ID A0A0V1A795_9BILA Unreviewed; 790 AA.
AC A0A0V1A795;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Magnesium transporter protein 1 {ECO:0000313|EMBL:KRY20314.1};
GN Name=Zmat2 {ECO:0000313|EMBL:KRY20314.1};
GN ORFNames=T12_9235 {ECO:0000313|EMBL:KRY20314.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY20314.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY20314.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY20314.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KRY20314.1}.
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DR EMBL; JYDQ01000026; KRY20314.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1A795; -.
DR STRING; 990121.A0A0V1A795; -.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000178; C:exosome (RNase complex); IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR019495; EXOSC1_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
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; PF10447; EXOSC1; 1.
DR Pfam; PF04756; OST3_OST6; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF110324; Ribosomal L27 protein-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Exosome {ECO:0000256|ARBA:ARBA00022835};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 440..459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 471..490
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 524..543
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 555..575
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 681..720
FT /note="Exosome complex component CSL4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10447"
FT REGION 217..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 790 AA; 92040 MW; 4CB5CD874F1BB6C9 CRC64;
MLSSARFVIP ILCLMHFRLK LYSQKNQKWF IIIFYFKAIT VLHFFKMEPA FNPGDHRRKW
DKVEYERLAR ERLEKEEESE KPNERFEPKE KKIREYLKPR DYKIDLDSKV GKSVVITKST
PASEAGGYYC NVCDCIVKDS INFLDHINGK KRKFLFLEQL LNIDQRNMGM SMRIKKSTLE
DVRARFSAKK QEAEERKKSY DIEERLREIQ EEERKMAEYK KQKRLEKSKR KRADLSDDED
DKNESDVSKL MGFKSLEFSR MNASYWLTAT VLCLTFLPLI NPQKTKKEQL SLEEKVTFMQ
DWLAKRSVLR LNNAKFQQYV RSSPRNYSVI ILLTSHSNRQ CRICSVVQDE FEVVASSYRF
TNMNSKRLYF VLADYEEAGE VFHTLGISAI PIILHVPPRG NLKRQDKMDF QRSGIQAEAI
AKWVHERTDV VIPVMRPPNY AGPVALFLLL MLVCGLLYMK RSSLDFLYNR NLWGFLALCI
TFAFLSGQMW NHIRSPPFFY HNPKTGQWTI FSQGTQMQFI VETYIVALIY MAITMGFILL
VDATDTKTSS SKTRFYAYAG IGLVVIVFSF LLSVFRLKYR GYPYRGKFVI PGEELFKEQE
ENIRSGYGCY VAHGYYFASL AGQLKLTKEN DCAVVEVVRE NSSTSILPSP QAVVTCRVTG
VANKYAKCTI LMVHNNVLPY PFVGIIRKEN VYGSAKNETE VSMYECFQEG DIVIAKVFSL
GDSFSYLLST EELELGVFVG YCKEKHKMQP TADKQHLHCE ICLTKEPRKI ADLESDEEIL
KWKRRHYGKR
//
