PRKN_MOUSE
ID PRKN_MOUSE Reviewed; 464 AA.
AC Q9WVS6; Q2KHJ9; Q9ES22; Q9ES23;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=E3 ubiquitin-protein ligase parkin {ECO:0000305};
DE EC=2.3.2.31 {ECO:0000250|UniProtKB:O60260};
DE AltName: Full=Parkin RBR E3 ubiquitin-protein ligase {ECO:0000250|UniProtKB:O60260};
GN Name=Prkn {ECO:0000250|UniProtKB:O60260};
GN Synonyms=Park2 {ECO:0000312|MGI:MGI:1355296};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Skeletal muscle;
RX PubMed=10818204; DOI=10.1007/s003350010080;
RA Kitada T., Asakawa S., Minoshima S., Mizuno Y., Shimizu N.;
RT "Molecular cloning, gene expression, and identification of a splicing
RT variant of the mouse parkin gene.";
RL Mamm. Genome 11:417-421(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=BALB/cJ; TISSUE=Kidney;
RX PubMed=11122330; DOI=10.1111/j.1460-9568.2000.01314.x;
RA Stichel C.C., Augustin M., Kuehn K., Zhu X.-R., Engels P., Ullmer C.,
RA Luebbert H.;
RT "Parkin expression in the adult mouse brain.";
RL Eur. J. Neurosci. 12:4181-4194(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11675120; DOI=10.1016/s0165-3806(01)00234-6;
RA Huynh D.P., Dy M., Nguyen D., Kiehl T.-R., Pulst S.M.;
RT "Differential expression and tissue distribution of parkin isoforms during
RT mouse development.";
RL Brain Res. Dev. Brain Res. 130:173-181(2001).
RN [5]
RP FUNCTION IN UBIQUITINATION, AND S-NITROSYLATION.
RX PubMed=15105460; DOI=10.1126/science.1093891;
RA Chung K.K.K., Thomas B., Li X., Pletnikova O., Troncoso J.C., Marsh L.,
RA Dawson V.L., Dawson T.M.;
RT "S-nitrosylation of parkin regulates ubiquitination and compromises
RT parkin's protective function.";
RL Science 304:1328-1331(2004).
RN [6]
RP FUNCTION IN APOPTOSIS, AND DISRUPTION PHENOTYPE.
RX PubMed=19801972; DOI=10.1038/ncb1981;
RA da Costa C.A., Sunyach C., Giaime E., West A., Corti O., Brice A., Safe S.,
RA Abou-Sleiman P.M., Wood N.W., Takahashi H., Goldberg M.S., Shen J.,
RA Checler F.;
RT "Transcriptional repression of p53 by parkin and impairment by mutations
RT associated with autosomal recessive juvenile Parkinson's disease.";
RL Nat. Cell Biol. 11:1370-1375(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-80, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, AND INTERACTION WITH AMBRA1.
RX PubMed=21753002; DOI=10.1523/jneurosci.1917-11.2011;
RA Van Humbeeck C., Cornelissen T., Hofkens H., Mandemakers W., Gevaert K.,
RA De Strooper B., Vandenberghe W.;
RT "Parkin interacts with Ambra1 to induce mitophagy.";
RL J. Neurosci. 31:10249-10261(2011).
RN [9]
RP FUNCTION, INTERACTION WITH CHPF, AND DISRUPTION PHENOTYPE.
RX PubMed=22082830; DOI=10.1093/hmg/ddr530;
RA Kuroda Y., Sako W., Goto S., Sawada T., Uchida D., Izumi Y., Takahashi T.,
RA Kagawa N., Matsumoto M., Matsumoto M., Takahashi R., Kaji R., Mitsui T.;
RT "Parkin interacts with Klokin1 for mitochondrial import and maintenance of
RT membrane potential.";
RL Hum. Mol. Genet. 21:991-1003(2012).
RN [10]
RP FUNCTION.
