Q9FZ49 (ALG9_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase
EC=2.4.1.259

Alternative name(s):
Alpha-1,2-mannosyltransferase ALG9
Asparagine-linked glycosylation protein 9
Dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase
EC=2.4.1.261

Gene names

Name:	ALG9
Ordered Locus Names:	At1g16900
ORF Names:	F6I1.10, F17F16.20

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	570 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for N-linked oligosaccharide assembly. Adds the seventh and the ninth mannose residues in an alpha-1,2 linkage onto the dolichol-PP-oligosaccharide precursors dolichol-PP-Man6GlcNAc2 and dolichol-PP-Man8GlcNAc2. Ref.4
Catalytic activity	Dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->3)-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate. Ref.4 Dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Probable.
Miscellaneous	In the absence of ALG9 activity, the N-glycans transferred to proteins are aberrant, indicating that the oligosaccharyltransferase (OST) complex is substrat tolerant.
Sequence similarities	Belongs to the glycosyltransferase 22 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Kinase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	GPI anchor biosynthetic process Inferred from electronic annotation. Source: InterPro oligosaccharide-lipid intermediate biosynthetic process Non-traceable author statement Ref.4. Source: UniProtKB
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intrinsic to endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro
Molecular function	GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity Non-traceable author statement Ref.4. Source: UniProtKB kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 570	570	Dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase		PRO_0000412587
Regions
	Transmembrane	129 – 149	21	Helical; Potential
	Transmembrane	160 – 180	21	Helical; Potential
	Transmembrane	208 – 228	21	Helical; Potential
	Transmembrane	237 – 257	21	Helical; Potential
	Transmembrane	297 – 317	21	Helical; Potential
	Transmembrane	324 – 344	21	Helical; Potential
	Transmembrane	349 – 369	21	Helical; Potential
	Transmembrane	381 – 401	21	Helical; Potential
	Compositional bias	14 – 21	8	Poly-Ser
	Compositional bias	257 – 260	4	Poly-Tyr
Amino acid modifications
	Glycosylation	473	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9FZ49 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: CE6885EA115D0997	FASTA	570	65,083
	10 20 30 40 50 60 MDLTTTRQRR PLISDSSSSS STKSYSKTDK PGRSNGGDAE DGGLRWFLPF IALCYLRYMS 70 80 90 100 110 120 ATSNIIHDCD EVFNYWEPLH YILYKSGFQT WEYSSNFALR SYLYILFHEL AGRPASWWFG 130 140 150 160 170 180 DDKVRVFYAV RLFLGLVSAV SDTVLVVALS RKYGKRIATY AVAMLCLTSG CFFASTSFLP 190 200 210 220 230 240 SSFSMYAISL SSGLLLFEKY AMAVAVSVVG VILGWPFSIL AFLPVVIYSL VKRFKQAFIA 250 260 270 280 290 300 GAVTTIFLLG VSLLVDYYYY KRWTSSVLNL LIYNVLGGGE SHLYGTEGAL FYIRNGFNNF 310 320 330 340 350 360 NFCFILAMLF VAIYPVIRRK YDRALLVVIS PMYIWLAFMS LQPHKEERFL YPIYPLICVS 370 380 390 400 410 420 ASAVIENIPE LFREKYSSRE SLLVTITKYM RPVILGCILC ASHSRTFALI NGYSAPLEVY 430 440 450 460 470 480 KLLEHHDDAG PGSVLCVGSE WHRYPSSFFV PHYISEVRWI DDGFRGLLPF PFNNTLGGTS 490 500 510 520 530 540 ASPPYFNNKN QASEEQYLKN IETCTFLIEL QLSRPYQYRG SDLSTWEAIA VLPYLDRELS 550 560 570 PAKYRSFFIP HMWQEKNVFG KYVALRRVPK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Mutations of an alpha1,6 mannosyltransferase inhibit endoplasmic reticulum-associated degradation of defective brassinosteroid receptors in Arabidopsis." Hong Z., Jin H., Fitchette A.C., Xia Y., Monk A.M., Faye L., Li J. Plant Cell 21:3792-3802(2009) [PubMed: 20023196] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC051629 Genomic DNA. Translation: AAF99843.1. CP002684 Genomic DNA. Translation: AEE29518.1. AY140061 mRNA. Translation: AAM98202.1. BT010395 mRNA. Translation: AAQ56838.1.
IPI	IPI00528313.
PIR	D86304.
RefSeq	NP_173134.2. NM_101551.3.
UniGene	At.41864.
3D structure databases
ProteinModelPortal	Q9FZ49.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9FZ49. 1 interaction.
STRING	Q9FZ49.
Protein family/group databases
CAZy	GT22. Glycosyltransferase Family 22.
Proteomic databases
PRIDE	Q9FZ49.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G16900.1; AT1G16900.1; AT1G16900.
GeneID	838261.
GenomeReviews	Gene locus AT1G16900 in contig CT485782_GR.
KEGG	ath:AT1G16900.
Organism-specific databases
TAIR	At1g16900.
Phylogenomic databases
eggNOG	KOG2515.
GeneTree	EPGT00050000009884.
HOGENOM	HBG736291.
InParanoid	Q9FZ49.
PhylomeDB	Q9FZ49.
ProtClustDB	CLSN2691194.
Gene expression databases
ArrayExpress	Q9FZ49.
Genevestigator	Q9FZ49.
Family and domain databases
InterPro	IPR005599. GPI_mannosylTrfase. [Graphical view]
KO	K03846.
PANTHER	PTHR22760. Alg9_trans. 1 hit.
Pfam	PF03901. Glyco_transf_22. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALG9_ARATH

Accession

Primary (citable) accession number: Q9FZ49

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 21, 2011
Last sequence update:	March 1, 2001
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program