PRKN_RAT
ID PRKN_RAT Reviewed; 465 AA.
AC Q9JK66; Q8K5C3; Q8K5C4; Q8K5C5; Q8K5C6; Q8VHY6; Q9JLL1; Q9JM64;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=E3 ubiquitin-protein ligase parkin {ECO:0000305};
DE EC=2.3.2.31 {ECO:0000269|PubMed:23661642};
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|RGD:61797};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6).
RC STRAIN=Sprague-Dawley;
RX PubMed=10686358; DOI=10.1016/s0169-328x(99)00286-7;
RA D'Agata V., Zhao W., Cavallaro S.;
RT "Cloning and distribution of the rat parkin mRNA.";
RL Brain Res. Mol. Brain Res. 75:345-349(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Hypothalamus;
RX PubMed=10737637; DOI=10.1046/j.1471-4159.2000.0741773.x;
RA Gu W.-J., Abbas N., Lagunes M.Z., Parent A., Pradier L., Bohme G.A.,
RA Agid Y., Hirsch E.C., Raisman-Vozari R., Brice A.;
RT "Cloning of rat parkin cDNA and distribution of parkin in rat brain.";
RL J. Neurochem. 74:1773-1776(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley;
RA Hattori N., Wang M., Mizuno Y.;
RT "The expression of parkin mRNA in developing, adult and ageing rat CNS.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Soda M., Imai Y., Takahashi R.;
RT "Molecular cloning of rat Parkin gene.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=12925569; DOI=10.1093/hmg/ddg269;
RA Huynh D.P., Scoles D.R., Nguyen D., Pulst S.M.;
RT "The autosomal recessive juvenile Parkinson disease gene product, parkin,
RT interacts with and ubiquitinates synaptotagmin XI.";
RL Hum. Mol. Genet. 12:2587-2597(2003).
RN [6]
RP INTERACTION WITH SUMO1.
RX PubMed=16955485; DOI=10.1002/jnr.21041;
RA Um J.W., Chung K.C.;
RT "Functional modulation of parkin through physical interaction with SUMO-
RT 1.";
RL J. Neurosci. Res. 84:1543-1554(2006).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (6.5 ANGSTROMS), X-RAY CRYSTALLOGRAPHY (2.8
RP ANGSTROMS) OF 141-465, RING-TYPE ZINC-FINGERS, CATALYTIC ACTIVITY, ACTIVE
RP SITE, AUTOUBIQUITINATION, ACTIVITY REGULATION, AND MUTAGENESIS OF TRP-403.
RX PubMed=23661642; DOI=10.1126/science.1237908;
RA Trempe J.F., Sauve V., Grenier K., Seirafi M., Tang M.Y., Menade M.,
RA Al-Abdul-Wahid S., Krett J., Wong K., Kozlov G., Nagar B., Fon E.A.,
RA Gehring K.;
RT "Structure of parkin reveals mechanisms for ubiquitin ligase activation.";
RL Science 340:1451-1455(2013).
CC -!- FUNCTION: Functions within a multiprotein E3 ubiquitin ligase complex,
CC catalyzing the covalent attachment of ubiquitin moieties onto substrate
CC proteins. Substrates include SYT11 and VDAC1. Other substrates are
CC BCL2, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, SNCAIP, SEPTIN5,
CC TOMM20, USP30, ZNF746, MIRO1 and AIMP2. Mediates monoubiquitination as
CC well as 'Lys-6', 'Lys-11', 'Lys-48'-linked and 'Lys-63'-linked
CC polyubiquitination of substrates depending on the context. Participates
CC in the removal and/or detoxification of abnormally folded or damaged
CC protein by mediating 'Lys-63'-linked polyubiquitination of misfolded
CC proteins such as PARK7: 'Lys-63'-linked polyubiquitinated misfolded
CC proteins are then recognized by HDAC6, leading to their recruitment to
CC aggresomes, followed by degradation. 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. Mediates
CC monoubiquitination of BCL2, thereby acting as a positive regulator of
CC autophagy. Protects against mitochondrial dysfunction during cellular
CC stress, by acting downstream of PINK1 to coordinate mitochondrial
CC quality control mechanisms that remove and replace dysfunctional
CC mitochondrial components. Depending on the severity of mitochondrial
CC damage and/or dysfunction, activity ranges from preventing apoptosis
CC and stimulating mitochondrial biogenesis to regulating mitochondrial
CC dynamics and eliminating severely damaged mitochondria via mitophagy.
