GenomeNet

Database: UniProt/TrEMBL
Entry: H3A2M2_LATCH
LinkDB: H3A2M2_LATCH
Original site: H3A2M2_LATCH 
ID   H3A2M2_LATCH            Unreviewed;       113 AA.
AC   H3A2M2;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 {ECO:0000256|ARBA:ARBA00018947, ECO:0000256|RuleBase:RU361136};
DE            Short=Oligosaccharyl transferase subunit DAD1 {ECO:0000256|RuleBase:RU361136};
GN   Name=DAD1 {ECO:0000313|Ensembl:ENSLACP00000003893.2};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000003893.2, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Proteomes:UP000008672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT   "The draft genome of Latimeria chalumnae.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000003893.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that
CC       catalyzes the initial transfer of a defined glycan
CC       (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-
CC       pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr
CC       consensus motif in nascent polypeptide chains, the first step in
CC       protein N-glycosylation. N-glycosylation occurs cotranslationally and
CC       the complex associates with the Sec61 complex at the channel-forming
CC       translocon complex that mediates protein translocation across the
CC       endoplasmic reticulum (ER). All subunits are required for a maximal
CC       enzyme activity. {ECO:0000256|RuleBase:RU361136}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU361136}.
CC   -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC       {ECO:0000256|RuleBase:RU361136}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU361136}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC       ECO:0000256|RuleBase:RU361136}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the DAD/OST2 family.
CC       {ECO:0000256|ARBA:ARBA00009386, ECO:0000256|RuleBase:RU361136}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AFYH01257757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01257758; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006013525.1; XM_006013463.2.
DR   AlphaFoldDB; H3A2M2; -.
DR   STRING; 7897.ENSLACP00000003893; -.
DR   Ensembl; ENSLACT00000003928.2; ENSLACP00000003893.2; ENSLACG00000003469.2.
DR   GeneID; 102347331; -.
DR   KEGG; lcm:102347331; -.
DR   CTD; 1603; -.
DR   eggNOG; KOG1746; Eukaryota.
DR   GeneTree; ENSGT00390000003324; -.
DR   HOGENOM; CLU_111220_2_1_1; -.
DR   InParanoid; H3A2M2; -.
DR   OMA; QSNPQNK; -.
DR   OrthoDB; 206600at2759; -.
DR   TreeFam; TF312846; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
DR   Bgee; ENSLACG00000003469; Expressed in pelvic fin and 6 other cell types or tissues.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR003038; DAD/Ost2.
DR   PANTHER; PTHR10705; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT DAD1; 1.
DR   PANTHER; PTHR10705:SF0; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT DAD1; 1.
DR   Pfam; PF02109; DAD; 1.
DR   PIRSF; PIRSF005588; DAD; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|RuleBase:RU361136};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU361136};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU361136}.
FT   TRANSMEM        30..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361136"
FT   TRANSMEM        55..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361136"
FT   TRANSMEM        93..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361136"
SQ   SEQUENCE   113 AA;  12589 MW;  F4B9B9EF0DA6EA48 CRC64;
     MSGSVLAVVS RFVEEYLSST PHRLKLVDSY LFYILLTGGL QFLYCLLVGT FPFNSFLSGF
     ISCVGSFVLA VCLRIQINPQ NKNEFLGISP ERAFADFLFA NVILHLVVIN FIG
//
DBGET integrated database retrieval system