JOKA2_SOLTU
ID JOKA2_SOLTU Reviewed; 862 AA.
AC M1BJF6;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Protein JOKA2 {ECO:0000303|PubMed:26765567};
DE AltName: Full=Protein NBR1 homolog {ECO:0000305};
GN Name=JOKA2 {ECO:0000303|PubMed:26765567};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44;
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2]
RP FUNCTION, INTERACTION WITH ATG8CL, AIM DOMAIN, AND MUTAGENESIS OF TRP-821
RP AND ILE-824.
RX PubMed=26765567; DOI=10.7554/elife.10856;
RA Dagdas Y.F., Belhaj K., Maqbool A., Chaparro-Garcia A., Pandey P.,
RA Petre B., Tabassum N., Cruz-Mireles N., Hughes R.K., Sklenar J., Win J.,
RA Menke F., Findlay K., Banfield M.J., Kamoun S., Bozkurt T.O.;
RT "An effector of the Irish potato famine pathogen antagonizes a host
RT autophagy cargo receptor.";
RL Elife 5:0-0(2016).
RN [3]
RP FUNCTION, INTERACTION WITH ATG8CL, SUBCELLULAR LOCATION, AND AIM DOMAIN.
RX PubMed=29932422; DOI=10.7554/elife.37476;
RA Dagdas Y.F., Pandey P., Tumtas Y., Sanguankiattichai N., Belhaj K.,
RA Duggan C., Leary A.Y., Segretin M.E., Contreras M.P., Savage Z.,
RA Khandare V.S., Kamoun S., Bozkurt T.O.;
RT "Host autophagy machinery is diverted to the pathogen interface to mediate
RT focal defense responses against the Irish potato famine pathogen.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Autophagic substrate that functions as host autophagy cargo
CC receptor (Probable). Requires ATG8 protein expression to be recognized
CC as an autophagic substrate (Probable). Activates ATG8CL-mediated
CC selective autophagy, and contributes to defense against the fungal
CC pathogen Phytophtora infestans (PubMed:26765567, PubMed:29932422).
CC {ECO:0000269|PubMed:26765567, ECO:0000269|PubMed:29932422,
CC ECO:0000305|PubMed:26765567, ECO:0000305|PubMed:29932422}.
CC -!- SUBUNIT: Interacts (via C-terminal AIM motif) with ATG8CL.
CC {ECO:0000269|PubMed:26765567, ECO:0000269|PubMed:29932422}.
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:29932422}.
CC Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:29932422}.
CC -!- DOMAIN: The ATG8 interacting motif (AIM) is required for the
CC interaction with ATG8CL (PubMed:26765567, PubMed:29932422). The AIM
CC motif is required for JOKA2 function as host autophagy cargo receptor
CC (PubMed:26765567, PubMed:29932422). {ECO:0000269|PubMed:26765567,
CC ECO:0000269|PubMed:29932422}.
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DR RefSeq; XP_006344472.1; XM_006344410.2.
DR RefSeq; XP_015162877.1; XM_015307391.1.
DR AlphaFoldDB; M1BJF6; -.
DR SMR; M1BJF6; -.
DR STRING; 4113.PGSC0003DMT400046670; -.
DR EnsemblPlants; PGSC0003DMT400046670; PGSC0003DMT400046670; PGSC0003DMG400018122.
DR GeneID; 102582603; -.
DR Gramene; PGSC0003DMT400046670; PGSC0003DMT400046670; PGSC0003DMG400018122.
DR KEGG; sot:102582603; -.
DR eggNOG; KOG4351; Eukaryota.
DR eggNOG; KOG4582; Eukaryota.
DR HOGENOM; CLU_017180_0_0_1; -.
DR InParanoid; M1BJF6; -.
DR OMA; RNHSEAM; -.
DR OrthoDB; 991378at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd14947; NBR1_like; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032350; N_BRCA1_central.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF16158; N_BRCA1_IG; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS51745; PB1; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW Autophagy; Cytoplasmic vesicle; Metal-binding; Plant defense;
KW Protein transport; Reference proteome; Transport; Vacuole; Zinc;
KW Zinc-finger.
FT CHAIN 1..862
FT /note="Protein JOKA2"
FT /id="PRO_0000447347"
FT DOMAIN 6..90
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DOMAIN 811..860
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT ZN_FING 442..492
FT /note="ZZ-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 92..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 817..824
FT /note="ATG8 interacting motif (AIM)"
FT /evidence="ECO:0000269|PubMed:21743474"
FT COMPBIAS 96..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 447
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 450
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 471
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 474
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MUTAGEN 821
FT /note="W->A: Loss of interaction with ATG8CL; when
FT associated with A-824."
FT /evidence="ECO:0000269|PubMed:26765567"
FT MUTAGEN 824
FT /note="I->A: Loss of interaction with ATG8CL; when
FT associated with A-821."
FT /evidence="ECO:0000269|PubMed:26765567"
SQ SEQUENCE 862 AA; 93977 MW; 21B6EAB982209C1A CRC64;
MAMESSIVIK VKYEETLRRF NACVINEKLD LDIGGLRDKI IQLFNFAHDA ELTLTYIDED
GDVVTLVDDE DLQDVMRQDL NPLRISARLN AGERSGRASA RSSGNSTPLR SPRVQPPFLN
LNSRVSDVLK YIPEPLRESV MKVCSDMTAS ASSSAPILAE LVDAMSEMGL SYYQNQASGS
QAVKEAGSCS GISKGNTKSA DGGMPNVKIG ESSPKKNRPL TALHGEPKPN ASNEAVDASV
KLVCKSETLE GDRTEDLSSS FKGSKAQTSL VNSLEKDKKF DVRSLDGRTI GYAYVRNSPI
PPEKTSDEQP SKGHPVAKPV DLGGSASSSK VKQCNWDSPN ADSSGSSINM PYDGFTPSGL
VHLNTVNVND SHNAGSSGSS MKMPYDGFRP AVRHLGPLIP VNACPFSGVP TVNNPIPPQN
FSFEVPLKRS HNHSDGTGTI FHKGVRCDGC GVHPITGPRF ISKVKENYDL CSICFAEMGN
DADYIRMDRP LTYPNPWSFK SLHDLHGRLR PRPPTVPQVI RGFGLKAGRP KLDSRFIQDV
NVLDGTIMAP LTRFTKIWRM KNNGNLVWPQ GTQLVWIGGD KLSDRFSVEL EITTAGLAVD
QELDVAVDFT APEHPGRYIS YWRLASASGQ KFGQRVWVLI QVDALLSVPK KGLVHEAFQG
LNLNLPPAGS GVSGPDIINV NSEPQNVLPE PKSSSTMELV DSVAEVNQNK EQEAKFPIND
SLLVGFGDKS SSPSASGSPI SYPVIDLTEK PSADSSMQPS AAVAMQAPLQ DARGNFEVEM
SLLQELEEMG FKQVDLNKEI LRKNEYDLEQ SVDDLCGVAE WDPILEELKE MGFCDKEMNK
KLLKKNNGSI KRVVMDLIAG EQ
