ID G3PS01_GASAC Unreviewed; 1151 AA.
AC G3PS01;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000020387.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000020387.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000020387.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 AlphaFoldDB; G3PS01; -.
DR STRING; 69293.ENSGACP00000020387; -.
DR Ensembl; ENSGACT00000020426.1; ENSGACP00000020387.1; ENSGACG00000015458.1.
DR eggNOG; KOG1958; Eukaryota.
DR GeneTree; ENSGT01030000234638; -.
DR InParanoid; G3PS01; -.
DR OMA; HPPRIAQ; -.
DR TreeFam; TF313152; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000015458; Expressed in liver and 11 other cell types or tissues.
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 CDD; cd10809; GH38N_AMII_GMII_SfManIII_like; 1.
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:SF70; ALPHA-MANNOSIDASE 2; 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|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:UP000007635};
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..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 486..577
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1151 AA; 130550 MW; DEDF413AEADF17AD CRC64;
SKMKRKLFPL LVGGVFCVVV MSLYRMLEMM QGAELQHLEA PAGQDFYRLQ QQIDKLERLL
SANNRLVVTL RDSLLHRQAP QGGGGAVNVS AGSAHSPADA PPGCRLAQGM KGRADGVQLL
DVYNLLPFDN ADGGAWKQGF EISYRGNEWD EQPLEVLLVP HSHNDPGWLK TFENYYQDQT
RHILNNMLIK LTEDSRRKMI WAEISYFSKW WNDIDEQKRE MVKRLVGAGQ LELVTGGWVM
ADEANSHYFA LLDQLIEGHQ WIQRHLGVRP RSGWAVDPFG HSPSMAYLLK GAGLSNMVIQ
RVHYAVKKHF AQQQTLEFLW RQSWDSSPRS DITCHMMPFY SYDVPHTCGP NPAVCCQFDF
HRLPGGRAMC PWKKSPQPIT EQNVQERALL LLDQYRQKSR LFRSHVLLVP LGDDFRFVEA
SEWDAQSGNY QKLFDYFDQH PELHVKARFG TLSDYFEALH RRLDAMGTAL PALRGDFFTY
ADRDDHYWSG YFTSRPFYKR LDRTLEATLR ATEILFSLAL AEMRRFRGDG LLVADFPVRE
HFRRLTAGRR SLALFQHHDG ITGTSRDPVV VDYGTRLFHS IMNLRQVLQS SAHWLLLLDK
SQYYHNQSKP FMQLDDVISA HNALPLKTPL ALSNEPRSLI IFNPTEQLRS SVISVVVDSP
DADVVDATTG QPMAAQISAV WAEPTQASTE QFQLDFVAEL PPLSLVVYHV TKASFGSAHR
ARYTFHRRGN PPAVQSEHFQ VSGLERPEAD APLSLSNKHI SIWSSPETGL LQKLRLLPGP
VREVQVQFLW YGTQRNQDKS GAYLFLPGEE GAQLYSSSEP PLVRVSRGPV FSDITSCFRH
FTHTVRLYHL DGHAGRSLEI SNMVDIRSEF NRELVMRLVS DVANGNRFYS DLNGFQMQQR
RTLQKLPLQA NFYPMTSAAF LQDATSRMSL LSAQSQAVAS LRPGELEVVL DRRLQQDDNR
GLGQGVTDNK LTASLYHLLL EDRRGGAEEV GGASVEHMSL LAHLTSLSLN HLPITMVAPS
DSQVPKLRPF LPLRSSLPCD VHLLNLRTLE DSQDKQESDS PSQEVALLLH RKGFDCSSAP
QAPLQCTWSA QEEVDLDRLF SPLRFHSVRR SGLTLLREDD QPESARQPAP PHVARLRPME
ISAFRVELAW T
//