ID ATG35_KOMPG Reviewed; 463 AA.
AC C4QVX6;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Autophagy-related protein 36;
GN Name=ATG35; OrderedLocusNames=PAS_chr1-1_0041;
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 INTERACTION WITH ATG28, FUNCTION, AND INDUCTION.
RX PubMed=21169734; DOI=10.4161/auto.7.4.14369;
RA Nazarko V.Y., Nazarko T.Y., Farre J.C., Stasyk O.V., Warnecke D.,
RA Ulaszewski S., Cregg J.M., Sibirny A.A., Subramani S.;
RT "Atg35, a micropexophagy-specific protein that regulates micropexophagic
RT apparatus formation in Pichia pastoris.";
RL Autophagy 7:375-385(2011).
CC -!- FUNCTION: Micropexophagy-specific protein required for efficient
CC micropexophagic apparatus (MIPA) formation but not for general
CC autophagy. {ECO:0000269|PubMed:21169734}.
CC -!- SUBUNIT: Interacts with ATG28. {ECO:0000269|PubMed:21169734}.
CC -!- INDUCTION: Expression is induced by methanol and glucose.
CC {ECO:0000269|PubMed:21169734}.
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DR EMBL; FN392319; CAY67399.1; -; Genomic_DNA.
DR RefSeq; XP_002489680.1; XM_002489635.1.
DR AlphaFoldDB; C4QVX6; -.
DR STRING; 644223.C4QVX6; -.
DR EnsemblFungi; CAY67399; CAY67399; PAS_chr1-1_0041.
DR GeneID; 8197558; -.
DR KEGG; ppa:PAS_chr1-1_0041; -.
DR eggNOG; KOG0825; Eukaryota.
DR HOGENOM; CLU_606994_0_0_1; -.
DR InParanoid; C4QVX6; -.
DR OMA; IPSQYII; -.
DR OrthoDB; 5490909at2759; -.
DR Proteomes; UP000000314; Chromosome 1.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProt.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR CDD; cd15489; PHD_SF; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR018527; Rubredoxin_Fe_BS.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45969; RING ZINC FINGER PROTEIN-RELATED; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00202; RUBREDOXIN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 2.
PE 1: Evidence at protein level;
KW Autophagy; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..463
FT /note="Autophagy-related protein 36"
FT /id="PRO_0000422170"
FT ZN_FING 5..45
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 85..131
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 229..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 53341 MW; 9D61A1B551D312A7 CRC64;
MEEVCSICLE VLVDKEAFTE PCLHYYHNEC IKEWTKRANT CPKCRRDYSQ IRIGEEVISV
KNRSLELHLV DETLEETRER LISYTNLCAL CEDPSTSLIY CESCGGSFHF NCIGIGDELD
SEWCCPLCGM FQNHLGEASN RNLISATPVG EGRRRVTSIV NTRRTNSIYR SHSNRPAQRA
HLMTDSDYTM IVDQHREKLL ESQLQESNTQ SSGEEESWKL LDEALKSGTQ NSQSSEFSTE
NNVVPLKNTH ELGRKLKKPR RASGIKKNVV ERSSSHQSTQ ILKPSSSLIS DLLLETRGNS
RHPSFTNSTQ KLTVEALQSH DPTLKLNIPK TETLSLDQKI VIQKLFIKPR LRNLYDSNTL
SKDNYIEINK IICRRLYDKF LQDQLALAYL KQVLEVKERL HGHDLKQFLA QFTHWSELND
FTDDKWQKQE TEGSCNHKQT QILSMFDSII DTMLQNELHK LLT
//
