GAS1_ARTBC
ID GAS1_ARTBC Reviewed; 545 AA.
AC D4ATC3;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=1,3-beta-glucanosyltransferase ARB_07487;
DE EC=2.4.1.- {ECO:0000250|UniProtKB:P22146};
DE AltName: Full=Glycolipid-anchored surface protein ARB_07487;
DE Flags: Precursor;
GN ORFNames=ARB_07487;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
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. Involved in cell wall biosynthesis and morphogenesis (By
CC similarity). {ECO:0000250|UniProtKB:P22146}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}. Cell
CC membrane {ECO:0000250|UniProtKB:P22146}; Lipid-anchor, GPI-anchor
CC {ECO:0000250|UniProtKB:P22146}. Secreted, cell wall
CC {ECO:0000250|UniProtKB:P22146}. Note=Identified as GPI-anchored plasma
CC membrane protein (GPI-PMP) as well as covalently-linked GPI-modified
CC cell wall protein (GPI-CWP) in the outer cell wall layer.
CC {ECO:0000250|UniProtKB:P22146}.
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 {ECO:0000250|UniProtKB:P22146}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family. {ECO:0000305}.
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DR EMBL; ABSU01000009; EFE33542.1; -; Genomic_DNA.
DR RefSeq; XP_003014182.1; XM_003014136.1.
DR AlphaFoldDB; D4ATC3; -.
DR SMR; D4ATC3; -.
DR STRING; 663331.D4ATC3; -.
DR PRIDE; D4ATC3; -.
DR EnsemblFungi; EFE33542; EFE33542; ARB_07487.
DR GeneID; 9521600; -.
DR KEGG; abe:ARB_07487; -.
DR eggNOG; ENOG502QPST; Eukaryota.
DR HOGENOM; CLU_021855_2_1_1; -.
DR OMA; EWNLDLY; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042123; F:glucanosyltransferase activity; IEA:UniProt.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0071852; P:fungal-type cell wall organization or biogenesis; IEA:UniProt.
DR InterPro; IPR004886; Glucanosyltransferase.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR012946; X8.
DR PANTHER; PTHR31468; PTHR31468; 1.
DR Pfam; PF03198; Glyco_hydro_72; 1.
DR Pfam; PF07983; X8; 1.
DR SMART; SM00768; X8; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Reference proteome;
KW Secreted; Signal; Transferase.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..512
FT /note="1,3-beta-glucanosyltransferase ARB_07487"
FT /evidence="ECO:0000255"
FT /id="PRO_5001341169"
FT PROPEP 513..545
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434665"
FT REGION 493..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT ACT_SITE 276
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT BINDING 106
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 133..141
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 174
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 175
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 216
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 221
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 308
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 512
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 88..117
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 230..363
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 248..279
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 384..437
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 393..464
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 412..419
FT /evidence="ECO:0000250|UniProtKB:Q06135"
SQ SEQUENCE 545 AA; 58825 MW; 2065B8ABEE25DA24 CRC64;
MKFSSLAAAT ALVAGSVVAA DLDPIVIKVG VRSALIPGWP KGGSKFFYKS NGTEFFMKGI
AYQQEFSTNG TSSDKNNYQD PLADVESCRR DIPLMQQLQT NTIRVYAIDP KKDHKQCMKL
LQDAGIYVVA DLSEPSTSII RDDPKWDDVL YTRYTSVVDE LAQYSNVIGF FAGNEVSNNS
TNTDASAFVK AAVRDMKAYI KQKNYRSMGV GYATNDDAEI RKDMTAYFNC NKQEESIDFW
GYNIYSWCGD SSYTESGYDK VVEEFKTFNV PVFFAEYGCN EVQPRKFTEV QALYGDKMTP
VVSGGIVYMY FQEENDYGLV KIEGGKPKKL PDFNSLQKQI SKIKPSGVQM DSYKPTNTAL
STCPKSSTWK ASVKLPPTPN KDLCSCMVKS LSCVAKPSVT GKELGKLFGT VCGSDKDACK
GITADATSGT YGAYSMCSPS EKLSFAFNQY YQHQSAKGNG ANACDFGGAA TAQKSEKPSG
SCANLVDQAG QDGTGSVTSA PGSGGNKPDQ GAASTISAPS VNLGIVKLGA YIFCAVLAGA
GMILI
