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Database: UniProt
Entry: A0A0A2L1M4_PENIT
LinkDB: A0A0A2L1M4_PENIT
Original site: A0A0A2L1M4_PENIT 
ID   A0A0A2L1M4_PENIT        Unreviewed;      1387 AA.
AC   A0A0A2L1M4;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Sterol 3-beta-glucosyltransferase {ECO:0000256|ARBA:ARBA00017894};
DE            EC=2.4.1.173 {ECO:0000256|ARBA:ARBA00012650};
DE   AltName: Full=Autophagy-related protein 26 {ECO:0000256|ARBA:ARBA00029843};
GN   ORFNames=PITC_015550 {ECO:0000313|EMBL:KGO70510.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO70510.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO70510.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO70510.1,
RC   ECO:0000313|Proteomes:UP000030104};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a sterol + UDP-alpha-D-glucose = a sterol 3-beta-D-glucoside +
CC         H(+) + UDP; Xref=Rhea:RHEA:22724, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15889, ChEBI:CHEBI:37424, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885; EC=2.4.1.173;
CC         Evidence={ECO:0000256|ARBA:ARBA00035583};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22725;
CC         Evidence={ECO:0000256|ARBA:ARBA00035583};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ergosterol + UDP-alpha-D-glucose = ergosteryl 3-beta-D-
CC         glucoside + H(+) + UDP; Xref=Rhea:RHEA:61836, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16933, ChEBI:CHEBI:52973, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885; Evidence={ECO:0000256|ARBA:ARBA00035586};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61837;
CC         Evidence={ECO:0000256|ARBA:ARBA00035586};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}. Preautophagosomal structure membrane
CC       {ECO:0000256|ARBA:ARBA00004623}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004623}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000256|ARBA:ARBA00006962}.
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:KGO70510.1}.
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DR   EMBL; JQGA01001039; KGO70510.1; -; Genomic_DNA.
DR   STRING; 40296.A0A0A2L1M4; -.
DR   HOGENOM; CLU_000537_6_0_1; -.
DR   OMA; YYAYLHR; -.
DR   OrthoDB; 76239at2759; -.
DR   PhylomeDB; A0A0A2L1M4; -.
DR   Proteomes; UP000030104; Unassembled WGS sequence.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0102203; F:brassicasterol glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102205; F:cholesterol alpha-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102202; F:soladodine glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016906; F:sterol 3-beta-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0030259; P:lipid glycosylation; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   CDD; cd13215; PH-GRAM1_AGT26; 1.
DR   CDD; cd13216; PH-GRAM2_AGT26; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 3.
DR   InterPro; IPR048066; ATG26_PH_GRAM1.
DR   InterPro; IPR048065; ATG26_PH_GRAM2.
DR   InterPro; IPR010610; EryCIII-like_C.
DR   InterPro; IPR004276; GlycoTrans_28_N.
DR   InterPro; IPR004182; GRAM.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   PANTHER; PTHR48050; STEROL 3-BETA-GLUCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR48050:SF25; STEROL 3-BETA-GLUCOSYLTRANSFERASE; 1.
DR   Pfam; PF06722; EryCIII-like_C; 1.
DR   Pfam; PF03033; Glyco_transf_28; 1.
DR   Pfam; PF02893; GRAM; 2.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00568; GRAM; 2.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KGO70510.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          281..378
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          86..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          573..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          858..879
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1327..1352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..151
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        481..504
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..537
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..588
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1387 AA;  154876 MW;  DA4D1CFB5240C11D CRC64;
     MRPLRDDAKR RADRQLSASM KPTSSNRPFS DRVPDRFKDG DDAQFDFTAP PRGMGSRDGN
     VHYMQQSLFS MIAAVGSKLD FHARFDESSD SDAEMEPQIE QTSGKLSSRT PAPTLDSRQP
     SKRLESNTLV LEERGRRHQR TRSDNKLLQR LPRLDSEGGA NESSNQPDSL LKMPPVRRTR
     SATPRAAPVL SRMVEAQSHF DLTSATPYLP PNPSKSTEDQ PQSSASALST RLMKMFGFAK
     PEKVLVEYAC SLLQSMLLQG YMYVTEGHIC FYAYLPKKSN VAIKSGCLSK RGRKNPTYHR
     YWFALKGDVL SYYADPSNLY FPSGHVDLRY GISASLADRK DGDAKDFQVT TDQRTYLYRA
     DSATSAKEWV KALQKVIFRT HYEGDSVKVS FPIANVIDLE ESPMADFAET FKIRVLDSGE
     TYAIDEVGRG TKRYHGSLLI TSQYFFSFFD SSQEAFNYIK GLVNAASAAT AMKEPQGEHD
     IQYQPESSRT THKRQSVSSV RVSDQRQRDS PRKRSSSVGI ENQGSADSFA EQGTGSSPII
     QSMTETTESA SQILHRSDVF QSPTMHTLQR RTLDVGETAR RRSDDMTPSA SARLDLDAAA
     GSPSGTLGGN ETTEDMRRVT GQSNPMQSSG PSSVTHLNEL VKAGAYPLQR AAGFAEYLKS
     RSKQMSTLLA TESMGYIEKV SGMWIGGQKH YGEREGPLLE DQNVDPEDNE GAFNYGDRFR
     AHFALPSSEK LQATYYAYLH RVLPLYGKIY ISQKKLCFRS LIPGTRTKMI LPFKDIENVE
     KEKGFRFGYH GLVVIIRGHE ELFFEFNASG SRDDCAVTLH QNLESVKFLV ESGLLADEER
     DEVEAAKAEH RMLQEARLDG PEEHDARPSL TEDSSETHPF FDDPRASIIN FKPLESLRIT
     CLTIGSRGDV QPYIALCKGL LAEGHKPKIA THAEFEPWIR KHGIDFAPVD GDPAELMRIC
     VENGMFTYSF LREASLKFRG WIDDLLSSAW IGCQGSDLLI ESPSAMAGVH IAEALRIPYF
     RGFTMPWTRT RAYPHAFAVP ENRMGGAYNY ITYVMFDNIF WKAIAGQVNR WRNNELGLKA
     TTLNKMQQNK VPFLYNYSPS VVAPPLDYPD WIRITGYWFL NEGTDWTPPI ELSNFISQAR
     ADGKKLVYIG FGSIVVSDPA ALTRTVIESV QKADVRCILS KGWSDRLGDP ASMKTEIPLP
     PAIHQIQSAP HDWLFSQIDA AAHHGGAGTT GASLRAGVPT IVKPFFGDQF FFGSRVEDLG
     VGICMKKLNV SVFSRALWEA THSERMIVKA RNLGIQIRNE DGVATAIQAI YRDLEYAKTL
     ARQKSLASST PFSPTPTAKT SPDGGDDDLD DIEEWTFVGD ETGFDISKRM RDRAASDADR
     LGSNMFQ
//
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