Reviewed, UniProtKB/Swiss-Prot Q55F69 (ALG3_DICDI)

Names and origin

Protein names

Recommended name:
    Probable dolichyl-phosphate-mannose--glycolipid alpha-mannosyltransferase
    EC=2.4.1.130
Alternative name(s):
    Dol-P-Man-dependent alpha(1-3)-mannosyltransferase
    Dolichyl-phosphate-mannose--glycolipid alpha-mannosyltransferase
    Asparagine-linked glycosylation protein 3 homolog

Gene names

Name:	alg3
ORF Names:	DDB_G0268238

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	446 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man5GlcNAc2-PP-Dol By similarity.
Catalytic activity	Transfers an alpha-D-mannosyl residue from dolichyl-phosphate D-mannose into membrane lipid-linked oligosaccharide.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the glycosyltransferase 58 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	dolichyl-phosphate-mannose-glycolipid alpha-mannosyltransferase 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 – 446	446	Probable dolichyl-phosphate-mannose--glycolipid alpha-mannosyltransferase		PRO_0000327763
Regions
	Transmembrane	17 – 37	21	Potential
	Transmembrane	103 – 123	21	Potential
	Transmembrane	155 – 175	21	Potential
	Transmembrane	177 – 197	21	Potential
	Transmembrane	214 – 234	21	Potential
	Transmembrane	237 – 257	21	Potential
	Transmembrane	294 – 314	21	Potential
	Transmembrane	336 – 356	21	Potential
	Transmembrane	372 – 392	21	Potential
	Transmembrane	407 – 427	21	Potential
	Compositional bias	135 – 150	16	Poly-Asn
	Compositional bias	441 – 446	6	Poly-Lys

Sequences

	Sequence		Length	Mass (Da)
	Q55F69-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: E209B9867CC60C62	FASTA	446	52,414
	10 20 30 40 50 60 MIENKVLPFI KNNQIKCFYT LASFLMIYEL CINKIIIDYV KYTEIDWSTY VQQVEVFLKG 70 80 90 100 110 120 IYDYTKIEGD TGPCVYPAGH LYVFSLLYNL TENGLNILKA QYIFAAIYIL LTFIVFSIYG 130 140 150 160 170 180 ESIKESIKQI TNKSNNNNNN NNNNNNNNNN VFLKIPFYII IFLCLSKRIH SIFALRMFND 190 200 210 220 230 240 CISMLLFYIS LYLIIKGRWN LGCLFFSCSV SVKMNVLLYS PALLFLLLST FGIWRTIPKL 250 260 270 280 290 300 MICGLVQVLL AIPFLMVNPQ GYLLRAFEFS RQFLYKWTVN WRFLPEHLFL NKSWALFLLS 310 320 330 340 350 360 IHLLFIILFF IKYIKKEQGG ISNILKRGSI NQNPKLLSVN YILLIMFTIN LIGVTFSRSL 370 380 390 400 410 420 HYQFYLWYFH TLPFLLWSTN YNLFLKIGFM CITEYAWNTY PSTSTSSLML FISNFILLIQ 430 440 LYFQPTINSL REDKNNSSGL KKKKTK

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000003 Genomic DNA. Translation: EAL73572.1.
RefSeq	XP_647664.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q55F69.
Genome annotation databases
GeneID	8616481.
KEGG	ddi:DDB_0231368.
Organism-specific databases
dictyBase	DDB_G0268238. alg3.
Phylogenomic databases
eggNOG	KOG2762.
HOGENOM	HBG525447.
OMA	LRLFNDC.
PhylomeDB	Q55F69.
Enzyme and pathway databases
BRENDA	2.4.1.130. 424.
Family and domain databases
InterPro	IPR007873. Glycosyltransferase_ALG3. [Graphical view]
PANTHER	PTHR12646. ALG3. 1 hit.
Pfam	PF05208. ALG3. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALG3_DICDI

Accession

Primary (citable) accession number: Q55F69

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	February 9, 2010
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)