RX PubMed=24192653; DOI=10.1161/circresaha.114.302734;
RA Bhandari P., Song M., Chen Y., Burelle Y., Dorn G.W. II;
RT "Mitochondrial contagion induced by Parkin deficiency in Drosophila hearts
RT and its containment by suppressing mitofusin.";
RL Circ. Res. 114:257-265(2014).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24898855; DOI=10.7554/elife.01958;
RA Yun J., Puri R., Yang H., Lizzio M.A., Wu C., Sheng Z.H., Guo M.;
RT "MUL1 acts in parallel to the PINK1/parkin pathway in regulating mitofusin
RT and compensates for loss of PINK1/parkin.";
RL Elife 3:E01958-E01958(2014).
RN [12]
RP FUNCTION.
RX PubMed=25474007; DOI=10.1371/journal.pgen.1004861;
RA Shiba-Fukushima K., Arano T., Matsumoto G., Inoshita T., Yoshida S.,
RA Ishihama Y., Ryu K.Y., Nukina N., Hattori N., Imai Y.;
RT "Phosphorylation of mitochondrial polyubiquitin by PINK1 promotes Parkin
RT mitochondrial tethering.";
RL PLoS Genet. 10:e1004861-e1004861(2014).
RN [13]
RP FUNCTION.
RX PubMed=29311685; DOI=10.1038/s41467-017-02593-y;
RA Wang C., Kang X., Zhou L., Chai Z., Wu Q., Huang R., Xu H., Hu M., Sun X.,
RA Sun S., Li J., Jiao R., Zuo P., Zheng L., Yue Z., Zhou Z.;
RT "Synaptotagmin-11 is a critical mediator of parkin-linked neurotoxicity and
RT Parkinson's disease-like pathology.";
RL Nat. Commun. 9:81-81(2018).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=32047033; DOI=10.1073/pnas.1909814117;
RA Ham S.J., Lee D., Yoo H., Jun K., Shin H., Chung J.;
RT "Decision between mitophagy and apoptosis by Parkin via VDAC1
RT ubiquitination.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:4281-4291(2020).
RN [15]
RP STRUCTURE BY NMR OF 1-76.
RX PubMed=12652124; DOI=10.1023/a:1022254432039;
RA Tashiro M., Okubo S., Shimotakahara S., Hatanaka H., Yasuda H.,
RA Kainosho M., Yokoyama S., Shindo H.;
RT "NMR structure of ubiquitin-like domain in PARKIN: gene product of familial
RT Parkinson's disease.";
RL J. Biomol. NMR 25:153-156(2003).
CC -!- FUNCTION: Functions within a multiprotein E3 ubiquitin ligase complex,
CC catalyzing the covalent attachment of ubiquitin moieties onto substrate
CC proteins (PubMed:32047033, PubMed:29311685). Substrates include SYT11
CC and VDAC1 (PubMed:32047033, PubMed:29311685). Other substrates are
CC BCL2, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, SNCAIP, SEPTIN5,
CC TOMM20, USP30, ZNF746, MIRO1 and AIMP2 (By similarity). Mediates
CC monoubiquitination as well as 'Lys-6', 'Lys-11', 'Lys-48'-linked and
CC 'Lys-63'-linked polyubiquitination of substrates depending on the
CC context (PubMed:32047033, PubMed:25474007). Participates in the removal
CC and/or detoxification of abnormally folded or damaged protein by
CC mediating 'Lys-63'-linked polyubiquitination of misfolded proteins such
CC as PARK7: 'Lys-63'-linked polyubiquitinated misfolded proteins are then
CC recognized by HDAC6, leading to their recruitment to aggresomes,
CC followed by degradation (By similarity). Mediates 'Lys-63'-linked
CC polyubiquitination of a 22 kDa O-linked glycosylated isoform of SNCAIP,
CC possibly playing a role in Lewy-body formation (By similarity).
