ID W5JT02_ANODA Unreviewed; 799 AA.
AC W5JT02;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=alpha-1,2-Mannosidase {ECO:0000256|RuleBase:RU361193};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361193};
GN ORFNames=AND_000922 {ECO:0000313|EMBL:ETN67271.1};
OS Anopheles darlingi (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43151 {ECO:0000313|EMBL:ETN67271.1};
RN [1] {ECO:0000313|EMBL:ETN67271.1, ECO:0000313|Proteomes:UP000000673}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20920257; DOI=10.1186/1471-2164-11-529;
RA Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.;
RT "Combination of measures distinguishes pre-miRNAs from other stem-loops in
RT the genome of the newly sequenced Anopheles darlingi.";
RL BMC Genomics 11:529-529(2010).
RN [2] {ECO:0000313|EMBL:ETN67271.1}
RP NUCLEOTIDE SEQUENCE.
RA Almeida L.G., Nicolas M.F., Souza R.C., Vasconcelos A.T.R.;
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ETN67271.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23761445;
RA Marinotti O., Cerqueira G.C., de Almeida L.G., Ferro M.I., Loreto E.L.,
RA Zaha A., Teixeira S.M., Wespiser A.R., Almeida E Silva A.,
RA Schlindwein A.D., Pacheco A.C., Silva A.L., Graveley B.R., Walenz B.P.,
RA Lima Bde A., Ribeiro C.A., Nunes-Silva C.G., de Carvalho C.R., Soares C.M.,
RA de Menezes C.B., Matiolli C., Caffrey D., Araujo D.A., de Oliveira D.M.,
RA Golenbock D., Grisard E.C., Fantinatti-Garboggini F., de Carvalho F.M.,
RA Barcellos F.G., Prosdocimi F., May G., Azevedo Junior G.M., Guimaraes G.M.,
RA Goldman G.H., Padilha I.Q., Batista Jda S., Ferro J.A., Ribeiro J.M.,
RA Fietto J.L., Dabbas K.M., Cerdeira L., Agnez-Lima L.F., Brocchi M.,
RA de Carvalho M.O., Teixeira Mde M., Diniz Maia Mde M., Goldman M.H.,
RA Cruz Schneider M.P., Felipe M.S., Hungria M., Nicolas M.F., Pereira M.,
RA Montes M.A., Cantao M.E., Vincentz M., Rafael M.S., Silverman N.,
RA Stoco P.H., Souza R.C., Vicentini R., Gazzinelli R.T., Neves Rde O.,
RA Silva R., Astolfi-Filho S., Maciel T.E., Urmenyi T.P., Tadei W.P.,
RA Camargo E.P., de Vasconcelos A.T.;
RT "The genome of Anopheles darlingi, the main neotropical malaria vector.";
RL Nucleic Acids Res. 41:7387-7400(2013).
RN [4] {ECO:0000313|EnsemblMetazoa:ADAC000922-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) 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 EMBL; ADMH02000240; ETN67271.1; -; Genomic_DNA.
DR AlphaFoldDB; W5JT02; -.
DR STRING; 43151.W5JT02; -.
DR EnsemblMetazoa; ADAC000922-RA; ADAC000922-PA; ADAC000922.
DR VEuPathDB; VectorBase:ADAC000922; -.
DR VEuPathDB; VectorBase:ADAR2_003603; -.
DR eggNOG; KOG2430; Eukaryota.
DR HOGENOM; CLU_003818_4_1_1; -.
DR OMA; NYVCANP; -.
DR OrthoDB; 942598at2759; -.
DR Proteomes; UP000000673; Unassembled WGS sequence.
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; ER DEGRADATION-ENHANCING ALPHA-MANNOSIDASE-LIKE PROTEIN 2; 1.
DR PANTHER; PTHR45679:SF2; ER DEGRADATION-ENHANCING ALPHA-MANNOSIDASE-LIKE PROTEIN 3; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000673}.
FT DOMAIN 667..755
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT REGION 776..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 149
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 294
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 388
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT ACT_SITE 406
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-1"
FT BINDING 492
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR601382-2"
SQ SEQUENCE 799 AA; 90389 MW; 7E0DE00FE319A278 CRC64;
MRTLASVNRW RRRPEMVFLL VVGLTVIFLA MVTMAEQIPT VPTQIHMSNK ERNELKEEAR
EMFYHAYRAY MDNAYPADEL MPLSCTGRYR GVTPSRGDLD DTLGNFSMTL VDTLDTLVVL
GDLEEFESAV KLVIKDVKFD NDIIVSVFET NIRMIGGLLS GHILAEYVQK QADVMSWYRG
ELLEMAKDLG YRLLPAFNTS TGIPHARVNL KHGMKVEALR HSRETCTACA GTILLEFAAL
SRLSGEPIFE VKAHAAMDAL WKMRHRSSEL MGTVLNVHSG DWIRRESGVG AGIDSYYEYC
LKSYILLGDE RYLARFNRHY NAIMKYISQG PMLLDVQMHR PHTKTRNFMD ALLAFWPGLQ
VLSGDLKPAV QTHEMLYQVM QMHTFIPEAF TFDFQVHWGQ HHLRPEFIES TYFLYRATGD
HYYLHAGKKA LKALQQHARV PCGYAAVNDV RTGKHEDRMD SYVLSETFKY LFLLFSDPAD
LILNIEDFIF TTEAHLLPLT LGVLGNHTMG VRDQEDQVHM LDYMRSCPSP NKLFPETVRR
PLRDLVTGVC PRISSPKRLR ASDFQASNAD HLRTVYDMGI TMVSLGEGKV QLLHSFYNAK
SPEDAERGLI FMQEMVELSK SNAIPNTQLQ AVAFKGKGDT DLHVLEAGPS HFGMELTKDM
SVVQQAVYAQ PIKLCSALKN AKEVRDKIVI MERGECTFVD KARRAQSAGA VAAIVFDNTP
NTSINNQQMF AMSGDGKDDV QIPVVFLFTK EAEQLMAAIK QQPTVELTLM SVSGLKERLE
RERADTTKTD TKSESKATP
//
