ID A0A132AI33_SARSC Unreviewed; 399 AA.
AC A0A132AI33;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Alpha-1,3/1,6-mannosyltransferase ALG2 {ECO:0000256|RuleBase:RU367136};
DE EC=2.4.1.132 {ECO:0000256|RuleBase:RU367136};
DE EC=2.4.1.257 {ECO:0000256|RuleBase:RU367136};
DE AltName: Full=GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase {ECO:0000256|RuleBase:RU367136};
GN ORFNames=QR98_0087760 {ECO:0000313|EMBL:KPM10225.1}, SSS_5542
GN {ECO:0000313|EMBL:KAF7491866.1};
OS Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC Sarcoptidae; Sarcoptinae; Sarcoptes.
OX NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM10225.1, ECO:0000313|Proteomes:UP000616769};
RN [1] {ECO:0000313|EMBL:KPM10225.1, ECO:0000313|Proteomes:UP000616769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM10225.1};
RX PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT "Draft genome of the scabies mite.";
RL Parasit. Vectors 8:585-585(2015).
RN [2] {ECO:0000313|Proteomes:UP000070412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=33001992;
RA Korhonen P.K., Gasser R.B., Ma G., Wang T., Stroehlein A.J., Young N.D.,
RA Ang C.S., Fernando D.D., Lu H.C., Taylor S., Reynolds S.L., Mofiz E.,
RA Najaraj S.H., Gowda H., Madugundu A., Renuse S., Holt D., Pandey A.,
RA Papenfuss A.T., Fischer K.;
RT "High-quality nuclear genome for Sarcoptes scabiei-A critical resource for
RT a neglected parasite.";
RL PLoS Negl. Trop. Dis. 14:0-0(2020).
RN [3] {ECO:0000313|EMBL:KAF7491866.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SSS_KF_BRIS2020 {ECO:0000313|EMBL:KAF7491866.1};
RA Korhonen P.K.K., Guangxu M.G., Wang T.W., Stroehlein A.J.S., Young N.D.,
RA Ang C.-S.A., Fernando D.W.F., Lu H.L., Taylor S.T., Ehtesham M.E.M.,
RA Najaraj S.H.N., Harsha G.H.G., Madugundu A.M., Renuse S.R., Holt D.H.,
RA Pandey A.P., Papenfuss A.P., Gasser R.B.G., Fischer K.F.;
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EnsemblMetazoa:KAF7491866.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2022) to UniProtKB.
CC -!- FUNCTION: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and
CC Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol
CC diphosphate. {ECO:0000256|ARBA:ARBA00003142,
CC ECO:0000256|RuleBase:RU367136}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc-diphosphodolichol + GDP + H(+); Xref=Rhea:RHEA:29519,
CC Rhea:RHEA-COMP:12624, Rhea:RHEA-COMP:12626, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:132510,
CC ChEBI:CHEBI:132511; EC=2.4.1.257;
CC Evidence={ECO:0000256|ARBA:ARBA00001514,
CC ECO:0000256|RuleBase:RU367136};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-beta-D-
CC Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol +
CC GDP + H(+); Xref=Rhea:RHEA:29515, Rhea:RHEA-COMP:11044, Rhea:RHEA-
CC COMP:12624, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:58472, ChEBI:CHEBI:132510; EC=2.4.1.132;
CC Evidence={ECO:0000256|ARBA:ARBA00001253,
CC ECO:0000256|RuleBase:RU367136};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU367136}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU367136}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC {ECO:0000256|RuleBase:RU367136}.
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DR EMBL; WVUK01000058; KAF7491866.1; -; Genomic_DNA.
DR EMBL; JXLN01014776; KPM10225.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A132AI33; -.
DR EnsemblMetazoa; SSS_5542s_mrna; KAF7491866.1; SSS_5542.
DR VEuPathDB; VectorBase:SSCA008033; -.
DR OMA; ENVQYHR; -.
DR OrthoDB; 1377at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000070412; Unassembled WGS sequence.
DR Proteomes; UP000616769; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004378; F:GDP-Man:Man1GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0102704; F:GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR CDD; cd03805; GT4_ALG2-like; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR027054; ALG2.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR PANTHER; PTHR45918; ALPHA-1,3/1,6-MANNOSYLTRANSFERASE ALG2; 1.
DR PANTHER; PTHR45918:SF1; ALPHA-1,3_1,6-MANNOSYLTRANSFERASE ALG2; 1.
DR Pfam; PF13439; Glyco_transf_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|RuleBase:RU367136,
KW ECO:0000313|EMBL:KAF7491866.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000070412};
KW Transferase {ECO:0000256|RuleBase:RU367136, ECO:0000313|EMBL:KAF7491866.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 13..172
FT /note="Glycosyltransferase subfamily 4-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13439"
FT DOMAIN 197..373
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
SQ SEQUENCE 399 AA; 46118 MW; 984D11F2D37F1E45 CRC64;
MLSIAFLHPD LGIGGAERLI IDCAIALKDS GHLVSIFTSH HDLNHCFEET KDGRINVVVA
GDWLPNSSFG HFKAFWAYLR MIYLTFFMVL NYRFDCIICD QVPSGIPIIK ASKQKCLFYC
HYPDQLLAKH DSLLKKIYRR PIDWFEEWTI NFADQVLVNS HFTQQVFRKT FKRFGSKIIT
EVLYPCVKFH SSHSEIDKND NKDDEYLSYF LSINRFERKK NLELAIEAME VLQNKLDQKS
SKKSIHLVIA GGYDLNNIEN IDYYEELIEK VKRSNLKDKV TFVRNLTDDQ KQSLLKRCIA
VIYTPENEHF GIVPLEAMYM KRPVIAANSG GPKETIIDEA TGFLCQTTPV SFAEAMMKFV
EDESLSNTMG TKAFVHVVNK FNYKNFKNDL NKIISKLVQ
//