CC Mediates monoubiquitination of BCL2, thereby acting as a positive
CC regulator of autophagy (By similarity). Protects against mitochondrial
CC dysfunction during cellular stress, by acting downstream of PINK1 to
CC coordinate mitochondrial quality control mechanisms that remove and
CC replace dysfunctional mitochondrial components (PubMed:32047033,
CC PubMed:25474007, PubMed:22082830, PubMed:24898855). Depending on the
CC severity of mitochondrial damage and/or dysfunction, activity ranges
CC from preventing apoptosis and stimulating mitochondrial biogenesis to
CC regulating mitochondrial dynamics and eliminating severely damaged
CC mitochondria via mitophagy (PubMed:32047033, PubMed:22082830,
CC PubMed:24898855). Activation and recruitment onto the outer membrane of
CC damaged/dysfunctional mitochondria (OMM) requires PINK1-mediated
CC phosphorylation of both PRKN and ubiquitin (PubMed:25474007). After
CC mitochondrial damage, functions with PINK1 to mediate the decision
CC between mitophagy or preventing apoptosis by inducing either the
CC poly- or monoubiquitination of VDAC1, respectively; polyubiquitination
CC of VDAC1 promotes mitophagy, while monoubiquitination of VDAC1
CC decreases mitochondrial calcium influx which ultimately inhibits
CC apoptosis (PubMed:32047033). When cellular stress results in
CC irreversible mitochondrial damage, promotes the autophagic degradation
CC of dysfunctional depolarized mitochondria (mitophagy) by promoting the
CC ubiquitination of mitochondrial proteins such as TOMM20, RHOT1/MIRO1,
CC MFN1 and USP30 (PubMed:21753002). Preferentially assembles 'Lys-6'-,
CC 'Lys-11'- and 'Lys-63'-linked polyubiquitin chains, leading to
CC mitophagy (By similarity). The PINK1-PRKN pathway also promotes fission
CC of damaged mitochondria by PINK1-mediated phosphorylation which
CC promotes the PRKN-dependent degradation of mitochondrial proteins
CC involved in fission such as MFN2 (PubMed:24192653). This prevents the
CC refusion of unhealthy mitochondria with the mitochondrial network or
CC initiates mitochondrial fragmentation facilitating their later
CC engulfment by autophagosomes (By similarity). Regulates motility of
CC damaged mitochondria via the ubiquitination and subsequent degradation
CC of MIRO1 and MIRO2; in motor neurons, this likely inhibits
CC mitochondrial intracellular anterograde transport along the axons which
CC probably increases the chance of the mitochondria undergoing mitophagy
CC in the soma (By similarity). Involved in mitochondrial biogenesis via
CC the 'Lys-48'-linked polyubiquitination of transcriptional repressor
CC ZNF746/PARIS which leads to its subsequent proteasomal degradation and
CC allows activation of the transcription factor PPARGC1A (By similarity).
CC Limits the production of reactive oxygen species (ROS) (By similarity).
CC Regulates cyclin-E during neuronal apoptosis (By similarity). In
CC collaboration with CHPF isoform 2, may enhance cell viability and
CC protect cells from oxidative stress (PubMed:22082830). Independently of
CC its ubiquitin ligase activity, protects from apoptosis by the
CC transcriptional repression of p53/TP53 (PubMed:19801972). May protect
CC neurons against alpha synuclein toxicity, proteasomal dysfunction,
CC GPR37 accumulation, and kainate-induced excitotoxicity (By similarity).
CC May play a role in controlling neurotransmitter trafficking at the
CC presynaptic terminal and in calcium-dependent exocytosis. May represent
CC a tumor suppressor gene (By similarity). {ECO:0000250|UniProtKB:O60260,
CC ECO:0000269|PubMed:19801972, ECO:0000269|PubMed:21753002,
CC ECO:0000269|PubMed:22082830, ECO:0000269|PubMed:24192653,
CC ECO:0000269|PubMed:24898855, ECO:0000269|PubMed:25474007,
CC ECO:0000269|PubMed:29311685, ECO:0000269|PubMed:32047033}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000250|UniProtKB:O60260};
CC -!- ACTIVITY REGULATION: In the autoinhibited state the side chain of Phe-
CC 462 inserts into a hydrophobic groove in RING-0, occluding the
CC ubiquitin acceptor site Cys-430, whereas the REP repressor element
CC binds RING-1 and blocks its E2-binding site. Activation of PRKN
CC requires 2 steps: (1) phosphorylation at Ser-65 by PINK1 and (2)
CC binding to phosphorylated ubiquitin, leading to unlock repression of
CC the catalytic Cys-430 by the RING-0 region via an allosteric mechanism
CC and converting PRKN to its fully-active form. According to another
CC report, phosphorylation at Ser-65 by PINK1 is not essential for
CC activation and only binding to phosphorylated ubiquitin is essential to
CC unlock repression. {ECO:0000250|UniProtKB:O60260}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Forms an E3 ubiquitin ligase complex with UBE2L3 or UBE2L6.
