ID   MOK14_SCHPO             Reviewed;        1369 AA.
AC   Q9Y704;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Cell wall alpha-1,3-glucan synthase mok14;
DE            EC=2.4.1.183;
GN   Name=mok14; ORFNames=SPCC63.04;
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].
RC   STRAIN=972 / ATCC 24843;
RA   Katayama S., Dai H., Arellano M., Perez P., Toda T.;
RT   "Fission yeast alpha-glucan synthase Mok1 localizes closely with actin and
RT   play a role essential for cell morphogenesis and protein kinase C
RT   function.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND IDENTIFICATION BY
RP   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   -!- 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   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AB018383; BAA76560.1; -; Genomic_DNA.
DR   EMBL; CU329672; CAB40008.1; -; Genomic_DNA.
DR   PIR; T43433; T43433.
DR   RefSeq; NP_587978.1; NM_001022969.2.
DR   AlphaFoldDB; Q9Y704; -.
DR   SMR; Q9Y704; -.
DR   BioGRID; 276069; 5.
DR   STRING; 4896.SPCC63.04.1; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   iPTMnet; Q9Y704; -.
DR   PaxDb; Q9Y704; -.
DR   PRIDE; Q9Y704; -.
DR   EnsemblFungi; SPCC63.04.1; SPCC63.04.1:pep; SPCC63.04.
DR   GeneID; 2539506; -.
DR   KEGG; spo:SPCC63.04; -.
DR   PomBase; SPCC63.04; mok14.
DR   VEuPathDB; FungiDB:SPCC63.04; -.
DR   eggNOG; ENOG502QSGC; Eukaryota.
DR   HOGENOM; CLU_252570_0_0_1; -.
DR   OMA; EMPGWWY; -.
DR   PhylomeDB; Q9Y704; -.
DR   PRO; PR:Q9Y704; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005619; C:ascospore wall; IDA:PomBase.
DR   GO; GO:0036362; C:ascus membrane; IDA:PomBase.
DR   GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR   GO; GO:0047657; F:alpha-1,3-glucan synthase activity; IBA:GO_Central.
DR   GO; GO:0033201; F:alpha-1,4-glucan synthase activity; IMP:PomBase.
DR   GO; GO:0070591; P:ascospore wall biogenesis; 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; IBA:GO_Central.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR013534; Starch_synth_cat_dom.
DR   Pfam; PF08323; Glyco_transf_5; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
PE   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Glycosyltransferase; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..1369
FT                   /note="Cell wall alpha-1,3-glucan synthase mok14"
FT                   /id="PRO_0000080332"
FT   MOD_RES         219
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   1369 AA;  156162 MW;  A0E0DA357EB88E9A CRC64;
     MNIKKKSFLF QFLFGWIVLS SAQWLSVLDE AENLNSSFSL ESVDSFAPVR PRFIIDEDFA
     EDYNLTVDIL HRPLQENFDS FFPNVEAYVE SGNSNGDLMS DNGKLDDLNS RAAYSALKAL
     QNSYGSSHLY RFTPYELFGQ SIWIEEAPEV NHVGWSIMFD NLGRYFLLEL RGLREVTFAL
     FITFSIVPII TGILTVYIYK KKYCVIKFNK SGRSKKKDSW LKRSKDELLR TDSANLLTLN
     DNDEPVMIRH SCKRTCILFA TLEYNIPEWN IKIKIGGLGV MAELMSKTLK QYDLVWVVPC
     VGDITYPVAE TAPSLVVKVV NQDYEVKVFY HYKDNIKYVL LDSPIFRKRT SHDPYPPRMD
     DISSAIFYSV WNQSIAAIIR REKVDIYHIN DYHGALAPIY NLPEVIPCAI SLHNAEFQGL
     WPLQSSIDER EVCGLFNVSK TICREYIQFG NAFNLMHCGV SYVRRHQSGY GVVGVSNKYG
     QRSWVRYPVF WSLKKIGQLP NPDPTDIGLS VNPVNQQLPD FAEYASVRKE NKRKAQEWAG
     LTIDDEADLL VFVGRWSVQK GIDILADLAP TLLEKFNIQL IVVGPLIDLY GKFAAEKFMY
     IMERYPGRVF SKPEFVHLPP FIFEGADFAL IPSRDEPFGL VAVEFGRRGA ICIGSRVGGL
     GEMPGWWYSV ESSSTAYLLK QLEKSCTLAL KSTPEMRHKL RIAALQQRFP VDEWVALYDR
     LIRNCIKAHN KQQQRRSIKS FFSCITPNKP TKDVNDILSE KSAFSPADYE HSIDIREHTS
     YDANSMDNDS DEDNYEQAES IISSLSSSAL SELSYISESS MNIGSRLDER FIDANGVAIR
     DFSAELTYLT PENSKGKLSI DHFLNKVQSR WHDEEHHYYK TGFRKRVYKY LKIKDKKSKD
     VDPDDDLVNQ LPLNAYTKPR YKSAASTRLN IYQRILYLKV FTWPLYTIFL SLGQILSISS
     FQLSLLSGFE DNNQISLYVI TGVFILSTIV WWGLYRNLPS VHSLSLPFAV YALAFLFTGI
     SSMSLPYHIR GWLSYAATWV YAIAAASGPL YFTLNFEDEH CSGLGSSITR ACVLQGVQQL
     WLSFLWLWGT LSSRLDYNYK VLLQPINSVY VVAGVWPVSF VLLSVCILLY KGLPPFYRQK
     PGSIPAFSKS LLHRKVVICF LISVINQNFW MSTLISQAWR FFWGSKLTKL WKIVVMTVSF
     LVGAWLIIFY VLRKLSNKHT WMVPVLGLGF GAIKWMHVFW GTSNVGIFLP WAGIAGPYLS
     RALWLWLGIL DSIQGIGNGL ILLQTLSRRH VTNTLMISQL AGSATSILAR FVSPTKTGPA
     NVFPDLTGYT PVDRAKPVAN APFWICLILN VALCIMYLRC YHRENISRP