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ATG21_CANAL
ID   ATG21_CANAL             Reviewed;         529 AA.
AC   Q5AI22; A0A1D8PCZ9;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Autophagy-related protein 21;
GN   Name=ATG21; OrderedLocusNames=CAALFM_C103330CA;
GN   ORFNames=CaO19.10548, CaO19.3030;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC   -!- FUNCTION: Required for cytoplasm to vacuole transport (Cvt) vesicles
CC       formation and mitophagy. Involved in binding of
CC       phosphatidylethanolamine to ATG8 and in recruitment of ATG8 and ATG5 to
CC       the pre-autophagosomal structure. Protects ATG8 from ARG4-mediated
CC       cleavage (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}. Vacuole membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Vacuolar
CC       and perivacuolar punctate structures. {ECO:0000250}.
CC   -!- DOMAIN: Contains a beta-propeller domain involved in specific binding
CC       to phosphatidylinositol 3,5-bisphosphate (PIP2). {ECO:0000250}.
CC   -!- DOMAIN: The L/FRRG motif is essential for the cytoplasm to vacuole
CC       transport (Cvt) pathway and for the recruitment of ATG8 and ATG16 to
CC       the PAS in nutrient-rich medium and in both its recruitment to and
CC       dissociation from the PAS under starvation conditions.
CC       {ECO:0000250|UniProtKB:Q02887}.
CC   -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
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DR   EMBL; CP017623; AOW26014.1; -; Genomic_DNA.
DR   RefSeq; XP_721528.1; XM_716435.2.
DR   AlphaFoldDB; Q5AI22; -.
DR   SMR; Q5AI22; -.
DR   STRING; 237561.Q5AI22; -.
DR   PRIDE; Q5AI22; -.
DR   GeneID; 3636859; -.
DR   KEGG; cal:CAALFM_C103330CA; -.
DR   CGD; CAL0000201683; orf19.10548.
DR   VEuPathDB; FungiDB:C1_03330C_A; -.
DR   eggNOG; KOG2110; Eukaryota.
DR   HOGENOM; CLU_025895_5_2_1; -.
DR   InParanoid; Q5AI22; -.
DR   OrthoDB; 1216824at2759; -.
DR   PRO; PR:Q5AI22; -.
DR   Proteomes; UP000000559; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IBA:GO_Central.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR   GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR   GO; GO:0006497; P:protein lipidation; IBA:GO_Central.
DR   GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
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; Cytoplasm; Membrane; Protein transport; Reference proteome;
KW   Repeat; Transport; Vacuole; WD repeat.
FT   CHAIN           1..529
FT                   /note="Autophagy-related protein 21"
FT                   /id="PRO_0000050876"
FT   REPEAT          271..311
FT                   /note="WD 1"
FT   REPEAT          321..361
FT                   /note="WD 2"
FT   REGION          49..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          362..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           318..322
FT                   /note="L/FRRG motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q02887"
FT   COMPBIAS        362..387
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   529 AA;  60019 MW;  A31F3C9C491028EB CRC64;
     MVTINDLSFN PDYSSISVST SDGFKIFNCE PFGEFYSSQE SPLRKSISNS LEDSAGCQNP
     THSKTDSQDT PARFPTAFLK MLFSTSLTIV VPQTQDNLGN RLLKIYNLKQ NLKICELNFP
     SSIIDIKLNR KRLLVVLDTG QLYIYDLSCV RLLKILQLSF NEHDGDQKFI GDLSADDSSW
     LIIPVQSTNN QTDLLNAETG SQPSTPKLTP SDSVINTGSY SQYLEFTRNS SLSNLKKKNK
     LITLEDIKND SEGWVVVYDT INLAPVVIFE AHHSTIARIC ISHRDNKVAT ASIKGTIIRI
     FDLKEFEGKV KVHKVKNLRR GHNLVKVNSL SFHNDNHILG CGSESNTIHL FKIHEEESDI
     CTNENSEDRT NHNSDYEDSD GDTSKSSEDL NENLANLLIS KPLDPVPMET EDKLSSSWFV
     KTKKLINNQY TSSIIKKLPY KDYFENLIWE PPQRSFAYIK LPEYAPHNEK DPRSNKVEIG
     FNNDLVFIAS YHTGNFYQYQ IPKQRGPVSS INEDDKREEC SLISQFNLI
 
 
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