CC Mediates 'Lys-63'-linked polyubiquitination by associating with UBE2V1.
CC Part of a SCF-like complex, consisting of PRKN, CUL1 and FBXW7.
CC Interacts with SNCAIP. Binds to the C2A and C2B domains of SYT11.
CC Interacts and regulates the turnover of SEPTIN5. Part of a complex,
CC including STUB1, HSP70 and GPR37. The amount of STUB1 in the complex
CC increases during ER stress. STUB1 promotes the dissociation of HSP70
CC from PRKN and GPR37, thus facilitating PRKN-mediated GPR37
CC ubiquitination. HSP70 transiently associates with unfolded GPR37 and
CC inhibits the E3 activity of PRKN, whereas, STUB1 enhances the E3
CC activity of PRKN through promotion of dissociation of HSP70 from PRKN-
CC GPR37 complexes. Interacts with PSMD4 and PACRG. Interacts with LRRK2.
CC Interacts with RANBP2. Interacts with SUMO1 but not SUMO2, which
CC promotes nuclear localization and autoubiquitination. Interacts (via
CC first RING-type domain) with AIMP2 (via N-terminus). Interacts with
CC PSMA7 and RNF41. Interacts with PINK1. Forms a complex with PINK1 and
CC PARK7. Interacts with CHPF, the interaction with isoform 2 may
CC facilitate PRKN transport into the mitochondria. Interacts with MFN2
CC (phosphorylated), promotes PRKN localization in dysfunctional
CC depolarized mitochondria. Interacts with FBXO7; this promotes
CC translocation to dysfunctional depolarized mitochondria. Interacts with
CC ZNF746. Interacts with heat shock protein 70 family members, including
CC HSPA1L, HSPA1A and HSPA8; interaction HSPA1L promotes translocation to
CC damaged mitochondria. Interacts with BAG4 and, to a lesser extent,
CC BAG5; interaction with BAG4 inhibits translocation to damaged
CC mitochondria. Forms a complex with PRKN and PARK7 (By similarity).
CC Interacts with AMBRA1 (PubMed:21753002). {ECO:0000250|UniProtKB:O60260,
CC ECO:0000269|PubMed:21753002}.
CC -!- INTERACTION:
CC Q9WVS6; Q6IQX7-2: Chpf; NbExp=3; IntAct=EBI-973635, EBI-9029659;
CC Q9WVS6; P47811: Mapk14; NbExp=3; IntAct=EBI-973635, EBI-298727;
CC Q9WVS6; Q9ERU9: Ranbp2; NbExp=2; IntAct=EBI-973635, EBI-643756;
CC Q9WVS6; P68510: Ywhah; NbExp=2; IntAct=EBI-973635, EBI-444641;
CC Q9WVS6; Q3U133: Znf746; NbExp=2; IntAct=EBI-973635, EBI-3862590;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:10818204,
CC ECO:0000305|PubMed:11122330}. Nucleus {ECO:0000250|UniProtKB:O60260}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:11122330}. Mitochondrion
CC {ECO:0000269|PubMed:32047033}. Mitochondrion outer membrane
CC {ECO:0000269|PubMed:11122330}. Cell projection, neuron projection
CC {ECO:0000269|PubMed:11675120}. Postsynaptic density
CC {ECO:0000269|PubMed:11122330}. Presynapse
CC {ECO:0000269|PubMed:11122330}. Note=Mainly localizes in the cytosol.
CC Co-localizes with SYT11 in neutrites. Co-localizes with SNCAIP in
CC brainstem Lewy bodies. Translocates to dysfunctional mitochondria that
CC have lost the mitochondrial membrane potential; recruitment to
CC mitochondria is PINK1-dependent. Mitochondrial localization also
CC gradually increases with cellular growth.
