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
//