ATG3_CRYNB
ID ATG3_CRYNB Reviewed; 385 AA.
AC P0CM35; Q55JM5; Q5K9X6;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=Autophagy-related protein 3;
DE AltName: Full=Autophagy-related E2-like conjugation enzyme ATG3;
GN Name=ATG3; OrderedLocusNames=CNBK3080;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
CC -!- FUNCTION: E2 conjugating enzyme required for the cytoplasm to vacuole
CC transport (Cvt) and autophagy. Required for selective autophagic
CC degradation of the nucleus (nucleophagy) as well as for mitophagy which
CC contributes to regulate mitochondrial quantity and quality by
CC eliminating the mitochondria to a basal level to fulfill cellular
CC energy requirements and preventing excess ROS production. Responsible
CC for the E2-like covalent binding of phosphatidylethanolamine to the C-
CC terminal Gly of ATG8. The ATG12-ATG5 conjugate plays a role of an E3
CC and promotes the transfer of ATG8 from ATG3 to phosphatidylethanolamine
CC (PE). This step is required for the membrane association of ATG8. The
CC formation of the ATG8-phosphatidylethanolamine conjugate is essential
CC for autophagy and for the cytoplasm to vacuole transport (Cvt). The
CC ATG8-PE conjugate mediates tethering between adjacent membranes and
CC stimulates membrane hemifusion, leading to expansion of the
CC autophagosomal membrane during autophagy (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Interacts with ATG8 through an intermediate thioester
CC bond through the C-terminal Gly of ATG8. Also interacts with the 40
CC amino acid C-terminal region of the E1-like ATG7 enzyme. Interacts also
CC with the ATG12-ATG5 conjugate. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The N-terminal region is involved in phosphatidylethanolamine-
CC binding and is required for ATG8-PE conjugation. {ECO:0000250}.
CC -!- DOMAIN: The flexible region (FR) is required for ATG7-binding.
CC {ECO:0000250}.
CC -!- DOMAIN: The handle region (HR) contains the ATG8 interaction motif
CC (AIM) and mediates binding to ATG8. It is crucial for the cytoplasm-to-
CC vacuole targeting pathway (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATG3 family. {ECO:0000305}.
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DR EMBL; AAEY01000053; EAL17957.1; -; Genomic_DNA.
DR RefSeq; XP_772604.1; XM_767511.1.
DR AlphaFoldDB; P0CM35; -.
DR SMR; P0CM35; -.
DR EnsemblFungi; AAW46088; AAW46088; CNK00360.
DR EnsemblFungi; EAL17957; EAL17957; CNBK3080.
DR GeneID; 4939008; -.
DR KEGG; cnb:CNBK3080; -.
DR VEuPathDB; FungiDB:CNBK3080; -.
DR HOGENOM; CLU_027518_2_0_1; -.
DR Proteomes; UP000001435; Chromosome 11.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019787; F:ubiquitin-like protein transferase activity; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR007135; Atg3/Atg10.
DR PANTHER; PTHR12866; PTHR12866; 1.
DR Pfam; PF03987; Autophagy_act_C; 1.
PE 3: Inferred from homology;
KW Autophagy; Cytoplasm; Protein transport; Transport;
KW Ubl conjugation pathway.
FT CHAIN 1..385
FT /note="Autophagy-related protein 3"
FT /id="PRO_0000410019"
FT REGION 88..208
FT /note="Flexible region"
FT /evidence="ECO:0000250"
FT REGION 126..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..359
FT /note="Handle region"
FT /evidence="ECO:0000250"
FT REGION 292..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 277
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 385 AA; 42799 MW; 34D67DEDB48BA73D CRC64;
MNNPLLAIQS QYWAVRDYLS PVLRESKFKE HGRITPEEFV AAGDFLTFKF PVWQWEKGES
SRARDFLPPD KQYLVTRNVP CLRRATAVDY TNADEDAEKL LSFLDDAEEA PGPDDDWVAT
HINRSPPHRP TDMDEIPDIP DSPTTAPTRE MAGLNVSSGG KLEEDEIPDI DDIPDMDEEG
LEDLEDDAAV RIVHPSEAEV NSTAGKNLLQ VRTYDCIISY DKHYQTPRFW LFGYDEHKNP
LTPAQVFQDV PADHAFKTMT MESFPHSGAQ LASVHPCKHA SVMKKFIDRM EAAQGPAPTA
EPETISSTSG TSGSAGGKEE KEKKKKWGLG SMVRKVTGGS VPKVEKDKDE VVTGVPVDFY
LVIFLKFIAS IVPTIEVDST TSTAL
