RAVZ_LEGPH
ID RAVZ_LEGPH Reviewed; 502 AA.
AC Q5ZUV9;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Cysteine protease RavZ {ECO:0000305};
DE EC=3.4.22.- {ECO:0000269|PubMed:23112293};
DE AltName: Full=Region allowing vacuole colocalization protein Z {ECO:0000303|PubMed:20880356};
GN Name=ravZ {ECO:0000303|PubMed:20880356, ECO:0000303|PubMed:23112293};
GN OrderedLocusNames=lpg1683 {ECO:0000312|EMBL:AAU27763.1};
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=20880356; DOI=10.1111/j.1462-5822.2010.01531.x;
RA Huang L., Boyd D., Amyot W.M., Hempstead A.D., Luo Z.Q., O'Connor T.J.,
RA Chen C., Machner M., Montminy T., Isberg R.R.;
RT "The E Block motif is associated with Legionella pneumophila translocated
RT substrates.";
RL Cell. Microbiol. 13:227-245(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF CYS-258.
RX PubMed=23112293; DOI=10.1126/science.1227026;
RA Choy A., Dancourt J., Mugo B., O'Connor T.J., Isberg R.R., Melia T.J.,
RA Roy C.R.;
RT "The Legionella effector RavZ inhibits host autophagy through irreversible
RT Atg8 deconjugation.";
RL Science 338:1072-1076(2012).
RN [4]
RP FUNCTION.
RX PubMed=28971069; DOI=10.3389/fcimb.2017.00384;
RA Kubori T., Bui X.T., Hubber A., Nagai H.;
RT "Legionella RavZ plays a role in preventing ubiquitin recruitment to
RT bacteria-containing vacuoles.";
RL Front. Cell. Infect. Microbiol. 7:384-384(2017).
RN [5]
RP FUNCTION.
RX PubMed=29458288; DOI=10.1080/15548627.2018.1437341;
RA Kauffman K.J., Yu S., Jin J., Mugo B., Nguyen N., O'Brien A., Nag S.,
RA Lystad A.H., Melia T.J.;
RT "Delipidation of mammalian Atg8-family proteins by each of the four ATG4
RT proteases.";
RL Autophagy 14:992-1010(2018).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=31722778; DOI=10.5483/bmbrep.2019.52.12.211;
RA Park S.W., Jun Y.W., Jeon P., Lee Y.K., Park J.H., Lee S.H., Lee J.A.,
RA Jang D.J.;
RT "LIR motifs and the membrane-targeting domain are complementary in the
RT function of RavZ.";
RL BMB Rep. 52:700-705(2019).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=31719622; DOI=10.1038/s41598-019-53372-2;
RA Park S.W., Jeon P., Jun Y.W., Park J.H., Lee S.H., Lee S., Lee J.A.,
RA Jang D.J.;
RT "Monitoring LC3- or GABARAP-positive autophagic membranes using modified
RT RavZ-based probes.";
RL Sci. Rep. 9:16593-16593(2019).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 63-MET-ASN-64 AND
RP 175-GLN--GLN-177.
RX PubMed=32686895; DOI=10.1002/cbic.202000359;
RA Yang A., Pantoom S., Wu Y.W.;
RT "Distinct mechanisms for processing autophagy protein LC3-PE by RavZ and
RT ATG4B.";
RL ChemBioChem 21:3377-3382(2020).
RN [9]
RP FUNCTION.
RX PubMed=32482642; DOI=10.1128/iai.00793-19;
RA Omotade T.O., Roy C.R.;
RT "Legionella pneumophila excludes autophagy adaptors from the ubiquitin-
RT labeled vacuole in which it resides.";
RL Infect. Immun. 88:0-0(2020).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=33298241; DOI=10.5483/bmbrep.2021.54.2.190;
RA Park J.H., Lee S.H., Park S.W., Jun Y.W., Kim K., Jeon P., Kim M.,
RA Lee J.A., Jang D.J.;
RT "Deciphering the role of a membrane-targeting domain in assisting endosomal
RT and autophagic membrane localization of a RavZ protein catalytic domain.";
RL BMB Rep. 54:118-123(2021).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=33909989; DOI=10.1016/j.molcel.2021.03.020;
RA Durgan J., Lystad A.H., Sloan K., Carlsson S.R., Wilson M.I., Marcassa E.,
RA Ulferts R., Webster J., Lopez-Clavijo A.F., Wakelam M.J., Beale R.,
RA Simonsen A., Oxley D., Florey O.;
RT "Non-canonical autophagy drives alternative ATG8 conjugation to
RT phosphatidylserine.";
RL Mol. Cell 81:2031-2040(2021).
