AGS1_SCHPO
ID AGS1_SCHPO Reviewed; 2410 AA.
AC Q9USK8; P78852; Q9URK2; Q9URT5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 3.
DT 25-MAY-2022, entry version 155.
DE RecName: Full=Cell wall alpha-1,3-glucan synthase ags1;
DE EC=2.4.1.183;
DE AltName: Full=Cell wall alpha-1,4-glucan synthase;
GN Name=ags1; Synonyms=mok1; ORFNames=SPCC1281.01, SPCC17A7.01, SPCC338.01c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10087262; DOI=10.1083/jcb.144.6.1173;
RA Katayama S., Hirata D., Arellano M., Perez P., Toda T.;
RT "Fission yeast alpha-glucan synthase Mok1 requires the actin cytoskeleton
RT to localize the sites of growth and plays an essential role in cell
RT morphogenesis downstream of protein kinase C function.";
RL J. Cell Biol. 144:1173-1186(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=9689051; DOI=10.1073/pnas.95.16.9161;
RA Hochstenbach F., Klis F.M., van den Ende H., van Donselaar E., Peters P.J.,
RA Klausner R.D.;
RT "Identification of a putative alpha-glucan synthase essential for cell wall
RT construction and morphogenesis in fission yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:9161-9166(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2044-2410.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [5]
RP INTERACTION WITH SAD1.
RX PubMed=14655046; DOI=10.1007/s00438-003-0938-8;
RA Miki F., Kurabayashi A., Tange Y., Okazaki K., Shimanuki M., Niwa O.;
RT "Two-hybrid search for proteins that interact with Sad1 and Kms1, two
RT membrane-bound components of the spindle pole body in fission yeast.";
RL Mol. Genet. Genomics 270:449-461(2004).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF GLU-1526.
RX PubMed=17472966; DOI=10.1074/jbc.m605147200;
RA Vos A., Dekker N., Distel B., Leunissen J.A., Hochstenbach F.;
RT "Role of the synthase domain of Ags1p in cell wall {alpha}-glucan
RT biosynthesis in fission yeast.";
RL J. Biol. Chem. 282:18969-18979(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1643; SER-1644; SER-1651;
RP THR-1653; SER-1738 AND SER-1812, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Required for alpha-1,3-glucan and alpha-1,4-glucan production
CC which are required for cell wall synthesis.
CC {ECO:0000269|PubMed:17472966}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19749, Rhea:RHEA-
CC COMP:11150, Rhea:RHEA-COMP:11151, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28100, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC EC=2.4.1.183;
CC -!- SUBUNIT: Interacts with sad1. {ECO:0000269|PubMed:14655046}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC {ECO:0000305}.
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DR EMBL; AB019183; BAA34054.1; -; Genomic_DNA.
DR EMBL; AF061180; AAC31430.1; -; Genomic_DNA.
DR EMBL; AF063305; AAC39519.1; -; mRNA.
DR EMBL; CU329672; CAA19332.1; -; Genomic_DNA.
DR EMBL; D89202; BAA13863.1; -; mRNA.
DR PIR; T43731; T43731.
DR RefSeq; NP_588165.3; NM_001023154.3.
DR AlphaFoldDB; Q9USK8; -.
DR IntAct; Q9USK8; 1.
DR STRING; 4896.SPCC1281.01.1; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR iPTMnet; Q9USK8; -.
DR MaxQB; Q9USK8; -.
DR PaxDb; Q9USK8; -.
DR PRIDE; Q9USK8; -.
DR GeneID; 2539007; -.
DR KEGG; spo:SPCC1281.01; -.
DR PomBase; SPCC1281.01; ags1.
DR eggNOG; ENOG502QSGC; Eukaryota.
DR HOGENOM; CLU_000488_0_0_1; -.
DR InParanoid; Q9USK8; -.
DR PhylomeDB; Q9USK8; -.
DR BRENDA; 2.4.1.B3; 5613.
