P46977 (STT3A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	705 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.7 Ref.8
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.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	co-translational protein modification Inferred from mutant phenotype Ref.9. Source: UniProtKB post-translational protein modification Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine Inferred from mutant phenotype Ref.9. Source: UniProtKB
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW oligosaccharyltransferase complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	dolichyl-diphosphooligosaccharide-protein glycotransferase activity Inferred from mutant phenotype Ref.9. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
IRAK2	O43187	2	EBI-719212,EBI-447733
Sarm1	Q6PDS3	2	EBI-719212,EBI-6117196	From a different organism.
TMEM173	Q86WV6	2	EBI-719212,EBI-2800345

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 705	705	Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A		PRO_0000072290
Regions
	Topological domain	1 – 17	17	Cytoplasmic Potential
	Transmembrane	18 – 38	21	Helical; Potential
	Topological domain	39 – 114	76	Lumenal Potential
	Transmembrane	115 – 135	21	Helical; Potential
	Topological domain	136 – 169	34	Cytoplasmic Potential
	Transmembrane	170 – 190	21	Helical; Potential
	Topological domain	191 – 208	18	Lumenal Potential
	Transmembrane	209 – 229	21	Helical; Potential
	Topological domain	230 – 235	6	Cytoplasmic Potential
	Transmembrane	236 – 259	24	Helical; Potential
	Topological domain	260 – 265	6	Lumenal Potential
	Transmembrane	266 – 286	21	Helical; Potential
	Topological domain	287 – 300	14	Cytoplasmic Potential
	Transmembrane	301 – 321	21	Helical; Potential
	Topological domain	322 – 359	38	Lumenal Potential
	Transmembrane	360 – 380	21	Helical; Potential
	Topological domain	381 – 383	3	Cytoplasmic Potential
	Transmembrane	384 – 404	21	Helical; Potential
	Topological domain	405	1	Lumenal Potential
	Transmembrane	406 – 426	21	Helical; Potential
	Topological domain	427 – 453	27	Cytoplasmic Potential
	Transmembrane	454 – 474	21	Helical; Potential
	Topological domain	475 – 705	231	Lumenal Potential
Amino acid modifications
	Glycosylation	537	1	N-linked (GlcNAc...) Ref.10
	Glycosylation	544	1	N-linked (GlcNAc...) Ref.10
	Glycosylation	548	1	N-linked (GlcNAc...) Ref.10
Experimental info
	Sequence conflict	61	1	A → S in AAL77539. Ref.2
	Sequence conflict	128	1	T → S in AAB05994. Ref.1
	Sequence conflict	133	1	H → L in AAB05994. Ref.1
	Sequence conflict	252	1	M → R in AAB05994. Ref.1
	Sequence conflict	270	1	A → G in AAB05994. Ref.1
	Sequence conflict	415	1	C → S in AAB05994. Ref.1
	Sequence conflict	454	1	N → I in AAB05994. Ref.1
	Sequence conflict	494	1	G → D in AAL77539. Ref.2
	Sequence conflict	681	1	A → G in AAB05994. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P46977 [UniParc]. Last modified April 8, 2008. Version 2. Checksum: 71426CA5598B51C4	FASTA	705	80,530
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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]	"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.
IPI	IPI00297492.
PIR	S70029.
RefSeq	NP_001265432.1. NM_001278503.1. NP_001265433.1. NM_001278504.1. NP_689926.1. NM_152713.4.
UniGene	Hs.504237. Hs.659244.
3D structure databases
ProteinModelPortal	P46977.
SMR	P46977. Positions 474-701.
ModBase	Search...
Protein-protein interaction databases
IntAct	P46977. 14 interactions.
MINT	MINT-1407187.
STRING	9606.ENSP00000376472.
Protein family/group databases
CAZy	GT66. Glycosyltransferase Family 66.
PTM databases
PhosphoSite	P46977.
Polymorphism databases
DMDM	182676409.
Proteomic databases
PaxDb	P46977.
PRIDE	P46977.
Protocols and materials databases
DNASU	3703.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000392708; ENSP00000376472; ENSG00000134910. ENST00000529196; ENSP00000436962; ENSG00000134910.
GeneID	3703.
KEGG	hsa:3703.
UCSC	uc001qcd.2. human.
Organism-specific databases
CTD	3703.
GeneCards	GC11P125462.
HGNC	HGNC:6172. STT3A.
HPA	HPA030735.
MIM	601134. gene.
neXtProt	NX_P46977.
PharmGKB	PA29969.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1287.
HOGENOM	HOG000157471.
HOVERGEN	HBG010606.
InParanoid	P46977.
KO	K07151.
OMA	IYIAYST.
OrthoDB	EOG7VHSWP.
PhylomeDB	P46977.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_17015. Metabolism of proteins.
SignaLink	P46977.
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	P46977.
Bgee	P46977.
CleanEx	HS_STT3A.
Genevestigator	P46977.
Family and domain databases
InterPro	IPR003674. Oligo_trans_STT3. [Graphical view]
Pfam	PF02516. STT3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	STT3A. human.
GenomeRNAi	3703.
NextBio	14511.
PRO	P46977.
SOURCE	Search...

Entry information

Entry name

STT3A_HUMAN

Accession

Primary (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:	November 13, 2013
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.