RN [12] {ECO:0007744|PDB:5CQC}
RP X-RAY CRYSTALLOGRAPHY (2.98 ANGSTROMS) OF 10-458, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVE SITES, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF
RP HIS-176; ASP-197; 211-TYR--ARG-217; 211-TYR--TYR-216; CYS-258; LYS-306;
RP ARG-343; 359-LYS--LYS-362 AND LYS-404.
RX PubMed=26343456; DOI=10.1016/j.devcel.2015.08.010;
RA Horenkamp F.A., Kauffman K.J., Kohler L.J., Sherwood R.K., Krueger K.P.,
RA Shteyn V., Roy C.R., Melia T.J., Reinisch K.M.;
RT "The Legionella anti-autophagy effector RavZ targets the autophagosome via
RT PI3P- and curvature-sensing motifs.";
RL Dev. Cell 34:569-576(2015).
RN [13] {ECO:0007744|PDB:5HZY, ECO:0007744|PDB:5IO3}
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 49-502, DOMAIN, AND MUTAGENESIS
RP OF 16-PHE--LEU-19; 29-PHE--LEU-32 AND 435-PHE--ILE-438.
RX PubMed=27791457; DOI=10.1080/15548627.2016.1243199;
RA Kwon D.H., Kim S., Jung Y.O., Roh K.H., Kim L., Kim B.W., Hong S.B.,
RA Lee I.Y., Song J.H., Lee W.C., Choi E.J., Hwang K.Y., Song H.K.;
RT "The 1:2 complex between RavZ and LC3 reveals a mechanism for deconjugation
RT of LC3 on the phagophore membrane.";
RL Autophagy 13:70-81(2017).
RN [14] {ECO:0007744|PDB:5XAD}
RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 12-34 IN COMPLEX WITH MAP1LC3B,
RP AND DOMAIN.
RX PubMed=28668392; DOI=10.1016/j.bbrc.2017.06.173;
RA Kwon D.H., Kim L., Kim B.W., Kim J.H., Roh K.H., Choi E.J., Song H.K.;
RT "A novel conformation of the LC3-interacting region motif revealed by the
RT structure of a complex between LC3B and RavZ.";
RL Biochem. Biophys. Res. Commun. 490:1093-1099(2017).
RN [15] {ECO:0007744|PDB:5MS2, ECO:0007744|PDB:5MS5}
RP X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 24-36 AND 39-46 IN COMPLEX WITH
RP MAP1LC3B, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, DOMAIN, AND
RP MUTAGENESIS OF PHE-29; 139-LEU--LEU-143; 180-LEU--ILE-182; LEU-208;
RP 211-TYR--TYR-216; TYR-211; PHE-212; TYR-216; 224-LEU--ILE-232;
RP 237-PHE--PHE-242 AND CYS-258.
RX PubMed=28395732; DOI=10.7554/elife.23905;
RA Yang A., Pantoom S., Wu Y.W.;
RT "Elucidation of the anti-autophagy mechanism of the Legionella effector
RT RavZ using semisynthetic LC3 proteins.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: Cysteine protease effector that inhibits host cell autophagy
CC by targeting lipid-conjugated ATG8 family proteins on pre-
CC autophagosomal structures (PubMed:23112293, PubMed:29458288,
CC PubMed:32686895, PubMed:31722778, PubMed:31719622, PubMed:33298241,
CC PubMed:26343456, PubMed:28395732). Specifically hydrolyzes the amide
CC bond between the C-terminal glycine residue and an adjacent aromatic
CC residue in ATG8 proteins conjugated to phosphatidylethanolamine (PE),
CC producing an ATG8 protein that cannot be reconjugated by host ATG7 and
CC ATG3 (PubMed:23112293, PubMed:29458288, PubMed:32686895,
CC PubMed:26343456, PubMed:28395732). Mechanistically, Ravz interacts with
CC ATG8 proteins conjugated to PE via its LIR motifs, extracts them from
CC the membrane of autophagosomes and integrates the PE part into its own
CC lipid-binding site (PubMed:28395732). It then removes the lipid
CC component of the ATG8 protein (PubMed:28395732). Also able to mediate
CC delipidation of ATG8 proteins conjugated to phosphatidylserine (PS)
CC during non-canonical autophagy (PubMed:33909989). Inhibits host
CC ubiquitin recruitment to bacteria-containing vacuoles, suggesting that
CC it is able to mediate delipidation of other proteins in addition to
CC ATG8 proteins (PubMed:28971069). It is however not involved in the
CC exclusion of autophagy adapters from bacteria-containing vacuoles
CC decorated with ubiquitin (PubMed:32482642).
