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=2.4.1.119

Alternative name(s):
B5
Integral membrane protein 1
Transmembrane protein TMC

Gene names

Name:	STT3A
Synonyms:	ITM1, TMC

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	705 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the N-oligosaccharyl transferase enzyme 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 By similarity.
Catalytic activity	Dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine.
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.
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	Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	post-translational protein modification Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine Inferred from sequence or structural similarity. 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 electronic annotation. Source: EC
Complete GO annotation...

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 – 300	41	Lumenal Potential
	Transmembrane	301 – 321	21	Helical; Potential
	Topological domain	322 – 359	38	Cytoplasmic Potential
	Transmembrane	360 – 380	21	Helical; Potential
	Topological domain	381 – 383	3	Lumenal Potential
	Transmembrane	384 – 404	21	Helical; Potential
	Topological domain	405	1	Cytoplasmic Potential
	Transmembrane	406 – 426	21	Helical; Potential
	Topological domain	427 – 453	27	Lumenal Potential
	Transmembrane	454 – 474	21	Helical; Potential
	Topological domain	475 – 705	231	Lumenal Potential
Amino acid modifications
	Glycosylation	381	1	N-linked (GlcNAc...) Potential
	Glycosylation	537	1	N-linked (GlcNAc...) Ref.9
	Glycosylation	544	1	N-linked (GlcNAc...) Ref.9
	Glycosylation	548	1	N-linked (GlcNAc...) Ref.9
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: 8838310] [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: 8634329] [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: 14702039] [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: 15489334] [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: 12887896] [Abstract] Cited for: COMPOSITION OF THE OLIGOSACCHARYLTRANSFERASE 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: 15835887] [Abstract] Cited for: COMPOSITION OF THE OLIGOSACCHARYLTRANSFERASE COMPLEX.
[9]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-537; ASN-544 AND ASN-548, MASS SPECTROMETRY. Tissue: Liver.
[10]	"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: 21269460] [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_689926.1. NM_152713.3.
UniGene	Hs.504237.
3D structure databases
ProteinModelPortal	P46977.
SMR	P46977. Positions 503-606.
ModBase	Search...
Protein-protein interaction databases
IntAct	P46977. 6 interactions.
MINT	MINT-1407187.
STRING	P46977.
Protein family/group databases
CAZy	GT66. Glycosyltransferase Family 66.
Polymorphism databases
DMDM	182676409.
Proteomic databases
PRIDE	P46977.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000392708; ENSP00000376472; ENSG00000134910.
GeneID	3703.
KEGG	hsa:3703.
UCSC	uc001qcd.1. human.
Organism-specific databases
CTD	3703.
GeneCards	GC11P125462.
H-InvDB	HIX0201674.
HGNC	HGNC:6172. STT3A.
HPA	HPA030735.
MIM	601134. gene.
neXtProt	NX_P46977.
PharmGKB	PA29969.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG05916.
GeneTree	ENSGT00390000015238.
HOGENOM	HBG314442.
HOVERGEN	HBG010606.
InParanoid	P46977.
OMA	SHRIYIA.
OrthoDB	EOG4SF95B.
PhylomeDB	P46977.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
Gene expression databases
ArrayExpress	P46977.
Bgee	P46977.
CleanEx	HS_STT3A.
Genevestigator	P46977.
GermOnline	ENSG00000134910. Homo sapiens.
Family and domain databases
InterPro	IPR003674. Oligo_trans_STT3. [Graphical view]
KO	K07151.
Pfam	PF02516. STT3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	14511.
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:	January 25, 2012
This is version 95 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.