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Database: UniProt
Entry: A0A3B4TRI5_SERDU
LinkDB: A0A3B4TRI5_SERDU
Original site: A0A3B4TRI5_SERDU 
ID   A0A3B4TRI5_SERDU        Unreviewed;       802 AA.
AC   A0A3B4TRI5;
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};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000008889.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000008889.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A3B4TRI5; -.
DR   Ensembl; ENSSDUT00000009065.1; ENSSDUP00000008889.1; ENSSDUG00000006456.1.
DR   GeneTree; ENSGT00940000165673; -.
DR   Proteomes; UP000261420; 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}.
FT   DOMAIN          599..692
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   REGION          758..802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        784..802
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        88
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   ACT_SITE        235
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   ACT_SITE        329
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   ACT_SITE        347
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT   BINDING         433
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601382-2"
SQ   SEQUENCE   802 AA;  90171 MW;  E8AD806A9908A1F8 CRC64;
     MFDHAYGSYM KYAYPADELM PLSCRGRVRG LEPNRGDIDD SLGKFSLTLI DTLDTLVVLN
     KLDEFEDAVR KAVKDVRLDN DVVVSVFETN IRVLGGLLGA HVMADLLRQR GDRMQWYQDE
     LLHMAKELGH RLLPAFNTTS GLPYPKVNLR YGVLNPLSRT GTESDTCTAC AGTMILEFAA
     LSRMSGESVF EEHARKAMDV LWDRRQRGSD LVGTVINIHN GEWVRRDSGV GAGIDSYYEY
     LMKAYILLGD NVFLERFNIH YSAIMKYISQ PPLLLNVHMH NPTVSVRSWM DSLLAFFPGL
     QVLRGDLKPA IETHEMLYQV TKQHKFLPEA FTTEFRVHWG QHLLRPEFAE STYYLYKATG
     DPYYLRVGQS IVEKLNAYAR VPCGFAAVQD VRTGAHEDRM DSFFLAEMFK YLYLLFSEKS
     QLPIDIDDYI FTTEAHLLPV SLSTTKPPSY KFCLTVEEDL FTHSCPSTET LFPNNPSFAK
     TIRDSYKYLT GVGRAFRPLP VREIELPLHD NGMEPVEFLK SMGISLTPLN ELFSKYESLQ
     EHKGVYRVKL VAEVSQTAEE EEVVPHVVQL ISPPFLGRTV LTAGPAKFGM DLSKQEHGVK
     GSIVKASPYT ACGPIDNTVE LKGRIALALR GDCMFAAKAR RLQEAGAIGV IFIDHREGSN
     SEETPLFQMV GDGDSTEDIT LALVFLFSRE GAVLTAALEE HHNVDVLLLP KERQLGHEKH
     VGMNIKLRLA EEGELEEGAA RGPTLEFVLE KDEVLLQEEE LGEERQSQQQ QKFCAKATEN
     DRTEPCSADS SQTPNSGPNT NP
//
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