ATG13_PICAN
ID ATG13_PICAN Reviewed; 701 AA.
AC A7KAJ8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Autophagy-related protein 13;
GN Name=ATG13;
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], AND FUNCTION.
RC STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC Y-5445;
RX PubMed=17204848; DOI=10.4161/auto.3595;
RA Meijer W.H., van der Klei I.J., Veenhuis M., Kiel J.A.K.W.;
RT "ATG genes involved in non-selective autophagy are conserved from yeast to
RT man, but the selective Cvt and pexophagy pathways also require organism-
RT specific genes.";
RL Autophagy 3:106-116(2007).
CC -!- FUNCTION: Activates the ATG1 kinase in a nutritional condition
CC dependent manner through the TOR pathway, leading to autophagy. Also
CC involved in cytoplasm to vacuole transport (Cvt) and more specifically
CC in Cvt vesicle formation. Seems to play a role in the switching
CC machinery regulating the conversion between the Cvt pathway and
CC autophagy. Finally, ATG13 is also required for glycogen storage during
CC stationary phase (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:17204848}.
CC -!- SUBUNIT: Interacts with ATG1 to form the ATG1-ATG13 kinase complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06628}.
CC Preautophagosomal structure {ECO:0000250|UniProtKB:Q06628}.
CC -!- SIMILARITY: Belongs to the ATG13 family. Fungi subfamily.
CC {ECO:0000305}.
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DR EMBL; EF107720; ABO31058.1; -; Genomic_DNA.
DR AlphaFoldDB; A7KAJ8; -.
DR SMR; A7KAJ8; -.
DR PRIDE; A7KAJ8; -.
DR PhylomeDB; A7KAJ8; -.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IEA:InterPro.
DR GO; GO:0000407; C:phagophore assembly site; IEA:UniProtKB-SubCell.
DR GO; GO:0000045; P:autophagosome assembly; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.30.900.10; -; 1.
DR InterPro; IPR040182; ATG13.
DR InterPro; IPR018731; Atg13_N.
DR InterPro; IPR036570; HORMA_dom_sf.
DR PANTHER; PTHR13430; PTHR13430; 1.
DR Pfam; PF10033; ATG13; 1.
PE 3: Inferred from homology;
KW Autophagy; Cytoplasm; Protein transport; Transport.
FT CHAIN 1..701
FT /note="Autophagy-related protein 13"
FT /id="PRO_0000317949"
FT REGION 319..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 701 AA; 77933 MW; 57BD2B86E7AC39AA CRC64;
MSSARRPSKL LSEKQSDKLA QIIQNFFLKA AHVIFHFRVA FPSVVLQPDD SYGAMGDTFS
QSKYNNRWFN LDLGNYEIPR TELSLWRNKD ILSLPPLVLE TFLDLRGLSS NQTLMLDDVI
VKTSKKSEIV LERWLIEFDL STFDNEVMEF PSIYKKIIIL FRSLYLLAGL LPSYRLRDKL
VKSKSKNSAI HVSCRILDGS KPITSKGRIG LSKKLLSEEE HTSSKKLQPV LTPIGALRVS
VSYRTNCNFQ VSDTEEALSS QFMLDHLPSV RTNYDSDGNS LTSPMDYLQN RVSSASIHWS
DQSPRRRSST RSVQLFKVGS INSSSSPPPG ATQSNQSVSS FSTSKPIPVT LNKTNSSASL
VPILRQNKDS LPKSIGSMVQ NQMQETGHQV SSNSRRFSSS FGSRFRTVSS RNNSLDGQLV
VANQPFSTPS NNPILHNFRS RNKSPSVSST ELGPSSSIYM DDDLDSFMKM LDSKPDLRFP
SNSPSVYEDP LANFKTFQKS NDFLALEQQQ HGSPTSNQIM IHSQSQTSQS QVFKRTVFSD
RSRRGSVSSN YSPSSQALRP GASAPMVTPS VTYGKFHASS GSPSNSSLAQ YLRHNSSPPA
SATAVATVHN SLRRLTSSSQ RTNTNSTNSS TRPVNPELLK LKSFNEDVFE SDDDEHDEHS
PRSTDTKSRN TGPSSGHAED DEDDLLFAMS DMTLAKNNQE F