ID A0A016TSW7_9BILA Unreviewed; 184 AA.
AC A0A016TSW7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Mannosyltransferase {ECO:0000256|RuleBase:RU363075};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU363075};
GN Name=Acey_s0078.g1188 {ECO:0000313|EMBL:EYC06094.1};
GN ORFNames=Y032_0078g1188 {ECO:0000313|EMBL:EYC06094.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC06094.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC (1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate +
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-
CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol + H(+); Xref=Rhea:RHEA:29535, Rhea:RHEA-COMP:9517,
CC Rhea:RHEA-COMP:9527, Rhea:RHEA-COMP:12629, Rhea:RHEA-COMP:12630,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:132517, ChEBI:CHEBI:132519; EC=2.4.1.260;
CC Evidence={ECO:0000256|ARBA:ARBA00034044};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU363075}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU363075}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 22 family.
CC {ECO:0000256|ARBA:ARBA00007063, ECO:0000256|RuleBase:RU363075}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU363075}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYC06094.1}.
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DR EMBL; JARK01001414; EYC06094.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016TSW7; -.
DR STRING; 53326.A0A016TSW7; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052917; F:dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichol alpha-1,6-mannosyltransferase; IEA:UniProtKB-EC.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR005599; GPI_mannosylTrfase.
DR PANTHER; PTHR22760:SF1; DOL-P-MAN:MAN(7)GLCNAC(2)-PP-DOL ALPHA-1,6-MANNOSYLTRANSFERASE; 1.
DR PANTHER; PTHR22760; GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF03901; Glyco_transf_22; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU363075};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU363075};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363075};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363075};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363075}.
FT TRANSMEM 46..71
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 78..94
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 100..124
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
SQ SEQUENCE 184 AA; 21034 MW; 99CDCE5E51C70E1C CRC64;
MKTFSSTAVT IPIDSLLWGR PIYPEFEVAI FNILQNRSHE YGVSPFLWYF YSCLPRGLMA
SLPLAILGLF LDRRLRPIVL PAVVFILLYS FLPHKELRFI MYAFPLINLS AAVFCARMLL
FLLASLALPI YDNIFTPCQS FYFCQNSCFS QPHALWIWSC ATTGCRLSTL FRTVGAGCKR
FSIC
//
