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Identification
HMDB Protein ID HMDBP02781
Secondary Accession Numbers
  • 8287
Name Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
Synonyms
  1. B5
  2. Integral membrane protein 1
  3. Oligosaccharyl transferase subunit STT3A
  4. STT3-A
  5. Transmembrane protein TMC
Gene Name STT3A
Protein Type Enzyme
Biological Properties
General Function Involved in oligosaccharyl transferase activity
Specific Function Catalytic subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). SST3A seems to be involved in complex substrate specificity. STT3A is present in the majority of OST complexes and mediates cotranslational N-glycosylation of most sites on target proteins, while STT3B-containing complexes are required for efficient cotranslational glycosylation and mediate glycosylation of sites that have been skipped by STT3A.
Pathways
  • N-Glycan biosynthesis
  • protein glycosylation
  • Protein processing in endoplasmic reticulum
Reactions
Dolichyl diphosphooligosaccharide + [protein]-L-asparagine → Dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine details
Dolichyl diphosphooligosaccharide + Protein asparagine → Dolichyl diphosphate + Glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine details
Protein asparagine + → Dolichyl diphosphate + details
GO Classification
Biological Process
post-translational protein modification
protein N-linked glycosylation via asparagine
co-translational protein modification
Cellular Component
oligosaccharyltransferase complex
integral to membrane
Component
membrane
cell part
Function
catalytic activity
transferase activity
transferase activity, transferring hexosyl groups
transferase activity, transferring glycosyl groups
oligosaccharyl transferase activity
Molecular Function
dolichyl-diphosphooligosaccharide-protein glycotransferase activity
Process
metabolic process
macromolecule metabolic process
macromolecule modification
protein modification process
protein amino acid glycosylation
Cellular Location
  1. Endoplasmic reticulum membrane
  2. Multi-pass membrane protein
Gene Properties
Chromosome Location 11
Locus 11q23.3
SNPs STT3A
Gene Sequence
>2118 bp
ATGACTAAGTTTGGATTTTTGCGATTGTCCTATGAGAAGCAGGACACACTTTTGAAGCTT
CTCATTCTGTCAATGGCTGCTGTATTATCCTTCTCCACTCGTCTGTTTGCTGTCCTGAGA
TTTGAAAGTGTTATCCATGAGTTTGATCCGTACTTTAATTATCGGACTACCAGGTTCCTG
GCTGAGGAGGGGTTTTATAAATTCCATAACTGGTTTGATGACCGAGCCTGGTACCCTTTG
GGACGAATCATTGGAGGAACAATTTACCCAGGTTTAATGATCACCTCTGCTGCAATCTAC
CATGTACTCCATTTTTTCCACATCACCATCGACATTCGGAATGTCTGTGTGTTCCTGGCC
CCTCTCTTCTCCTCCTTCACCACCATCGTCACGTACCACCTTACCAAAGAGCTCAAGGAT
GCAGGGGCTGGGCTTCTTGCTGCTGCCATGATTGCTGTAGTTCCTGGATATATCTCCCGA
TCTGTGGCTGGCTCCTATGATAATGAAGGGATTGCCATCTTTTGCATGCTACTCACCTAC
TACATGTGGATCAAGGCAGTAAAGACTGGTTCCATCTGTTGGGCAGCTAAGTGTGCCCTT
GCTTATTTCTACATGGTCTCGTCATGGGGAGGTTATGTGTTCCTGATCAACTTAATTCCT
CTCCACGTCCTCGTGCTGATGCTCACAGGCCGTTTCTCTCACCGGATCTATGTGGCCTAC
TGTACTGTTTACTGCCTGGGCACTATACTTTCTATGCAGATCTCCTTTGTGGGTTTCCAG
CCTGTCCTTTCATCAGAGCACATGGCAGCCTTTGGGGTCTTTGGTCTCTGCCAGATCCAT
GCCTTTGTGGATTACCTGCGCAGCAAGTTGAATCCACAACAATTTGAAGTTCTTTTCCGG
AGCGTCATCTCTCTGGTAGGCTTTGTCCTTCTCACCGTGGGAGCTCTCCTCATGCTGACA
GGAAAAATATCTCCCTGGACGGGGCGTTTCTACTCACTGCTGGATCCCTCTTATGCTAAG
AACAACATCCCCATCATTGCTTCTGTGTCTGAGCATCAGCCCACAACCTGGTCCTCATAC
TATTTTGACCTGCAGCTCCTCGTCTTCATGTTTCCAGTTGGCCTCTATTACTGCTTTAGC
AACCTGTCTGATGCCCGGATTTTTATCATCATGTATGGTGTGACCAGCATGTACTTTTCA
GCTGTAATGGTGCGTCTAATGCTAGTGTTGGCACCTGTTATGTGCATTCTCTCTGGCATT
GGAGTCTCCCAGGTGCTGTCCACATACATGAAGAATCTGGACATAAGTCGTCCAGACAAG
AAGAGCAAGAAGCAACAGGATTCCACCTACCCTATTAAGAATGAAGTGGCAAGTGGGATG
ATACTGGTCATGGCTTTCTTTCTCATCACCTACACCTTTCATTCAACCTGGGTGACCAGT
GAGGCCTACTCTTCTCCGTCCATTGTACTATCTGCCCGTGGTGGGGATGGCAGTAGGATC
ATATTTGATGACTTCCGAGAAGCATATTATTGGCTTCGTCATAATACTCCAGAGGATGCG
AAGGTCATGTCCTGGTGGGATTATGGCTATCAGATTACAGCTATGGCAAACCGAACAATT
TTAGTGGACAATAACACATGGAATAATACCCATATTTCTCGAGTAGGGCAGGCAATGGCG
TCCACAGAGGAAAAAGCCTATGAGATCATGAGGGAGCTCGATGTCAGCTATGTGCTGGTC
ATTTTTGGAGGCCTCACTGGGTATTCCTCTGATGATATCAACAAGTTTCTTTGGATGGTC
CGGATTGGAGGGAGCACAGATACAGGCAAACATATCAAGGAGAATGACTATTATACTCCA
ACTGGGGAGTTCCGTGTGGACCGTGAAGGTTCTCCAGTGCTGCTCAACTGCCTCATGTAC
AAGATGTGTTACTATCGCTTTGGACAGGTTTACACAGAAGCCAAGCGTCCTCCAGGCTTT
GACCGTGTCCGAAATGCTGAGATTGGGAATAAAGACTTTGAGCTTGATGTCCTGGAGGAA
GCATATACCACAGAACATTGGCTGGTCAGGATATACAAGGTAAAGGACCTGGATAATCGA
GGCTTGTCAAGGACATAA
Protein Properties
Number of Residues 705
Molecular Weight 80528.83
Theoretical pI 8.076
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
MTKFGFLRLSYEKQDTLLKLLILSMAAVLSFSTRLFAVLRFESVIHEFDPYFNYRTTRFL
AEEGFYKFHNWFDDRAWYPLGRIIGGTIYPGLMITSAAIYHVLHFFHITIDIRNVCVFLA
PLFSSFTTIVTYHLTKELKDAGAGLLAAAMIAVVPGYISRSVAGSYDNEGIAIFCMLLTY
YMWIKAVKTGSICWAAKCALAYFYMVSSWGGYVFLINLIPLHVLVLMLTGRFSHRIYVAY
CTVYCLGTILSMQISFVGFQPVLSSEHMAAFGVFGLCQIHAFVDYLRSKLNPQQFEVLFR
SVISLVGFVLLTVGALLMLTGKISPWTGRFYSLLDPSYAKNNIPIIASVSEHQPTTWSSY
YFDLQLLVFMFPVGLYYCFSNLSDARIFIIMYGVTSMYFSAVMVRLMLVLAPVMCILSGI
GVSQVLSTYMKNLDISRPDKKSKKQQDSTYPIKNEVASGMILVMAFFLITYTFHSTWVTS
EAYSSPSIVLSARGGDGSRIIFDDFREAYYWLRHNTPEDAKVMSWWDYGYQITAMANRTI
LVDNNTWNNTHISRVGQAMASTEEKAYEIMRELDVSYVLVIFGGLTGYSSDDINKFLWMV
RIGGSTDTGKHIKENDYYTPTGEFRVDREGSPVLLNCLMYKMCYYRFGQVYTEAKRPPGF
DRVRNAEIGNKDFELDVLEEAYTTEHWLVRIYKVKDLDNRGLSRT
GenBank ID Protein 158261103
UniProtKB/Swiss-Prot ID P46977
UniProtKB/Swiss-Prot Entry Name STT3A_HUMAN
PDB IDs Not Available
GenBank Gene ID AK290040
GeneCard ID STT3A
GenAtlas ID STT3A
HGNC ID HGNC:6172
References
General References
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  4. Kelleher DJ, Karaoglu D, Mandon EC, Gilmore R: Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties. Mol Cell. 2003 Jul;12(1):101-11. [PubMed:12887896 ]
  5. Shibatani T, David LL, McCormack AL, Frueh K, Skach WR: Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits. Biochemistry. 2005 Apr 26;44(16):5982-92. [PubMed:15835887 ]
  6. Hong G, Deleersnijder W, Kozak CA, Van Marck E, Tylzanowski P, Merregaert J: Molecular cloning of a highly conserved mouse and human integral membrane protein (Itm1) and genetic mapping to mouse chromosome 9. Genomics. 1996 Feb 1;31(3):295-300. [PubMed:8838310 ]
  7. Lissy NA, Bellacosa A, Sonoda G, Miller PD, Jhanwar SC, Testa JR: Isolation, characterization, and mapping to human chromosome 11q24-25 of a cDNA encoding a highly conserved putative transmembrane protein, TMC. Biochim Biophys Acta. 1996 May 2;1306(2-3):137-41. [PubMed:8634329 ]