Reviewed, UniProtKB/Swiss-Prot Q9Y7I4 (ALG3_SCHPO)

Names and origin

Protein names

Recommended name:
    Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl 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

Gene names

Name:	alg3
ORF Names:	SPAC7D4.06c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	406 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man5GlcNAc(2)-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 Probable.
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	integral to endoplasmic reticulum membrane Inferred by curator. Source: GeneDB_SPombe
Molecular function	dolichyl-phosphate-mannose-glycolipid alpha-mannosyltransferase activity Inferred by curator. Source: GeneDB_SPombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 406	406	Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase		PRO_0000327764
Regions
	Transmembrane	72 – 92	21	Potential
	Transmembrane	107 – 127	21	Potential
	Transmembrane	129 – 149	21	Potential
	Transmembrane	186 – 206	21	Potential
	Transmembrane	214 – 234	21	Potential
	Transmembrane	261 – 281	21	Potential
	Transmembrane	313 – 333	21	Potential
	Transmembrane	349 – 369	21	Potential
	Transmembrane	376 – 396	21	Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9Y7I4-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 039E40A16A9359C8	FASTA	406	46,992
	10 20 30 40 50 60 MSSVETRNSF NPFRVLFDLG SYGWLHPSRL LLLEIPFVFA IISKVPYTEI DWIAYMEQVN 70 80 90 100 110 120 SFLLGERDYK SLVGCTGPLV YPGGHVFLYT LLYYLTDGGT NIVRAQYIFA FVYWITTAIV 130 140 150 160 170 180 GYLFKIVRAP FYIYVLLILS KRLHSIFILR LFNDGFNSLF SSLFILSSCK KKWVRASILL 190 200 210 220 230 240 SVACSVKMSS LLYVPAYLVL LLQILGPKKT WMHIFVIIIV QILFSIPFLA YFWSYWTQAF 250 260 270 280 290 300 DFGRAFDYKW TVNWRFIPRS IFESTSFSTS ILFLHVALLV AFTCKHWNKL SRATPFAMVN 310 320 330 340 350 360 SMLTLKPLPK LQLATPNFIF TALATSNLIG ILCARSLHYQ FYAWFAWYSP YLCYQASFPA 370 380 390 400 PIVIGLWMLQ EYAWNVFPST KLSSLIAVCV PLITILKLYT SDYRKP

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAB16723.2.
PIR	T39084.
RefSeq	NP_593853.1.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GT58. Glycosyltransferase Family 58.
Genome annotation databases
GeneID	2542768.
KEGG	spo:SPAC7D4.06c.
NMPDR	fig|4896.1.peg.3823.
Organism-specific databases
GeneDB_Spombe	SPAC7D4.06c.
Phylogenomic databases
OMA	Q9Y7I4. LRLFNDC.
Enzyme and pathway databases
BRENDA	2.4.1.130. 653.
Gene expression databases
ArrayExpress	Q9Y7I4.
Family and domain databases
InterPro	IPR007873. Glycosyltransferase_ALG3. [Graphical view]
PANTHER	PTHR12646. ALG3. 1 hit.
Pfam	PF05208. ALG3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALG3_SCHPO

Accession

Primary (citable) accession number: Q9Y7I4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	November 1, 1999
Last modified:	June 16, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)