ID   ATG26_PICAN             Reviewed;        1241 AA.
AC   A7KAK6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 61.
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};
OS   Pichia angusta (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=870730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC   Y-5445;
RX   PubMed=17204848; DOI=10.4161/auto.3595;
RA   Meijer W.H., van der Klei I.J., Veenhuis M., Kiel J.A.K.W.;
RT   "ATG genes involved in non-selective autophagy are conserved from yeast to
RT   man, but the selective Cvt and pexophagy pathways also require organism-
RT   specific genes.";
RL   Autophagy 3:106-116(2007).
CC   -!- FUNCTION: Probable sterol 3-beta-glucosyltransferase that mediates
CC       autophagic degradation of peroxisomes (pexophagy) (PubMed:17204848).
CC       Also required for cytoplasm to vacuole transport (Cvt) and autophagic
CC       degradation of mitochondria (mitophagy) and nuclei (nucleophagy) (By
CC       similarity). {ECO:0000250|UniProtKB:Q2U0C3,
CC       ECO:0000269|PubMed:17204848}.
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       Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q2U0C3};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:Q2U0C3}.
CC   -!- DOMAIN: The GRAM and PH domains are required for the localization of
CC       ATG26 to the preautophagosomal structure (PAS) and are involved in
CC       autophagy (By similarity). {ECO:0000250|UniProtKB:Q2U0C3}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000305}.
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DR   EMBL; EF107728; ABO31066.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7KAK6; -.
DR   SMR; A7KAK6; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   BRENDA; 2.4.1.173; 2587.
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   GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   Gene3D; 2.30.29.30; -; 3.
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; 1.
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   Autophagy; Cytoplasm; Glycosyltransferase; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Protein transport; Repeat;
KW   Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW   Sterol metabolism; Transferase; Transport.
FT   CHAIN           1..1241
FT                   /note="Sterol 3-beta-glucosyltransferase"
FT                   /id="PRO_0000318047"
FT   DOMAIN          220..267
FT                   /note="GRAM 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          271..373
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          609..675
FT                   /note="GRAM 2"
FT                   /evidence="ECO:0000255"
FT   REGION          1..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          124..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          499..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          720..741
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..157
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..553
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1241 AA;  139706 MW;  DD2EF8120266BE7B CRC64;
     MSGIESTEEP CDSMTESQSL SPLEPEERQT RKDSGLQSQS LTKRHFAFSP HRLITSISRH
     TSPHKPRPKS ESRVPVPKLH SLPPQRLASP ERDKPSIEGI SKSFVSFLTA ASVYAGFQDL
     EGEDQQVSPD DVSAGESEDQ QADESSDEQE DDDQDDRTFY ATDPSPTELT INENTPLPEP
     EPPRRTLRKA RSRFEFSVVK RLSENENDQL AQKRAIALSN KLKRTFDISD TDVFISDYPC
     WLMGDVLLQG HLYITKHHIL FFAFLPKKQG SISKSGALTT KSYPSLREHR KWAVLRNNTF
     SVYSNSTDLY FPLLVIDLRT ALRAEILQSS STKQNPSKPV WIRIITESRT HWFLADNLAS
     ARSWVSSLKK HIFASRNKGD QVAIKIPLQN VVDLELTSVI GVTKNLRIKV IESADTFAID
     DYFLMFFSRG EKAVEDIKKV IHDAGMEISE GTSTESEDEQ GVDNNLLKSK IELLKKSPSM
     VQTSSKSNVP VIRMDEPADD FSQEQESAES SKPVSDDEIV SADDNQELEE KQPQDNLANA
     EKENHDKVSR ANSRRTWSTR SLVQGLTAIT QGWMSPSPMA HFDEKYAVLR GEEDSYFVKD
     AEQRKAATER FRKHFSLTDG EKLIATYHAY LVKGIPAYGK IYLGSNEMCF RSTLPGTGTI
     MILPFSDIEN VNKEKGFRFG YSGLVVVIHG HEELFFEFAS DQARDDCEFM LLKQMDMFKK
     GSTDSSPPNA SEGSSDESCN LAESNTSLAS ARLRMFENRI HDAIGLDVPI IIEEHPLTKT
     KVRPLKSYRF TLLTIGSRGD VQPYIALGKA LMKEGHQVRI VTHAEFEPWI KKHGIRFASI
     AGDPSELMAL MVTHPTINYN FIKEAKSKFR SWIDDLLVTS WKACQDTDIL IESPSSICGI
     HIAEKLQIPY FRAFTMPWTR TRAYPHAFMV PDQKLGGAYN YMTHVAFENG YWRGTAHQVN
     KWRVETLGLP KTSLAEMKQN NVPFLYNVSP TVFPPSVDFA EWVKVTGYWF LDESETYQPP
     EVLTKFIEQA RKDGKKVVYI GFGSIVVSKP SELTQAVVDA VLEADVRCIL NKGWSDRLGT
     KTEIEVVLPP EIYNAGSVPH DWLFPQIDAA VHHGGSGTTG ASLRFGVPTI IKPFFGDQKF
     YAGRVEDLGC GVSLKDLNYK SLARALKEVT TNTRIIEKAK LVGARIRSET GVQTAIETIY
     NEMEYARSLS ISKVKQVSVV KSDEEFDDDK DEEVEGSWLL V