CC {ECO:0000250|UniProtKB:O60260}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9WVS6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9WVS6-2; Sequence=VSP_011714, VSP_011715;
CC Name=3;
CC IsoId=Q9WVS6-3; Sequence=VSP_011713, VSP_011716;
CC -!- TISSUE SPECIFICITY: Expressed in all subdivisions of the brain (at
CC protein level) (PubMed:11675120). Highly expressed in brainstem,
CC cranial nerve, pontine, cerebellar nuclei, indusium griseum, nuclei
CC reticularis, strata oriens and laccunosum moleculare of the hippocampal
CC CA2 region (PubMed:11122330). Low levels were found in the
CC telencephalon and diencephalon (PubMed:11122330). Expressed in heart,
CC liver, skeletal muscle, kidney and testis (PubMed:10818204).
CC {ECO:0000269|PubMed:10818204, ECO:0000269|PubMed:11122330,
CC ECO:0000269|PubMed:11675120}.
CC -!- DEVELOPMENTAL STAGE: In late 10 dpc weakly expressed in postmitotic
CC neurons in the mantle layer of the developing nervous system (at
CC protein level). Expression increased at 11-12 dpc (at protein level).
CC At 15-16 dpc, as more specialized neurons and nonneural cells are
CC formed, expression is more tissue specific (at protein level).
CC Expression was highest in the neurites, moderate levels were observed
CC in the migrating postmitotic neurons in the intermediate and neopallial
CC layers (at protein level). In the diencephalon and other CNS regions,
CC while the weakest level of expression was observed in the cell bodies
CC (at protein level). In nonneural tissues, high levels of expression
CC were found in the muscle walls of the intestine, the blood vessels and
CC the dermis (at protein level). {ECO:0000269|PubMed:11675120}.
CC -!- DOMAIN: The ubiquitin-like domain binds the PSMD4 subunit of 26S
CC proteasomes. {ECO:0000250|UniProtKB:O60260}.
CC -!- DOMAIN: The RING-type 1 zinc finger domain is required to repress
CC p53/TP53 transcription. {ECO:0000250|UniProtKB:O60260}.
CC -!- DOMAIN: Members of the RBR family are atypical E3 ligases. They
CC interact with the E2 conjugating enzyme UBE2L3 and function like HECT-
CC type E3 enzymes: they bind E2s via the first RING domain, but require
CC an obligate trans-thiolation step during the ubiquitin transfer,
CC requiring a conserved cysteine residue in the second RING domain.
CC {ECO:0000250|UniProtKB:O60260}.
CC -!- PTM: Auto-ubiquitinates in an E2-dependent manner leading to its own
CC degradation. Also polyubiquitinated by RNF41 for proteasomal
CC degradation. {ECO:0000250|UniProtKB:O60260}.
CC -!- PTM: S-nitrosylated. {ECO:0000269|PubMed:15105460}.
CC -!- PTM: Phosphorylated. Activation requires phosphorylation at Ser-65 by
CC PINK1 and binding to PINK1 phosphorylated ubiquitin. Phosphorylation at
CC Thr-174 by PINK1 and at Thr-216 is important for mitochondrial
CC localization. {ECO:0000250|UniProtKB:O60260}.
CC -!- DISRUPTION PHENOTYPE: In brain, increased protein levels of p53/TP53
CC and CHPF (PubMed:19801972, PubMed:22082830). Cortical neurons display a
CC slight increase in process fragmentation but no dendritic retraction
CC (PubMed:24898855). {ECO:0000269|PubMed:19801972,
CC ECO:0000269|PubMed:22082830, ECO:0000269|PubMed:24898855}.
CC -!- SIMILARITY: Belongs to the RBR family. Parkin subfamily. {ECO:0000305}.
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DR EMBL; AB019558; BAA82404.1; -; mRNA.
DR EMBL; AF250293; AAG13890.1; -; mRNA.
DR EMBL; AF250294; AAG13891.1; -; mRNA.
DR EMBL; AF250295; AAG13892.1; -; mRNA.
DR EMBL; BC113204; AAI13205.1; -; mRNA.
DR CCDS; CCDS79506.1; -. [Q9WVS6-1]
DR RefSeq; NP_001304655.1; NM_001317726.1.
