ENG2_SCHPO
ID ENG2_SCHPO Reviewed; 706 AA.
AC Q09850;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Ascus wall endo-1,3(4)-beta-glucanase {ECO:0000303|PubMed:19542306};
DE AltName: Full=Endo-1,3(4)-beta-glucanase 2;
DE Short=Endo-1,3-beta-glucanase 2;
DE Short=Endo-1,4-beta-glucanase 2;
DE EC=3.2.1.6 {ECO:0000269|PubMed:19542306};
DE AltName: Full=Laminarinase-2;
GN Name=eng2 {ECO:0000312|PomBase:SPAC23D3.10c};
GN ORFNames=SPAC23D3.10c {ECO:0000312|PomBase:SPAC23D3.10c};
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 FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-537.
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-beta-glucan in the ascus wall. {ECO:0000269|PubMed:19542306}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->3)- or (1->4)-linkages in beta-D-glucans
CC when the glucose residue whose reducing group is involved in the
CC linkage to be hydrolyzed is itself substituted at C-3.; EC=3.2.1.6;
CC Evidence={ECO:0000269|PubMed:19542306};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}. Ascus epiplasm {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: Severely decreases occurrence of ascospore
CC release from ascus during sporulation (PubMed:19542306). Decreases
CC sporulation-specific endo-1,3-beta-glucanase activity
CC (PubMed:19542306). {ECO:0000269|PubMed:19542306}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 81 family. {ECO:0000305}.
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DR EMBL; CU329670; CAA91245.1; -; Genomic_DNA.
DR PIR; S62501; S62501.
DR RefSeq; NP_594547.1; NM_001019976.2.
DR AlphaFoldDB; Q09850; -.
DR SMR; Q09850; -.
DR BioGRID; 277982; 11.
DR STRING; 4896.SPAC23D3.10c.1; -.
DR CAZy; GH81; Glycoside Hydrolase Family 81.
DR SwissPalm; Q09850; -.
DR MaxQB; Q09850; -.
DR PaxDb; Q09850; -.
DR EnsemblFungi; SPAC23D3.10c.1; SPAC23D3.10c.1:pep; SPAC23D3.10c.
DR GeneID; 2541480; -.
DR KEGG; spo:SPAC23D3.10c; -.
DR PomBase; SPAC23D3.10c; eng2.
DR VEuPathDB; FungiDB:SPAC23D3.10c; -.
DR eggNOG; KOG2254; Eukaryota.
DR HOGENOM; CLU_005482_2_1_1; -.
DR InParanoid; Q09850; -.
DR OMA; WVNMLVR; -.
DR PhylomeDB; Q09850; -.
DR PRO; PR:Q09850; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:1990819; C:actin fusion focus; IDA:PomBase.
DR GO; GO:0072324; C:ascus epiplasm; IDA:PomBase.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; IC:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IDA:PomBase.
DR GO; GO:0052861; F:glucan endo-1,3-beta-glucanase activity, C-3 substituted reducing group; IEA:UniProtKB-EC.
DR GO; GO:0052862; F:glucan endo-1,4-beta-glucanase activity, C-3 substituted reducing group; IEA:UniProtKB-EC.
DR GO; GO:0044347; P:cell wall polysaccharide catabolic process; IC:PomBase.
DR GO; GO:0072000; P:extracellular polysaccharide catabolic process involved in ascospore release from ascus; IDA:PomBase.
DR GO; GO:1904541; P:fungal-type cell wall disassembly involved in conjugation with cellular fusion; IGI:PomBase.
DR InterPro; IPR005200; Endo-beta-glucanase.
DR InterPro; IPR040720; GH81_C.
DR InterPro; IPR040451; GH81_N.
DR PANTHER; PTHR31983; PTHR31983; 1.
DR Pfam; PF17652; Glyco_hydro81C; 1.
DR Pfam; PF03639; Glyco_hydro_81; 1.
PE 1: Evidence at protein level;
KW Glycosidase; Hydrolase; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..706
FT /note="Ascus wall endo-1,3(4)-beta-glucanase"
FT /id="PRO_0000215818"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 537
FT /note="E->A: Severely decreases occurrence of ascospore
FT release from ascus during sporulation."
FT /evidence="ECO:0000269|PubMed:19542306"
SQ SEQUENCE 706 AA; 77948 MW; 7AA4A9BED26C37B6 CRC64;
MDVLVPIYTG PINPVFPSRA HPSPPLGLTS NLFPIQTNKF YGNLYIGTRH NPSWSHPYSV
TWLNGSSYYG LAISHIDDSQ RVFGPDPESV PCQYYFNPAG LYSIIISARE FASGNLLSLD
QSRHFSIQAT LSATTSGSGT IILPIVAGMG FVSGYYTNLT PVFNSSILFS SITKINFSRG
YKYRIQLTDG KIWFLYAFPT SSSSTFNLTL ASNSQLTTST KFTGLIQICK VPNESVNNSY
PDTIYDASAG VYTTSISLSA QVSGTTGEYW FRFATAGYTN LNPLMFALPH HMQSFGSDTQ
AYKTGLGLAS TTMGIMFAYA TKTWHLIEKN LPTQVGFLPI PWNGGSNTYS PTALAAIRAA
CATDINFDVV NASNLDSMYT SGKIVAMYAQ VCLVASRILG DSTLTNTGLT KLKQAMARFT
TNTQMYPLVY DTTYKGIIST AGYSSPLADY GNTYYNDHHF HWGYHIYACA VIGLLDPSWL
VNDNIRYVNA LLRDSANPSE SDTYFAMFRN FDWFVGHSWA TGIFESGDGK DEESTSEDFN
FLYATKLWGM VRNDTVLINR ANLMLAVLKN SLNTYIYMTP TTSVQPSQIL GNYVTGITFM
NKVDYATYFS AEEYCKQGIH MIPTTPISGY LRSPSYVQQD WNAKIAPIIN TFSNNWTGIL
WSNYAIYDPK TAYNTFAAST FTADKIDNGA SKTWYLAMAA GMGGSP
