GAS2_SCHPO
ID GAS2_SCHPO Reviewed; 459 AA.
AC Q9USU5; P78785; Q1L852;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=1,3-beta-glucanosyltransferase gas2;
DE EC=2.4.1.-;
DE Flags: Precursor;
GN Name=gas2; ORFNames=SPBC29A10.08;
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 [MRNA].
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 [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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:16823372}. Secreted {ECO:0000305|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13796.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D89134; BAA13796.1; ALT_INIT; mRNA.
DR EMBL; CU329671; CAA22436.1; -; Genomic_DNA.
DR PIR; T40063; T40063.
DR RefSeq; NP_596053.1; NM_001021964.2.
DR AlphaFoldDB; Q9USU5; -.
DR SMR; Q9USU5; -.
DR BioGRID; 276818; 4.
DR STRING; 4896.SPBC29A10.08.1; -.
DR CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR CAZy; GH72; Glycoside Hydrolase Family 72.
DR MaxQB; Q9USU5; -.
DR PaxDb; Q9USU5; -.
DR EnsemblFungi; SPBC29A10.08.1; SPBC29A10.08.1:pep; SPBC29A10.08.
DR GeneID; 2540287; -.
DR KEGG; spo:SPBC29A10.08; -.
DR PomBase; SPBC29A10.08; gas2.
DR VEuPathDB; FungiDB:SPBC29A10.08; -.
DR eggNOG; ENOG502QPST; Eukaryota.
DR HOGENOM; CLU_021855_2_1_1; -.
DR InParanoid; Q9USU5; -.
DR OMA; EVTILEC; -.
DR PhylomeDB; Q9USU5; -.
DR PRO; PR:Q9USU5; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; TAS: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:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
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:0006074; P:(1->3)-beta-D-glucan metabolic process; IDA:BHF-UCL.
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 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 2: Evidence at transcript level;
KW Cell wall biogenesis/degradation; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Reference proteome; Secreted; Signal; Transferase.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..459
FT /note="1,3-beta-glucanosyltransferase gas2"
FT /id="PRO_0000353132"
FT ACT_SITE 156
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 263
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 87
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 155
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="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 295
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 CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 69..98
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 211..350
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 235..266
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 374..427
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 383..449
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 402..409
FT /evidence="ECO:0000250|UniProtKB:Q06135"
SQ SEQUENCE 459 AA; 50614 MW; 2963E07D173F6B3F CRC64;
MVSFTKFTLQ LLSASAAFAY FEPLTIKGRK FFKNDTQFYI KGVAYQPAVD AEETSTIVDP
LAEVNYKNCT EDAKIISNLG ANVIRVYAVN ASLNHDKCME AFRNESIYVF LDLANPKTGI
DRDTPTWNTD QFSSYQSVID TFQKYNNTGA FFAGNEVVNN ASNAPAVAYV RAAVRDSKNY
IKSKKYRTIP VGYAGADIPV VRTELAAYLS CNATKLNNDT NSETDFLGYN MYEWCGHSDF
YTSGYAARTQ ELENFTIPIF LSEFGCNKVT PRVFTEVQAI YSDNMTNVWS GGIVYEYSQE
VNDYGLVNVS STGERVLTTD YNNLKKQWAS ISPNITYKHS YNPNGTIPEC PSRNKTSWAV
SANAFPVTPN TTICSNAVKN LKCSANGTPS GSKISQVLSE LCYYDNKACS SISSDPYEGT
YGNYTGCTGV QQLSIALNAY TQDHGADSCS WGGVGELKA
