Reviewed, UniProtKB/Swiss-Prot Q9USK8 (AGS1_SCHPO)

Names and origin

Protein names

Recommended name:
    Cell wall alpha-1,3-glucan synthase ags1
    EC=2.4.1.183
Alternative name(s):
    Cell wall alpha-1,4-glucan synthase

Gene names

Name:	ags1
Synonyms:	mok1
ORF Names:	SPCC1281.01, SPCC338.01c, SPCC17A7.01

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	2410 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Required for alpha-1,3-glucan and alpha-1,4-glucan production which are required for cell wall synthesis. Ref.6
Catalytic activity	UDP-glucose + (alpha-D-glucosyl-(1->3))(n) = UDP + (alpha-D-glucosyl-(1->3))(n+1).
Subunit structure	Interacts with sad1. Ref.5
Sequence similarities	Belongs to the glycosyltransferase 1 family.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Molecular function	Glycosyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	alpha-glucan biosynthetic process Ref.6 Inferred from mutant phenotype. Source: GeneDB_SPombe cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW cellular polysaccharide catabolic process Inferred by curator. Source: GeneDB_SPombe fungal-type cell wall biogenesis Ref.2 Inferred from mutant phenotype. Source: GeneDB_SPombe
Cellular component	external side of plasma membrane Ref.6 Traceable author statement. Source: GeneDB_SPombe integral to plasma membrane Ref.6 Traceable author statement. Source: GeneDB_SPombe internal side of plasma membrane Ref.6 Traceable author statement. Source: GeneDB_SPombe
Molecular function	alpha-1,3-glucan synthase activity Inferred from electronic annotation. Source: EC alpha-1,4-glucan synthase activity Ref.6 Inferred from mutant phenotype. Source: GeneDB_SPombe cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2410	2410	Cell wall alpha-1,3-glucan synthase ags1		PRO_0000080328
Amino acid modifications
	Modified residue	1643	1	Phosphoserine Ref.7
	Modified residue	1644	1	Phosphoserine Ref.7
	Modified residue	1651	1	Phosphoserine Ref.7
	Modified residue	1653	1	Phosphothreonine Ref.7
	Modified residue	1738	1	Phosphoserine Ref.7
	Modified residue	1812	1	Phosphoserine Ref.7
Experimental info
	Mutagenesis	1526	1	E → A: No accumulation of alpha-1,4-glucan. Ref.6
	Sequence conflict	256	1	F → Y in CAA19332. Ref.3
	Sequence conflict	1849	1	V → A in BAA34054. Ref.1
	Sequence conflict	2028	1	G → C in BAA34054. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9USK8-1 [UniParc]. Last modified February 12, 2003. Version 3. Checksum: 3C0959CDAEA1092C	FASTA	2,410	272,106
	10 20 30 40 50 60 MHGLQGLCFR RAVIALALLL FHSVFAAPYS EDEEPWNLNQ NKNASSVLEY SGEWADHDFF 70 80 90 100 110 120 PSPDNWRMSF ITVILDRWYD GDPSNNDIEK TPFEYDISEV SFRNGGDIVG LELSLDYLEG 130 140 150 160 170 180 LGTQGIYIAG TPFVNMPWGA DQYSPLDYTI LDHHLGTIDQ WRSTITAMHE RGMYLVVDLT 190 200 210 220 230 240 VATLGDLIGM VGHLNDTSGV DFNLNEYNAM WKTSEYRYVD FNFTNVYNTS CEYPRFWGED 250 260 270 280 290 300 GGPVSIQFKG CYVSDFDHYG DTEAFGSHPD WQRQLSKFAS VQDRLRDWKP DVAEKLMHLS 310 320 330 340 350 360 CLVISMLDVD GFRIDKATQM TADFIVDWSM YVRECAAKYN KKNFLIVGEV TGSSSYGSIY 370 380 390 400 410 420 YNRGRQPDQR PPNVTAAFNY TSDESQYSLR DSDHYGFDGS AFHYSIYRAL LRFLGMDSKM 430 440 450 460 470 480 EIDFDVSSVL TTAWNGIQIN