GAS4_SCHPO
ID GAS4_SCHPO Reviewed; 456 AA.
AC Q9Y7Y7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=1,3-beta-glucanosyltransferase gas4;
DE EC=2.4.1.-;
DE Flags: Precursor;
GN Name=gas4; ORFNames=SPBC342.03;
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] {ECO:0000312|EMBL:CAB46773.1}
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] {ECO:0000305}
RP GPI-ANCHOR AT SER-432.
RX PubMed=12845604; DOI=10.1002/yea.1007;
RA De Groot P.W., Hellingwerf K.J., Klis F.M.;
RT "Genome-wide identification of fungal GPI proteins.";
RL Yeast 20:781-796(2003).
RN [3]
RP FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-157 AND
RP GLU-257.
RX PubMed=18410286; DOI=10.1111/j.1365-2958.2008.06233.x;
RA de Medina-Redondo M., Arnaiz-Pita Y., Fontaine T., Del Rey F., Latge J.P.,
RA Vazquez de Aldana C.R.;
RT "The beta-1,3-glucanosyltransferase gas4p is essential for ascospore wall
RT maturation and spore viability in Schizosaccharomyces pombe.";
RL Mol. Microbiol. 68:1283-1299(2008).
CC -!- FUNCTION: Splits internally a 1,3-beta-glucan molecule and transfers
CC the newly generated reducing end (the donor) to the non-reducing end of
CC another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta
CC linkage, resulting in the elongation of 1,3-beta-glucan chains in the
CC cell wall. Involved in spore wall assembly.
CC {ECO:0000269|PubMed:18410286}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18410286};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:18410286}. Note=Localizes
CC to the ascospore periphery during sporulation.
CC -!- INDUCTION: Strongly induced during sporulation.
CC {ECO:0000269|PubMed:18410286}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family. {ECO:0000255}.
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DR EMBL; CU329671; CAB46773.1; -; Genomic_DNA.
DR PIR; T40276; T40276.
DR RefSeq; NP_596746.1; NM_001023766.2.
DR AlphaFoldDB; Q9Y7Y7; -.
DR SMR; Q9Y7Y7; -.
DR BioGRID; 277436; 6.
DR STRING; 4896.SPBC342.03.1; -.
DR CAZy; GH72; Glycoside Hydrolase Family 72.
DR PaxDb; Q9Y7Y7; -.
DR PRIDE; Q9Y7Y7; -.
DR EnsemblFungi; SPBC342.03.1; SPBC342.03.1:pep; SPBC342.03.
DR GeneID; 2540920; -.
DR KEGG; spo:SPBC342.03; -.
DR PomBase; SPBC342.03; gas4.
DR VEuPathDB; FungiDB:SPBC342.03; -.
DR eggNOG; ENOG502QRZZ; Eukaryota.
DR HOGENOM; CLU_021855_1_0_1; -.
DR InParanoid; Q9Y7Y7; -.
DR OMA; FNCGSDE; -.
DR PhylomeDB; Q9Y7Y7; -.
DR PRO; PR:Q9Y7Y7; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005628; C:prospore membrane; IDA:PomBase.
DR GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IDA:PomBase.
DR GO; GO:0034412; P:ascospore wall beta-glucan biosynthetic process; IDA:PomBase.
DR GO; GO:0031321; P:ascospore-type prospore assembly; IMP:PomBase.
DR GO; GO:0034411; P:cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0071970; P:fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process; IDA:PomBase.
DR InterPro; IPR004886; Glucanosyltransferase.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31468; PTHR31468; 1.
DR Pfam; PF03198; Glyco_hydro_72; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Reference proteome;
KW Signal; Transferase.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..432
FT /note="1,3-beta-glucanosyltransferase gas4"
FT /id="PRO_0000315936"
FT PROPEP 433..456
FT /note="Removed in mature form"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:12845604"
FT /id="PRO_0000315937"
FT REGION 334..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 157
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O74687"
FT ACT_SITE 257
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O74687"
FT BINDING 86
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="1"
FT /ligand_note="donor substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT BINDING 156
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="1"
FT /ligand_note="donor substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT BINDING 157
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="2"
FT /ligand_note="acceptor substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT BINDING 197
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="2"
FT /ligand_note="acceptor substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT BINDING 202
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="2"
FT /ligand_note="acceptor substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT BINDING 296
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="1"
FT /ligand_note="donor substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT LIPID 432
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:12845604"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 68..97
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 211..350
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 229..260
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT MUTAGEN 157
FT /note="E->Q: Leads to abnormal spore morphology and
FT unviable spores."
FT /evidence="ECO:0000269|PubMed:18410286"
FT MUTAGEN 257
FT /note="E->Q: Leads to abnormal spore morphology and
FT unviable spores."
FT /evidence="ECO:0000269|PubMed:18410286"
SQ SEQUENCE 456 AA; 50763 MW; F1B4FBFE5D1A7F8B CRC64;
MGVANIIYAL FLLGPSIFLK ATAQTHPIVI KGNAFFDSKT NERFYIRGVD YQPGGSSSLV
DPLASRSCKK DVEIFKKLGI NTVRVYQVDN SADHDKCMNA LSEAGIYVIL DLNTYRHSIS
RAHPALSYNK VYLQHLFATI DAFKGYDNVL GFFSGNEVVN DEDTTAITWV KAVTRDVKAY
IKKHSDRHIP VGYSAADVAE NRLQLAHYFN CGDESERADF YAFNMYEWCG YSSMTVSGYY
DRIKEFSNYS IPLFLSEFGC NTVEINDDTT PNRPFTEIEA IYSHDMTPVF SGGLVYEYSA
EPNHYGLVVI DKDDERRVSR NFITLMKQYA KTPNPKGDGG YKKAGSPSKC PANSTQFNAW
EKLPEMPEGA KIYMEKGAGE PLGIEGPTNM WSPFHDGDDD ESTSRRPKPK NKPSNVTSTT
SYTSGMTSSS ESGSSKIGVA FCQALFITVL IATLSF
