BGS3_SCHPO
ID BGS3_SCHPO Reviewed; 1826 AA.
AC Q9P377; Q9UU03;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=1,3-beta-glucan synthase component bgs3;
DE EC=2.4.1.34;
DE AltName: Full=1,3-beta-D-glucan-UDP glucosyltransferase;
GN Name=bgs3; ORFNames=SPAC19B12.03;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12582133; DOI=10.1128/ec.2.1.159-169.2003;
RA Martin V., Garcia B., Carnero E., Duran A., Sanchez Y.;
RT "Bgs3p, a putative 1,3-beta-glucan synthase subunit, is required for cell
RT wall assembly in Schizosaccharomyces pombe.";
RL Eukaryot. Cell 2:159-169(2003).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 159-339.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-885, 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 -!- FUNCTION: Required for cell wall biosynthesis and cell elongation.
CC {ECO:0000269|PubMed:12582133}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-
CC COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12582133}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:12582133}. Note=Found at the
CC growing tips during interphase and at the septum prior to cytokinesis.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000305}.
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DR EMBL; AJ249371; CAC69670.1; -; Genomic_DNA.
DR EMBL; CU329670; CAC00551.1; -; Genomic_DNA.
DR EMBL; AB027891; BAA87195.1; -; Genomic_DNA.
DR RefSeq; NP_594766.1; NM_001020193.2.
DR AlphaFoldDB; Q9P377; -.
DR BioGRID; 279046; 1.
DR STRING; 4896.SPAC19B12.03.1; -.
DR CAZy; GT48; Glycosyltransferase Family 48.
DR iPTMnet; Q9P377; -.
DR MaxQB; Q9P377; -.
DR PaxDb; Q9P377; -.
DR PRIDE; Q9P377; -.
DR EnsemblFungi; SPAC19B12.03.1; SPAC19B12.03.1:pep; SPAC19B12.03.
DR GeneID; 2542591; -.
DR KEGG; spo:SPAC19B12.03; -.
DR PomBase; SPAC19B12.03; bgs3.
DR VEuPathDB; FungiDB:SPAC19B12.03; -.
DR eggNOG; KOG0916; Eukaryota.
DR HOGENOM; CLU_000844_0_1_1; -.
DR InParanoid; Q9P377; -.
DR OMA; FTFEALW; -.
DR PhylomeDB; Q9P377; -.
DR PRO; PR:Q9P377; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IC:PomBase.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030427; C:site of polarized growth; IDA:PomBase.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; ISO:PomBase.
DR GO; GO:0046527; F:glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR GO; GO:0051274; P:beta-glucan biosynthetic process; IMP:PomBase.
DR GO; GO:0071970; P:fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process; TAS:PomBase.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IMP:PomBase.
DR GO; GO:0051278; P:fungal-type cell wall polysaccharide biosynthetic process; IBA:GO_Central.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 1.