EDAVNINTGT VEPLHMYGVA NHDVFRWGAI ENGTARLILG 490 500 510 520 530 540 TMITSLLFPG IPLLYYGDEQ GMYVLDNSAN NYLYGRQAMN SARAWYIHGC YNGSATSYPT 550 560 570 580 590 600 VDLSPAQRGC QDSWNYLDHF DIASAHRNVY RNIHSIRRHY LSLSEGWRFD HIANWTDDVY 610 620 630 640 650 660 FPDSQPYASP MGLYSVLRGP MKEIQDFDSI TNASNVSKSE VWVLYANRND THLWSYDCTD 670 680 690 700 710 720 EDSAIIGPWK SGTTLRNLIY PYDTIELEDS WNSSWGCIPN IELDPYAFKL YVPEEDFIEN 730 740 750 760 770 780 DPIITSLTPE HDARVVASGN EIDLTIEFSR SMDCDSIKNA LSVVSSTRPK NTTAVIDVDS 790 800 810 820 830 840 SFCRNYSEDA STSLHGQTAG RFAWYGTLTN IDPGIHRISL KSVPTSDFSS RTLSTDNFLI 850 860 870 880 890 900 RVGSTNNPIV HYSANYSDTL LIMQDGDLYI NHSAPGAVLF RYSTDFQSHW SDWEEYNGGL 910 920 930 940 950 960 TKVQASNWTG TRRQGWEGHH IHVQYWSDLG GSANHMQQSD YGFKYRRFLP HMFLEGDFNE 970 980 990 1000 1010 1020 YGYDSGVENR FLQKSDFYWE AGFISETYPA AIQLNVWGMN PDGIPDKTRV YGSQGNSTVL 1030 1040 1050 1060 1070 1080 SRSDPASLVG NNITIYHPPP HGYLSYKILL RDDDMIYRLA PSGEWGVSIA IYVLCIVIPP 1090 1100 1110 1120 1130 1140 LSAIVVSWAF KNSFYTVKFN KHGNNDLGKF YPLKSLVPFR KKNDLDSPAK VTPVVSGVSA 1150 1160 1170 1180 1190 1200 RKKKCVLIAT LEYDITDWKI RIKIGGLGVM AQLMAQHLKH EDLVWVVPCV GDVVYPEAEE 1210 1220 1230 1240 1250 1260 ASPIEVKIID QTYTINVYHH YLDNIKYVLL DAPVFRRQTS KEPYPARMDD LGSAIFYSAW 1270 1280 1290 1300 1310 1320 NQCIAEVIRR NPIDIYHIND YHGALAPCYL LPDIIPCALS LHNAEFQGLW PLRTPEEKEE 1330 1340 1350 1360 1370 1380 VCAVYNISQR VCTKYVQFGN VFNLLHAAVS YIRIHQKGFG AVGVSNKYGK RSWARYPIFW 1390 1400 1410 1420 1430 1440 GLKKIGKLPN PDPTDTDEIV DDKAVAITDI DPDMEKSKVE HKRLAQEWAG LEVNEKYDLL 1450 1460 1470 1480 1490 1500 VFVGRWSSQK GIDLIADIAP SLLESYKVQL ICVGPIIDLY GKFAAEKLDV LQKKYPTRVF 1510 1520 1530 1540 1550 1560 SQPKFTQLPP YIFSGADFAL IPSRDEPFGL VAVEFGRKGA LGIGARVGGL GQMPGWWYSV 1570 1580 1590 1600 1610 1620 ESSATPHLLK QFEQACQQAL SSSQRTRARL RARSAKQRFP VSQWKAKLEA LTDGCIKCSQ 1630 1640 1650 1660 1670 1680 KYGRNSRSRS SFYSLIHESF SRSSEVLPTS SDTNLDAKRA EEAEMIMIET PPTAEANTGA 1690 1700 1710 1720 1730 1740 KLDRSLSLGS RRGPGHTTED DASDGLDTIQ EESMTAGDST SGGSDISRYR AERLNPDSHS 1750 1760 1770 1780 1790 1800 PSEYSFDSGD YEFDPQRSYY YDDLFDDDTT IRNAPSFRPQ MGSFDAEHAV GATFSQDDLS 1810 1820 1830 1840 1850 1860 DPARSVDSDS VSPPLPPFVA GSNPNARNNN NPYFYGNLHT ESSLSLASVM SGKEKRDFSL 1870 1880 1890 1900 1910 1920 TRVEETFTDE DGQALRSFSE KLQKLNAKNS KDDLCIEQYL MKSERSFFHE RRAIKLGLQK 1930 1940 1950 1960 1970 1980 PNKLHVNELS SHSGTEESES LSNGQTSYDD IIAMTDESNY TQLGDDDFKT IHGLKKFMLF 1990 2000 2010 2020 2030 2040 KIYDWPIYSI FLALGQILAA TAYQLTLFTG TSNIQTYEIY SVCAFFIGAS FVWWFMFARL 2050 2060 2070 2080 2090 2100 PSYYVLSIPW LFYAVALFLV GLPAFDTVAP GRVWITNVAA WIYAIASASG SIFFSLNFGE 2110 2120 2130 2140 2150 2160 EGAVQTRIWV FRACLVQGVQ QVWSAALWYW GAHLNKRLTA GEANTFKMSP AIPSITWPLS 2170 2180 2190 2200 2210 2220 AVSILIFALL FKGLPEYYRQ LSGSIPAFYK SLLRRKLVVW FCISVFLQNF WLSSLNGRSW 2230 2240 2250 2260 2270 2280 SYLWDIGNIH QWQIFLLIVA FYIVLWALLL GVLAWISRTH SWIICVFGVG LGAPRWLQQF 2290 2300 2310 2320 2330 2340 WATSNIGLYL PWAGYSGPYL GRTLWLWLGV LDAIQSVGIG MILLQTLTRR HVASTLMTGQ 2350 2360 2370 2380 2390 2400 IVGAVATMIG RGASPNREGP ANVFIDFTKW NHGDGSSILA SAPFWINIIC QLAICVGYLA 2410 FFRRENLSRP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Fission yeast alpha-glucan synthase Mok1 