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Protein kinase C iota type (EC 2.7.11.13) (Atypical protein kinase C-lambda/iota) (aPKC-lambda/iota) (nPKC-iota)

 KPCI_MOUSE              Reviewed;         595 AA.
Q62074;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
16-JUN-2009, sequence version 3.
22-NOV-2017, entry version 189.
RecName: Full=Protein kinase C iota type;
EC=2.7.11.13;
AltName: Full=Atypical protein kinase C-lambda/iota;
Short=aPKC-lambda/iota;
AltName: Full=nPKC-iota;
Name=Prkci; Synonyms=Pkcl;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7513693;
Akimoto K., Mizuno K., Osada S., Hirai S., Tanuma S., Suzuki K.,
Ohno S.;
"A new member of the third class in the protein kinase C family, PKC
lambda, expressed dominantly in an undifferentiated mouse embryonal
carcinoma cell line and also in many tissues and cells.";
J. Biol. Chem. 269:12677-12683(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION.
PubMed=9971737; DOI=10.1083/jcb.144.3.413;
Uberall F., Hellbert K., Kampfer S., Maly K., Villunger A.,
Spitaler M., Mwanjewe J., Baier-Bitterlich G., Baier G.,
Grunicke H.H.;
"Evidence that atypical protein kinase C-lambda and atypical protein
kinase C-zeta participate in Ras-mediated reorganization of the F-
actin cytoskeleton.";
J. Cell Biol. 144:413-425(1999).
[4]
SUBUNIT OF A COMPLEX CONTAINING PARD6B; PARD3 AND CDC42.
PubMed=10934474; DOI=10.1038/35019573;
Joberty G., Petersen C., Gao L., Macara I.G.;
"The cell-polarity protein Par6 links Par3 and atypical protein kinase
C to Cdc42.";
Nat. Cell Biol. 2:531-539(2000).
[5]
INTERACTION WITH SQSTM1 AND MAP2K5, AND MUTAGENESIS OF ARG-27; VAL-28;
LYS-29; TRP-70; ASP-72; GLU-74; ASP-76; GLN-83 AND GLU-85.
PubMed=12813044; DOI=10.1074/jbc.M303221200;
Lamark T., Perander M., Outzen H., Kristiansen K., Oevervatn A.,
Michaelsen E., Bjoerkoey G., Johansen T.;
"Interaction codes within the family of mammalian Phox and Bem1p
domain-containing proteins.";
J. Biol. Chem. 278:34568-34581(2003).
[6]
FUNCTION.
PubMed=12832475; DOI=10.1128/MCB.23.14.4892-4900.2003;
Imamura T., Huang J., Usui I., Satoh H., Bever J., Olefsky J.M.;
"Insulin-induced GLUT4 translocation involves protein kinase C-lambda-
mediated functional coupling between Rab4 and the motor protein
kinesin.";
Mol. Cell. Biol. 23:4892-4900(2003).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15322187; DOI=10.4049/jimmunol.173.5.3250;
Soloff R.S., Katayama C., Lin M.Y., Feramisco J.R., Hedrick S.M.;
"Targeted deletion of protein kinase C lambda reveals a distribution
of functions between the two atypical protein kinase C isoforms.";
J. Immunol. 173:3250-3260(2004).
[8]
FUNCTION.
PubMed=14615604; DOI=10.1210/me.2003-0087;
Bandyopadhyay G., Standaert M.L., Sajan M.P., Kanoh Y., Miura A.,
Braun U., Kruse F., Leitges M., Farese R.V.;
"Protein kinase C-lambda knockout in embryonic stem cells and
adipocytes impairs insulin-stimulated glucose transport.";
Mol. Endocrinol. 18:373-383(2004).
[9]
FUNCTION.
PubMed=16267237; DOI=10.1523/JNEUROSCI.3657-05.2005;
Koike C., Nishida A., Akimoto K., Nakaya M.A., Noda T., Ohno S.,
Furukawa T.;
"Function of atypical protein kinase C lambda in differentiating
photoreceptors is required for proper lamination of mouse retina.";
J. Neurosci. 25:10290-10298(2005).
[10]
INTERACTION WITH WDFY2.
PubMed=16792529; DOI=10.1042/BJ20060511;
Fritzius T., Burkard G., Haas E., Heinrich J., Schweneker M.,
Bosse M., Zimmermann S., Frey A.D., Caelers A., Bachmann A.S.,
Moelling K.;
"A WD-FYVE protein binds to the kinases Akt and PKCzeta/lambda.";
Biochem. J. 399:9-20(2006).