CC Activation and recruitment onto the outer membrane of
CC damaged/dysfunctional mitochondria (OMM) requires PINK1-mediated
CC phosphorylation of both PRKN and ubiquitin. After mitochondrial damage,
CC functions with PINK1 to mediate the decision between mitophagy or
CC preventing apoptosis by inducing either the poly- or monoubiquitination
CC of VDAC1, respectively; polyubiquitination of VDAC1 promotes mitophagy,
CC while monoubiquitination of VDAC1 decreases mitochondrial calcium
CC influx which ultimately inhibits apoptosis. When cellular stress
CC results in irreversible mitochondrial damage, promotes the autophagic
CC degradation of dysfunctional depolarized mitochondria (mitophagy) by
CC promoting the ubiquitination of mitochondrial proteins such as TOMM20,
CC RHOT1/MIRO1, MFN1 and USP30. Preferentially assembles 'Lys-6'-, 'Lys-
CC 11'- and 'Lys-63'-linked polyubiquitin chains, leading to mitophagy.
CC The PINK1-PRKN pathway also promotes fission of damaged mitochondria by
CC PINK1-mediated phosphorylation which promotes the PRKN-dependent
CC degradation of mitochondrial proteins involved in fission such as MFN2.
CC This prevents the refusion of unhealthy mitochondria with the
CC mitochondrial network or initiates mitochondrial fragmentation
CC facilitating their later engulfment by autophagosomes. Regulates
CC motility of damaged mitochondria via the ubiquitination and subsequent
CC degradation 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. Involved in mitochondrial biogenesis via the 'Lys-48'-
CC linked polyubiquitination of transcriptional repressor ZNF746/PARIS
CC which leads to its subsequent proteasomal degradation and allows
CC activation of the transcription factor PPARGC1A. Limits the production
CC of reactive oxygen species (ROS). Regulates cyclin-E during neuronal
CC apoptosis. In collaboration with CHPF isoform 2, may enhance cell
CC viability and protect cells from oxidative stress. Independently of its
CC ubiquitin ligase activity, protects from apoptosis by the
CC transcriptional repression of p53/TP53. May protect neurons against
CC alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation,
CC and kainate-induced excitotoxicity. May play a role in controlling
CC neurotransmitter trafficking at the presynaptic terminal and in
CC calcium-dependent exocytosis. May represent a tumor suppressor gene.
CC {ECO:0000250|UniProtKB:O60260}.
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:0000269|PubMed:23661642};
CC -!- ACTIVITY REGULATION: In the autoinhibited state the side chain of Phe-
CC 463 inserts into a hydrophobic groove in RING-0, occluding the
CC ubiquitin acceptor site Cys-431, 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-431 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 ECO:0000269|PubMed:23661642}.
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. Interacts with
CC AMBRA1 (By similarity). {ECO:0000250|UniProtKB:O60260,
CC ECO:0000250|UniProtKB:Q9WVS6}.
CC -!- INTERACTION:
CC Q9JK66; D4A054: Ranbp2; NbExp=2; IntAct=EBI-973793, EBI-973937;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12925569}.
CC Nucleus {ECO:0000250|UniProtKB:O60260}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:O60260}. Mitochondrion
CC {ECO:0000250|UniProtKB:O60260}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q9WVS6}. Cell projection, neuron projection
CC {ECO:0000269|PubMed:12925569}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q9WVS6}. Presynapse
CC {ECO:0000250|UniProtKB:Q9WVS6}. 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=6;
CC Name=1;
CC IsoId=Q9JK66-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JK66-2; Sequence=VSP_011722, VSP_011723;
CC Name=3;
CC IsoId=Q9JK66-3; Sequence=VSP_011717;
CC Name=4;
CC IsoId=Q9JK66-4; Sequence=VSP_011718;
CC Name=5;
CC IsoId=Q9JK66-5; Sequence=VSP_011719;
CC Name=6;
CC IsoId=Q9JK66-6; Sequence=VSP_011717, VSP_011720, VSP_011721;
CC -!- TISSUE SPECIFICITY: Largely confined to neuronal elements, including
CC fibers and neuropil. Highly expressed at the forebrain level, in
CC pyramidal cells of layer V, in various cortical regions and cerebellum.