DR RefSeq; NP_057903.1; NM_016694.4. [Q9WVS6-1]
DR PDB; 1MG8; NMR; -; A=1-76.
DR PDB; 2ZEQ; X-ray; 1.65 A; A=1-76.
DR PDB; 3B1L; X-ray; 1.85 A; X=1-76.
DR PDBsum; 1MG8; -.
DR PDBsum; 2ZEQ; -.
DR PDBsum; 3B1L; -.
DR AlphaFoldDB; Q9WVS6; -.
DR BMRB; Q9WVS6; -.
DR SMR; Q9WVS6; -.
DR BioGRID; 206136; 31.
DR DIP; DIP-37657N; -.
DR IntAct; Q9WVS6; 14.
DR MINT; Q9WVS6; -.
DR STRING; 10090.ENSMUSP00000140587; -.
DR iPTMnet; Q9WVS6; -.
DR PhosphoSitePlus; Q9WVS6; -.
DR PaxDb; Q9WVS6; -.
DR PRIDE; Q9WVS6; -.
DR ProteomicsDB; 291593; -. [Q9WVS6-1]
DR ProteomicsDB; 291594; -. [Q9WVS6-2]
DR ProteomicsDB; 291595; -. [Q9WVS6-3]
DR Antibodypedia; 4264; 811 antibodies from 51 providers.
DR DNASU; 50873; -.
DR Ensembl; ENSMUST00000191124; ENSMUSP00000140587; ENSMUSG00000023826. [Q9WVS6-1]
DR GeneID; 50873; -.
DR KEGG; mmu:50873; -.
DR UCSC; uc008akj.1; mouse. [Q9WVS6-3]
DR UCSC; uc008akk.1; mouse. [Q9WVS6-1]
DR CTD; 5071; -.
DR MGI; MGI:1355296; Prkn.
DR VEuPathDB; HostDB:ENSMUSG00000023826; -.
DR eggNOG; KOG0006; Eukaryota.
DR GeneTree; ENSGT00390000011034; -.
DR HOGENOM; CLU_050804_0_0_1; -.
DR InParanoid; Q9WVS6; -.
DR OMA; FAEFFFK; -.
DR OrthoDB; 1140368at2759; -.
DR PhylomeDB; Q9WVS6; -.
DR Reactome; R-MMU-5205685; PINK1-PRKN Mediated Mitophagy.
DR Reactome; R-MMU-5689877; Josephin domain DUBs.
DR Reactome; R-MMU-9646399; Aggrephagy.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 50873; 2 hits in 68 CRISPR screens.
DR ChiTaRS; Prkn; mouse.
DR EvolutionaryTrace; Q9WVS6; -.
DR PRO; PR:Q9WVS6; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9WVS6; protein.
DR Bgee; ENSMUSG00000023826; Expressed in hindlimb stylopod muscle and 108 other tissues.
DR ExpressionAtlas; Q9WVS6; baseline and differential.
DR Genevisible; Q9WVS6; MM.
DR GO; GO:0016235; C:aggresome; ISO:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0097708; C:intracellular vesicle; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0099073; C:mitochondrion-derived vesicle; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:1990452; C:Parkin-FBXW7-Cul1 ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0097602; F:cullin family protein binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:1990444; F:F-box domain binding; ISO:MGI.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0043274; F:phospholipase binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0015631; F:tubulin binding; ISO:MGI.
DR GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:MGI.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR GO; GO:0070842; P:aggresome assembly; ISO:MGI.
DR GO; GO:0000422; P:autophagy of mitochondrion; ISS:UniProtKB.
DR GO; GO:1904881; P:cellular response to hydrogen sulfide; ISO:MGI.
DR GO; GO:1905232; P:cellular response to L-glutamate; ISO:MGI.
DR GO; GO:0097237; P:cellular response to toxic substance; IDA:ParkinsonsUK-UCL.
DR GO; GO:0042417; P:dopamine metabolic process; IMP:MGI.
DR GO; GO:0051583; P:dopamine uptake involved in synaptic transmission; IMP:MGI.
DR GO; GO:0010994; P:free ubiquitin chain polymerization; ISO:MGI.
