ID A0A1Q3ENX9_LENED Unreviewed; 1147 AA.
AC A0A1Q3ENX9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|RuleBase:RU361174, ECO:0000256|RuleBase:RU368065};
DE Includes:
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
DE Includes:
DE RecName: Full=Protein ARV {ECO:0000256|RuleBase:RU368065};
GN ORFNames=LENED_010994 {ECO:0000313|EMBL:GAW08886.1};
OS Lentinula edodes (Shiitake mushroom) (Lentinus edodes).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Lentinula.
OX NCBI_TaxID=5353 {ECO:0000313|EMBL:GAW08886.1, ECO:0000313|Proteomes:UP000188533};
RN [1] {ECO:0000313|EMBL:GAW08886.1, ECO:0000313|Proteomes:UP000188533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAW08886.1,
RC ECO:0000313|Proteomes:UP000188533};
RG Lentinula edodes genome sequencing consortium;
RA Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA Konno N.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAW08886.1, ECO:0000313|Proteomes:UP000188533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAW08886.1,
RC ECO:0000313|Proteomes:UP000188533};
RA Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA Konno N.;
RT "A genome survey and senescence transcriptome analysis in Lentinula
RT edodes.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mediator of sterol homeostasis involved in sterol uptake,
CC trafficking and distribution into membranes.
CC {ECO:0000256|RuleBase:RU368065}.
CC -!- FUNCTION: Regulates also the sphingolipid metabolism.
CC {ECO:0000256|RuleBase:RU368065}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8; Evidence={ECO:0000256|RuleBase:RU361174};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU368065}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU368065}. Golgi apparatus membrane
CC {ECO:0000256|RuleBase:RU368065}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU368065}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ARV1 family. {ECO:0000256|ARBA:ARBA00009187,
CC ECO:0000256|RuleBase:RU368065}.
CC -!- SIMILARITY: Belongs to the ZPR1 family.
CC {ECO:0000256|ARBA:ARBA00008354}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000256|ARBA:ARBA00007495, ECO:0000256|RuleBase:RU361174}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU368065}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAW08886.1}.
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; BDGU01000822; GAW08886.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3ENX9; -.
DR STRING; 5353.A0A1Q3ENX9; -.
DR Proteomes; UP000188533; Unassembled WGS sequence.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IEA:UniProtKB-UniRule.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032366; P:intracellular sterol transport; IEA:UniProtKB-UniRule.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0097036; P:regulation of plasma membrane sterol distribution; IEA:UniProtKB-UniRule.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016125; P:sterol metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.120.1040; ZPR1, A/B domain; 2.
DR Gene3D; 2.20.25.420; ZPR1, zinc finger domain; 2.
DR InterPro; IPR007290; Arv1.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR004457; Znf_ZPR1.
DR InterPro; IPR040141; ZPR1.
DR InterPro; IPR042451; ZPR1_A/B_dom.
DR InterPro; IPR042452; ZPR1_Znf1/2.
DR NCBIfam; TIGR00310; ZPR1_znf; 1.
DR PANTHER; PTHR10876; ZINC FINGER PROTEIN ZPR1; 1.
DR PANTHER; PTHR10876:SF0; ZINC FINGER PROTEIN ZPR1; 1.
DR Pfam; PF04161; Arv1; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR Pfam; PF03367; zf-ZPR1; 2.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SMART; SM00709; Zpr1; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361174};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU368065};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361174};
KW Golgi apparatus {ECO:0000256|RuleBase:RU368065};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU368065};
KW Lipid transport {ECO:0000256|RuleBase:RU368065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368065};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361174};
KW Reference proteome {ECO:0000313|Proteomes:UP000188533};
KW Sphingolipid metabolism {ECO:0000256|RuleBase:RU368065};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU368065};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU368065};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU368065};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT TRANSMEM 654..677
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368065"
FT TRANSMEM 697..721
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368065"
FT DOMAIN 841..1144
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT ACT_SITE 1058
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 1147 AA; 127204 MW; FF9C0EAE05A5B0E0 CRC64;
MSHDAKEQLF PAIGTIADRA DQLPENGASA NSDEDRPMQE IESLCMKCGE QGITRMLLTS
IPYFREIIVM SFRCEHCGAS NNEIQSAGTI RPEGTLYTAR ILARSDLNRQ IVRSANASIV
IPELQLTLPS SARGQLTTVE GLIRDIVSDL SIDQPLRRVQ DEDSYTKIQS LIDKLIEILG
DDEVEDEAVD DQNNASARAA SEKDLPMPAF TVKLDDPSGN SWIEFIGSMS DPKWNMRNYP
RTLQQNIELG LVAAPDESAS VVQGAAKLSL NDDADEVVGG GAEGTDEEIY VFPGTCSSCG
HPLDTMMKKV NIPYFKDIII MSTNCDRCGY RDNEVKSGAA ISEHGKRMTL KVEDREDLSR
DILKSETAGL SIPEIDLVLT HGTLGGRFTT LEGILEQVYE ELSDKIFSGD SASNTPEAMQ
ERVRFEKFLG DLKEIKSAAR PFTLVLDDPL ANSYIQNLYA PDPDPAMTVE SYERTWDQNE
ELGLNDMKVE GYESDRASNS LKHPESIMPI CTTCTRWLPY LYTVYQSAYN LRLDQCPNCH
SFADPYVEHD ELTLLIDLLL LKRAVYRHLL YNRGSEPRRE DGTIGKDSGE QHRITNGREL
SRWRLVLRLG STLTFVDAFI RWSHLSVRPA SNELEKSLII SPWAIETISR FTTIFFGCCI
ETIAFHAGVI FACYSVLRAL NFRFWRSQSD IRREFRFSLI PLVLFYSSFT KLFFLFLLTI
WRPSRSPLER DGNIPVSMPF DFDILSVLNF MTDNNLDREW IVRNVMGGMS AGFGLRDINP
LFTTVIILFG WMTKTVQYSL SWIGIPQSGS GTVTAKARAA TSTARSNTAA KAAGKLYFGS
ATDNPFLDED ATYKAILSDN TLFGQLSPEN AMKWDATEPE QGVFTFTNGD VIVALAQANG
QIMRGHNTVW GSQLPSWVSD SGFDNATLIS VMQNHVSTVI GHYKGQIWDV VNEPFNDDGT
LASNVFFETI GPTYIDLALQ AASAADPNAK LYINDFNIEG EGAKATAMEN LVTDLKSRGI
PIDGIGLESH FILGEIPTTL QAQMEAFTAL GVEVAVTELD IRMTLPETDA LLAQQQTDYQ
TVVSACTAVA DCVGVSALTL VICHLLRSTD KYSWVPSTFA GQGDADPWDE NLEMKPAYDG
IIAGFSS
//