[11]
INTERACTION WITH VAMP2.
PubMed=17313651; DOI=10.1111/j.1742-4658.2007.05702.x;
Fritzius T., Frey A.D., Schweneker M., Mayer D., Moelling K.;
"WD-repeat-propeller-FYVE protein, ProF, binds VAMP2 and protein
kinase Czeta.";
FEBS J. 274:1552-1566(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-411, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-563, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Lung, Pancreas, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[14]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 231-595 IN COMPLEX WITH RAT
PARD3 PEPTIDE, PHOSPHORYLATION AT THR-563, AND PSEUDOSUBSTRATE MOTIF.
PubMed=22579248; DOI=10.1016/j.str.2012.02.022;
Wang C., Shang Y., Yu J., Zhang M.;
"Substrate recognition mechanism of atypical protein kinase Cs
revealed by the structure of PKCiota in complex with a substrate
peptide from Par-3.";
Structure 20:791-801(2012).
-!- FUNCTION: Calcium- and diacylglycerol-independent serine/
threonine-protein kinase that plays a general protective role
against apoptotic stimuli, is involved in NF-kappa-B activation,
cell survival, differentiation and polarity, and contributes to
the regulation of microtubule dynamics in the early secretory
pathway. Is necessary for BCR-ABL oncogene-mediated resistance to
apoptotic drug in leukemia cells, protecting leukemia cells
against drug-induced apoptosis. In cultured neurons, prevents
amyloid beta protein-induced apoptosis by interrupting cell death
process at a very early step. In glioblastoma cells, may function
downstream of phosphatidylinositol 3-kinase (PI3K) and PDPK1 in
the promotion of cell survival by phosphorylating and inhibiting
the pro-apoptotic factor BAD. Can form a protein complex in non-
small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and
regulate ECT2 oncogenic activity by phosphorylation, which in turn
promotes transformed growth and invasion. In response to nerve
growth factor (NGF), acts downstream of SRC to phosphorylate and
activate IRAK1, allowing the subsequent activation of NF-kappa-B
and neuronal cell survival. Functions in the organization of the
apical domain in epithelial cells by phosphorylating EZR. This
step is crucial for activation and normal distribution of EZR at
the early stages of intestinal epithelial cell differentiation.
Forms a protein complex with LLGL1 and PARD6B independently of
PARD3 to regulate epithelial cell polarity. Plays a role in
microtubule dynamics in the early secretory pathway through
interaction with RAB2A and GAPDH and recruitment to vesicular
tubular clusters (VTCs). In human coronary artery endothelial
cells (HCAEC), is activated by saturated fatty acids and mediates
lipid-induced apoptosis (By similarity). Downstream of PI3K is
required for insulin-stimulated glucose transport. Activates RAB4A
and promotes its association with KIF3A which is required for the
insulin-induced SLC2A4/GLUT4 translocation in adipocytes. Is
essential in early embryogenesis and development of
differentiating photoreceptors by playing a role in the
establishment of epithelial and neuronal polarity. {ECO:0000250,
ECO:0000269|PubMed:12832475, ECO:0000269|PubMed:14615604,
ECO:0000269|PubMed:15322187, ECO:0000269|PubMed:16267237,
ECO:0000269|PubMed:9971737}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Atypical PKCs (PRKCI and PRKCZ) exhibit an
elevated basal enzymatic activity (that may be due to the
interaction with SMG1 or SQSTM1) and are not regulated by
diacylglycerol, phosphatidylserine, phorbol esters or calcium
ions. Two specific sites, Thr-411 (activation loop of the kinase
domain) and Thr-563 (turn motif), need to be phosphorylated for
its full activation (By similarity). Might also be a target for
novel lipid activators that are elevated during nutrient-
stimulated insulin secretion. {ECO:0000250}.
-!- SUBUNIT: Forms a complex with SQSTM1 and MP2K5 (PubMed:12813044).
Interacts directly with SQSTM1 (Probable). Interacts with IKBKB.
Interacts with PARD6A, PARD6B and PARD6G. Part of a quaternary
complex containing aPKC, PARD3, a PARD6 protein (PARD6A, PARD6B or
PARD6G) and a GTPase protein (CDC42 or RAC1) (PubMed:10934474).
