ID A0A2U3Z4M8_LEPWE Unreviewed; 796 AA.
AC A0A2U3Z4M8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN Name=LOC102748436 {ECO:0000313|RefSeq:XP_006750698.1};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006750698.1};
RN [1] {ECO:0000313|RefSeq:XP_006750698.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006750698.1};
RG RefSeq;
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 RefSeq; XP_006750698.1; XM_006750635.2.
DR AlphaFoldDB; A0A2U3Z4M8; -.
DR STRING; 9713.A0A2U3Z4M8; -.
DR GeneID; 102748436; -.
DR KEGG; lww:102748436; -.
DR OrthoDB; 5474711at2759; -.
DR Proteomes; UP000245341; Unplaced.
DR GO; GO:0004559; F:alpha-mannosidase activity; IEA:UniProtKB-EC.
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; 2.60.40.1360; -; 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; 2.
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 InterPro; IPR048534; Man2a1-like_dom.
DR PANTHER; PTHR11607; ALPHA-MANNOSIDASE; 1.
DR PANTHER; PTHR11607:SF3; LYSOSOMAL ALPHA-MANNOSIDASE; 1.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 1.
DR Pfam; PF01074; Glyco_hydro_38N; 1.
DR Pfam; PF21260; Laman-like_dom; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361199};
KW Hydrolase {ECO:0000256|RuleBase:RU361199};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361199};
KW Reference proteome {ECO:0000313|Proteomes:UP000245341};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT DOMAIN 177..256
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 796 AA; 89582 MW; 97847C16A5B1CA7B CRC64;
MGFDGFFFGR LDYQDKGVRK KKQEMEQVWR ASASLEPPVA DLFTSVLPNI YNPPEKLCWD
TLCADKPFVE DPRSPEYNAK ELVDYFLQLA TAQGQNYRTN HTIMTMGSDF QYENANMWFK
NLDRLIELVN AQQQANGSRV NVLYSTPACY LWELNKANLT WSVKQDDFFP YADGPHKFWT
GYFSSRPALK RYERLSYNFL QVCNQLEALA GPAANVGPYG SGDSAPLNEA MAVLQHHDAV
SGTSRQHVAN DYARQLAAGW GPCEVLLSNA LARLSGSKED FMYCRNLNIS VCPLSQTAKS
FQVTIYNPLG RKVDWMVRLP VSDHIFDVRD PNGTIVPSDV VRLPSSDSSD LLFSASVPAL
GFSVYSVTQV PGRSPHAHNR QPRSQKSWTH GLAIQNEYLQ ARFDPDTGLL VELENLDQNL
LLPVRQAFYW YNASVGDNLS TQVSGAYIFR PNRQEPLIVS HWAQTHVVKT PLVQEVHQNF
SAWCSQVIRL YPGQRHLELE WTVGPIPVGD GWGKEIISRF DTVLETKGLF YTDSNGREIL
ERRRDYRPTW KLNQTEPVAG NYYPVNSRIY IRDGKMQLTV LTDRSQGGSS LKDGSMELMV
HRRLLKDDGR GVGEPLLEEG LGLWVRGRHL VLLDKAPTAA TRHRLQAEKE LLAPQVVLAP
GGGAPYHPGV APRKQFSGLR RELPPSVHLL TLARWDRTTL LLRLEHQFAV GEGSGNLSSP
VTLDLRDLFS AFTITYLQET TLAANQLRAS ASRLKWTPAT GPTAQPSPSR LDPAAITLQP
MEIRTFLALV QWKEHG
//