GAS5_SCHPO
ID GAS5_SCHPO Reviewed; 510 AA.
AC O13692;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=1,3-beta-glucanosyltransferase gas5;
DE Flags: Precursor;
GN Name=gas5; ORFNames=SPAC11E3.13c;
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 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; CAB11192.1; -; Genomic_DNA.
DR PIR; T37541; T37541.
DR RefSeq; NP_594938.1; NM_001020369.2.
DR AlphaFoldDB; O13692; -.
DR SMR; O13692; -.
DR BioGRID; 279427; 29.
DR STRING; 4896.SPAC11E3.13c.1; -.
DR CAZy; GH72; Glycoside Hydrolase Family 72.
DR MaxQB; O13692; -.
DR PaxDb; O13692; -.
DR PRIDE; O13692; -.
DR EnsemblFungi; SPAC11E3.13c.1; SPAC11E3.13c.1:pep; SPAC11E3.13c.
DR GeneID; 2542989; -.
DR KEGG; spo:SPAC11E3.13c; -.
DR PomBase; SPAC11E3.13c; gas5.
DR VEuPathDB; FungiDB:SPAC11E3.13c; -.
DR eggNOG; ENOG502QRZZ; Eukaryota.
DR HOGENOM; CLU_021855_1_0_1; -.
DR InParanoid; O13692; -.
DR OMA; CADFFAC; -.
DR PhylomeDB; O13692; -.
DR PRO; PR:O13692; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; NAS:PomBase.
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:0042124; F:1,3-beta-glucanosyltransferase activity; IDA: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: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 wall; Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Reference proteome; Secreted; Signal;
KW Transferase.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..485
FT /note="1,3-beta-glucanosyltransferase gas5"
FT /id="PRO_0000010492"
FT PROPEP 486..510
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000377427"
FT REGION 424..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 159
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 261
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 158
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 159
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 200
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 205
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 300
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 485
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 70..99
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 214..353
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 232..264
FT /evidence="ECO:0000250|UniProtKB:Q06135"
SQ SEQUENCE 510 AA; 53693 MW; 3D515CCDB5651087 CRC64;
MNFLHFLTTS LLLLGGSRLA LADSASSAIK IKGNAFFNSD TNERFYVRGV DYQPGGSSTL
VDPLADTSIC KRDLPYLQGL NINTIRVYQV DNSANHDECM SALQDAGIYV ILDLATSSNS
ISRLDAASSY NAVFLQGIFA TIDAFKNYTN VLGFFAGNEV ANTAENSATT TWVKAALRDA
KEYISKNSDR DIPVGYSAAD VAEIRVQCAD FFACGNSSVR ADFYGMNMYE WCGADSSFTI
SGYDQRMEEF ANYSIPLFLS EYGCNDVTKE SDGTPDRPFD EVDAIFSSEM SSVFSGGLVY
QYSEEGNNYG LVVIDGDNVT ISKNYETLKE KYASAANYTG DGDYSSSPAT LTCPADDSYF
TSFPLPTMPS EAKGFIESGA GQPLGFNAPS NQEFSANATA LVSPGPHSVS TTINTNIVQA
TISQSSTSGS SSGSSSASTT ASSSSVSSGS SISSGSSSMS TSYTSASGSS AHSSGSSSGS
SSATSSASTF NLSRFYVFAG ILAISGLVFA