DR PRO; PR:Q9USK8; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005619; C:ascospore wall; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0000935; C:division septum; IDA:PomBase.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0071575; C:integral component of external side of plasma membrane; TAS:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IDA:PomBase.
DR GO; GO:0032178; C:medial membrane band; EXP:PomBase.
DR GO; GO:0035841; C:new growing cell tip; IDA:PomBase.
DR GO; GO:0035840; C:old growing cell tip; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0031520; C:plasma membrane of cell tip; EXP:PomBase.
DR GO; GO:0047657; F:alpha-1,3-glucan synthase activity; IMP:PomBase.
DR GO; GO:0033201; F:alpha-1,4-glucan synthase activity; IMP:PomBase.
DR GO; GO:0030979; P:alpha-glucan biosynthetic process; IMP:PomBase.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0070600; P:fungal-type cell wall (1->3)-alpha-glucan biosynthetic process; IMP:PomBase.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IMP:PomBase.
DR GO; GO:0031671; P:primary cell septum biogenesis; IMP:PomBase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013534; Starch_synth_cat_dom.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF08323; Glyco_transf_5; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Glycosyltransferase;
KW Multifunctional enzyme; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..2410
FT /note="Cell wall alpha-1,3-glucan synthase ags1"
FT /id="PRO_0000080328"
FT REGION 1685..1706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1796..1827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1643
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1644
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1651
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1653
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1738
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1812
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 1526
FT /note="E->A: No accumulation of alpha-1,4-glucan."
FT /evidence="ECO:0000269|PubMed:17472966"
FT CONFLICT 256
FT /note="F -> Y (in Ref. 3; CAA19332)"
FT /evidence="ECO:0000305"
FT CONFLICT 1849
FT /note="V -> A (in Ref. 1; BAA34054)"
FT /evidence="ECO:0000305"
FT CONFLICT 2028
FT /note="G -> C (in Ref. 1; BAA34054)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2410 AA; 272106 MW; 3C0959CDAEA1092C CRC64;
MHGLQGLCFR RAVIALALLL FHSVFAAPYS EDEEPWNLNQ NKNASSVLEY SGEWADHDFF
PSPDNWRMSF ITVILDRWYD GDPSNNDIEK TPFEYDISEV SFRNGGDIVG LELSLDYLEG