requires the actin cytoskeleton to localize the sites of growth and plays an essential role in cell morphogenesis downstream of protein kinase C function." Katayama S., Hirata D., Arellano M., Perez P., Toda T. J. Cell Biol. 144:1173-1186(1999) [PubMed: 10087262] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Identification of a putative alpha-glucan synthase essential for cell wall construction and morphogenesis in fission yeast." Hochstenbach F., Klis F.M., van den Ende H., van Donselaar E., Peters P.J., Klausner R.D. Proc. Natl. Acad. Sci. U.S.A. 95:9161-9166(1998) [PubMed: 9689051] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[3]	"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.
[4]	"Identification of open reading frames in Schizosaccharomyces pombe cDNAs." Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H. DNA Res. 4:363-369(1997) [PubMed: 9501991] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2044-2410. Strain: PR745.
[5]	"Two-hybrid search for proteins that interact with Sad1 and Kms1, two membrane-bound components of the spindle pole body in fission yeast." Miki F., Kurabayashi A., Tange Y., Okazaki K., Shimanuki M., Niwa O. Mol. Genet. Genomics 270:449-461(2004) [PubMed: 14655046] [Abstract] Cited for: INTERACTION WITH SAD1.
[6]	"Role of the synthase domain of Ags1p in cell wall {alpha}-glucan biosynthesis in fission yeast." Vos A., Dekker N., Distel B., Leunissen J.A., Hochstenbach F. J. Biol. Chem. 282:18969-18979(2007) [PubMed: 17472966] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLU-1526.
[7]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1643; SER-1644; SER-1651; THR-1653; SER-1738 AND SER-1812, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB019183 Genomic DNA. Translation: BAA34054.1. AF061180 Genomic DNA. Translation: AAC31430.1. AF063305 mRNA. Translation: AAC39519.1. CU329672 Genomic DNA. Translation: CAA19332.1. D89202 mRNA. Translation: BAA13863.1.
PIR	T43731.
RefSeq	NP_588165.3.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9USK8. 1 interaction.
Protein family/group databases
CAZy	GH13. Glycoside Hydrolase Family 13. GT5. Glycosyltransferase Family 5.
Genome annotation databases
GeneID	2539007.
GenomeReviews	Gene locus ags1 in contig CU329672_GR.
KEGG	spo:SPCC1281.01.
Organism-specific databases
GeneDB_Spombe	SPCC1281.01.
Phylogenomic databases
HOGENOM	HBG326621.
OrthoDB	EOG9XKWQ8.
Enzyme and pathway databases
BRENDA	2.4.1.183. 653.
Gene expression databases
ArrayExpress	Q9USK8.
Family and domain databases
InterPro	IPR006047. Glyco_hydro_13_cat. IPR017853. Glyco_hydro_catalytic_core. IPR013781. Glyco_hydro_sg_catalytic. IPR001296. Glyco_trans_1. IPR013534. Glyco_transf_5. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF00128. Alpha-amylase. 1 hit. PF08323. Glyco_transf_5. 1 hit. PF00534. Glycos_transf_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AGS1_SCHPO

Accession

Primary (citable) accession number: Q9USK8
Secondary accession number(s): P78852, Q9URK2, Q9URT5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	February 12, 2003
Last modified:	December 15, 2009
This is version 80 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)