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ATG12_NEOFI
ID   ATG12_NEOFI             Reviewed;         174 AA.
AC   A1DMW6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Ubiquitin-like protein ATG12;
DE   AltName: Full=Autophagy-related protein 12;
GN   Name=atg12; ORFNames=NFIA_054850;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Ubiquitin-like protein involved in cytoplasm to vacuole
CC       transport (Cvt), autophagy vesicles formation, mitophagy, and
CC       nucleophagy. Conjugation with atg5 through a ubiquitin-like conjugating
CC       system involving also atg7 as an E1-like activating enzyme and atg10 as
CC       an E2-like conjugating enzyme, is essential for its function. The
CC       atg12-atg5 conjugate functions as an E3-like enzyme which is required
CC       for lipidation of atg8 and atg8 association to the vesicle membranes
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a conjugate with atg5. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATG12 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAW16137.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; DS027698; EAW16137.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001258034.1; XM_001258033.1.
DR   AlphaFoldDB; A1DMW6; -.
DR   SMR; A1DMW6; -.
DR   STRING; 36630.CADNFIAP00004468; -.
DR   EnsemblFungi; EAW16137; EAW16137; NFIA_054850.
DR   GeneID; 4584549; -.
DR   KEGG; nfi:NFIA_054850; -.
DR   eggNOG; KOG3439; Eukaryota.
DR   OrthoDB; 1525971at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000045; P:autophagosome assembly; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR007242; Atg12.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR13385; PTHR13385; 1.
DR   Pfam; PF04110; APG12; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
PE   3: Inferred from homology;
KW   Autophagy; Isopeptide bond; Membrane; Protein transport;
KW   Reference proteome; Transport; Ubl conjugation pathway.
FT   CHAIN           1..174
FT                   /note="Ubiquitin-like protein ATG12"
FT                   /id="PRO_0000317935"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        174
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-163 in atg5)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   174 AA;  18891 MW;  9E80627564A3A343 CRC64;
     MDSPSPENPS GTNSPNPKSP QITGSRLSHR PAISQRPDLD SNTRSTPIPD DEHGADLPMT
     MSASVVLSSL PRDAHRALAD AEAVDTGKVT VRFQPLPSAP ILKNRVFKIS ASQKFETVVK
     FLRKKLDCKD TDSVFCYVNS VFAPGLDEGV GGLWRCFKTD DQLIVSYSMT PAFG
 
 
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