AGN2_SCHPO
ID AGN2_SCHPO Reviewed; 433 AA.
AC O94510; Q5ZEQ1;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Ascus wall endo-1,3-alpha-glucanase;
DE AltName: Full=Endo-1,3-alpha-glucanase agn2;
DE AltName: Full=Glucan endo-1,3-alpha-glucosidase agn2;
DE EC=3.2.1.59;
GN Name=agn2 {ECO:0000312|PomBase:SPBC646.06c};
GN ORFNames=SPBC646.06c {ECO:0000312|PomBase:SPBC646.06c};
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], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ND080;
RX PubMed=15194814; DOI=10.1091/mbc.e04-04-0319;
RA Dekker N., Speijer D., Grun C.H., Van Den Berg M., De Haan A.,
RA Hochstenbach F.;
RT "Role of the alpha-glucanase Agn1p in fission-yeast cell separation.";
RL Mol. Biol. Cell 15:3903-3914(2004).
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 FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19542306; DOI=10.1128/ec.00148-09;
RA Encinar del Dedo J., Duenas E., Arnaiz Y., del Rey F.,
RA Vazquez de Aldana C.R.;
RT "{beta}-glucanase Eng2 is required for ascus wall endolysis after
RT sporulation in the fission yeast Schizosaccharomyces pombe.";
RL Eukaryot. Cell 8:1278-1286(2009).
CC -!- FUNCTION: Promotes the release of ascospores from asci by hydrolyzing
CC 1,3-alpha-glucan in the ascus wall. {ECO:0000269|PubMed:15194814,
CC ECO:0000269|PubMed:19542306}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->3)-alpha-D-glucosidic linkages in
CC isolichenin, pseudonigeran and nigeran.; EC=3.2.1.59;
CC -!- SUBCELLULAR LOCATION: Ascus epiplasm {ECO:0000269|PubMed:15194814,
CC ECO:0000269|PubMed:19542306}.
CC -!- DEVELOPMENTAL STAGE: Present during vegetative growth at low level (at
CC protein level) (PubMed:19542306). The level increases throughout
CC meiosis and reaches its highest during sporulation (at protein level)
CC (PubMed:19542306). {ECO:0000269|PubMed:19542306}.
CC -!- DISRUPTION PHENOTYPE: Abolishes ascospore release from ascus during
CC sporulation. {ECO:0000269|PubMed:19542306}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 71 family. {ECO:0000305}.
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DR EMBL; AY626902; AAT84065.1; -; mRNA.
DR EMBL; CU329671; CAH58744.1; -; Genomic_DNA.
DR PIR; T40582; T40582.
DR RefSeq; XP_001713124.1; XM_001713072.2.
DR AlphaFoldDB; O94510; -.
DR SMR; O94510; -.
DR BioGRID; 277637; 8.
DR STRING; 4896.SPBC646.06c.1; -.
DR CAZy; GH71; Glycoside Hydrolase Family 71.
DR MaxQB; O94510; -.
DR PaxDb; O94510; -.
DR EnsemblFungi; SPBC646.06c.1; SPBC646.06c.1:pep; SPBC646.06c.
DR PomBase; SPBC646.06c; agn2.
DR VEuPathDB; FungiDB:SPBC646.06c; -.
DR eggNOG; ENOG502RSZT; Eukaryota.
DR HOGENOM; CLU_019141_0_0_1; -.
DR InParanoid; O94510; -.
DR OMA; AHFMMGL; -.
DR PhylomeDB; O94510; -.
DR PRO; PR:O94510; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:1990819; C:actin fusion focus; IDA:PomBase.
DR GO; GO:0072324; C:ascus epiplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0051118; F:glucan endo-1,3-alpha-glucosidase activity; IDA:PomBase.
DR GO; GO:0072316; P:alpha-glucan catabolic process involved in ascospore release from ascus; IDA:PomBase.
DR GO; GO:0071998; P:ascospore release from ascus; IMP:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0072000; P:extracellular polysaccharide catabolic process involved in ascospore release from ascus; IMP:PomBase.
DR GO; GO:1904541; P:fungal-type cell wall disassembly involved in conjugation with cellular fusion; IGI:PomBase.
DR CDD; cd11577; GH71; 1.
DR InterPro; IPR005197; Glyco_hydro_71.
DR Pfam; PF03659; Glyco_hydro_71; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..433
FT /note="Ascus wall endo-1,3-alpha-glucanase"
FT /id="PRO_0000119035"
SQ SEQUENCE 433 AA; 48066 MW; 7FA86E53523BC675 CRC64;
MASLTTALPN KAVVAHFMMG LTYNYAQSDF QNDIQNAISL GLDGFVLNFG NDSWMMSKLT
LMYNAADALN LQFLLYLNLD MSEMSTVPAS TLVTYVQTFA NRGHQARINN NVVVGTFLGQ
DINFGQSSVN QGWQVAFKNA LASAGINIFF MPTWPLDAST IYQTYPVADG FCKWNCWPYY
TSSPTSDAED LVYIQNSKAT NKKYMATVSP IFYTHFTSKN YSFFSEGLWF TRWMQLIKDQ
PNYVQVLTWN DYGESTYIGP TNYAADFPVI GSNSHEWVDS FTHAPLSYSL PLFIQMYKQN
TTGLPSNFSG ISQLYVTYRV HSKNATASSD SIPRPDNYQN SSDVISVISF AKSSYTLRVS
VNGTVLGTTN VNAGVQSANV SFIVNNTAAA GLPLFQILNG TTVIAQGYGP LNILGNNSVV
LYNFNFCTTR ISW
