GAS1_SCHPO
ID GAS1_SCHPO Reviewed; 542 AA.
AC Q9P378; P78853;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=1,3-beta-glucanosyltransferase gas1;
DE EC=2.4.1.-;
DE Flags: Precursor;
GN Name=gas1; ORFNames=SPAC19B12.02c;
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 [LARGE SCALE MRNA] OF 268-542.
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 [3]
RP SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND PROBABLE
RP GPI-ANCHOR.
RX PubMed=17230583; DOI=10.1002/yea.1443;
RA de Groot P.W.J., Yin Q.Y., Weig M., Sosinska G.J., Klis F.M.,
RA de Koster C.G.;
RT "Mass spectrometric identification of covalently bound cell wall proteins
RT from the fission yeast Schizosaccharomyces pombe.";
RL Yeast 24:267-278(2007).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:17230583}. Membrane {ECO:0000269|PubMed:17230583};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:17230583}.
CC Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP).
CC -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC reticulum and serves to target the protein to the cell surface. There,
CC the glucosamine-inositol phospholipid moiety is cleaved off and the
CC GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family. {ECO:0000305}.
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DR EMBL; CU329670; CAC00550.1; -; Genomic_DNA.
DR EMBL; D89203; BAA13864.1; -; mRNA.
DR PIR; T43004; T43004.
DR RefSeq; NP_594765.1; NM_001020192.2.
DR AlphaFoldDB; Q9P378; -.
DR SMR; Q9P378; -.
DR BioGRID; 279039; 3.
DR STRING; 4896.SPAC19B12.02c.1; -.
DR CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR CAZy; GH72; Glycoside Hydrolase Family 72.
DR MaxQB; Q9P378; -.
DR PaxDb; Q9P378; -.
DR EnsemblFungi; SPAC19B12.02c.1; SPAC19B12.02c.1:pep; SPAC19B12.02c.
DR GeneID; 2542584; -.
DR KEGG; spo:SPAC19B12.02c; -.
DR PomBase; SPAC19B12.02c; gas1.
DR VEuPathDB; FungiDB:SPAC19B12.02c; -.
DR eggNOG; ENOG502QPST; Eukaryota.
DR HOGENOM; CLU_021855_2_1_1; -.
DR InParanoid; Q9P378; -.
DR OMA; GAYSMCT; -.
DR PhylomeDB; Q9P378; -.
DR PRO; PR:Q9P378; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; TAS:PomBase.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0071944; C:cell periphery; IDA:BHF-UCL.
DR GO; GO:0043188; C:cell septum edging; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA: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:0000936; C:primary cell septum; IDA:BHF-UCL.
DR GO; GO:0030427; C:site of polarized growth; IDA:BHF-UCL.
DR GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0000902; P:cell morphogenesis; IMP:BHF-UCL.
DR GO; GO:0034411; P:cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR GO; GO:0034407; P:cell wall (1->3)-beta-D-glucan metabolic process; IMP:BHF-UCL.
DR GO; GO:0000917; P:division septum assembly; IMP:BHF-UCL.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:BHF-UCL.
DR GO; GO:0071970; P:fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process; IDA:PomBase.
DR GO; GO:0071940; P:fungal-type cell wall assembly; IMP:BHF-UCL.
DR InterPro; IPR004886; Glucanosyltransferase.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR012946; X8.
DR PANTHER; PTHR31468; PTHR31468; 1.
DR Pfam; PF03198; Glyco_hydro_72; 1.
DR Pfam; PF07983; X8; 1.
DR SMART; SM00768; X8; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Reference proteome; Secreted; Signal;
KW Transferase.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..516
FT /note="1,3-beta-glucanosyltransferase gas1"
FT /id="PRO_0000010491"
FT PROPEP 517..542
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000377426"
FT REGION 490..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 157
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 258
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 88
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 198
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 203
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 290
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 516
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 70..99
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 212..345
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 230..261
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 367..419
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 376..439
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 395..400
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT CONFLICT 268..278
FT /note="TFSEIVALFSD -> HSLSLLPRSET (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 285..293
FT /note="SGGIAYQYF -> VWWHCLPIW (in Ref. 2; BAA13864)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 542 AA; 58116 MW; 1D243FDA5AD2EC3A CRC64;
MKFSILSLAV AGLVGLAKAS VSPVHVDGRY FFYENGTRFF LKGIAYQPNV DDSDTEGTLF
VDPLSDGDAC SRDVPYFQEL SVNAIRVYAV NASLDHSACM QAFQDAGIYV LSDLAQPYEA
ISSSDPTWTV DLFSRYTEVV DSLAPYDNML GFIAGNEVIQ NNTNTNAAAF VKAAVRDVKS
YIKSSGYRQI PVGYSTNDEE VTRDPMAYYF DCGDDDDHVD FYGINIYEWC GDSDFVSSGY
QERTEEFSNM TVPMIFSEFG CIEVRPRTFS EIVALFSDNM TDVWSGGIAY QYFESENEYG
VVTVSGDSVS TLTDFPYLSS RYASVIPSAS YESTMSATLT ATMSCQATNS AWMAATSLPP
TPSEAVCECM DSTRSCVIND DVSSDDYSDL FSYVCNEISC DGITANGTYP GQYGSYSYCD
AKQQLDYVLD AYYSAKGDCD FSGSATLVSA SSATGTCASY LSAAGSSATN AISLTADSNA
VSRNSSASTM STSYTSGSGS SNSSGSSSNS SSKSSSGASS YNLNMVITFL SVVIGGTAVL
FI
