ID   ATG21_PICAN             Reviewed;         388 AA.
AC   Q5QJC0;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Autophagy-related protein 21;
GN   Name=ATG21;
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].
RC   STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC   Y-5445;
RX   PubMed=9683670; DOI=10.1007/s002940050360;
RA   van der Klei I.J., van der Heide M., Baerends R.J.S., Rechinger K.-B.,
RA   Nicolay K., Kiel J.A.K.W., Veenhuis M.;
RT   "The Hansenula polymorpha per6 mutant is affected in two adjacent genes
RT   which encode dihydroxyacetone kinase and a novel protein, Pak1p, involved
RT   in peroxisome integrity.";
RL   Curr. Genet. 34:1-11(1998).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC   Y-5445;
RX   PubMed=15556634; DOI=10.1016/j.febslet.2004.10.055;
RA   Leao-Helder A.N., Krikken A.M., Gellissen G., van der Klei I.J.,
RA   Veenhuis M., Kiel J.A.K.W.;
RT   "Atg21p is essential for macropexophagy and microautophagy in the yeast
RT   Hansenula polymorpha.";
RL   FEBS Lett. 577:491-495(2004).
CC   -!- FUNCTION: Involved in peroxisome sequestration to the vacuole during
CC       macropexophagy. Also required for microautophagy.
CC       {ECO:0000269|PubMed:15556634}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15556634}. Membrane
CC       {ECO:0000269|PubMed:15556634}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:15556634}. Vacuole membrane
CC       {ECO:0000269|PubMed:15556634}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:15556634}. Note=Vacuolar and other perivacuolar
CC       punctate structures.
CC   -!- DOMAIN: Contains a beta-propeller domain involved in specific binding
CC       to phosphatidylinositol 3,5-bisphosphate (PIP2). {ECO:0000250}.
CC   -!- DOMAIN: The L/FRRG motif is essential for the cytoplasm to vacuole
CC       transport (Cvt) pathway and for the recruitment of ATG8 and ATG16 to
CC       the PAS in nutrient-rich medium and in both its recruitment to and
CC       dissociation from the PAS under starvation conditions.
CC       {ECO:0000250|UniProtKB:Q02887}.
CC   -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
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DR   EMBL; AY383554; AAR87854.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5QJC0; -.
DR   SMR; Q5QJC0; -.
DR   PhylomeDB; Q5QJC0; -.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00320; WD40; 2.
DR   SUPFAM; SSF50978; SSF50978; 1.
PE   3: Inferred from homology;
KW   Autophagy; Cytoplasm; Membrane; Protein transport; Repeat; Transport;
KW   Vacuole; WD repeat.
FT   CHAIN           1..388
FT                   /note="Autophagy-related protein 21"
FT                   /id="PRO_0000050880"
FT   REPEAT          179..219
FT                   /note="WD 1"
FT   REPEAT          224..263
FT                   /note="WD 2"
FT   MOTIF           220..224
FT                   /note="L/FRRG motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q02887"
SQ   SEQUENCE   388 AA;  42854 MW;  A7D90EE035FDFD92 CRC64;
     MALRSISFNQ DYTCLAAGFD AAYKVYNCDP FGECFQKADD GGANLVEMLF STSLIAVVGI
     GDKPANTMRK LKIINTKRKA VICELTFPTA ILYVKMNRKR LVVVLVDQIF VYDVSCMKLL
     HSIEASAGLD DRIICDLCAD DESVLVFQQS GSSDELAANA GTVVVFDALQ IQPINVIECH
     RSPLQRIAVS KDGRLLATAS VKGTIVRVFR VADGRKVHEF RRGSYTAQIS CLSFNVDATV
     LCCSSNTGTV HFFRLDDVDR RRSTGSIDAN IDGSETLPRE SSITEEESSE INRLINSQLG
     GHNGFAKKKS AESLKNFIWS KSKTYLPSQI NSILEPKRDY AFIKLTTEVE SVVGLVDNNC
     YVATRAGDFF VYSVQPGQCV LLKHYKIE