DR GO; GO:0007612; P:learning; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0000266; P:mitochondrial fission; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; ISO:MGI.
DR GO; GO:0051646; P:mitochondrion localization; ISO:MGI.
DR GO; GO:0007005; P:mitochondrion organization; ISS:ParkinsonsUK-UCL.
DR GO; GO:0099074; P:mitochondrion to lysosome transport; ISO:MGI.
DR GO; GO:0000423; P:mitophagy; IGI:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:MGI.
DR GO; GO:0044828; P:negative regulation by host of viral genome replication; ISO:MGI.
DR GO; GO:0032232; P:negative regulation of actin filament bundle assembly; ISO:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903382; P:negative regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; ISO:MGI.
DR GO; GO:1903542; P:negative regulation of exosomal secretion; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0033132; P:negative regulation of glucokinase activity; ISO:MGI.
DR GO; GO:0046676; P:negative regulation of insulin secretion; ISO:MGI.
DR GO; GO:1905366; P:negative regulation of intralumenal vesicle formation; ISO:MGI.
DR GO; GO:1902254; P:negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator; ISO:MGI.
DR GO; GO:0046329; P:negative regulation of JNK cascade; ISS:ParkinsonsUK-UCL.
DR GO; GO:0090258; P:negative regulation of mitochondrial fission; ISO:MGI.
DR GO; GO:0010637; P:negative regulation of mitochondrial fusion; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; ISO:MGI.
DR GO; GO:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:1902283; P:negative regulation of primary amine oxidase activity; ISO:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISO:MGI.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISO:MGI.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISO:MGI.
DR GO; GO:1904049; P:negative regulation of spontaneous neurotransmitter secretion; ISO:MGI.
DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0070050; P:neuron cellular homeostasis; ISS:ParkinsonsUK-UCL.
DR GO; GO:0042415; P:norepinephrine metabolic process; IMP:MGI.
DR GO; GO:0061734; P:parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; ISO:MGI.
DR GO; GO:1903599; P:positive regulation of autophagy of mitochondrion; ISO:MGI.
DR GO; GO:1903861; P:positive regulation of dendrite extension; IGI:ParkinsonsUK-UCL.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; ISS:ParkinsonsUK-UCL.
DR GO; GO:0010636; P:positive regulation of mitochondrial fusion; ISO:MGI.
DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; ISO:MGI.
DR GO; GO:1901526; P:positive regulation of mitophagy; ISO:MGI.
DR GO; GO:0098779; P:positive regulation of mitophagy in response to mitochondrial depolarization; ISO:MGI.
DR GO; GO:0051582; P:positive regulation of neurotransmitter uptake; ISO:MGI.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; ISO:MGI.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:1902530; P:positive regulation of protein linear polyubiquitination; IMP:ParkinsonsUK-UCL.
DR GO; GO:1905477; P:positive regulation of protein localization to membrane; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; ISO:MGI.
DR GO; GO:0010498; P:proteasomal protein catabolic process; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:ParkinsonsUK-UCL.
DR GO; GO:0030163; P:protein catabolic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0031648; P:protein destabilization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0085020; P:protein K6-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0070585; P:protein localization to mitochondrion; IMP:ParkinsonsUK-UCL.
DR GO; GO:0019538; P:protein metabolic process; IMP:MGI.
DR GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:ParkinsonsUK-UCL.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
DR GO; GO:1900407; P:regulation of cellular response to oxidative stress; ISS:ParkinsonsUK-UCL.
DR GO; GO:0042053; P:regulation of dopamine metabolic process; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IGI:ParkinsonsUK-UCL.
DR GO; GO:0010821; P:regulation of mitochondrion organization; ISS:ParkinsonsUK-UCL.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IMP:MGI.
DR GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
DR GO; GO:0031396; P:regulation of protein ubiquitination; ISO:MGI.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISO:MGI.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:ParkinsonsUK-UCL.
DR GO; GO:0006979; P:response to oxidative stress; ISS:ParkinsonsUK-UCL.
DR GO; GO:0001964; P:startle response; IMP:MGI.
