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OSTC_XENTR
ID   OSTC_XENTR              Reviewed;         149 AA.
AC   Q28IL7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Oligosaccharyltransferase complex subunit ostc {ECO:0000250|UniProtKB:Q9NRP0};
GN   Name=ostc {ECO:0000250|UniProtKB:Q9NRP0}; Synonyms=dc2;
GN   ORFNames=TNeu100m23.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Small intestine;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specific component of the STT3A-containing form of the
CC       oligosaccharyl transferase (OST) complex that catalyzes the initial
CC       transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from
CC       the lipid carrier dolichol-pyrophosphate to an asparagine residue
CC       within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains,
CC       the first step in protein N-glycosylation. N-glycosylation occurs
CC       cotranslationally and the complex associates with the Sec61 complex at
CC       the channel-forming translocon complex that mediates protein
CC       translocation across the endoplasmic reticulum (ER). All subunits are
CC       required for a maximal enzyme activity. {ECO:0000250|UniProtKB:Q9NRP0}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:Q9NRP0}.
CC   -!- SUBUNIT: Specific component of the STT3A-containing form of the
CC       oligosaccharyltransferase (OST) complex.
CC       {ECO:0000250|UniProtKB:P86218}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the OSTC family. {ECO:0000305}.
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DR   EMBL; CR760329; CAJ83010.1; -; mRNA.
DR   EMBL; BC157801; AAI57802.1; -; mRNA.
DR   RefSeq; NP_001016656.1; NM_001016656.2.
DR   RefSeq; XP_012818053.1; XM_012962599.2.
DR   RefSeq; XP_017948883.1; XM_018093394.1.
DR   AlphaFoldDB; Q28IL7; -.
DR   SMR; Q28IL7; -.
DR   PaxDb; Q28IL7; -.
DR   Ensembl; ENSXETT00000045608; ENSXETP00000045608; ENSXETG00000021099.
DR   GeneID; 549410; -.
DR   KEGG; xtr:549410; -.
DR   CTD; 58505; -.
DR   Xenbase; XB-GENE-974364; ostc.
DR   eggNOG; KOG3356; Eukaryota.
DR   HOGENOM; CLU_109136_1_0_1; -.
DR   InParanoid; Q28IL7; -.
DR   OMA; TNMETSY; -.
DR   OrthoDB; 1575260at2759; -.
DR   PhylomeDB; Q28IL7; -.
DR   TreeFam; TF323315; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000021099; Expressed in testis and 14 other tissues.
DR   ExpressionAtlas; Q28IL7; baseline.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; IBA:GO_Central.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6.
DR   InterPro; IPR042416; OSTC.
DR   PANTHER; PTHR13160; PTHR13160; 1.
DR   Pfam; PF04756; OST3_OST6; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..149
FT                   /note="Oligosaccharyltransferase complex subunit ostc"
FT                   /id="PRO_0000320608"
FT   TOPO_DOM        1..32
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        54..83
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        105..117
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        139..149
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   149 AA;  16811 MW;  F021575B10E106D3 CRC64;
     MESLYRVPFT VLECPNLKLK KPSWLHMPSA MTVYAMVVVS YFLITGGIIY DVIVEPPSVG
     SMTDEHGHQR PVAFLAYRVN GQYIMEGLAS SFLFTMGGLG FIILDRSNAP NIPKLNRFLL
     LFIGFVCVLL SFFMARVFMR MKLPGYLMG
 
 
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