LGTQGIYIAG TPFVNMPWGA DQYSPLDYTI LDHHLGTIDQ WRSTITAMHE RGMYLVVDLT
VATLGDLIGM VGHLNDTSGV DFNLNEYNAM WKTSEYRYVD FNFTNVYNTS CEYPRFWGED
GGPVSIQFKG CYVSDFDHYG DTEAFGSHPD WQRQLSKFAS VQDRLRDWKP DVAEKLMHLS
CLVISMLDVD GFRIDKATQM TADFIVDWSM YVRECAAKYN KKNFLIVGEV TGSSSYGSIY
YNRGRQPDQR PPNVTAAFNY TSDESQYSLR DSDHYGFDGS AFHYSIYRAL LRFLGMDSKM
EIDFDVSSVL TTAWNGIQIN EDAVNINTGT VEPLHMYGVA NHDVFRWGAI ENGTARLILG
TMITSLLFPG IPLLYYGDEQ GMYVLDNSAN NYLYGRQAMN SARAWYIHGC YNGSATSYPT
VDLSPAQRGC QDSWNYLDHF DIASAHRNVY RNIHSIRRHY LSLSEGWRFD HIANWTDDVY
FPDSQPYASP MGLYSVLRGP MKEIQDFDSI TNASNVSKSE VWVLYANRND THLWSYDCTD
EDSAIIGPWK SGTTLRNLIY PYDTIELEDS WNSSWGCIPN IELDPYAFKL YVPEEDFIEN
DPIITSLTPE HDARVVASGN EIDLTIEFSR SMDCDSIKNA LSVVSSTRPK NTTAVIDVDS
SFCRNYSEDA STSLHGQTAG RFAWYGTLTN IDPGIHRISL KSVPTSDFSS RTLSTDNFLI
RVGSTNNPIV HYSANYSDTL LIMQDGDLYI NHSAPGAVLF RYSTDFQSHW SDWEEYNGGL
TKVQASNWTG TRRQGWEGHH IHVQYWSDLG GSANHMQQSD YGFKYRRFLP HMFLEGDFNE
YGYDSGVENR FLQKSDFYWE AGFISETYPA AIQLNVWGMN PDGIPDKTRV YGSQGNSTVL
SRSDPASLVG NNITIYHPPP HGYLSYKILL RDDDMIYRLA PSGEWGVSIA IYVLCIVIPP
LSAIVVSWAF KNSFYTVKFN KHGNNDLGKF YPLKSLVPFR KKNDLDSPAK VTPVVSGVSA
RKKKCVLIAT LEYDITDWKI RIKIGGLGVM AQLMAQHLKH EDLVWVVPCV GDVVYPEAEE
ASPIEVKIID QTYTINVYHH YLDNIKYVLL DAPVFRRQTS KEPYPARMDD LGSAIFYSAW
NQCIAEVIRR NPIDIYHIND YHGALAPCYL LPDIIPCALS LHNAEFQGLW PLRTPEEKEE
VCAVYNISQR VCTKYVQFGN VFNLLHAAVS YIRIHQKGFG AVGVSNKYGK RSWARYPIFW
GLKKIGKLPN PDPTDTDEIV DDKAVAITDI DPDMEKSKVE HKRLAQEWAG LEVNEKYDLL
VFVGRWSSQK GIDLIADIAP SLLESYKVQL ICVGPIIDLY GKFAAEKLDV LQKKYPTRVF
SQPKFTQLPP YIFSGADFAL IPSRDEPFGL VAVEFGRKGA LGIGARVGGL GQMPGWWYSV
ESSATPHLLK QFEQACQQAL SSSQRTRARL RARSAKQRFP VSQWKAKLEA LTDGCIKCSQ
KYGRNSRSRS SFYSLIHESF SRSSEVLPTS SDTNLDAKRA EEAEMIMIET PPTAEANTGA
KLDRSLSLGS RRGPGHTTED DASDGLDTIQ EESMTAGDST SGGSDISRYR AERLNPDSHS
PSEYSFDSGD YEFDPQRSYY YDDLFDDDTT IRNAPSFRPQ MGSFDAEHAV GATFSQDDLS
DPARSVDSDS VSPPLPPFVA GSNPNARNNN NPYFYGNLHT ESSLSLASVM SGKEKRDFSL
TRVEETFTDE DGQALRSFSE KLQKLNAKNS KDDLCIEQYL MKSERSFFHE RRAIKLGLQK
PNKLHVNELS SHSGTEESES LSNGQTSYDD IIAMTDESNY TQLGDDDFKT IHGLKKFMLF
KIYDWPIYSI FLALGQILAA TAYQLTLFTG TSNIQTYEIY SVCAFFIGAS FVWWFMFARL
PSYYVLSIPW LFYAVALFLV GLPAFDTVAP GRVWITNVAA WIYAIASASG SIFFSLNFGE
EGAVQTRIWV FRACLVQGVQ QVWSAALWYW GAHLNKRLTA GEANTFKMSP AIPSITWPLS
AVSILIFALL FKGLPEYYRQ LSGSIPAFYK SLLRRKLVVW FCISVFLQNF WLSSLNGRSW
SYLWDIGNIH QWQIFLLIVA FYIVLWALLL GVLAWISRTH SWIICVFGVG LGAPRWLQQF
WATSNIGLYL PWAGYSGPYL GRTLWLWLGV LDAIQSVGIG MILLQTLTRR HVASTLMTGQ
IVGAVATMIG RGASPNREGP ANVFIDFTKW NHGDGSSILA SAPFWINIIC QLAICVGYLA
FFRRENLSRP
