ID   ATG37_KOMPG             Reviewed;         409 AA.
AC   C4R8D7;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Autophagy-related protein 37;
GN   OrderedLocusNames=PAS_chr4_0602;
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864;
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(2009).
RN   [2]
RP   INDUCTION, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH ATG30 AND PEX3,
RP   BINDING TO PALMITOYL-COA, PHOSPHORYLATION, AND FUNCTION.
RX   PubMed=24535825; DOI=10.1083/jcb.201307050;
RA   Nazarko T.Y., Ozeki K., Till A., Ramakrishnan G., Lotfi P., Yan M.,
RA   Subramani S.;
RT   "Peroxisomal Atg37 binds Atg30 or palmitoyl-CoA to regulate phagophore
RT   formation during pexophagy.";
RL   J. Cell Biol. 204:541-557(2014).
CC   -!- FUNCTION: Acyl-CoA binding protein which acts as the peroxisome
CC       receptor for pexophagy. Required for both micropexophagy and
CC       macropexophagy, but not for the cytoplasm to vacuole transport (Cvt) or
CC       autophagy pathways. Required for functional micropexophagic apparatus
CC       (MIPA) and relocation of ATG11 to the peroxisome-sequestering arms of
CC       the vacuole. Binds palmytoyl-CoA but not oleyl-CoA.
CC       {ECO:0000269|PubMed:24535825}.
CC   -!- SUBUNIT: Interacts with ATG30 and PEX3. {ECO:0000269|PubMed:24535825}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC       {ECO:0000269|PubMed:24535825}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:24535825}. Note=Localization to the peroxisome is
CC       ATG30-dependent.
CC   -!- INDUCTION: Repressed in glucose and ethanol media, but induced under
CC       peroxisome proliferation conditions in methanol and oleate media.
CC       {ECO:0000269|PubMed:24535825}.
CC   -!- PTM: Phosphorylated. {ECO:0000269|PubMed:24535825}.
CC   -!- SIMILARITY: Belongs to the ATG37 family. {ECO:0000305}.
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DR   EMBL; FN392322; CAY71862.1; -; Genomic_DNA.
DR   RefSeq; XP_002494041.1; XM_002493996.1.
DR   AlphaFoldDB; C4R8D7; -.
DR   SMR; C4R8D7; -.
DR   STRING; 644223.C4R8D7; -.
DR   PRIDE; C4R8D7; -.
DR   EnsemblFungi; CAY71862; CAY71862; PAS_chr4_0602.
DR   GeneID; 8200867; -.
DR   KEGG; ppa:PAS_chr4_0602; -.
DR   eggNOG; KOG0817; Eukaryota.
DR   HOGENOM; CLU_756699_0_0_1; -.
DR   InParanoid; C4R8D7; -.
DR   Proteomes; UP000000314; Chromosome 4.
DR   GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR   GO; GO:0000062; F:fatty-acyl-CoA binding; IDA:UniProtKB.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0030242; P:autophagy of peroxisome; IMP:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.80.10; -; 1.
DR   InterPro; IPR000582; Acyl-CoA-binding_protein.
DR   InterPro; IPR035984; Acyl-CoA-binding_sf.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   Pfam; PF00887; ACBP; 1.
DR   SUPFAM; SSF47027; SSF47027; 1.
DR   PROSITE; PS51228; ACB_2; 1.
PE   1: Evidence at protein level;
KW   Autophagy; Lipid-binding; Membrane; Peroxisome; Phosphoprotein;
KW   Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..409
FT                   /note="Autophagy-related protein 37"
FT                   /id="PRO_0000430145"
FT   TOPO_DOM        1..313
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        314..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        335..409
FT                   /note="Peroxisomal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          5..103
FT                   /note="ACB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
SQ   SEQUENCE   409 AA;  45908 MW;  B859011D331EF3E1 CRC64;
     MSESIDRVFV KAIGTIRTLS SRTGYGGLPR PPIENRVKLY GLYKQATEGD VAGVMERPLG
     DSPEAEAAKR KWDAWRSEQG TSKTEAKRQY ISYLIDTMKQ FASDTTEARE LLSELEYLWN
     QISDVSPNDS SDSESNAGPA QLLQNHAQLL SRDISVVDDP ITSSGMDPMY NPSFQRHNSS
     RFINASTAER LNSLSNYYSN LNPTPPLSSR RYQGSVTPRN VDFIKWQNDI NNSINKLNHD
     LQLLANRRLQ SSASDPLYSK RGSDLTHDDF VNDISSSSSN RRFRARRNQP LVSKVLLGTI
     SLLLKLIKTV IKHVAIDAVI IAVLVAVIKR SIIIPNLISN EISLQKIHHS ELESNSSIKG
     DSNGGRLTIV LPFINGKDFF QENSLLGKLL KVFHDYVDHV SRIRLIKRN