CC Expressed in the nucleus of diagonal band of Broca, nucleus basalis,
CC bed nucleus of the stria terminalis, and olfactory tubercle. Moderate
CC expression is seen in most neurons of the subthalamic nucleus, heart,
CC skeletal muscle and testis. Moderate expression was found in frontal
CC cortex, parietal cortex, cerebellum, heart, skeletal muscle and testis.
CC {ECO:0000269|PubMed:10737637}.
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 (PubMed:23661642). Also polyubiquitinated by RNF41 for
CC proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:O60260,
CC ECO:0000269|PubMed:23661642}.
CC -!- PTM: S-nitrosylated. {ECO:0000250|UniProtKB:O60260}.
CC -!- PTM: Phosphorylated. Activation requires phosphorylation at Ser-65 by
CC PINK1 and binding to PINK1 phosphorylated ubiquitin. Phosphorylation at
CC Thr-175 by PINK1 and at Thr-217 is important for mitochondrial
CC localization. {ECO:0000250|UniProtKB:O60260}.
CC -!- SIMILARITY: Belongs to the RBR family. Parkin subfamily. {ECO:0000305}.
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DR EMBL; AF343574; AAL73348.1; -; mRNA.
DR EMBL; AF381277; AAM21452.1; -; mRNA.
DR EMBL; AF381278; AAM21453.1; -; mRNA.
DR EMBL; AF381279; AAM21454.1; -; mRNA.
DR EMBL; AF381280; AAM21455.1; -; mRNA.
DR EMBL; AF381281; AAM21456.1; -; mRNA.
DR EMBL; AF168004; AAF34874.1; -; mRNA.
DR EMBL; AF210434; AAG37013.1; -; mRNA.
DR EMBL; AF257234; AAF68666.1; -; mRNA.
DR EMBL; AB039878; BAA92431.1; -; mRNA.
DR RefSeq; NP_064478.1; NM_020093.1.
DR PDB; 2KNB; NMR; -; A=1-76.
DR PDB; 4K7D; X-ray; 2.80 A; A/B/C=141-465.
DR PDB; 4K95; X-ray; 6.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-465.
DR PDB; 4ZYN; X-ray; 2.54 A; A/B=1-465.
DR PDBsum; 2KNB; -.
DR PDBsum; 4K7D; -.
DR PDBsum; 4K95; -.
DR PDBsum; 4ZYN; -.
DR AlphaFoldDB; Q9JK66; -.
DR BMRB; Q9JK66; -.
DR SMR; Q9JK66; -.
DR BioGRID; 248590; 17.
DR DIP; DIP-37656N; -.
DR IntAct; Q9JK66; 1.
DR MINT; Q9JK66; -.
DR STRING; 10116.ENSRNOP00000040511; -.
DR iPTMnet; Q9JK66; -.
DR PhosphoSitePlus; Q9JK66; -.
DR PaxDb; Q9JK66; -.
DR Ensembl; ENSRNOT00000096213; ENSRNOP00000077507; ENSRNOG00000055547. [Q9JK66-1]
DR Ensembl; ENSRNOT00000107769; ENSRNOP00000088932; ENSRNOG00000055547. [Q9JK66-3]
DR GeneID; 56816; -.
DR KEGG; rno:56816; -.
DR CTD; 5071; -.
DR RGD; 61797; Prkn.
DR eggNOG; KOG0006; Eukaryota.
DR GeneTree; ENSGT00390000011034; -.
DR InParanoid; Q9JK66; -.
DR OrthoDB; 1140368at2759; -.
DR PhylomeDB; Q9JK66; -.
DR Reactome; R-RNO-5205685; PINK1-PRKN Mediated Mitophagy.
