ATG26_CRYNB
ID ATG26_CRYNB Reviewed; 1585 AA.
AC P0CN91; Q55W70; Q5KK25;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Sterol 3-beta-glucosyltransferase {ECO:0000305};
DE EC=2.4.1.173 {ECO:0000305};
DE AltName: Full=Autophagy-related protein 26 {ECO:0000250|UniProtKB:Q06321};
GN Name=ATG26 {ECO:0000250|UniProtKB:Q06321}; OrderedLocusNames=CNBC2670;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
CC -!- FUNCTION: Probable sterol 3-beta-glucosyltransferase that is not
CC involved in cytoplasm to vacuole transport (Cvt), pexophagy or
CC nonselective autophagy (By similarity). {ECO:0000250|UniProtKB:Q06321}.
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; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06321}.
CC Membrane {ECO:0000250|UniProtKB:Q06321}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q06321}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000305}.
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DR EMBL; AAEY01000013; EAL22129.1; -; Genomic_DNA.
DR RefSeq; XP_776776.1; XM_771683.1.
DR AlphaFoldDB; P0CN91; -.
DR SMR; P0CN91; -.
DR PRIDE; P0CN91; -.
DR EnsemblFungi; EAL22129; EAL22129; CNBC2670.
DR GeneID; 4934932; -.
DR KEGG; cnb:CNBC2670; -.
DR VEuPathDB; FungiDB:CNBC2670; -.
DR HOGENOM; CLU_000537_6_0_1; -.
DR Proteomes; UP000001435; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C: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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030259; P:lipid glycosylation; IEA:InterPro.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR Gene3D; 2.30.29.30; -; 2.
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 Pfam; PF03033; Glyco_transf_28; 1.
DR Pfam; PF02893; GRAM; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00201; UDPGT; 1.
DR SMART; SM00568; GRAM; 2.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Glycosyltransferase; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Repeat; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transferase.
FT CHAIN 1..1585
FT /note="Sterol 3-beta-glucosyltransferase"
FT /id="PRO_0000410100"
FT DOMAIN 387..555
FT /note="GRAM 1"
FT /evidence="ECO:0000255"
FT DOMAIN 438..530
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 862..933
FT /note="GRAM 2"
FT /evidence="ECO:0000255"
FT REGION 1..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1499..1552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..193
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1532..1550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1585 AA; 176690 MW; 7052DD840295E352 CRC64;
MSPPISPTPP PLQPPFPPTA IARGPDRPDP PPQHQQAAES LVNAAAQHVA PTCPPTSDEL
PQMEDQATNS SNDSLIPSRQ APNQEETENA ITAGTPPDEM EPTKDAQTVR FSSSSPASYS
THEYPTEEIN EPRTSSRAPN TASSQMAESS FDFRSSRDIG SIRMGASALV SALNALPWEE
DDDSDDGEDD DEFIEPARGS SSTIYERKQR PQTPSTSHGF HPTHTLHFPF RQNAIARRAC
QPGTTELDYQ YATPETSSRR TSAAGSESSS EGEVPLPKGF VSHPNLIVPS GEGEAAAHPD
PKLISDRITK EQQIADVEEQ AEILRSAEEQ EMRLGKEFVP PKSRDSADLN VDAALREGGS
EREDVIEEQM QTNEAEKRLT RNEKLAERLM EVFGLEEREE VLEEMKCWLL RSVMLKGYMY
LTKRHICFFA NMPNENNLLV KSGPLHKKAS RSKLNTKFWV VLKNDVLSWY ESTSDPYFPK
GNISLQYCHS CDAVSGTRFK VRTSERNYTF TADTESSRDE WVKAIQKVMF KTQHEGETIK
LIIPLEAIVD VEKSPTLEFT ETIEVKCIDA EDQMSVDSYF FASFPDNDYA FSAIQKLVRE
RPSPPELPRI SSVTTIHANQ EPLDTSHATI KRHGTDSSAE KLGMASHRPF RKISSVLKPL
ILKSSDGEPL EEHSQGPHHN DEDASHLPHI EAISNRRRSE EESDNDYFDG YPPRQVGPPP
PSMNDDARNW RPSWIRKPAS KLFGSSPSGS FVSHPGRLPT DSSTTVTESG PSLRSRTGRT
KQASVTEVIE PPIQYEEEVS EDEMSNKPSV VDSNSAETAR KRAARLSWTS ETSSGSQMVK
SKSDFSMLGS ESGHSESAET VRKFRTFFAL SDKEELIDHF PGYLYRVLPV SGRFFISTNY
FCFRSSQLLY KTKESFRLMI IPIRDLYGLK AQKAFRFGHS GLTVVIKGHE EIFIEFRSAS
RRKACIALLE ERMEAVRLSG ENTIVDSHKI EARIMEDLDE STPVEPKSPW PVSPSPLFGS
TTSTSFLEFK PEPMKITCLT IGSRGDVQPY IALCKGLQAE GHITKIATHG EYKAWVEGHG
IAFESVGGDP AELMQMCVDN GMFTVSFLKE GLQKFRGWLD DLLNSSWEAC QGSDLLIESP
SAMSGIHVAE ALRIPYYRAF TMPWTRTRAY PHAFAVPEHG RGGPYNYMTY TMFDQVFWRA
ISGQVNRWRR NVLGLDATTF DKMEQHKVPF LYNFSPTVVP PPLDWTEWIH VTGYWFLDKA
DEKQGEKSWT PPQGLVDFID KAHGEEKKVV YIGFGSIVVS DPEEMTRCVV EAVVNSGVCA
ILSKGWSDRG SKKGEPKGDS EGADGVKYPP EIFAIDSIDH GWLFPRIDAA CHHGGAGTTG
ASLRAGIPTI IKPFFGDQAF WAERVESLNV GSSIRRLTSH QLASALIKAT TDEKQISKAR
VVGEMIRKEN GITRAIEAIY RDLEYAKSII KSLPSTDDRT PERISSLLHP LTTADLSFNR
VRSRSRSRSR SSQGRFSPRR HTVDDDGWSV VSGGSRSRSG SASAVTSPER RPLNIGSALG
SHVFKTALLP NTFGKWRNLE EGDDR
