ID A0A3B5ARE9_9TELE Unreviewed; 872 AA.
AC A0A3B5ARE9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=alpha-1,2-Mannosidase {ECO:0000256|RuleBase:RU361193};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361193};
GN Name=LOC103371381 {ECO:0000313|RefSeq:XP_008298914.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000024028.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000024028.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_008298914.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_008298914.1; XM_008300692.1.
DR AlphaFoldDB; A0A3B5ARE9; -.
DR STRING; 144197.ENSSPAP00000024028; -.
DR Ensembl; ENSSPAT00000024421.1; ENSSPAP00000024028.1; ENSSPAG00000018150.1.
DR GeneID; 103371381; -.
DR GeneTree; ENSGT00940000165673; -.
DR OrthoDB; 942598at2759; -.
DR Proteomes; UP000261400; Unplaced.
DR Proteomes; UP000694891; Unplaced.
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 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; IPR001382; Glyco_hydro_47.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR036026; Seven-hairpin_glycosidases.
DR PANTHER; PTHR45679:SF1; ALPHA-1,2-MANNOSIDASE; 1.
DR PANTHER; PTHR45679; ER DEGRADATION-ENHANCING ALPHA-MANNOSIDASE-LIKE PROTEIN 2; 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:UP000694891};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..36
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 37..872
FT /note="alpha-1,2-Mannosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041074664"
FT DOMAIN 661..754
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT REGION 827..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 144
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 291
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 385
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 403
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT BINDING 489
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-2"
SQ SEQUENCE 872 AA; 97205 MW; 86A7991DE6E12FDD CRC64;
MRRSGGKLCR SLGPSSATGM ILKTLLITGL LGWAKCQESQ SMTEEEMTVI RHQIIEMFDH
AYGSYMKYAY PADELMPLSC RGRVRGQEPN RGDIDDSLGK FSLTLIDTLD TLVVLNKLDE
FEDAVRKAVK DVRLDNDVVV SVFETNIRVL GGLLGGHVMA DLLRQRGDRM QWYRDELLHM
AKELGHRLLP AFNTTSGLPY PKVNLRYGVL NPLSRTGTES DTCTACAGTM ILEFAALSRL
SGESVFEEHA RKALDVLWER RQRGSDLVGT VINIHNGEWV RRDSGVGAGI DSYYEYLMKA
YILLGDNVFL ERFNVHYSAI MKYISQPPLL LNVHMHNPTV SVRSWMDSLL AFFPGLQVLR
GDLKPAIETH EMLYQVTKQH KFLPEAFTTE FRVHWGQHLL RPEFAESTYY LYKATGDPYY
LRVGQSIVEK LNAYARVPCG FAAVQDVRTG THEDRMDSFF LAEMFKYLYL LFSEKSQLPI
NIDDYIFTTE AHLLPVSLST TQPPCHGNNT ETVPVSQEED LFTHSCPSTE TLFPNNPSFA
KTIRDSYKYL TGVGRAFHPL PVREIELPLH DNGMEPVEFL KSMGISLTPL NEVTAGDTGI
LKEHKGVYRV KLVAEVSQVP EEEVVVPHVV QLISPPFLGR TVLTAGPAKF GMDLTKQEHG
VKGSIVKASP YTACGPIDNA AELKGHIALA LRGDCMFAAK ARWLQEAGAI GVVFIDHREG
SNSEETPLFQ MVGDGDSTED ITLPLVFLFS REGAVLTGAL EKHRNVDVLL LPKERQLGHD
KAEKPVSMNI KLRLAEEGEL EDGAAGGPTL ELVLENDEVL LKEAVEEELR GNRQSQQQHH
FCTKATEDDR TEPCSADSSA ASNSNSGPDT NP
//