CC {ECO:0000269|PubMed:23112293, ECO:0000269|PubMed:26343456,
CC ECO:0000269|PubMed:28395732, ECO:0000269|PubMed:28971069,
CC ECO:0000269|PubMed:29458288, ECO:0000269|PubMed:31719622,
CC ECO:0000269|PubMed:31722778, ECO:0000269|PubMed:32482642,
CC ECO:0000269|PubMed:32686895, ECO:0000269|PubMed:33298241,
CC ECO:0000269|PubMed:33909989}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-C-terminal L-amino acid-glycyl-
CC phosphatidylethanolamide + H2O = 1,2-diacyl-sn-glycero-3-
CC phosphoethanolamine-N-glycine + [protein]-C-terminal
CC L-amino acid; Xref=Rhea:RHEA:67664, Rhea:RHEA-
CC COMP:17323, Rhea:RHEA-COMP:17349, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:90782, ChEBI:CHEBI:172870, ChEBI:CHEBI:172941;
CC Evidence={ECO:0000269|PubMed:23112293, ECO:0000269|PubMed:26343456,
CC ECO:0000269|PubMed:28395732, ECO:0000269|PubMed:32686895,
CC ECO:0000269|PubMed:33298241};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-C-terminal L-amino acid-glycyl-phosphatidylserine +
CC H2O = 1,2-diacyl-sn-glycero-3-phospho-L-serine-N-glycine + [protein]-
CC C-terminal L-amino acid; Xref=Rhea:RHEA:67912,
CC Rhea:RHEA-COMP:17326, Rhea:RHEA-COMP:17349, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:90782, ChEBI:CHEBI:172942, ChEBI:CHEBI:176543;
CC Evidence={ECO:0000269|PubMed:33909989};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20880356}. Host
CC cytoplasmic vesicle membrane {ECO:0000269|PubMed:23112293,
CC ECO:0000269|PubMed:26343456, ECO:0000269|PubMed:31719622,
CC ECO:0000269|PubMed:31722778, ECO:0000269|PubMed:33298241}.
CC Note=Translocated into the host cell via the type IV secretion system
CC (T4SS) (Probable). In host cells, localizes to mature autophagosome
CC membranes (PubMed:23112293, PubMed:31722778, PubMed:31719622,
CC PubMed:33298241, PubMed:26343456). {ECO:0000269|PubMed:23112293,
CC ECO:0000269|PubMed:26343456, ECO:0000269|PubMed:31719622,
CC ECO:0000269|PubMed:31722778, ECO:0000269|PubMed:33298241,
CC ECO:0000305|PubMed:23112293}.
CC -!- DOMAIN: The LIR motifs (LC3-interacting regions) are required for the
CC interaction with ATG8 family proteins (PubMed:31722778,
CC PubMed:27791457, PubMed:28668392, PubMed:28395732). The LIR motifs 1
CC and 2 at the N-terminus bind one ATG8 protein and the LIR motif 3 at
CC the C-terminus binds another ATG8 protein (PubMed:31722778,
CC PubMed:27791457). Among ATG8 proteins, the LIR motif 3 has preference
CC for host GABARAP (GABARAP GABARAPL1, GABARAPL2) compared to LC3
CC (MAP1LC3A, MAP1LC3B, MAP1LC3C) (PubMed:31719622).
