ID   K9IVI4_PIG              Unreviewed;       933 AA.
AC   K9IVI4;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=alpha-1,2-Mannosidase {ECO:0000256|RuleBase:RU361193};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361193};
GN   Name=EDEM3 {ECO:0000313|EMBL:JAA53648.1};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|EMBL:JAA53648.1};
RN   [1] {ECO:0000313|EMBL:JAA53648.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Dawson H.D., Chen C.T.;
RT   "Global Gene Expression Profiling of Alveolar Macrophages by Deep
RT   Sequencing.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:HDA93547.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30723633; DOI=.7717/peerj.6374;
RA   Gilbert D.G.;
RT   "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL   PeerJ 7:E6374-E6374(2019).
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; DQIR01138071; HDA93547.1; -; Transcribed_RNA.
DR   EMBL; GACC01000159; JAA53648.1; -; mRNA.
DR   RefSeq; XP_013835385.1; XM_013979931.1.
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   2: Evidence at transcript level;
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}.
FT   DOMAIN          688..774
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   REGION          791..908
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        808..824
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        884..906
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"
SQ   SEQUENCE   933 AA;  104429 MW;  F3B96B874FE049A1 CRC64;
     MSGAGGGRGC GSRVPQRAPW NLVAATAALC LVSATSVWTA GAAPMSREEK QRLGNQVLEM
     FDHAYGNYME HAYPADELMP LTCRGRVRGQ EPSRGDVDDA LGKFSLTLID SLDTLVVLNK
     TKEFEDAVRK 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
     IIFDVEDYIF TTEAHLLPLW LSTTNQSISK KNTTSDYTEL 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 KEGSIILDAM
     REYEEVEVLL SDKAKDRDPD MENEEQPSSE NDFQNQSAEQ MASGSQEVDL VDEESPEEGS
     SNSHPDSSSP ADRDSAAGGP PSEQNSHPTE SPEPTRLDGE CTDLDNQLEQ QSDTEEDSNP
     NVSWGKKVQP IDSILADWNE DIEAFEMMEK DEL
//