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Eukaryotic translation initiation factor 2-alpha kinase 3 (EC 2.7.11.1) (PRKR-like endoplasmic reticulum kinase) (Pancreatic eIF2-alpha kinase)

 E2AK3_RAT               Reviewed;        1108 AA.
Q9Z1Z1;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
12-SEP-2018, entry version 154.
RecName: Full=Eukaryotic translation initiation factor 2-alpha kinase 3;
EC=2.7.11.1;
AltName: Full=PRKR-like endoplasmic reticulum kinase;
AltName: Full=Pancreatic eIF2-alpha kinase;
Flags: Precursor;
Name=Eif2ak3; Synonyms=Pek, Perk;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
TISSUE=Pancreatic islet;
PubMed=9819435; DOI=10.1128/MCB.18.12.7499;
Shi Y., Vattem K.M., Sood R., An J., Liang J., Stramm L.E., Wek R.C.;
"Identification and characterization of pancreatic eukaryotic
initiation factor 2 alpha-subunit kinase, PEK, involved in
translational control.";
Mol. Cell. Biol. 18:7499-7509(1998).
[2]
MUTAGENESIS OF LYS-614.
PubMed=10026192; DOI=10.1074/jbc.274.9.5723;
Shi Y., An J., Liang J., Hayes S.E., Sandusky G.E., Stramm L.E.,
Yang N.N.;
"Characterization of a mutant pancreatic eIF-2alpha kinase, PEK, and
co-localization with somatostatin in islet delta cells.";
J. Biol. Chem. 274:5723-5730(1999).
[3]
SUBUNIT.
PubMed=10854322; DOI=10.1038/35014014;
Bertolotti A., Zhang Y., Hendershot L.M., Harding H.P., Ron D.;
"Dynamic interaction of BiP and ER stress transducers in the unfolded-
protein response.";
Nat. Cell Biol. 2:326-332(2000).
-!- FUNCTION: Metabolic-stress sensing protein kinase that
phosphorylates the alpha subunit of eukaryotic translation
initiation factor 2 (eIF-2-alpha/EIF2S1) on 'Ser-52' during the
unfolded protein response (UPR) and in response to low amino acid
availability. Converts phosphorylated eIF-2-alpha/EIF2S1 either in
a global protein synthesis inhibitor, leading to a reduced overall
utilization of amino acids, or to a translation initiation
activator of specific mRNAs, such as the transcriptional activator
ATF4, and hence allowing ATF4-mediated reprogramming of amino acid
biosynthetic gene expression to alleviate nutrient depletion.
Serves as a critical effector of unfolded protein response (UPR)-
induced G1 growth arrest due to the loss of cyclin-D1 (CCND1).
Involved in control of mitochondrial morphology and function.
{ECO:0000250|UniProtKB:Q9Z2B5}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ACTIVITY REGULATION: Perturbation in protein folding in the
endoplasmic reticulum (ER) promotes reversible dissociation from
HSPA5/BIP and oligomerization, resulting in
transautophosphorylation and kinase activity induction.
-!- SUBUNIT: Interacts with DNAJC3 and MFN2 (By similarity). Forms
dimers with HSPA5/BIP in resting cells (By similarity).
Oligomerizes in ER-stressed cells (PubMed:10854322). Interacts
with TMEM33 (By similarity). Interacts with PDIA6 (By similarity).
{ECO:0000250|UniProtKB:Q9NZJ5, ECO:0000250|UniProtKB:Q9Z2B5,
ECO:0000269|PubMed:10854322}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
type I membrane protein.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- INDUCTION: By ER stress.
-!- DOMAIN: The lumenal domain senses perturbations in protein folding
in the ER, probably through reversible interaction with HSPA5/BIP.
-!- PTM: Autophosphorylated. Phosphorylated at Tyr-611 following
endoplasmic reticulum stress, leading to activate its tyrosine-
protein kinase activity. Dephosphorylated by PTPN1/TP1B, leading
to inactivate its enzyme activity (By similarity). {ECO:0000250}.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- PTM: ADP-ribosylated by PARP16 upon ER stress, which increases
kinase activity. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. GCN2 subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; AF096835; AAC83801.1; -; mRNA.
PIR; T17455; T17455.
RefSeq; NP_113787.1; NM_031599.2.
UniGene; Rn.24897; -.
ProteinModelPortal; Q9Z1Z1; -.
SMR; Q9Z1Z1; -.
STRING; 10116.ENSRNOP00000008451; -.
iPTMnet; Q9Z1Z1; -.
PhosphoSitePlus; Q9Z1Z1; -.
PaxDb; Q9Z1Z1; -.
PRIDE; Q9Z1Z1; -.
Ensembl; ENSRNOT00000008451; ENSRNOP00000008451; ENSRNOG00000006069.
GeneID; 29702; -.
KEGG; rno:29702; -.
UCSC; RGD:70884; rat.
CTD; 9451; -.
RGD; 70884; Eif2ak3.
eggNOG; KOG1033; Eukaryota.
eggNOG; ENOG410XS0B; LUCA.
GeneTree; ENSGT00530000062984; -.
HOGENOM; HOG000112308; -.
HOVERGEN; HBG051431; -.