DR Reactome; R-RNO-5689877; Josephin domain DUBs.
DR Reactome; R-RNO-9646399; Aggrephagy.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; Q9JK66; -.
DR PRO; PR:Q9JK66; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0016235; C:aggresome; ISS:ParkinsonsUK-UCL.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0097708; C:intracellular vesicle; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:1990452; C:Parkin-FBXW7-Cul1 ubiquitin ligase complex; ISS:ParkinsonsUK-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0098793; C:presynapse; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:ParkinsonsUK-UCL.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:ParkinsonsUK-UCL.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISS:ParkinsonsUK-UCL.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0008013; F:beta-catenin binding; ISO:RGD.
DR GO; GO:0051087; F:chaperone binding; ISO:RGD.
DR GO; GO:0097602; F:cullin family protein binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:1990444; F:F-box domain binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0031072; F:heat shock protein binding; ISO:RGD.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0019900; F:kinase binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043274; F:phospholipase binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:0015631; F:tubulin binding; ISO:RGD.
DR GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:RGD.
DR GO; GO:0008344; P:adult locomotory behavior; ISS:ParkinsonsUK-UCL.
DR GO; GO:0070842; P:aggresome assembly; ISS:ParkinsonsUK-UCL.
DR GO; GO:0000422; P:autophagy of mitochondrion; IDA:ParkinsonsUK-UCL.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:1904881; P:cellular response to hydrogen sulfide; IDA:RGD.
DR GO; GO:1905232; P:cellular response to L-glutamate; IDA:RGD.
DR GO; GO:1904845; P:cellular response to L-glutamine; IEP:RGD.
DR GO; GO:0071287; P:cellular response to manganese ion; IEP:RGD.
DR GO; GO:0097237; P:cellular response to toxic substance; ISS:ParkinsonsUK-UCL.
DR GO; GO:0042417; P:dopamine metabolic process; ISO:RGD.
DR GO; GO:0051583; P:dopamine uptake involved in synaptic transmission; ISO:RGD.
DR GO; GO:0010994; P:free ubiquitin chain polymerization; ISO:RGD.
DR GO; GO:0007612; P:learning; ISO:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0000266; P:mitochondrial fission; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; IMP:RGD.
DR GO; GO:0051646; P:mitochondrion localization; IDA:ParkinsonsUK-UCL.
DR GO; GO:0007005; P:mitochondrion organization; ISS:ParkinsonsUK-UCL.
DR GO; GO:0099074; P:mitochondrion to lysosome transport; ISO:RGD.
DR GO; GO:0000423; P:mitophagy; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0044828; P:negative regulation by host of viral genome replication; ISO:RGD.
DR GO; GO:0032232; P:negative regulation of actin filament bundle assembly; ISO:RGD.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:RGD.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISS:ParkinsonsUK-UCL.
DR GO; GO:1903382; P:negative regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; IMP:RGD.
DR GO; GO:1903542; P:negative regulation of exosomal secretion; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0033132; P:negative regulation of glucokinase activity; ISS:ParkinsonsUK-UCL.
DR GO; GO:0046676; P:negative regulation of insulin secretion; ISS:ParkinsonsUK-UCL.
DR GO; GO:1905366; P:negative regulation of intralumenal vesicle formation; ISO:RGD.
DR GO; GO:1902254; P:negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator; ISO:RGD.
DR GO; GO:0046329; P:negative regulation of JNK cascade; ISS:ParkinsonsUK-UCL.
DR GO; GO:0090258; P:negative regulation of mitochondrial fission; IMP:RGD.
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:RGD.
DR GO; GO:1901215; P:negative regulation of neuron death; IGI:MGI.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IGI:ParkinsonsUK-UCL.
DR GO; GO:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; ISS:ParkinsonsUK-UCL.
DR GO; GO:1902283; P:negative regulation of primary amine oxidase activity; ISO:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:ParkinsonsUK-UCL.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IMP:RGD.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISS:ParkinsonsUK-UCL.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISS:ParkinsonsUK-UCL.
DR GO; GO:1904049; P:negative regulation of spontaneous neurotransmitter secretion; ISO:RGD.
DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IMP:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0070050; P:neuron cellular homeostasis; ISS:ParkinsonsUK-UCL.
DR GO; GO:0042415; P:norepinephrine metabolic process; ISO:RGD.
DR GO; GO:0061734; P:parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IMP:RGD.
DR GO; GO:1903599; P:positive regulation of autophagy of mitochondrion; ISO:RGD.
DR GO; GO:1903861; P:positive regulation of dendrite extension; ISO:RGD.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:ParkinsonsUK-UCL.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:RGD.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; ISS:ParkinsonsUK-UCL.
DR GO; GO:0010636; P:positive regulation of mitochondrial fusion; ISS:ParkinsonsUK-UCL.
DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IMP:RGD.
DR GO; GO:1901526; P:positive regulation of mitophagy; IMP:RGD.
DR GO; GO:0098779; P:positive regulation of mitophagy in response to mitochondrial depolarization; ISO:RGD.
DR GO; GO:0051582; P:positive regulation of neurotransmitter uptake; ISO:RGD.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; ISO:RGD.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:RGD.
DR GO; GO:1902530; P:positive regulation of protein linear polyubiquitination; ISO:RGD.
DR GO; GO:1905477; P:positive regulation of protein localization to membrane; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:ParkinsonsUK-UCL.
DR GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; ISS:ParkinsonsUK-UCL.
DR GO; GO:0010498; P:proteasomal protein catabolic process; ISO:RGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:ParkinsonsUK-UCL.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:ParkinsonsUK-UCL.
DR GO; GO:0031648; P:protein destabilization; ISS:UniProtKB.
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:ParkinsonsUK-UCL.
DR GO; GO:0070585; P:protein localization to mitochondrion; IDA:ParkinsonsUK-UCL.
DR GO; GO:0019538; P:protein metabolic process; ISO:RGD.
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:RGD.
DR GO; GO:0016567; P:protein ubiquitination; IDA:ParkinsonsUK-UCL.
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:RGD.
DR GO; GO:0010468; P:regulation of gene expression; IMP:RGD.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISO:RGD.
DR GO; GO:0010821; P:regulation of mitochondrion organization; ISS:ParkinsonsUK-UCL.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; ISO:RGD.
DR GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
DR GO; GO:0031396; P:regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0051412; P:response to corticosterone; IEP:RGD.
DR GO; GO:1904643; P:response to curcumin; IEP:RGD.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEP:RGD.
DR GO; GO:0014850; P:response to muscle activity; IEP:RGD.
DR GO; GO:0006979; P:response to oxidative stress; ISS:ParkinsonsUK-UCL.
DR GO; GO:0006986; P:response to unfolded protein; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0001964; P:startle response; ISO:RGD.
DR GO; GO:0001963; P:synaptic transmission, dopaminergic; ISO:RGD.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; ISO:RGD.
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 DisProt; DP01850; -.
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; Synapse; Transcription; Transcription regulation; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..465
FT /note="E3 ubiquitin-protein ligase parkin"
FT /id="PRO_0000058578"
FT DOMAIN 1..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT ZN_FING 141..225
FT /note="RING-type 0; atypical"
FT ZN_FING 238..293
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 313..377
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 418..449
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 71..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..237
FT /note="Necessary for PINK1-dependent localization to
FT mitochondria"
FT /evidence="ECO:0000250|UniProtKB:O60260"
FT REGION 204..238
FT /note="SYT11 binding 1"
FT /evidence="ECO:0000250|UniProtKB:O60260"
FT REGION 234..465
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 257..293
FT /note="SYT11 binding 2"
FT /evidence="ECO:0000250|UniProtKB:O60260"
FT REGION 378..410
FT /note="REP"
FT /evidence="ECO:0000269|PubMed:23661642"
FT ACT_SITE 431
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221,
FT ECO:0000269|PubMed:23661642"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 368
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 421
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 457
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 461
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:0000250|UniProtKB:Q9WVS6"
FT MOD_RES 175
FT /note="Phosphothreonine; by PINK1"
FT /evidence="ECO:0000250|UniProtKB:O60260"
FT MOD_RES 217
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60260"
FT VAR_SEQ 1..191
FT /note="Missing (in isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10686358"
FT /id="VSP_011717"
FT VAR_SEQ 57
FT /note="Q -> QHPQDGFCHKSHLAVHNLSQQDVTQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10686358"
FT /id="VSP_011718"
FT VAR_SEQ 179..206
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:10686358"
FT /id="VSP_011719"
FT VAR_SEQ 390..394
FT /note="AYRVD -> EDVCT (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:10686358"
FT /id="VSP_011720"
FT VAR_SEQ 395..465
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:10686358"
FT /id="VSP_011721"
FT VAR_SEQ 429..446
FT /note="GGCMHMKCPQPQCKLEWC -> ERMHVQYTMCIPGAHGGY (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:10686358"
FT /id="VSP_011722"
FT VAR_SEQ 447..465
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10686358"
FT /id="VSP_011723"
FT MUTAGEN 403
FT /note="W->A: Increased autoubiquitination."