DR GO; GO:0001963; P:synaptic transmission, dopaminergic; IMP:MGI.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:ParkinsonsUK-UCL.
DR GO; GO:0055069; P:zinc ion homeostasis; ISS:ParkinsonsUK-UCL.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR003977; Parkin.
DR InterPro; IPR041565; Parkin_Znf-RING.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR041170; Znf-RING_14.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF17976; zf-RING_12; 1.
DR Pfam; PF17978; zf-RING_14; 1.
DR PIRSF; PIRSF037880; Parkin; 1.
DR PRINTS; PR01475; PARKIN.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Autophagy; Cell projection; Cytoplasm;
KW Endoplasmic reticulum; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; S-nitrosylation; Synapse; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..464
FT /note="E3 ubiquitin-protein ligase parkin"
FT /id="PRO_0000058577"
FT DOMAIN 1..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT ZN_FING 140..224
FT /note="RING-type 0; atypical"
FT ZN_FING 237..292
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 312..376
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 417..448
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 70..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..236
FT /note="Necessary for PINK1-dependent localization to
FT mitochondria"
FT /evidence="ECO:0000250|UniProtKB:O60260"
FT REGION 203..237
FT /note="SYT11 binding 1"
FT /evidence="ECO:0000250|UniProtKB:O60260"
FT REGION 233..464
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 256..292
FT /note="SYT11 binding 2"
FT /evidence="ECO:0000250|UniProtKB:O60260"
FT REGION 377..409
FT /note="REP"
FT /evidence="ECO:0000250|UniProtKB:Q9JK66"
FT ACT_SITE 430
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 367
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 376
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 417
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 445
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 448
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 456
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 460
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT MOD_RES 65
FT /note="Phosphoserine; by PINK1"
FT /evidence="ECO:0000250|UniProtKB:O60260"
FT MOD_RES 80
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 174
FT /note="Phosphothreonine; by PINK1"
FT /evidence="ECO:0000250|UniProtKB:O60260"
FT MOD_RES 216
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60260"
FT VAR_SEQ 244..261
FT /note="RSPVLVFQCNHRHVICLD -> SHLPLSSGASVWTRPHLH (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:11122330"
FT /id="VSP_011713"
FT VAR_SEQ 245..254
FT /note="SPVLVFQCNH -> FMRMSKHRTS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11122330"
FT /id="VSP_011714"
FT VAR_SEQ 255..464
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11122330"
FT /id="VSP_011715"
FT VAR_SEQ 262..464
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11122330"
FT /id="VSP_011716"
FT CONFLICT 137
FT /note="P -> PA (in Ref. 1 and 2; AAG13890)"
FT /evidence="ECO:0000305"
FT STRAND 1..11
FT /evidence="ECO:0007829|PDB:2ZEQ"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:2ZEQ"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:2ZEQ"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:2ZEQ"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:2ZEQ"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2ZEQ"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:2ZEQ"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:2ZEQ"
SQ SEQUENCE 464 AA; 51618 MW; 5574A285A9A1B080 CRC64;
MIVFVRFNSS YGFPVEVDSD TSILQLKEVV AKRQGVPADQ LRVIFAGKEL PNHLTVQNCD
LEQQSIVHIV QRPRRRSHET NASGGDEPQS TSEGSIWESR SLTRVDLSSH TLPVDSVGLA
VILDTDSKRD SEAARGPVKP TYNSFFIYCK GPCHKVQPGK LRVQCGTCKQ ATLTLAQGPS
CWDDVLIPNR MSGECQSPDC PGTRAEFFFK CGAHPTSDKD TSVALNLITS NRRSIPCIAC
TDVRSPVLVF QCNHRHVICL DCFHLYCVTR LNDRQFVHDA QLGYSLPCVA GCPNSLIKEL
HHFRILGEEQ YTRYQQYGAE ECVLQMGGVL CPRPGCGAGL LPEQGQRKVT CEGGNGLGCG
FVFCRDCKEA YHEGDCDSLL EPSGATSQAY RVDKRAAEQA RWEEASKETI KKTTKPCPRC
NVPIEKNGGC MHMKCPQPQC KLEWCWNCGC EWNRACMGDH WFDV
