PINK1_CAEEL
ID PINK1_CAEEL Reviewed; 641 AA.
AC Q09298;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Serine/threonine-protein kinase pink-1, mitochondrial;
DE EC=2.7.11.1;
DE AltName: Full=PTEN-induced kinase 1 homolog;
DE Flags: Precursor;
GN Name=pink-1; ORFNames=EEED8.9;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25896323; DOI=10.1038/nature14300;
RA Palikaras K., Lionaki E., Tavernarakis N.;
RT "Coordination of mitophagy and mitochondrial biogenesis during ageing in C.
RT elegans.";
RL Nature 521:525-528(2015).
CC -!- FUNCTION: Protects against mitochondrial dysfunction during cellular
CC stress, potentially by phosphorylating mitochondrial proteins (By
CC similarity). Plays a role in mitophagy (PubMed:25896323).
CC {ECO:0000250|UniProtKB:Q9BXM7, ECO:0000269|PubMed:25896323}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in daf-2, isp-1, or clk-1
CC mutant backgrounds suppresses their increased lifespan phenotype.
CC {ECO:0000269|PubMed:25896323}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; FO081042; CCD68737.1; -; Genomic_DNA.
DR PIR; T15919; T15919.
DR RefSeq; NP_495017.1; NM_062616.4.
DR AlphaFoldDB; Q09298; -.
DR SMR; Q09298; -.
DR STRING; 6239.EEED8.9; -.
DR EPD; Q09298; -.
DR PaxDb; Q09298; -.
DR PRIDE; Q09298; -.
DR EnsemblMetazoa; EEED8.9.1; EEED8.9.1; WBGene00017137.
DR GeneID; 173918; -.
DR KEGG; cel:CELE_EEED8.9; -.
DR UCSC; EEED8.9; c. elegans.
DR CTD; 173918; -.
DR WormBase; EEED8.9; CE28904; WBGene00017137; pink-1.
DR eggNOG; KOG4158; Eukaryota.
DR GeneTree; ENSGT00390000001206; -.
DR HOGENOM; CLU_028921_0_0_1; -.
DR InParanoid; Q09298; -.
DR OMA; RAPEIRC; -.
DR OrthoDB; 335630at2759; -.
DR PhylomeDB; Q09298; -.
DR Reactome; R-CEL-5205685; PINK1-PRKN Mediated Mitophagy.
DR PRO; PR:Q09298; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00017137; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:WormBase.
DR GO; GO:0048846; P:axon extension involved in axon guidance; IMP:WormBase.
DR GO; GO:0007411; P:axon guidance; IMP:WormBase.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:WormBase.
DR GO; GO:0007005; P:mitochondrion organization; IMP:WormBase.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IBA:GO_Central.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:WormBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IGI:WormBase.
DR CDD; cd14018; STKc_PINK1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR040110; PINK1_STKc.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Transit peptide.
FT TRANSIT 1..74
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 75..641
FT /note="Serine/threonine-protein kinase pink-1,
FT mitochondrial"
FT /id="PRO_0000086839"
FT DOMAIN 137..483
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 338
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 143..151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 641 AA; 73054 MW; FA2DE9B72CD44657 CRC64;
MSMKRFGKAA YRIANELVAK GGRLPIFQRF LPRIFPATYN LGVHVVLKKA PFPRQNALRI
ARLVTRHGRV FRPFSSVIIE RHRFQNQNDW RRKFQPIRKE LPRNVDLVER IRQIFGNSLR
YNEDLKSTEW PNRIDSYEFG EFLGQGCNAA VYSARLANSD AESSGNTHYG AGFNEVTNIL
AEIPPVSKVA QKKFPLAIKL MFNFEHDRDG DAHLLKSMGN ELAPYPNAAK LLNGQMGTFR
PLPAKHPNVV RIQTAFIDSL KVLPDAIERY PDALHTARWY ESIASEPKTM YVVMRRYRQT
LHEYVWTRHR NYWTGRVIIA QLLEACTYLH KHKVAQRDMK SDNILLEYDF DDEIPQLVVA
DFGCALACDN WQVDYESDEV SLGGNAKTKA PEIATAVPGK NVKVNFEMAD TWAAGGLSYE
VLTRSNPFYK LLDTATYQES ELPALPSRVN FVARDVIFDL LKRDPNERVK PNIAANALNL
SLFRMGEDVK QMMEKCGISQ MTTLLAGSSK VLSQKINSRL DKVMNLITAE TIMANLAPHL
ISRAERQLRA TFLSRMNRED IWRSLQYFFP AGVQLDTPAT SSDCLETISS LMSSFSNDSE
NYEKQQKPAK NGYNNVPLLL RNVIRTDADG INGIVHRVRS K