CC {ECO:0000269|PubMed:27791457, ECO:0000269|PubMed:28395732,
CC ECO:0000269|PubMed:28668392, ECO:0000269|PubMed:31719622,
CC ECO:0000269|PubMed:31722778}.
CC -!- DOMAIN: The membrane targeting (MT) region binds phosphatidylinositol
CC 3-monophosphate (PI3P) (PubMed:26343456). The MT region, together with
CC the alpha-3 helix promote localization to high-curvature membranes,
CC intimating localization to highly curved domains in autophagosome
CC intermediate membranes (PubMed:26343456). The alpha-3 helix is involved
CC in extraction of the phosphatidylethanolamine (PE) moiety and docking
CC of the acyl chains into the lipid-binding site (PubMed:28395732).
CC {ECO:0000269|PubMed:26343456, ECO:0000269|PubMed:28395732}.
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DR EMBL; AE017354; AAU27763.1; -; Genomic_DNA.
DR RefSeq; WP_010947410.1; NC_002942.5.
DR RefSeq; YP_095710.1; NC_002942.5.
DR PDB; 5CQC; X-ray; 2.98 A; A=10-458.
DR PDB; 5HZY; X-ray; 2.55 A; A=49-502.
DR PDB; 5IO3; X-ray; 2.74 A; A=1-502.
DR PDB; 5IZV; X-ray; 2.81 A; A/B=1-502.
DR PDB; 5MS2; X-ray; 2.47 A; A=1-431.
DR PDB; 5MS5; X-ray; 1.53 A; A/B=24-36, A/B=39-46.
DR PDB; 5MS7; X-ray; 2.80 A; A=20-502.
DR PDB; 5MS8; X-ray; 2.85 A; A=1-487.
DR PDB; 5XAD; X-ray; 1.88 A; C/D=12-34.
DR PDBsum; 5CQC; -.
DR PDBsum; 5HZY; -.
DR PDBsum; 5IO3; -.
DR PDBsum; 5IZV; -.
DR PDBsum; 5MS2; -.
DR PDBsum; 5MS5; -.
DR PDBsum; 5MS7; -.
DR PDBsum; 5MS8; -.
DR PDBsum; 5XAD; -.
DR SMR; Q5ZUV9; -.
DR STRING; 272624.lpg1683; -.
DR PaxDb; Q5ZUV9; -.
DR PRIDE; Q5ZUV9; -.
DR EnsemblBacteria; AAU27763; AAU27763; lpg1683.
DR GeneID; 66490815; -.
DR KEGG; lpn:lpg1683; -.
DR PATRIC; fig|272624.6.peg.1764; -.
DR eggNOG; ENOG5031DWI; Bacteria.
DR HOGENOM; CLU_559960_0_0_6; -.
DR OMA; EITAFCA; -.
DR Proteomes; UP000000609; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033648; C:host intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR GO; GO:0140321; P:negative regulation by symbiont of host autophagy; IDA:UniProtKB.
DR GO; GO:0051697; P:protein delipidation; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Host cytoplasmic vesicle; Host membrane; Hydrolase; Membrane;
KW Protease; Reference proteome; Secreted; Thiol protease; Virulence.
FT CHAIN 1..502
FT /note="Cysteine protease RavZ"
FT /id="PRO_0000454158"
FT REGION 49..325
FT /note="Catalytic region"
FT /evidence="ECO:0000303|PubMed:27791457"
FT REGION 211..217
FT /note="Alpha-3 helix"
FT /evidence="ECO:0000303|PubMed:26343456"
FT REGION 326..431
FT /note="Membrane targeting region"
FT /evidence="ECO:0000303|PubMed:27791457"
FT MOTIF 9..23
FT /note="LIR 1"
FT /evidence="ECO:0000269|PubMed:27791457"
FT MOTIF 23..37
FT /note="LIR 2"
FT /evidence="ECO:0000269|PubMed:27791457"
FT MOTIF 429..443
FT /note="LIR 3"
FT /evidence="ECO:0000269|PubMed:27791457"
FT ACT_SITE 176
FT /evidence="ECO:0000269|PubMed:26343456"
FT ACT_SITE 197
FT /evidence="ECO:0000269|PubMed:26343456"
FT ACT_SITE 258
FT /evidence="ECO:0000269|PubMed:23112293,
FT ECO:0000269|PubMed:26343456, ECO:0000269|PubMed:28395732"
FT MUTAGEN 16..19
FT /note="FEEL->AEEA: In mLIR1; only binds one ATG8 protein
FT instead of two."
