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Database: UniProt
Entry: A0A1Q3ENX9_LENED
LinkDB: A0A1Q3ENX9_LENED
Original site: A0A1Q3ENX9_LENED 
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}.
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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
//
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