FT /evidence="ECO:0000269|PubMed:23661642"
FT CONFLICT 24
FT /note="F -> C (in Ref. 1; AAF34874)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="E -> A (in Ref. 3; BAA92431)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="K -> R (in Ref. 3; BAA92431)"
FT /evidence="ECO:0000305"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:4ZYN"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:4ZYN"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:4ZYN"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:4ZYN"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:4ZYN"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:4ZYN"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:4ZYN"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:4ZYN"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:4ZYN"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:4ZYN"
FT STRAND 156..166
FT /evidence="ECO:0007829|PDB:4ZYN"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:4ZYN"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:4K7D"
FT HELIX 183..187
FT /evidence="ECO:0007829|PDB:4ZYN"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:4K7D"
FT STRAND 205..215
FT /evidence="ECO:0007829|PDB:4ZYN"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:4ZYN"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:4ZYN"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:4ZYN"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:4K7D"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:4ZYN"
FT HELIX 261..274
FT /evidence="ECO:0007829|PDB:4ZYN"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:4ZYN"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:4ZYN"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:4ZYN"
FT HELIX 301..307
FT /evidence="ECO:0007829|PDB:4ZYN"
FT HELIX 309..316
FT /evidence="ECO:0007829|PDB:4ZYN"
FT HELIX 318..326
FT /evidence="ECO:0007829|PDB:4ZYN"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:4K7D"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:4ZYN"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:4K7D"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:4K7D"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:4ZYN"
FT HELIX 395..400
FT /evidence="ECO:0007829|PDB:4ZYN"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:4K7D"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:4ZYN"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:4ZYN"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:4ZYN"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:4K7D"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:4K7D"
FT TURN 439..441
FT /evidence="ECO:0007829|PDB:4ZYN"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:4K7D"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:4ZYN"
FT HELIX 455..461
FT /evidence="ECO:0007829|PDB:4ZYN"
SQ SEQUENCE 465 AA; 51709 MW; E13CF170AD6D042B CRC64;
MIVFVRFNSS YGFPVEVDSD TSIFQLKEVV AKRQGVPADQ LRVIFAGKEL QNHLTVQNCD
LEQQSIVHIV QRPQRKSHET NASGGDKPQS TPEGSIWEPR SLTRVDLSSH ILPADSVGLA
VILDTDSKSD SEAARGPEAK PTYHSFFVYC KGPCHKVQPG KLRVQCGTCR QATLTLAQGP
SCWDDVLIPN RMSGECQSPD CPGTRAEFFF KCGAHPTSDK DTSVALNLIT NNSRSIPCIA
CTDVRNPVLV FQCNHRHVIC LDCFHLYCVT RLNDRQFVHD AQLGYSLPCV AGCPNSLIKE
LHHFRILGEE QYNRYQQYGA EECVLQMGGV LCPRPGCGAG LLPEQGQKKV TCEGGNGLGC
GFVFCRDCKE AYHEGECDSM FEASGATSQA YRVDQRAAEQ ARWEEASKET IKKTTKPCPR
CNVPIEKNGG CMHMKCPQPQ CKLEWCWNCG CEWNRACMGD HWFDV
