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P46977 (STT3A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A

Short name=Oligosaccharyl transferase subunit STT3A
Short name=STT3-A
EC=2.4.99.18
Alternative name(s):
B5
Integral membrane protein 1
Transmembrane protein TMC
Gene names
Name:STT3A
Synonyms:ITM1, TMC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length705 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.9

Catalytic activity

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.

Pathway

Protein modification; protein glycosylation.

Subunit structure

Component of the oligosaccharyltransferase (OST) complex By similarity. OST seems to exist in different forms which contain at least RPN1, RPN2, OST48, DAD1, OSTC, KRTCAP2 and either STT3A or STT3B. OST can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes. Also identified as part of a complex which includes CANX, DERL1, DERL2, DDOST/OST48, RPN1, RPN2, SELK, VIMP, STT3A AND VCP. This contains known members of the OST complex and may be a form of this complex. Ref.7 Ref.8 Ref.12

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Tissue specificity

Expressed at high levels in placenta, liver, muscle and pancreas, and at very low levels in brain, lung and kidney. Expressed in skin fibroblasts (at protein level). Ref.7

Sequence similarities

Belongs to the STT3 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IRAK2O431872EBI-719212,EBI-447733
Sarm1Q6PDS32EBI-719212,EBI-6117196From a different organism.
TMEM173Q86WV62EBI-719212,EBI-2800345

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 705705Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
PRO_0000072290

Regions

Topological domain1 – 1717Cytoplasmic Potential
Transmembrane18 – 3821Helical; Potential
Topological domain39 – 11476Lumenal Potential
Transmembrane115 – 13521Helical; Potential
Topological domain136 – 16934Cytoplasmic Potential
Transmembrane170 – 19021Helical; Potential
Topological domain191 – 20818Lumenal Potential
Transmembrane209 – 22921Helical; Potential
Topological domain230 – 2356Cytoplasmic Potential
Transmembrane236 – 25924Helical; Potential
Topological domain260 – 2656Lumenal Potential
Transmembrane266 – 28621Helical; Potential
Topological domain287 – 30014Cytoplasmic Potential
Transmembrane301 – 32121Helical; Potential
Topological domain322 – 35938Lumenal Potential
Transmembrane360 – 38021Helical; Potential
Topological domain381 – 3833Cytoplasmic Potential
Transmembrane384 – 40421Helical; Potential
Topological domain4051Lumenal Potential
Transmembrane406 – 42621Helical; Potential
Topological domain427 – 45327Cytoplasmic Potential
Transmembrane454 – 47421Helical; Potential
Topological domain475 – 705231Lumenal Potential

Amino acid modifications

Glycosylation5371N-linked (GlcNAc...) Ref.10
Glycosylation5441N-linked (GlcNAc...) Ref.10
Glycosylation5481N-linked (GlcNAc...) Ref.10

Experimental info

Sequence conflict611A → S in AAL77539. Ref.2
Sequence conflict1281T → S in AAB05994. Ref.1
Sequence conflict1331H → L in AAB05994. Ref.1
Sequence conflict2521M → R in AAB05994. Ref.1
Sequence conflict2701A → G in AAB05994. Ref.1
Sequence conflict4151C → S in AAB05994. Ref.1
Sequence conflict4541N → I in AAB05994. Ref.1
Sequence conflict4941G → D in AAL77539. Ref.2
Sequence conflict6811A → G in AAB05994. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P46977 [UniParc].

Last modified April 8, 2008. Version 2.
Checksum: 71426CA5598B51C4

FASTA70580,530
        10         20         30         40         50         60 
MTKFGFLRLS YEKQDTLLKL LILSMAAVLS FSTRLFAVLR FESVIHEFDP YFNYRTTRFL 

        70         80         90        100        110        120 
AEEGFYKFHN WFDDRAWYPL GRIIGGTIYP GLMITSAAIY HVLHFFHITI DIRNVCVFLA 

       130        140        150        160        170        180 
PLFSSFTTIV TYHLTKELKD AGAGLLAAAM IAVVPGYISR SVAGSYDNEG IAIFCMLLTY 

       190        200        210        220        230        240 
YMWIKAVKTG SICWAAKCAL AYFYMVSSWG GYVFLINLIP LHVLVLMLTG RFSHRIYVAY 

       250        260        270        280        290        300 
CTVYCLGTIL SMQISFVGFQ PVLSSEHMAA FGVFGLCQIH AFVDYLRSKL NPQQFEVLFR 

       310        320        330        340        350        360 
SVISLVGFVL LTVGALLMLT GKISPWTGRF YSLLDPSYAK NNIPIIASVS EHQPTTWSSY 

       370        380        390        400        410        420 
YFDLQLLVFM FPVGLYYCFS NLSDARIFII MYGVTSMYFS AVMVRLMLVL APVMCILSGI 

