ID BTGC_ASPTN Reviewed; 655 AA. AC Q0CI96; DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot. DT 15-JUN-2010, sequence version 2. DT 22-FEB-2023, entry version 61. DE RecName: Full=Probable glucan endo-1,3-beta-glucosidase btgC; DE EC=3.2.1.39; DE AltName: Full=Endo-1,3-beta-glucanase btgC; DE AltName: Full=Laminarinase btgC; GN Name=btgC; ORFNames=ATEG_06588; OS Aspergillus terreus (strain NIH 2624 / FGSC A1156). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=341663; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIH 2624 / FGSC A1156; RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M., RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K., RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R., RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J., RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W., RA Nierman W.C., Milne T., Madden K.; RT "Annotation of the Aspergillus terreus NIH2624 genome."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Glucanases play a role in cell expansion during growth, in CC cell-cell fusion during mating, and in spore release during CC sporulation. This enzyme may be involved in beta-glucan degradation. CC Active on laminarin and lichenan (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)- CC beta-D-glucans.; EC=3.2.1.39; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=EAU33132.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=EAU33132.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; CH476602; EAU33132.1; ALT_SEQ; Genomic_DNA. DR RefSeq; XP_001215766.1; XM_001215766.1. DR AlphaFoldDB; Q0CI96; -. DR SMR; Q0CI96; -. DR STRING; 341663.Q0CI96; -. DR GlyCosmos; Q0CI96; 3 sites, No reported glycans. DR EnsemblFungi; EAU33132; EAU33132; ATEG_06588. DR GeneID; 4322381; -. DR eggNOG; ENOG502QTKT; Eukaryota. DR OrthoDB; 675117at2759; -. DR Proteomes; UP000007963; Unassembled WGS sequence. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProtKB-EC. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR16631; GLUCAN 1,3-BETA-GLUCOSIDASE; 1. DR PANTHER; PTHR16631:SF17; GLUCAN ENDO-1,3-BETA-GLUCOSIDASE BTGC; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Cell membrane; Cell wall biogenesis/degradation; KW Glycoprotein; Hydrolase; Membrane; Polysaccharide degradation; KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. FT CHAIN 1..655 FT /note="Probable glucan endo-1,3-beta-glucosidase btgC" FT /id="PRO_0000395127" FT TOPO_DOM 1..282 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 283..303 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 304..655 FT /note="Extracellular" FT /evidence="ECO:0000255" FT REGION 1..61 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 89..114 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 305..338 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..36 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 310..324 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 458 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:O22317" FT ACT_SITE 557 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:O22317" FT CARBOHYD 426 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 576 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 602 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 655 AA; 69420 MW; C2560B77C3B3CAC5 CRC64; MSGDPRSFSF NQGDDHPIDS SQQPLHPTNT MADSYSDRNW GAPGGLDHTH SMRTQSTATP GMDNLGPAAV GGGISGIALG VANSHDRQSG VDAFRDTDGG NFPAERGYNA PGSDNPYVPP PPAAAYDSSD NLTARSGAYG SSAALAAAAS APAGASNTSR RSFVDSPYQG VGALDAGPYQ RQSVYNNGDY PLVINPDEII DDGDDGFALP NSKSAGHKSR AVPAAAAGAA GGAAAGGLLG GIFKSKAAAE GPSYGPVPGA GIEAAEKGQW AKPKPGTGSR KRGWIVGIIL AVVIVGAIVG GAVGGTLGNR EKESPSSSET ASGDEKVNGD LGKDSDEIKS LMNNPNLHKV FPGMDYTPWG TQYPLCQKYP PSQNNVTRDI AVLSQLTNTV RLYGTDCNQT EMVLHAIDRL ELTEMKLWLG VWIDTNKTTC ERQLNQLYDV LDKTKDHSIF KGAIIGNEAL YRAGSSIAEA EKTLISYMTE VRDHFKKNNI NIPIATSDLG DNWNAELVKA SDVVMANVHP FFAGVSVDLA ASWTWDFWNN HNLVLTKGTD KKQIISEVGW PSGGGNDCGD GGNCPNDSAG SVAGIDEMNQ FMSDWVCQAL DNGTDYFWFE AFDEPWKIVY NTKNENWEDK WGLMDPARNL KDGLKIPDCG GKTAT //