ATG28_KOMPG
ID ATG28_KOMPG Reviewed; 612 AA.
AC C4R159;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Autophagy-related protein 28;
GN Name=ATG28; OrderedLocusNames=PAS_chr2-1_0596;
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16874081; DOI=10.4161/auto.2226;
RA Stasyk O.V., Stasyk O.G., Mathewson R.D., Farre J.-C., Nazarko V.Y.,
RA Krasovska O.S., Subramani S., Cregg J.M., Sibirny A.A.;
RT "Atg28, a novel coiled-coil protein involved in autophagic degradation of
RT peroxisomes in the methylotrophic yeast Pichia pastoris.";
RL Autophagy 2:30-38(2006).
RN [3]
RP FUNCTION.
RX PubMed=19605559; DOI=10.1091/mbc.e09-03-0221;
RA Nazarko T.Y., Farre J.C., Subramani S.;
RT "Peroxisome size provides insights into the function of autophagy-related
RT proteins.";
RL Mol. Biol. Cell 20:3828-3839(2009).
RN [4]
RP INTERACTION WITH ATG35, 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: Required for the autophagic degradation of peroxisomes called
CC pexophagy, but not essential for general autophagy. Involved in
CC resistance to elevated pH. {ECO:0000269|PubMed:16874081,
CC ECO:0000269|PubMed:19605559, ECO:0000269|PubMed:21169734}.
CC -!- SUBUNIT: Interacts with ATG35. {ECO:0000269|PubMed:21169734}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16874081}. Vacuole
CC membrane {ECO:0000269|PubMed:16874081}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16874081}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:16874081}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16874081}. Note=Concentration increases at the
CC vacuolar and cytoplasmic vesicular membranes during the course of
CC pexophagy.
CC -!- INDUCTION: Expression is induced by methanol and glucose.
CC {ECO:0000269|PubMed:21169734}.
CC -!- SIMILARITY: Belongs to the ATG28 family. {ECO:0000305}.
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DR EMBL; FN392320; CAY69233.1; -; Genomic_DNA.
DR RefSeq; XP_002491513.1; XM_002491468.1.
DR AlphaFoldDB; C4R159; -.
DR SMR; C4R159; -.
DR EnsemblFungi; CAY69233; CAY69233; PAS_chr2-1_0596.
DR GeneID; 8198033; -.
DR KEGG; ppa:PAS_chr2-1_0596; -.
DR HOGENOM; CLU_480673_0_0_1; -.
DR InParanoid; C4R159; -.
DR Proteomes; UP000000314; Chromosome 2.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
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.
PE 1: Evidence at protein level;
KW Autophagy; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Membrane;
KW Protein transport; Reference proteome; Transport; Vacuole.
FT CHAIN 1..612
FT /note="Autophagy-related protein 28"
FT /id="PRO_0000422167"
FT REGION 44..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 214..296
FT /evidence="ECO:0000255"
SQ SEQUENCE 612 AA; 69519 MW; 3A514D587563E46E CRC64;
MICLFGNCNC QTGIFGLYDY VSFLYHSPSS CRVRLVLSLP ASPNHMEEQS PKFESSFPRR
TSEGPVDDVG KSPPASFYRE LLANKAQQPQ LSEDEEDHNP KDFLFKEDSE DELLIPDSEN
HNSSSTSPRK FKVENIRWGS DTLNGSILPL NSQGSNLQSL LSNVGELEHL LSKDVAKHSK
YLKEQSSKVE KARANIVTNL TRLSLVLSSI FNTYQAKAQD KQAILDKIEE WEDEKKSLLD
DMKEVLSTDD NADGETHKFL ELASESINVE NEIEALETRL KQLKIKQRTL KNECFQSQGI
IESRLSNFVQ AVEKIEMRER KSIEQVVQQL SENQLGYWND NLALEVMNGL TINPGDISLV
EEYEPVDILK QVESLEKPTI AADYHLPKNT NKQASRFTRQ LLEFNYKCQP KLNVYPVVGL
ITKELKEDSA KEQEYKHRYD QVTHTLSALK DSFALIYHTE QQLQSITQST QDLKDFQSLM
NQMVESLLKT HSEADQYNLY LAKDVLAQEI SIIHQALNKL NQSTEYSSVE SDNVKNHDGL
LFQTFSKAQE RTKLPSIKSA TSIRYAPSLY NSLSPTSTSK TTAKGEVNYD AGINKYTKVK
EVLRSGKGNK DE