       430        440        450        460        470        480 
GVSQVLSTYM KNLDISRPDK KSKKQQDSTY PIKNEVASGM ILVMAFFLIT YTFHSTWVTS 

       490        500        510        520        530        540 
EAYSSPSIVL SARGGDGSRI IFDDFREAYY WLRHNTPEDA KVMSWWDYGY QITAMANRTI 

       550        560        570        580        590        600 
LVDNNTWNNT HISRVGQAMA STEEKAYEIM RELDVSYVLV IFGGLTGYSS DDINKFLWMV 

       610        620        630        640        650        660 
RIGGSTDTGK HIKENDYYTP TGEFRVDREG SPVLLNCLMY KMCYYRFGQV YTEAKRPPGF 

       670        680        690        700 
DRVRNAEIGN KDFELDVLEE AYTTEHWLVR IYKVKDLDNR GLSRT 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of a highly conserved mouse and human integral membrane protein (Itm1) and genetic mapping to mouse chromosome 9."
Hong G., Deleersnjider W., Kozak C.A., van Marck E., Tylzanowski P., Merregaert J.
Genomics 31:295-300(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Isolation, characterization, and mapping to human chromosome 11q24-25 of a cDNA encoding a highly conserved putative transmembrane protein, TMC."
Lissy N.A., Bellacosa A., Sonoda G., Miller P.D., Jhanwar S.C., Testa J.R.
Biochim. Biophys. Acta 1306:137-141(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Hippocampus.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Duodenum and Lung.
[7]"Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties."
Kelleher D.J., Karaoglu D., Mandon E.C., Gilmore R.
Mol. Cell 12:101-111(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX, TISSUE SPECIFICITY.
[8]"Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits."
Shibatani T., David L.L., McCormack A.L., Frueh K., Skach W.R.
Biochemistry 44:5982-5992(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX.
[9]"Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms."
Ruiz-Canada C., Kelleher D.J., Gilmore R.
Cell 136:272-283(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-537; ASN-544 AND ASN-548.
Tissue: Liver.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis."
Shchedrina V.A., Everley R.A., Zhang Y., Gygi S.P., Hatfield D.L., Gladyshev V.N.
J. Biol. Chem. 286:42937-42948(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH CANX; DERL1; DERL2; DDOST; RPN1; RPN2; SELK; VCP AND VIMP.
[13]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L38961 mRNA. Translation: AAB05994.1.
L47337 mRNA. Translation: AAL77539.1.
AK290040 mRNA. Translation: BAF82729.1.
AK290657 mRNA. Translation: BAF83346.1.
BT007100 mRNA. Translation: AAP35764.1.
CH471065 Genomic DNA. Translation: EAW67647.1.
BC020965 mRNA. Translation: AAH20965.1.
BC048348 mRNA. Translation: AAH48348.2.
PIRS70029.
RefSeqNP_001265432.1. NM_001278503.1.
NP_001265433.1. NM_001278504.1.
NP_689926.1. NM_152713.4.
UniGeneHs.504237.
Hs.659244.

3D structure databases

ProteinModelPortalP46977.
SMRP46977. Positions 20-183, 474-701.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109908. 10 interactions.
IntActP46977. 14 interactions.
MINTMINT-1407187.
STRING9606.ENSP00000376472.

Protein family/group databases

CAZyGT66. Glycosyltransferase Family 66.

PTM databases

PhosphoSiteP46977.

Polymorphism databases

DMDM182676409.

Proteomic databases

PaxDbP46977.
PRIDEP46977.

Protocols and materials databases

DNASU3703.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000392708; ENSP00000376472; ENSG00000134910.
ENST00000529196; ENSP00000436962; ENSG00000134910.
GeneID3703.
KEGGhsa:3703.
UCSCuc001qcd.2. human.

Organism-specific databases

CTD3703.
GeneCardsGC11P125462.
HGNCHGNC:6172. STT3A.
HPAHPA030735.
MIM601134. gene.
neXtProtNX_P46977.
Orphanet370921. STT3A-CDG.
PharmGKBPA29969.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1287.
HOGENOMHOG000157471.
HOVERGENHBG010606.
InParanoidP46977.
KOK07151.
OMAIYIAYST.
OrthoDBEOG7VHSWP.
PhylomeDBP46977.
TreeFamTF300822.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
SignaLinkP46977.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressP46977.
BgeeP46977.
CleanExHS_STT3A.
GenevestigatorP46977.

Family and domain databases

InterProIPR003674. Oligo_trans_STT3.
[Graphical view]
PfamPF02516. STT3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSTT3A. human.
GenomeRNAi3703.
NextBio14511.
PROP46977.
SOURCESearch...

Entry information

Entry nameSTT3A_HUMAN
AccessionPrimary (citable) accession number: P46977
Secondary accession number(s): Q86XU9, Q8TE35, Q8WUB4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: April 8, 2008
Last modified: April 16, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM