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ATG18_PICAN
ID   ATG18_PICAN             Reviewed;         525 AA.
AC   Q5QA94;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Autophagy-related protein 18;
GN   Name=ATG18;
OS   Pichia angusta (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=870730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC   Y-5445;
RX   PubMed=15556634; DOI=10.1016/j.febslet.2004.10.055;
RA   Leao-Helder A.N., Krikken A.M., Gellissen G., van der Klei I.J.,
RA   Veenhuis M., Kiel J.A.K.W.;
RT   "Atg21p is essential for macropexophagy and microautophagy in the yeast
RT   Hansenula polymorpha.";
RL   FEBS Lett. 577:491-495(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC   Y-5445;
RX   PubMed=14613885; DOI=10.1016/s1567-1356(03)00125-9;
RA   Ramezani-Rad M., Hollenberg C.P., Lauber J., Wedler H., Griess E.,
RA   Wagner C., Albermann K., Hani J., Piontek M., Dahlems U., Gellissen G.;
RT   "The Hansenula polymorpha (strain CBS4732) genome sequencing and
RT   analysis.";
RL   FEMS Yeast Res. 4:207-215(2003).
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; AY756175; AAV74416.1; -; Genomic_DNA.
DR   PDB; 5LTD; X-ray; 2.50 A; A/B=1-525.
DR   PDB; 5LTG; X-ray; 2.00 A; A/B=1-525.
DR   PDBsum; 5LTD; -.
DR   PDBsum; 5LTG; -.
DR   AlphaFoldDB; Q5QA94; -.
DR   SMR; Q5QA94; -.
DR   PhylomeDB; Q5QA94; -.
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; -; 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   1: Evidence at protein level;
KW   3D-structure; Autophagy; Endosome; Membrane; Protein transport; Repeat;
KW   Transport; Vacuole; WD repeat.
FT   CHAIN           1..525
FT                   /note="Autophagy-related protein 18"
FT                   /id="PRO_0000050870"
FT   REPEAT          220..260
FT                   /note="WD 1"
FT   REPEAT          265..304
FT                   /note="WD 2"
FT   REGION          307..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           261..265
FT                   /note="L/FRRG motif"
FT                   /evidence="ECO:0000250|UniProtKB:P43601"
FT   COMPBIAS        319..333
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..362
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..385
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..402
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          35..39
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          43..50
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          53..58
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   TURN            59..62
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          63..69
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          73..79
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          82..91
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          100..105
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   TURN            106..109
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          110..116
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          123..126
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          128..135
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          138..143
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   TURN            144..146
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          149..154
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          173..177
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          202..208
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   TURN            209..212
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          213..223
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          225..230
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          236..241
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          245..251
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   TURN            252..254
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          257..262
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          270..275
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          279..286
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          290..295
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          440..444
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          453..466
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          486..497
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          500..507
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   TURN            509..511
FT                   /evidence="ECO:0007829|PDB:5LTG"
FT   STRAND          516..522
FT                   /evidence="ECO:0007829|PDB:5LTG"
SQ   SEQUENCE   525 AA;  57936 MW;  17B8515CFE309952 CRC64;
     MASPNPLAFE AATAAHEVAA SYVTEHKPRK NDNINFANFN QDFSCVSVGY SNGYKIYNCE
     PFGQCYSKSD GSIGIVEMLF SSSLLAIVGM GEQHSLSPRR LKIINTKRQT TICELTFPGA
     ILAVKLNRER LVVLLEETIY IYDINNMRLL HTIETPSNPN GLIALSPSSE NNYLAYPSPQ
     KLAPNPQTEV TLHSNPQTVR NGDVIIFDAK TLQPTSVIEA HRTSLAAIAL SKDGLLLATA
     SDKGTIIRVF SVATGIKLYQ FRRGTYPTKI YSLAFSPDNR FVIASSATET VHIFRLGEEE
     AANTIKSANK KARLTKAQVP NPLETSPDIY PHNQHTSSDE DEELNEDEED LDGDEDEDLE
     DDAHVPVSLQ RGRSSSSTGS FHSSESMTDK LKEPLVDNSR KSVARMLRRT SQSLGRKAAE
     KMGTYLPPKF SSILEPNRHF ASLKVPASKE TKTVVGVGSK IWDDLIPSVY LKDDANSITE
     TSEDLVNKKL VHIMVITSEG FFYKFGLDPE RGGDCVLLHQ QSLFG
 
 
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