ID A0A3P9Q1H0_POERE Unreviewed; 1120 AA.
AC A0A3P9Q1H0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN Name=MAN2A2 {ECO:0000313|Ensembl:ENSPREP00000027910.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000027910.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000027910.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000027910.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361199};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU361199};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792, ECO:0000256|RuleBase:RU361199}.
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DR STRING; 8081.ENSPREP00000027910; -.
DR Ensembl; ENSPRET00000028217.1; ENSPREP00000027910.1; ENSPREG00000018857.1.
DR GeneTree; ENSGT01030000234638; -.
DR OMA; GEMEIMQ; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000018857; Expressed in caudal fin and 1 other cell type or tissue.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004559; F:alpha-mannosidase activity; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR Gene3D; 1.20.1270.50; Glycoside hydrolase family 38, central domain; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR011682; Glyco_hydro_38_C.
DR InterPro; IPR015341; Glyco_hydro_38_cen.
DR InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR InterPro; IPR000602; Glyco_hydro_38_N.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR InterPro; IPR013780; Glyco_hydro_b.
DR PANTHER; PTHR11607; ALPHA-MANNOSIDASE; 1.
DR PANTHER; PTHR11607:SF57; ALPHA-MANNOSIDASE 2X; 1.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 1.
DR Pfam; PF01074; Glyco_hydro_38N; 1.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361199};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361199};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361199};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 475..561
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1120 AA; 127275 MW; 34B4D8F0436A059A CRC64;
MKLRKQVTVC GGAIFCVAVF SLYLMLDRVQ HDPARRQNGG NFPRSQISVL QNRIEQLEQL
LEENHQIISH IKDSVMELTD TGAVSPSGHL PFRSANGSWV LPFDGRPTFL ALKPQDCQFT
VGTRAQTDVQ VNVPLFKIRS ICVSLGPPVL LGWVKTFDKY FTDQTQHILN NMVVKLAEDS
RRKFIWSEIS FFAKWWETAD VYKQEAMRKL ILGGQLEMVT GGWVMTDEAN SHYFAMIDQL
IEGHQWLERN LGITPQSGWA VDPFGHSATM PYLLKRANVT SMLIQRIHYS IKKHFSSTRS
LEFMWRQAWD TGSSTDIFCH MMPFYSYDVP HTCGPDPKIC CQFDFKRLPG GRINCPWKVP
PKSVVEANVA ERAQLLLDQY RKKSKLYRSK VLLVPLGDDF RYDKAQEWDQ QYINYQKLFD
YMNSHPELHV QAQFGTLTEY FTALYKAYGV PQGSRPGDFP VLSGDFFAYA DREDHYWTGY
YTSRPFYKSL DRVIESHLRG AEILYSLAVA NARHAGMEGR YPVTDYALLV DARRSVGLFQ
HHDAIAGTAK ENVALDYGTK LLRALIGLKR VIINAAHFLV MKNKEFYRFY QTEPFLETDD
RRATQDSLPQ RTLIELDPAR PRYLVLFNPI EQERLCTVTV LVNTVRVRVL TEDGQTLPVQ
LSAQWSSATQ MSATFMVRLP PLGLAVFHLY DSADSPMTIR SDTLLRLSGR SVSARALDPL
PVRSQPADAQ TFYISTQTLT LGFSGTTGLL ESIKCKDDPQ EIKVQMQFMI YGTSPSKDKS
GAYLFLPDGK PKPYNQKEPP AVRVVEGPLF SEVVAQYQHF QQTVRIHNVP GVYGLSVDIT
ILVDIRDQTN KELSMRLVTS IQNGDVFYTD LNGYQIQPRR FYQKLPLQGN FYPMSSQAYI
QDSHHRLTLH TAQALGVSSL DSGQLEVIMD RRLMQDDNRG LGQGLKDNKK TANRFRLLLE
RRSIDNKMMD SATTSFPSMV SHXTSSLLNH EVLALPVLPK RRGIPPLQTF APLKTVIPCD
VHLLNLRSIQ TQKDPESPSP YTALLLHRLA INCGFEGQNL GFNCSTTQGR LSVSNLFKNV
DLQLLQPMSL TLMHSSKPLA NDSIISLEPM EISAFKLKLH
//