BGS2_SCHPO
ID BGS2_SCHPO Reviewed; 1894 AA.
AC O13967; Q96WS3;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=1,3-beta-glucan synthase component bgs2;
DE EC=2.4.1.34;
DE AltName: Full=1,3-beta-D-glucan-UDP glucosyltransferase;
DE AltName: Full=Meiotic expression up-regulated protein 21;
GN Name=bgs2; Synonyms=meu21; ORFNames=SPAC24C9.07c;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1717-1894.
RC STRAIN=CD16-1;
RX PubMed=11376151; DOI=10.1093/nar/29.11.2327;
RA Watanabe T., Miyashita K., Saito T.T., Yoneki T., Kakihara Y.,
RA Nabeshima K., Kishi Y.A., Shimoda C., Nojima H.;
RT "Comprehensive isolation of meiosis-specific genes identifies novel
RT proteins and unusual non-coding transcripts in Schizosaccharomyces pombe.";
RL Nucleic Acids Res. 29:2327-2337(2001).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=11069657; DOI=10.1046/j.1365-2958.2000.02118.x;
RA Martin V., Ribas J.C., Carnero E., Duran A., Sanchez Y.;
RT "bgs2+, a sporulation-specific glucan synthase homologue is required for
RT proper ascospore wall maturation in fission yeast.";
RL Mol. Microbiol. 38:308-321(2000).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10922478; DOI=10.1016/s0014-5793(00)01828-7;
RA Liu J., Tang X., Wang H., Balasubramanian M.;
RT "Bgs2p, a 1,3-beta-glucan synthase subunit, is essential for maturation of
RT ascospore wall in Schizosaccharomyces pombe.";
RL FEBS Lett. 478:105-108(2000).
CC -!- FUNCTION: Has a role in ascospore development where it is required for
CC the assembly of a functional spore wall. {ECO:0000269|PubMed:10922478,
CC ECO:0000269|PubMed:11069657}.
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: Prospore membrane {ECO:0000269|PubMed:10922478,
CC ECO:0000269|PubMed:11069657}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10922478, ECO:0000269|PubMed:11069657}.
CC -!- INDUCTION: By sporulation. {ECO:0000269|PubMed:11069657}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB11264.2; -; Genomic_DNA.
DR EMBL; AB054305; BAB60872.1; -; mRNA.
DR PIR; T38348; T38348.
DR RefSeq; NP_594032.1; NM_001019457.2.
DR AlphaFoldDB; O13967; -.
DR BioGRID; 278083; 2.
DR STRING; 4896.SPAC24C9.07c.1; -.
DR CAZy; GT48; Glycosyltransferase Family 48.
DR PaxDb; O13967; -.
DR EnsemblFungi; SPAC24C9.07c.1; SPAC24C9.07c.1:pep; SPAC24C9.07c.
DR GeneID; 2541586; -.
DR KEGG; spo:SPAC24C9.07c; -.
DR PomBase; SPAC24C9.07c; bgs2.
DR VEuPathDB; FungiDB:SPAC24C9.07c; -.
DR eggNOG; KOG0916; Eukaryota.
DR HOGENOM; CLU_000844_0_1_1; -.
DR InParanoid; O13967; -.
DR OMA; IFVVAYM; -.
DR PhylomeDB; O13967; -.