FT /evidence="ECO:0000269|PubMed:27791457"
FT MUTAGEN 29..32
FT /note="FDLL->ADLA: In mLIR2; only binds one ATG8 protein
FT instead of two."
FT /evidence="ECO:0000269|PubMed:27791457"
FT MUTAGEN 29
FT /note="F->A: Reduced ability to cleave lipid-conjugated
FT ATG8 family proteins."
FT /evidence="ECO:0000269|PubMed:28395732"
FT MUTAGEN 63..64
FT /note="MN->AA: Abolished ability to cleave lipid-conjugated
FT ATG8 family proteins."
FT /evidence="ECO:0000269|PubMed:32686895"
FT MUTAGEN 139..143
FT /note="LDRRL->DDRRD: Reduced ability to cleave lipid-
FT conjugated ATG8 family proteins."
FT /evidence="ECO:0000269|PubMed:28395732"
FT MUTAGEN 175..177
FT /note="QHQ->AQA: Does not affect ability to cleave lipid-
FT conjugated ATG8 family proteins."
FT /evidence="ECO:0000269|PubMed:32686895"
FT MUTAGEN 176
FT /note="H->A: Abolished ability to cleave lipid-conjugated
FT ATG8 family proteins; when associated with A-258."
FT /evidence="ECO:0000269|PubMed:26343456"
FT MUTAGEN 180..182
FT /note="LTI->DTD: Reduced ability to cleave lipid-conjugated
FT ATG8 family proteins."
FT /evidence="ECO:0000269|PubMed:28395732"
FT MUTAGEN 197
FT /note="D->A: Abolished ability to cleave lipid-conjugated
FT ATG8 family proteins."
FT /evidence="ECO:0000269|PubMed:26343456"
FT MUTAGEN 208
FT /note="L->D: Reduced ability to cleave lipid-conjugated
FT ATG8 family proteins."
FT /evidence="ECO:0000269|PubMed:28395732"
FT MUTAGEN 211..217
FT /note="YFKGKYR->AAAGAAA: Reduced binding to membranes."
FT /evidence="ECO:0000269|PubMed:26343456"
FT MUTAGEN 211..216
FT /note="YFKGKY->DDKGKD: Reduced binding to membranes.
FT Abolished ability to cleave lipid-conjugated ATG8 family
FT proteins."
FT /evidence="ECO:0000269|PubMed:26343456,
FT ECO:0000269|PubMed:28395732"
FT MUTAGEN 211
FT /note="Y->D: Reduced ability to cleave lipid-conjugated
FT ATG8 family proteins."
FT /evidence="ECO:0000269|PubMed:28395732"
FT MUTAGEN 212
FT /note="F->D: Reduced ability to cleave lipid-conjugated
FT ATG8 family proteins."
FT /evidence="ECO:0000269|PubMed:28395732"
FT MUTAGEN 216
FT /note="Y->D: Slightly reduced ability to cleave lipid-
FT conjugated ATG8 family proteins."
FT /evidence="ECO:0000269|PubMed:28395732"
FT MUTAGEN 224..232
FT /note="LTQSIEKAI->DTQSDEKAD: Reduced ability to cleave
FT lipid-conjugated ATG8 family proteins."
FT /evidence="ECO:0000269|PubMed:28395732"
FT MUTAGEN 237..242
FT /note="FTLGKF->DTDGKD: Reduced ability to cleave lipid-
FT conjugated ATG8 family proteins."
FT /evidence="ECO:0000269|PubMed:28395732"
FT MUTAGEN 258
FT /note="C->A,S: Abolished ability to cleave lipid-conjugated
FT ATG8 family proteins. Abolished ability to cleave lipid-
FT conjugated ATG8 family proteins; when associated with A-
FT 176."
FT /evidence="ECO:0000269|PubMed:23112293,
FT ECO:0000269|PubMed:28395732, ECO:0000269|PubMed:31719622"
FT MUTAGEN 306
FT /note="K->A: Reduced binding to phosphatidylinositol 3-
FT monophosphate (PI3P); when associated with A-404."
