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Database: UniProt
Entry: Q29MN1_DROPS
LinkDB: Q29MN1_DROPS
Original site: Q29MN1_DROPS 
ID   Q29MN1_DROPS            Unreviewed;       330 AA.
AC   Q29MN1; A0A6I8UJP3;
DT   04-APR-2006, integrated into UniProtKB/TrEMBL.
DT   04-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   SubName: Full=Tumor suppressor candidate 3 {ECO:0000313|RefSeq:XP_001356598.1};
GN   Name=LOC4816963 {ECO:0000313|RefSeq:XP_001356598.1};
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245 {ECO:0000313|Proteomes:UP000001819, ECO:0000313|RefSeq:XP_001356598.1};
RN   [1] {ECO:0000313|RefSeq:XP_001356598.1}
RP   IDENTIFICATION.
RC   STRAIN=MV2-25 {ECO:0000313|RefSeq:XP_001356598.1};
RC   TISSUE=Whole body {ECO:0000313|RefSeq:XP_001356598.1};
RG   RefSeq;
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|ARBA:ARBA00002791}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the OST3/OST6 family.
CC       {ECO:0000256|ARBA:ARBA00009561}.
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DR   RefSeq; XP_001356598.1; XM_001356562.3.
DR   AlphaFoldDB; Q29MN1; -.
DR   SMR; Q29MN1; -.
DR   STRING; 46245.Q29MN1; -.
DR   EnsemblMetazoa; FBtr0282069; FBpp0280507; FBgn0080608.
DR   GeneID; 4816963; -.
DR   KEGG; dpo:4816963; -.
DR   eggNOG; KOG2603; Eukaryota.
DR   HOGENOM; CLU_052855_0_0_1; -.
DR   InParanoid; Q29MN1; -.
DR   OMA; VLFGMYS; -.
DR   Proteomes; UP000001819; Chromosome 4.
DR   Bgee; FBgn0080608; Expressed in female reproductive system and 2 other cell types or tissues.
DR   ExpressionAtlas; Q29MN1; baseline.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016477; P:cell migration; IEA:EnsemblMetazoa.
DR   GO; GO:0035010; P:encapsulation of foreign target; IEA:EnsemblMetazoa.
DR   GO; GO:1903830; P:magnesium ion transmembrane transport; IEA:EnsemblMetazoa.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR12692; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR12692:SF0; GH11935P; 1.
DR   Pfam; PF04756; OST3_OST6; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001819};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ   SEQUENCE   330 AA;  36977 MW;  DE3FF71A132F7B13 CRC64;
     MRLVRNTLLG ALVVLAVCLI YAAAQAKPKT GLSLSEKVQN LVEMNAKKPL LRFNGPKFRE
     YVKNSPRNYS MIVMLTALAP SRQCQICRHA HDEFAIVANS YRFSSVYSNK LFFAMVDFDE
     GSEVFQLLRL NTAPVFMHFP AKGKPKGADT MDIHRVGFAA DSIAKFVAER VDVTIRIFRP
     PNYSGTVAMI TLVALVGSFL YIRRNNLEFL YNKNLWGAIA VFFCFAMISG QMWNHIRGPP
     LVHKSQNGGV AYIHGSSQGQ LVVETYIVMF LNAMIVLGMI LLIESGTSKG HNKNRIMAMV
     GLVLVTVFFS FLLSVFRSKA QGYPYSFLFK
//
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