位置:首页 > 蛋白库 > AGS1_SCHPO
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024