FT /evidence="ECO:0000269|PubMed:26343456"
FT MUTAGEN 343
FT /note="R->A: Strongly reduced binding to
FT phosphatidylinositol 3-monophosphate (PI3P); when
FT associated with 359-A--A-362."
FT /evidence="ECO:0000269|PubMed:26343456"
FT MUTAGEN 359..362
FT /note="KTAK->ATAA: Strongly reduced binding to
FT phosphatidylinositol 3-monophosphate (PI3P); when
FT associated with A-343."
FT /evidence="ECO:0000269|PubMed:26343456"
FT MUTAGEN 404
FT /note="K->A: Reduced binding to phosphatidylinositol 3-
FT monophosphate (PI3P); when associated with A-306."
FT /evidence="ECO:0000269|PubMed:26343456"
FT MUTAGEN 435..438
FT /note="FVTI->AVTA: In mLIR3; only binds one ATG8 protein
FT instead of two."
FT /evidence="ECO:0000269|PubMed:27791457"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:5XAD"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:5XAD"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:5XAD"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:5MS2"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:5MS2"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:5MS2"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:5MS2"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:5MS2"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:5MS2"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:5CQC"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:5MS2"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:5MS2"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:5MS7"
FT STRAND 99..108
FT /evidence="ECO:0007829|PDB:5MS2"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:5MS2"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:5MS2"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:5MS8"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:5HZY"
FT HELIX 137..152
FT /evidence="ECO:0007829|PDB:5MS2"
FT STRAND 157..170
FT /evidence="ECO:0007829|PDB:5MS2"
FT STRAND 176..185
FT /evidence="ECO:0007829|PDB:5MS2"
FT TURN 186..189
FT /evidence="ECO:0007829|PDB:5MS2"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:5MS2"
FT HELIX 206..211
FT /evidence="ECO:0007829|PDB:5MS2"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:5MS2"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:5IO3"
FT HELIX 221..232
FT /evidence="ECO:0007829|PDB:5MS2"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:5IO3"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:5MS7"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:5MS2"
FT HELIX 255..275
FT /evidence="ECO:0007829|PDB:5MS2"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:5MS2"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:5MS2"
FT HELIX 295..307
FT /evidence="ECO:0007829|PDB:5MS2"
FT HELIX 312..321
FT /evidence="ECO:0007829|PDB:5MS2"
FT HELIX 329..345
FT /evidence="ECO:0007829|PDB:5MS2"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:5IO3"
FT HELIX 359..379
FT /evidence="ECO:0007829|PDB:5MS2"
FT HELIX 384..397
FT /evidence="ECO:0007829|PDB:5MS2"
FT HELIX 400..412
FT /evidence="ECO:0007829|PDB:5MS2"
FT HELIX 418..422
FT /evidence="ECO:0007829|PDB:5MS2"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:5MS2"
SQ SEQUENCE 502 AA; 56242 MW; 698B442E58770745 CRC64;
MKGKLTGKDK LIVDEFEELG EQESDIDEFD LLEGDEKLPG DSELDKTTSI YPPETSWEVN
KGMNSSRLHK LYSLFFDKSS AFYLGDDVSV LEDKPLTGAY GFQSKKNDQQ IFLFRPDSDY
VAGYHVDAKS DAGWVNDKLD RRLSEISEFC SKATQPATFI LPFVEMPTDI TKGVQHQVLL
TISYDPKSKQ LTPTVYDSIG RDTYSESLSS YFKGKYRTTC DEILTQSIEK AIKSTDFTLG
KFTRAAYNHQ NRLTEGNCGS YTFRTIKEVI SSSAQGTEVK IPGSGYITSN SYLTSQHVQD
IESCIKYRNL GVVDIESALT EGKTLPVQLS EFIVALEDYG KLRSQQSEKS MLNFIGYSKT
AKLTAVELLI GILNDIKGKN EISESQYDKL VKEVDCLMDS SLGKLVQFHL KNLGAESLQK
LVLPCVKFDD TIDDFVTIEK DELFDVPDIT GEELASKKGI EQGALDKEAL LKQKQIKTDL
LDLREEDKTG LKKPLHGGIK VK
