ID H0ZIL0_TAEGU Unreviewed; 1149 AA.
AC H0ZIL0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN Name=MAN2A2 {ECO:0000313|Ensembl:ENSTGUP00000010427.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000010427.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000010427.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000010427.2}
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; H0ZIL0; -.
DR STRING; 59729.ENSTGUP00000010427; -.
DR Ensembl; ENSTGUT00000010537.2; ENSTGUP00000010427.2; ENSTGUG00000010087.2.
DR GeneTree; ENSGT01030000234638; -.
DR HOGENOM; CLU_004690_1_0_1; -.
DR InParanoid; H0ZIL0; -.
DR OMA; GHQWLKY; -.
DR TreeFam; TF313152; -.
DR Proteomes; UP000007754; Chromosome 10.
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:0016799; F:hydrolase activity, hydrolyzing N-glycosyl compounds; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR CDD; cd11667; GH38N_Man2A2; 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: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|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:UP000007754};
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 501..587
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1149 AA; 129636 MW; 38A03FF07FAFEE01 CRC64;
MKLKKQVTVC GAAIFCVAVF SLYLMLDRVQ HDPTRHQSGG NFPRSQISVL QNRIEQLEQL
LEENHEIISH IKDSVLELTA HAEGQPALPQ HPLNGSWVLP PESRPSFLSV SPQDCQFALG
GKGQSPDLQM LAVYSLLPFD NQDGGVWKQG FDITYEPNEW DTEPLQVFVV PHSHNDPGWI
KTFDKYYYDQ TQHILNSMVL KMQEDPRRRF IWSEISFFSK WWDNISAQKQ AAVRRLVGNG
QLEMVTGGWV MPDEANSHYF AMIDQLIEGH QWLEKNIGVT PRSGWAVDPF GYSSTMPYLL
KRSNLTAMLI QRVHYAIKKH FAATQNLEFM WRQAWDPDAS TDIFCHMMPF YSYDVPHTCG
PDPKICCQFD FKRLPGGRIN CPWKVPPRAI TDANVAERAQ LLLDQYRKKS KLYRSKVLLV
PLGDDFRYDK PQEWDAQFLN YQRIFDFLNS RPDLHVQAQF GTLSDYFDAL YKKVGIVPGM
RPPGFPVLTG DFFSYADRED HYWTGYFTSR PFYKSLDRVL EAHLRGAEIL YSLALAHARH
AGADGRYPLS DYALLSNARR NLGLFQHHDA IAGTAKEAVA VDYGVRLLHS LTNLKRVIIN
AAHYLVLGDK DTYHHDPAAP FLGMDETRSS QDSLPERTVV KLGTSPRFLV VFNPLEQERL
SVVPVLVDSP HVRVLSEEGQ PLPSQLSAVW NSATDVVPNV YQVSVLARLP ALGLRVLQLH
KSSDGHATPR SSTRLYLHGR DMAVHKPEAV PLHVFPAAAA DFCLENQHLQ ACFVGRTGLL
QSLRPAGEEQ AHRVSSEFLV YGTRTSKDKS GAYLFLPDGE AKPYAPKDPP VVRVMEGPLF
SEVASYYQHV QTVVRLYNVP GVEGLSLDVS CLVDIRDHIN KELALRFSTD IESDDTFFTD
LNGFQIQPRR YQQKLPLQAN FYPMPAMAYI QDMQSRLTLL TAQALGVTSL HSGQLEVILD
RRLMQDDNRG LGQGLKDNKR TCNRFRLLLE RRSTANKVQD ERPISFPSLL SHITSVHQNA
EALVMPVALE KPALPALRSF VPLATTLPCD FHILNLRMLQ AEDESLPSAE AALILHRKGF
DCSLEAKNLG FNCTTSQGKL ALGGLFQGLE LGSLQPTSLT LMYPLGTASN STNIHLDPME
IATFRIRLG
//
