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Database: UniProt
Entry: A0A2K5JB32_COLAP
LinkDB: A0A2K5JB32_COLAP
Original site: A0A2K5JB32_COLAP 
ID   A0A2K5JB32_COLAP        Unreviewed;       173 AA.
AC   A0A2K5JB32;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Oligosaccharyltransferase complex subunit {ECO:0000256|RuleBase:RU366060};
OS   Colobus angolensis palliatus (Peters' Angolan colobus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Colobus.
OX   NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000026119.1, ECO:0000313|Proteomes:UP000233080};
RN   [1] {ECO:0000313|Ensembl:ENSCANP00000026119.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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. May be involved in N-
CC       glycosylation of APP (amyloid-beta precursor protein). Can modulate
CC       gamma-secretase cleavage of APP by enhancing endoprotelysis of PSEN1.
CC       {ECO:0000256|RuleBase:RU366060}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC       {ECO:0000256|RuleBase:RU366060}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000256|ARBA:ARBA00004240}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU366060}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU366060}.
CC   -!- SIMILARITY: Belongs to the OSTC family. {ECO:0000256|ARBA:ARBA00009376,
CC       ECO:0000256|RuleBase:RU366060}.
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DR   AlphaFoldDB; A0A2K5JB32; -.
DR   STRING; 336983.ENSCANP00000026119; -.
DR   Ensembl; ENSCANT00000049127.1; ENSCANP00000026119.1; ENSCANG00000036468.1.
DR   OMA; RFFMATR; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000233080; Unplaced.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6.
DR   InterPro; IPR042416; OSTC.
DR   PANTHER; PTHR13160; OLIGOSACCHARYLTRANSFERASE COMPLEX SUBUNIT OSTC; 1.
DR   PANTHER; PTHR13160:SF9; OLIGOSACCHARYLTRANSFERASE COMPLEX SUBUNIT OSTC; 1.
DR   Pfam; PF04756; OST3_OST6; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU366060};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233080};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU366060};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU366060}.
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU366060"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU366060"
FT   TRANSMEM        116..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU366060"
SQ   SEQUENCE   173 AA;  19207 MW;  228FF35EFC8F0AF9 CRC64;
     KNYPGVMVGT TLAATNMETL YCVPFFLKKP PWLPMPSAMT LCALVVAGII FDVIVEPPSV
     GSMTDEHRHQ RPVAFLAYRV NGQYIMEGLV SSFLFTMGGL GFIILDPSNA PNIPKLNRFL
     IFIGFVCVLL RFFMATRVFM RMKLPGYLMG YGASEKKSVD TGFNEVLKVV PVL
//
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