DR SMART; SM01205; FKS1_dom1; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Membrane; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1826
FT /note="1,3-beta-glucan synthase component bgs3"
FT /id="PRO_0000121723"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 543..563
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 597..617
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 637..657
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 660..680
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1272..1292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1329..1349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1375..1397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1417..1437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1438..1458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1531..1551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1571..1591
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1607..1627
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1642..1662
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1701..1721
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1770..1790
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 34..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 885
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1826 AA; 210828 MW; 01D991608BB7AEBB CRC64;
MDYKKGEHSP SSSIQILSDD ATINSNYAYG EQLQSNDQYN NIQHPAPSFA NPFIHEQDDS
YSDILEEEPD EDAYDSPERP SSTEEFISQD ESNISAGSSF MFPYNRGHPL SKRHDSIMVD
EFGHEYIVEG DSIASADEAI DYDALYASWT AETKAPILAI DIENIYIELA MKFGFQWDNM
RNMFDYLMVM LDSRASRMTP QEALLTLHAD YIGGPQSNFK KWYFACKMDQ FDLKSGVLSF
ISRDPSTQVP YKDMSSCEAL WISRMDELSN YERIEQLALY LLCWGEANNV RFMPECLCFI
YKVAYDYLIS PSFKEQKNPA PKDYFLDNCI TPLYNLMHDQ QYEIRDQKYV RKEKDHASII
GYDDINQMFW YSKGLKALLL SDGSRIMDAD VASRYFLLAD IQWQRVCYKS FRESRTWLHF
LHNFSRIWIL HISVFWYFTV YNSPTIYTPN FHYLEGTQPA RAAKWCAPAL AGAVASFISF
LALILEAYFV PRNNPGAQPV IPRLIFVSIL IALNIVPAAF IFGFSNATQQ HYRSREIVGY
VHFFFSIGCV AYQSFIPLPF LLGPRFKFRS SSRKYLANSY FTNDIASLPW GRTLLSAALW
ITVFIAKFVE SYYFLTLSVR DPIRFLQRMK PYDCYDFMIG ASLCSHQPKF LLSLVYLTDL
VLFFLDTYLW YMLISTMFSI AYSFYMGSAI WTPWRVIFSN LPRRIYFTLL AYKDLSTEFK
PKIYVGQIWN SIMISMYREH LLSLEHLKGL LYQQVGSEYF GKQTFQSPKF FMEAAKGLNK
WDAFFRRNSE AERRISFFAQ SLGGKIPDAV PVPKMPSFTV LIPHYGEKIL LSLREIIREQ
DPMSRITLLE YLKQLYPNDW DNFVQDTKLM AGDVGVEETK SDVKSEKGKK QGTVKEDLPF
YCIGFKSTAP EYTLRTRIWA SLRSQTLYRT ASGMMNYSRA LKLLYRVEQP NLLDDCDGNF
ERLEHQLEQM AYRKFRLCIS MQRYAKFNRD EYENAEFLLR AHPELQIAYL DQDPSEDGEE
PKVYATLING FCPFENGRRL PKYRIRLSGN PILGDGKADN QNMALPFVRG EYLQLIDANQ
DNYIEECMKI RNVLSEFEEM DCATLTPYTK KGNARHPVAM LGAREYVFSE NSGILGDVAA
GKEQTFGTLF SRSLALIGGK LHYGHPDFLN TIFMTTRGGV SKAQKGLHVN EDIYAGMTAL
QRGGRIKHCD YFQCGKGRDL GFGTIINFTT KIGTGMGEQS LSREYFYLGT QLPFFRMLSF
YYAHAGFHLN NVFIMISMQL LMLVFVNLGA MYHTVEICDY QAGAAINASL YPPGCYMLKP
VLDWIRRCII SIFIVFFISF LPLVVHDLLE KGVIRAVARL CKQIFSLSPM FEVFVTQNYA
NSIFTNLTYG GARYIATGRG LATTRVPFSV LYSLYTGSSI YLGSRLIMML LFGTMTVWTT
HYVYFWVTMF ALVICPFIYN PHQFSFVDFF VDYREFLRWL SRGNTKGHAH SWIGFCRLAR
TRITGVNRKV KGSPSNKLTM DMPRAGLRNV IFTEVFLPAC FAFFTICAYT FMNSQPGLED
KSRAVNGFIR IWIMAALPIA ISTAALLILL MFSCMLGPLL RKCSKRYGAV LAALAHAVSV
FGLVFTFEAL WFLEAWSFSK TVLGCIVIFA IHRLVFKLVV VFLLPREVAS GENNYSWWDG
HWFGRKGIPY MPIQFIREFM CKVVEMNLFA MDFILSHCIL FSLTPILCIP FIDIPHSVLL
FWLHPSRQIR PPIYTRKQNQ LRRRTFYRYS LLFFALLCTF VAMIVVPLVL DQKLSYQFKF
ENSVKFFRLM QPSLGVLPNT NKNTSE
