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ATG18_COCIM
ID   ATG18_COCIM             Reviewed;         417 AA.
AC   Q1DKJ3; J3K2F7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Autophagy-related protein 18;
GN   Name=ATG18; ORFNames=CIMG_09170;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
CC   -!- FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis
CC       and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
CC       Necessary for proper vacuole morphology. Plays an important role in
CC       osmotically-induced vacuole fragmentation. Required for cytoplasm to
CC       vacuole transport (Cvt) vesicle formation, pexophagy and starvation-
CC       induced autophagy. Involved in correct ATG9 trafficking to the pre-
CC       autophagosomal structure. Might also be involved in premeiotic DNA
CC       replication (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the PI(3,5)P2 regulatory complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Vacuole
CC       membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC       Endosome membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}.
CC   -!- DOMAIN: The N-terminus might form a beta-propeller domain involved in
CC       specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2),
CC       leading to the association of the protein to the membrane.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The L/FRRG motif is essential for the cytoplasm to vacuole
CC       transport (Cvt) pathway, for the recruitment of ATG8 and ATG16 to the
CC       PAS in nutrient-rich medium, and for its recruitment to and
CC       dissociation from the PAS under starvation conditions.
CC       {ECO:0000250|UniProtKB:P43601}.
CC   -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
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DR   EMBL; GG704915; EAS27966.3; -; Genomic_DNA.
DR   RefSeq; XP_001239549.1; XM_001239548.2.
DR   AlphaFoldDB; Q1DKJ3; -.
DR   SMR; Q1DKJ3; -.
DR   STRING; 246410.Q1DKJ3; -.
DR   EnsemblFungi; EAS27966; EAS27966; CIMG_09170.
DR   GeneID; 4558284; -.
DR   KEGG; cim:CIMG_09170; -.
DR   VEuPathDB; FungiDB:CIMG_09170; -.
DR   InParanoid; Q1DKJ3; -.
DR   OMA; PSRDFAW; -.
DR   OrthoDB; 1216824at2759; -.
DR   Proteomes; UP000001261; Unassembled WGS sequence.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0034045; C:phagophore assembly site 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.
DR   Gene3D; 2.130.10.10; -; 2.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   SMART; SM00320; WD40; 2.
DR   SUPFAM; SSF50978; SSF50978; 1.
PE   3: Inferred from homology;
KW   Autophagy; Endosome; Membrane; Protein transport; Reference proteome;
KW   Repeat; Transport; Vacuole; WD repeat.
FT   CHAIN           1..417
FT                   /note="Autophagy-related protein 18"
FT                   /id="PRO_0000318001"
FT   REPEAT          1..36
FT                   /note="WD 1"
FT   REPEAT          76..114
FT                   /note="WD 2"
FT   REPEAT          185..225
FT                   /note="WD 3"
FT   REPEAT          230..269
FT                   /note="WD 4"
FT   REPEAT          300..346
FT                   /note="WD 5"
FT   REPEAT          355..395
FT                   /note="WD 6"
FT   REGION          267..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           226..230
FT                   /note="L/FRRG motif"
FT                   /evidence="ECO:0000250|UniProtKB:P43601"
SQ   SEQUENCE   417 AA;  45539 MW;  3BB0AE7210CDD695 CRC64;
     MSMNFVTFNQ DYSYLAVGTS KGFRIFTTDP FGKSYETKEG NIAILEMLFS TSLVAVILSP
     RRLQIMNTKR QSVICELTFP TTVLAIRLNR KRLVIVLEDQ IYIYDIQTMK LVYTIETSPN
     PNAICALAPS SDNCYLAYPL PQKAPPPSFS PPSHGPPSNT HIPPTSGEVL IFDAYKLEAV
     NVVEAHKSPL SFLALNSEGT LLATASDKGT IIRVFSVPAA HKLYQFRRGS MPSRIYSMSF
     NITSTLLCVS SATETIHIFK LGQQQGLSKT SSPSRKLESS RGSGDESAVE SASSEMSSRK
     HNGTFMGMIR RTSQNVGNSF AATVGGYLPK GVTEMWEPER DFAWIKLPKS NGGNGGSGPV
     RSVVAMSSNT PQVMVVTSEG NFYVFNIDLS KGGEGTLVKQ YSVLDSSDRM GSTDLDY
 
 
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