Part of a complex with LLGL1 and PARD6B. Interacts with
ADAP1/CENTA1. Interaction with SMG1, through the ZN-finger domain,
activates the kinase activity. Interacts with CDK7. Forms a
complex with RAB2A and GAPDH involved in recruitment onto the
membrane of vesicular tubular clusters (VTCs). Interacts with ECT2
('Thr-359' phosphorylated form) (By similarity). Interacts with
VAMP2 (PubMed:17313651). Interacts with WDFY2 (via WD repeats 1-3)
(PubMed:16792529). {ECO:0000250|UniProtKB:P41743,
ECO:0000269|PubMed:10934474, ECO:0000269|PubMed:12813044,
ECO:0000269|PubMed:16792529, ECO:0000269|PubMed:17313651,
ECO:0000305}.
-!- INTERACTION:
Q8R1S4:Mtss1; NbExp=4; IntAct=EBI-82016, EBI-15622277;
Q8TEW0:PARD3 (xeno); NbExp=7; IntAct=EBI-82016, EBI-81968;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P41743}.
Membrane {ECO:0000250|UniProtKB:P41743}. Endosome
{ECO:0000250|UniProtKB:P41743}. Nucleus
{ECO:0000250|UniProtKB:P41743}. Note=Transported into the endosome
through interaction with SQSTM1/p62. After phosphorylation by SRC,
transported into the nucleus through interaction with KPNB1.
Colocalizes with CDK7 in the cytoplasm and nucleus. Transported to
vesicular tubular clusters (VTCs) through interaction with RAB2A.
{ECO:0000250|UniProtKB:P41743}.
-!- DOMAIN: The PB1 domain mediates interaction with SQSTM1.
-!- DOMAIN: The C1 zinc finger does not bind diacylglycerol (DAG).
{ECO:0000250}.
-!- DOMAIN: The pseudosubstrate motif resembles the sequence around
sites phosphorylated on target proteins, except the presence of a
non-phosphorylatable residue in place of Ser, it modulates
activity by competing with substrates.
-!- PTM: Upon neuronal growth factor (NGF) stimulation, phosphorylated
by SRC at Tyr-264, Tyr-279 and Tyr-333. Phosphorylation on Tyr-264
facilitates binding to KPNB1/importin-beta regulating entry of
PRKCI into the nucleus. Phosphorylation on Tyr-333 is important
for NF-kappa-B stimulation (By similarity). Phosphorylation at
Thr-411 in the activation loop is not mandatory for activation.
{ECO:0000250, ECO:0000269|PubMed:22579248}.
-!- DISRUPTION PHENOTYPE: Embryonic lethal at 9.5 dpc.
{ECO:0000269|PubMed:15322187}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. PKC subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH21630.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA32499.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; D28577; BAA32499.1; ALT_INIT; mRNA.
EMBL; BC021630; AAH21630.1; ALT_INIT; mRNA.
CCDS; CCDS17289.2; -.
PIR; A53758; A53758.
RefSeq; NP_032883.2; NM_008857.3.
UniGene; Mm.291554; -.
PDB; 4DC2; X-ray; 2.40 A; A=231-595.
PDBsum; 4DC2; -.
ProteinModelPortal; Q62074; -.
SMR; Q62074; -.
BioGrid; 202200; 31.
CORUM; Q62074; -.
DIP; DIP-32555N; -.
IntAct; Q62074; 32.
MINT; MINT-4100000; -.
STRING; 10090.ENSMUSP00000103884; -.
iPTMnet; Q62074; -.
PhosphoSitePlus; Q62074; -.
EPD; Q62074; -.
MaxQB; Q62074; -.
PaxDb; Q62074; -.
PRIDE; Q62074; -.
Ensembl; ENSMUST00000108249; ENSMUSP00000103884; ENSMUSG00000037643.
GeneID; 18759; -.
KEGG; mmu:18759; -.
UCSC; uc008ovs.1; mouse.
CTD; 5584; -.
MGI; MGI:99260; Prkci.
eggNOG; KOG0695; Eukaryota.
eggNOG; ENOG410ZMG2; LUCA.
GeneTree; ENSGT00820000126964; -.
HOGENOM; HOG000233033; -.
HOVERGEN; HBG108317; -.
InParanoid; Q62074; -.
KO; K06069; -.
OMA; KGDIMIT; -.
OrthoDB; EOG091G03Q9; -.
TreeFam; TF102004; -.
BRENDA; 2.7.11.13; 3474.
Reactome; R-MMU-209543; p75NTR recruits signalling complexes.