DR PRO; PR:O13967; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IC: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:0005628; C:prospore membrane; IDA:PomBase.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IMP: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:0034413; P:ascospore wall (1->3)-beta-D-glucan biosynthetic process; 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 2: Evidence at transcript level;
KW Glycosyltransferase; Meiosis; Membrane; Reference proteome; Sporulation;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1894
FT /note="1,3-beta-glucan synthase component bgs2"
FT /id="PRO_0000121722"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 655..675
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 710..730
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 731..751
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1338..1358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1394..1414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1476..1498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1503..1525
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1598..1618
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1637..1657
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1673..1693
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1697..1717
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1778..1798
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1837..1857
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1894 AA; 219183 MW; 2DBA28A471AAED21 CRC64;
MSWHEQDYGF GTSSENSKIN SDEFEDSMDV TEFNNPGEES TYPQANSWND SNKTKDIAEY
YDYSWSGQRE ANQQIPQPVP VQPRYPDEQN FSMNGETYPS EAYDYDYSGQ EEAINAMNIL
QGNLERSNEY YSEGVPYSEE DLGAYAGGMT EDDQMYSNFN ETGEFNLDIG SSKFSYLNAK
NPYPAWIAEN SIPITAENIL EIFQELQAKF GFQYDSMLNM YDFFMVLLDS RSSRMDAENA
LKSLHADYIG GRNANYRKWY FSSSMDIDDS VGLQNCKFSS NGPKIKQAKK KQKRKSNKAE
TEGTNEPETS VQIDPLNVSM ENWENEMKNL DCETQVRQLA LYLLCWGEAN NIRFCPECLC
FIFKLANDFM QSEDYAKSEP IEDDCFYLDN VITPLYEFIR DQQFELLDGK LVRRERDHAQ
IIGYDDINQL FWYPEGIARI VTVDGTQLIT LPKWERFHKL SEVDWKKAFY KTFYESRSWF
HLVTNFNRIW VIHFTTYWYY TVFNSPTIIE KNFRQSVGPK PIPSCHWTSV SLGGAVATLL
MLLATIFEWI HVPRKFPGSR PLLKRFLILI LFFILNVAPT VFVFGFSTEE QQRTTGRLTV
AIVHFIFSVF TFIYFSLVPL NNLFHRAYKS SSRTHLANRY FTADYARLQI NDMCVSWGLW
LLVFGAKFTE SYFFLSLSFR DPILVLSTMK PYLCNITFLG SHLCIWQPKI LLGIMYVTDL
VLFFLDTYLW YILVNTVFSV ARSFFLGISI WTPWRNIFAR MPKRIYSKIL CTPEVDSSYK
PKVLVSQIWN SIIISLYREH LLAIEHVQRL IYHQVNSLDG DGSKTLKTPT FFVSQEDSSF
NTEYFPAHSE AERRLSFFAQ SLATPIPEPI PVDAMPTFTV LVPHYGEKIL LSLKEIIREQ
DKLSRVTLLE YLKQLHANEW KCFVRDTKIL AEEDALSNQD LNSQDESMKA EQLHKKFDDL
PFYCIGFKNA TPEYTLRTRI WASLRSQTLY RTVSGFMNYS RAIKLLYRVE NPDVAQLFEG
QMDVLEYELD RMASRKFKMC VSMQRYAKFT ADEIENTEFI LRAYPDLLIA YLDEDPPKEG
ETTPQLYAAL IDGYSELDEN KKRKPKYRIK LSGNPILGDG KSDNQNLSLP FYRGEYIQLI
DANQDNYLEE CLKIRSILAE FEAFDLKTND PYAETNALYQ NNPVAIMGAR EYIFSENIGI
LGDVAAGKEQ TFGTLFARTM AQIGGKLHYG HPDFLNAIYM TTRGGVSKAQ KGLHVNEDIY
AGMTALQRGG RIKHCEYYQC GKGRDLGFGS ILNFTTKIGT GMGEQMVSRE YYYLGTQLPF
DRFLSFYYAH PGFHINNIFI MLSVQLFMVV LVNLGGMYHV VTVCDYDHDQ KLTVPMRPEG
CYQLNPVVNW LKRCIISIFI VFFISFVPLT VQELTERGAW RALTRLGKHF ASFSPMFEVF
ACQTYAQSVI ANLSFGGARY IGTGRGFATA RLSFSLLFSR FAGPSIYLGS RTLLMLLFGT
MTVWIPHLIY FWISTLAMCI SPFIFNPHQF SWTDFFVDYR EFIRWLSRGN SRSHINSWIG
YCRLTRTRIT GYKRRLLGVP VSKGVIDTSR AHFTNMFFTE IFIPLMLVPL TLVSYFFIDS
QPGNPDPSKV TNPILRILIL AFLPIIVAAV VSMTFAGMAC MMGPLLDLCC KKFGAVLAAL
AHGITVFMFI IVFEVSWYLE AWCLAKTVLS MLCIIAIQRF FFKIIQVLFL TRELKHDGTN
LAWWTGKWYS RGLGFHALSQ PSRELICKMT ELNFFAADFF LCHLLLFLML PVLLIPFIDR
WHSMMLFWLK PSKQIRPPIY SMRQNRLRKK IVQRYGTMFF LLLIAFLALI IIPLVVAKDL
LANFEMDILR TYGLMQPRDT NWTENGTNWT TVNE
