AGN1_SCHPO
ID AGN1_SCHPO Reviewed; 424 AA.
AC O13716; Q6F6J1; Q9USE2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Glucan endo-1,3-alpha-glucosidase agn1;
DE EC=3.2.1.59;
DE AltName: Full=Endo-1,3-alpha-glucanase agn1;
DE Flags: Precursor;
GN Name=agn1; ORFNames=SPAC14C4.09;
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, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=972 / ATCC 24843;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 23-62.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
CC -!- FUNCTION: Has a role in cell separation where it is required for the
CC degradation of the cell wall material surrounding the septum (the
CC septum edging) which must be hydrolyzed before full separation of the
CC daughter cells can occur. Hydrolyzes 1,3-alpha-glucan predominantly
CC into pentasaccharides. {ECO:0000269|PubMed:15194814}.
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 -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15194814}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15194814}. Secreted,
CC cell wall {ECO:0000269|PubMed:15194814}. Note=Associates with the cell
CC wall.
CC -!- PTM: Not glycosylated.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 71 family. {ECO:0000305}.
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DR EMBL; AY626901; AAT84064.1; -; mRNA.
DR EMBL; CU329670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB027828; BAA87132.1; -; Genomic_DNA.
DR PIR; T37694; T37694.
DR AlphaFoldDB; O13716; -.
DR SMR; O13716; -.
DR STRING; 4896.SPAC14C4.09.1; -.
DR CAZy; GH71; Glycoside Hydrolase Family 71.
DR CLAE; MUT71A_SCHPO; -.
DR PaxDb; O13716; -.
DR EnsemblFungi; SPAC14C4.09.1; SPAC14C4.09.1:pep; SPAC14C4.09.
DR PomBase; SPAC14C4.09; agn1.
DR VEuPathDB; FungiDB:SPAC14C4.09; -.
DR eggNOG; ENOG502RZ85; Eukaryota.
DR HOGENOM; CLU_019141_0_0_1; -.
DR InParanoid; O13716; -.
DR OMA; KITAYMQ; -.
DR PhylomeDB; O13716; -.
DR PRO; PR:O13716; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:1990819; C:actin fusion focus; IDA:PomBase.
DR GO; GO:0005576; C:extracellular region; IDA:PomBase.
DR GO; GO:0043332; C:mating projection tip; IDA:PomBase.
DR GO; GO:0051118; F:glucan endo-1,3-alpha-glucosidase activity; IDA:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030995; P:cell septum edging catabolic process; 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; Cell wall; Cell wall biogenesis/degradation;
KW Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000305"
FT CHAIN 21..424
FT /note="Glucan endo-1,3-alpha-glucosidase agn1"
FT /id="PRO_0000012111"
SQ SEQUENCE 424 AA; 46974 MW; 2D680FDB8C56AEBF CRC64;
MKLVLFLVLL FSALINLTNA DKMVVAHFIV GNTYPYTVSN WEEDIQDAIA VGIDGFALNM
GSDAWQVERI EDAYDAAASV SSDFKLFISF DMSIISADAD FIEGVVRRFA DKPNQLYYDG
KVFVSTFAGE TDTFGYSDVS TGWDSAVKEP LASAGYPIYF VPSWTSLGQG ALEESVADGF
LSWNAWPTTD ADMNDNDDIG YQNLANSLGK LYVAPVSPWF YTHLSYKNWA YKSDWLIIDR
WNEMLSVQPD MIEVLTWNDY GESHYIGNIQ GALPAGSEGY VDGFDHTAWR YLMSPYISAY
KLGLSEPYIN FESLFYWYRP TPKSATATAD SLSYPSGGDY MEDEIFVLVY LLQSAEVTVT
CGSTTQTFSG VPGVNQFTIP METNASPSFT VARQGGTLAS GTGPEIVDSL SIYNFNAYTG
VLYF