Reactome; R-MMU-420029; Tight junction interactions.
PRO; PR:Q62074; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000037643; -.
CleanEx; MM_PRKCI; -.
ExpressionAtlas; Q62074; baseline and differential.
Genevisible; Q62074; MM.
GO; GO:0045177; C:apical part of cell; IDA:MGI.
GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
GO; GO:0005923; C:bicellular tight junction; IEA:Ensembl.
GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0000139; C:Golgi membrane; IEA:GOC.
GO; GO:0045171; C:intercellular bridge; ISO:MGI.
GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0043220; C:Schmidt-Lanterman incisure; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
GO; GO:0004697; F:protein kinase C activity; IDA:BHF-UCL.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0007015; P:actin filament organization; IMP:MGI.
GO; GO:0016477; P:cell migration; IEA:Ensembl.
GO; GO:0045216; P:cell-cell junction organization; ISS:UniProtKB.
GO; GO:0034613; P:cellular protein localization; IEA:Ensembl.
GO; GO:0032869; P:cellular response to insulin stimulus; IMP:BHF-UCL.
GO; GO:0035089; P:establishment of apical/basal cell polarity; IMP:MGI.
GO; GO:0042462; P:eye photoreceptor cell development; IMP:MGI.
GO; GO:0048194; P:Golgi vesicle budding; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0034351; P:negative regulation of glial cell apoptotic process; ISS:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; ISS:UniProtKB.
GO; GO:0060252; P:positive regulation of glial cell proliferation; ISS:UniProtKB.
GO; GO:0046326; P:positive regulation of glucose import; IMP:BHF-UCL.
GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:BHF-UCL.
GO; GO:0006468; P:protein phosphorylation; IDA:BHF-UCL.
GO; GO:0070555; P:response to interleukin-1; IEA:Ensembl.
CDD; cd00029; C1; 1.
CDD; cd06404; PB1_aPKC; 1.
CDD; cd05618; STKc_aPKC_iota; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR034661; aPKC_iota.
InterPro; IPR020454; DAG/PE-bd.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR034877; PB1_aPKC.
InterPro; IPR000270; PB1_dom.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR012233; PKC.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00130; C1_1; 1.
Pfam; PF00564; PB1; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
PIRSF; PIRSF000554; PKC_zeta; 1.
PRINTS; PR00008; DAGPEDOMAIN.
SMART; SM00109; C1; 1.
SMART; SM00666; PB1; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS51745; PB1; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm;
Developmental protein; Endosome; Kinase; Membrane; Metal-binding;
Nucleotide-binding; Nucleus; Phosphoprotein; Proto-oncogene;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Tumor suppressor; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P41743}.
CHAIN 2 595 Protein kinase C iota type.
/FTId=PRO_0000055711.
DOMAIN 25 108 PB1. {ECO:0000255|PROSITE-
ProRule:PRU01081}.
DOMAIN 253 521 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 522 595 AGC-kinase C-terminal.
ZN_FING 140 190 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 259 267 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 2 252 Regulatory domain. {ECO:0000250}.
REGION 2 28 Required for interaction with RAB2.
{ECO:0000250}.
REGION 72 91 Interaction with PARD6A. {ECO:0000250}.
MOTIF 125 134 Pseudosubstrate.
ACT_SITE 377 377 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 282 282 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylproline.
{ECO:0000250|UniProtKB:P41743}.
MOD_RES 3 3 Phosphothreonine.
{ECO:0000250|UniProtKB:P41743}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000250|UniProtKB:P41743}.
MOD_RES 8 8 Phosphoserine.
{ECO:0000250|UniProtKB:P41743}.
MOD_RES 9 9 Phosphothreonine.
{ECO:0000250|UniProtKB:P41743}.
MOD_RES 264 264 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P41743}.
MOD_RES 279 279 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P41743}.
MOD_RES 333 333 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P41743}.
MOD_RES 411 411 Phosphothreonine.
{ECO:0000244|PubMed:17242355}.
MOD_RES 563 563 Phosphothreonine.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:22579248}.
MUTAGEN 27 27 R->A: No effect on interaction with
SQSTM1. {ECO:0000269|PubMed:12813044}.
MUTAGEN 28 28 V->A: No effect on interaction with
SQSTM1; when associated with A-29.
{ECO:0000269|PubMed:12813044}.
MUTAGEN 29 29 K->A: No effect on interaction with
SQSTM1; when associated with A-118.
{ECO:0000269|PubMed:12813044}.
