Q96WW6 (ALG2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-1,3/1,6-mannosyltransferase alg2
EC=2.4.1.132
EC=2.4.1.257

Alternative name(s):
Asparagine-linked glycosylation protein 2
GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase
GDP-Man:Man(1)GlcNAc(2)-PP-dolichol mannosyltransferase
GDP-Man:Man(2)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase

Gene names

Name:	alg2
ORF Names:	SPBC11B10.01, SPBC32H8.14, pi010

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	511 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Mannosylates Man2GlcNAc(2)-dolichol diphosphate and Man1GlcNAc(2)-dolichol diphosphate to form Man3GlcNAc(2)-dolichol diphosphate By similarity.
Catalytic activity	GDP-D-mannose + D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = GDP + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-GlcNAc-diphosphodolichol. GDP-D-mannose + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = GDP + D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.

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	oligosaccharide-lipid intermediate biosynthetic process Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	GDP-Man:Man1GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity Inferred from sequence or structural similarity. Source: GeneDB_Spombe glycolipid 6-alpha-mannosyltransferase activity Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 511	511	Alpha-1,3/1,6-mannosyltransferase alg2		PRO_0000080269
Regions
	Transmembrane	82 – 104	23	Helical; Potential
	Transmembrane	118 – 138	21	Helical; Potential
	Transmembrane	448 – 468	21	Helical; Potential
	Transmembrane	486 – 506	21	Helical; Potential
Amino acid modifications
	Glycosylation	304	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	220 – 224	5	Missing in BAA21387. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q96WW6 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: F4A54D44FB26743E	FASTA	511	57,850
	10 20 30 40 50 60 MSQENSVHRS STKKTPIKIA FIHPDLGIGG AERLVVDAAV GLQSLGKEVV VFTSHCDKKH 70 80 90 100 110 120 CFEEIRDGTI KVKVYGDWLP SSIFGRLSIF CSSLRQVYLT MILLTNYMHF DAIIVDQLST 130 140 150 160 170 180 CVPFLLLASQ MILFYCHFPD KYLAKRGGIL KKLYRIPFDT VEAESVRLAD RIVVNSKFTA 190 200 210 220 230 240 SVFKKAFPKI RKPLRIVHPC VDIEAASKPL EFQLPEKILY LRYSQRKLLI SVNRFERKKD 250 260 270 280 290 300 IRLAIDAFSA LRDLSANRFP EYLLLVAGGY DIRVSENRRY LKELQEFCEQ KDLSYTTVKD 310 320 330 340 350 360 NWDNITVAPS TNVLFLLSVP SKVRDALISS SRILLYTPEN EHFGIVPLEA MLRKVPVLAQ 370 380 390 400 410 420 TNGGPLETVI DGKNGWLRPR DAKIWGNVIY EATTSTTYDT AAMGEAGSEW VKNEFSTDAM 430 440 450 460 470 480 ARKFESEIMS GIRSITPEKR LMRRVNGLLA VFVLFMLFWG TCIIAATVPF AIIKLYFAQT 490 500 510 YSSVKLGFML GTCIVSVSFL TFTVYAKLTN L

References

[1]	"A 38 kb segment containing the cdc2 gene from the left arm of fission yeast chromosome II: sequence analysis and characterization of the genomic DNA and cDNAs encoded on the segment." Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K., Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y., Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M. Yeast 16:71-80(2000) [PubMed: 10620777] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[2]	"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: 972 / ATCC 24843.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB004534 Genomic DNA. Translation: BAA21387.2. CU329671 Genomic DNA. Translation: CAC37504.1.
RefSeq	NP_595621.2. NM_001021515.1.
3D structure databases
ProteinModelPortal	Q96WW6.
ModBase	Search...
Protein-protein interaction databases
STRING	Q96WW6.
Protein family/group databases
CAZy	GT4. Glycosyltransferase Family 4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2539854.
GenomeReviews	Gene locus alg2 in contig CU329671_GR.
KEGG	spo:SPBC11B10.01.
NMPDR	fig|4896.1.peg.1486.
Organism-specific databases
GeneDB_Spombe	SPBC11B10.01.
Phylogenomic databases
eggNOG	fuNOG05648.
GeneTree	EFGT00050000003719.
HOGENOM	HBG320579.
OMA	GDWLPRS.
OrthoDB	EOG47DDQK.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-003700-MONOMER.
Gene expression databases
ArrayExpress	Q96WW6.
Family and domain databases
InterPro	IPR001296. Glyco_trans_1. [Graphical view]
KO	K03843.
Pfam	PF00534. Glycos_transf_1. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALG2_SCHPO

Accession

Primary (citable) accession number: Q96WW6
Secondary accession number(s): O13604, Q96WV8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	December 1, 2001
Last modified:	January 25, 2012
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program