REF2P_DROSI
ID REF2P_DROSI Reviewed; 599 AA.
AC Q24629;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Protein ref(2)P;
DE AltName: Full=Refractory to sigma P;
GN Name=ref(2)P;
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IM2;
RX PubMed=8583891; DOI=10.1093/oxfordjournals.molbev.a025555;
RA Wayne M.L., Contamine D., Kreitman M.;
RT "Molecular population genetics of ref(2)P, a locus which confers viral
RT resistance in Drosophila.";
RL Mol. Biol. Evol. 13:191-199(1996).
CC -!- FUNCTION: Required for selective autophagy activation by ubiquitinated
CC proteins. Implicated in sigma rhabdovirus multiplication and necessary
CC for male fertility. Involved in activating transcription of Drs.
CC {ECO:0000250|UniProtKB:P14199}.
CC -!- SUBUNIT: Interacts with aPKC and Traf6. {ECO:0000250|UniProtKB:P14199}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P14199}. Cytoplasm
CC {ECO:0000250|UniProtKB:P14199}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U23930; AAA98842.1; -; Genomic_DNA.
DR AlphaFoldDB; Q24629; -.
DR SMR; Q24629; -.
DR ChiTaRS; ref(2)P; fly.
DR GO; GO:0005776; C:autophagosome; IEA:EnsemblMetazoa.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0061912; P:selective autophagy; ISS:UniProtKB.
DR GO; GO:0030382; P:sperm mitochondrion organization; IEA:EnsemblMetazoa.
DR CDD; cd14320; UBA_SQSTM; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR033741; SQSTM_UBA.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF16577; UBA_5; 1.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS51745; PB1; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Repeat; Transcription;
KW Zinc; Zinc-finger.
FT CHAIN 1..599
FT /note="Protein ref(2)P"
FT /id="PRO_0000097238"
FT DOMAIN 3..88
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT REPEAT 386..393
FT /note="1"
FT REPEAT 399..406
FT /note="2"
FT REPEAT 407..413
FT /note="3"
FT DOMAIN 550..595
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT ZN_FING 122..173
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 192..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..413
FT /note="3 X 8 AA repeats of S-A-N-Q-S-X-X-P"
FT REGION 507..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
SQ SEQUENCE 599 AA; 65431 MW; 4FEE038C3C6970EB CRC64;
MPEKLLKITY QGAGPQKKIN AYLRMPSQNY TILRREIELY LFQERQLPKC DVRTFWIDAD
QDEIEIVNQN DYEIFLAKCE SNMHVQVAPL APIEEPKATK QEGSSANAEA PSVDDPSNFT
IHDSVQCDGC GLAPLIGFRY KCVQCSNFDL CQKCESAHKH PEHLMLRMPT NNGPGMVDAW
FTGPGLGRRC GRRSRGHCPF QEASQPAPAA EPARDSRRER RHARRHAGVL SQFVEMMTNL
PLNTTTATAP AEPQKPKAAE QTESPPQAEP TVTAEKATES EAKPTEPMKV NTDQSVPTTE
DPVTTPRSTE PTTPVINLDN LSQIVPPEYM RAGIEILNNF SEMFSKMIDT TDVGDSGIFA
PSTTSSAENK KPEEQSQSSG QSAASSASQS AVPSAAPSAN QSNVPSANQS ATPSISGSIS
DAQLETEPLN PKPLETTTET EQDRRRSDSL DPEWQLIDNA YSANNSNLIN LDTTNPTAAP
QQPVRDFGQL GELLRQHMNE EARVEQASAN TQTAQVDTVS TSTSTTSVTT NSVGTSPAAP
DDKRTVPVYH TDERINQSIH AMMAMGFSNE GAWLTQLLES VQGNIPAALD VMHVSQTRN
