKLGNQVLEM
FDHAYGNYME HAYPADELMP LTCRGRVRGQ EPSRGDVDDA LGKFSLTLID SLDTLVVLNK
TKEFEDAVKK VLRDVNLDND VVVSVFETNI RVLGGLLGGH SLAIMLKEKG EYMQWYNDEL
LQMAKQLGYK LLPAFNTTSG LPYPRINLKF GIRKPEARTG TETDTCTACA GTLILEFAAL
SRFTGATIFE EYARKALDFL WEKRQRSSNL VGVTINIHTG DWVRKDSGVG AGIDSYYEYL
LKAYVLLGDD SFLERFNTHY DAIMRYISQP PLLLDVHIHK PMLNARTWMD ALLAFFPGLQ
VLKGDIRPAI ETHEMLYQVI KKHNFLPEAF TTDFRVHWAQ HPLRPEFAES TYFLYKATGD
PYYLEVGKTL IENLNKYARV PCGFAAMKDV RTGSHEDRMD SFFLAEMFKY LYLLFADKED
IIFDIEDYIF TTEAHLLPLW LSTTNQSISK KNTTSEYTEL DDSNFDWTCP NTQILFPNDP
LYAQSIREPL KNVVDKSCPR GIIRVEESFR SGAKPPLRAR DFMATNPEHL EILKKMGVSL
IHLKDGRVQL VQHAIQAASS IDAEDGLRFM QEMIELSSQQ QKEQQLPPRA VQIVSHPFFG
RVVLTAGPAQ FGLDLSKHKE TRGFVASSKP YNGCSELTNP EAVMGKIALI QRGQCMFAEK
ARNIQNAGAI GGIVIDDNEG SSSDTAPLFQ MAGDGKDTDD IKIPMLFLFS KEGSIILDAI
REYEEVEVLL SDKAKDRDPE MENEEQPSSE NDSQNQSAEQ ITSSSQEVDL VDQESPEESS
LNSEPESSPA DTDNAASVSA SEQNSHPKEN RETANLDGEC TDLDNQLQEQ SETEEDSSPN
VSWGKKVQPI DSILADWNED IEAFEMMEKD EL
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