MUTAGEN 70 70 W->A: Loss of interaction with SQSTM1.
{ECO:0000269|PubMed:12813044}.
MUTAGEN 72 72 D->A: Loss of interaction with SQSTM1.
{ECO:0000269|PubMed:12813044}.
MUTAGEN 74 74 E->A: Loss of interaction with SQSTM1.
{ECO:0000269|PubMed:12813044}.
MUTAGEN 76 76 D->A: Loss of interaction with SQSTM1.
{ECO:0000269|PubMed:12813044}.
MUTAGEN 83 83 Q->A: No effect on interaction with
SQSTM1. {ECO:0000269|PubMed:12813044}.
MUTAGEN 85 85 E->A: Loss of interaction with SQSTM1.
{ECO:0000269|PubMed:12813044}.
HELIX 250 252 {ECO:0000244|PDB:4DC2}.
STRAND 253 261 {ECO:0000244|PDB:4DC2}.
STRAND 263 272 {ECO:0000244|PDB:4DC2}.
TURN 273 275 {ECO:0000244|PDB:4DC2}.
STRAND 278 285 {ECO:0000244|PDB:4DC2}.
HELIX 286 288 {ECO:0000244|PDB:4DC2}.
HELIX 297 308 {ECO:0000244|PDB:4DC2}.
STRAND 317 322 {ECO:0000244|PDB:4DC2}.
STRAND 324 332 {ECO:0000244|PDB:4DC2}.
HELIX 339 346 {ECO:0000244|PDB:4DC2}.
HELIX 351 370 {ECO:0000244|PDB:4DC2}.
HELIX 380 382 {ECO:0000244|PDB:4DC2}.
STRAND 383 385 {ECO:0000244|PDB:4DC2}.
STRAND 391 393 {ECO:0000244|PDB:4DC2}.
HELIX 416 418 {ECO:0000244|PDB:4DC2}.
HELIX 421 424 {ECO:0000244|PDB:4DC2}.
HELIX 432 447 {ECO:0000244|PDB:4DC2}.
TURN 453 456 {ECO:0000244|PDB:4DC2}.
HELIX 466 475 {ECO:0000244|PDB:4DC2}.
HELIX 486 495 {ECO:0000244|PDB:4DC2}.
TURN 500 502 {ECO:0000244|PDB:4DC2}.
TURN 508 510 {ECO:0000244|PDB:4DC2}.
HELIX 511 517 {ECO:0000244|PDB:4DC2}.
TURN 519 523 {ECO:0000244|PDB:4DC2}.
HELIX 526 530 {ECO:0000244|PDB:4DC2}.
HELIX 548 550 {ECO:0000244|PDB:4DC2}.
HELIX 553 556 {ECO:0000244|PDB:4DC2}.
HELIX 567 570 {ECO:0000244|PDB:4DC2}.
HELIX 575 578 {ECO:0000244|PDB:4DC2}.
SEQUENCE 595 AA; 68203 MW; 6AC612D1E9264825 CRC64;
MPTQRDSSTM SHTVACGGGG DHSHQVRVKA YYRGDIMITH FEPSISFEGL CSEVRDMCSF
DNEQPFTMKW IDEEGDPCTV SSQLELEEAF RLYELNKDSE LLIHVFPCVP ERPGMPCPGE
DKSIYRRGAR RWRKLYCANG HTFQAKRFNR RAHCAICTDR IWGLGRQGYK CINCKLLVHK
KCHKLVTIEC GRHSLPPEPM MPMDQTMHPD HTQTVIPYNP SSHESLDQVG EEKEAMNTRE
SGKASSSLGL QDFDLLRVIG RGSYAKVLLV RLKKTDRIYA MKVVKKELVN DDEDIDWVQT
EKHVFEQASN HPFLVGLHSC FQTESRLFFV IEYVNGGDLM FHMQRQRKLP EEHARFYSAE
ISLALNYLHE RGIIYRDLKL DNVLLDSEGH IKLTDYGMCK EGLRPGDTTS TFCGTPNYIA
PEILRGEDYG FSVDWWALGV LMFEMMAGRS PFDIVGSSDN PDQNTEDYLF QVILEKQIRI
PRSLSVKAAS VLKSFLNKDP KERLGCHPQT GFADIQGHPF FRNVDWDMME QKQVVPPFKP
NISGEFGLDN FDSQFTNEPV QLTPDDDDIV RKIDQSEFEG FEYINPLLMS AEECV


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