InParanoid; Q9Z1Z1; -.
KO; K08860; -.
OMA; KWKPLIH; -.
OrthoDB; EOG091G01X1; -.
PhylomeDB; Q9Z1Z1; -.
TreeFam; TF101511; -.
Reactome; R-RNO-381042; PERK regulates gene expression.
PRO; PR:Q9Z1Z1; -.
Proteomes; UP000002494; Chromosome 4.
Bgee; ENSRNOG00000006069; Expressed in 10 organ(s), highest expression level in colon.
Genevisible; Q9Z1Z1; RN.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; IDA:RGD.
GO; GO:0051879; F:Hsp90 protein binding; IDA:ParkinsonsUK-UCL.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:RGD.
GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:0034198; P:cellular response to amino acid starvation; ISS:UniProtKB.
GO; GO:0070417; P:cellular response to cold; ISS:UniProtKB.
GO; GO:0042149; P:cellular response to glucose starvation; IEA:Ensembl.
GO; GO:0036492; P:eiF2alpha phosphorylation in response to endoplasmic reticulum stress; ISS:UniProtKB.
GO; GO:0031018; P:endocrine pancreas development; ISS:UniProtKB.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISS:UniProtKB.
GO; GO:0006983; P:ER overload response; ISS:UniProtKB.
GO; GO:0032055; P:negative regulation of translation in response to stress; IDA:RGD.
GO; GO:0001503; P:ossification; ISS:UniProtKB.
GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IEA:Ensembl.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
GO; GO:0060734; P:regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation; ISS:UniProtKB.
GO; GO:1902235; P:regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
GO; GO:1990737; P:response to manganese-induced endoplasmic reticulum stress; IEP:ParkinsonsUK-UCL.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
Pfam; PF00069; Pkinase; 2.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF50998; SSF50998; 2.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ADP-ribosylation; ATP-binding; Complete proteome;
Endoplasmic reticulum; Glycoprotein; Kinase; Membrane;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Signal; Stress response; Transferase;
Translation regulation; Transmembrane; Transmembrane helix;
Unfolded protein response.
SIGNAL 1 27 {ECO:0000255}.
CHAIN 28 1108 Eukaryotic translation initiation factor
2-alpha kinase 3.
/FTId=PRO_0000024324.
TOPO_DOM 28 506 Lumenal. {ECO:0000255}.
TRANSMEM 507 527 Helical. {ECO:0000255}.
TOPO_DOM 528 1108 Cytoplasmic. {ECO:0000255}.
DOMAIN 585 1069 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 591 599 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 47 50 Poly-Ala.
COMPBIAS 223 228 Poly-Glu.
ACT_SITE 929 929 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 614 614 ATP.
MOD_RES 611 611 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9NZJ5}.
MOD_RES 707 707 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NZJ5}.
MOD_RES 974 974 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9Z2B5}.
MOD_RES 1086 1086 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NZJ5}.
CARBOHYD 253 253 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 614 614 K->A: Loss of activity.
{ECO:0000269|PubMed:10026192}.
SEQUENCE 1108 AA; 124770 MW; B3716B1FD26ED32B CRC64;
MERATQPRPR ALLLLFLLLG CAAGISAVAR ARSLLAPTSD TAFGLGAAAA PTSAARVPAV
ATAEVTVEDA EALPAASGEQ ESRATESDDD VELRPRGRSL VIISTLDGRI AALDAENHGK
KQWDLDVGSG SLVSSSLSKP EVFGNKMIIP SLDGDLFQWD RDRESMEAVP FTVESLLESS
YKFGDDVVLV GGKSLTTYGL SAYSGKLRYI CSALGCRRWD SDEMEEEEDI LLLQRTQKTV
RAVGPRSGSE KWNFSVGHFE LRYIPDMETR AGFIESTFKL GGNKEDSKII SDVEEQDVDT
VIKVSVADWK VMAFSKKGGR LEWEYQFCTP IASAWLVRDG KVIPISLFDD TSYTANEEVL
EDEEDIVEAA RGATENSVYL GMYRGQLYLQ SSVRVSEKFP TRPKALESVN GESAIIPLPT
IKWKPLIHSP SRTPVLVGSD EFDKCLSNDK YSHEEYSNGA LSILQYPYDN GYYLPYYKRE
RNKRSTQITV RFLDSPHYSK NIRKKDPILL LHWWKEIFGT ILLCIVATTF IVRRLFHPQP
HRQRKESETQ CQTESKYDSV SADNSDNSWN DIKHSGYVSR YLTDFEPIQC MGRGGFGVVF
EAKNKVDDCN YAIKRIRLPN RELAREKVMR EVKALAKLEH PGIVRYFNAW LETPPEKWQE
EMDEIWLKDE STDWPLSSPS PMDAPSVKIR QMDPFSTKEQ IEVIAPSPER SRSFSVGISC
GRTSSSESQF SPLEFSGTDC GDNSDSEDAA HNLQDSCLTD CDMEDGTVDG DDEGHSFELC
PSEASPYTRS REGTSSSIVF EDSGCDNASS KEDPRMNRLH NGHHYVNKLT EFKHSSSRSS
SEATLSTSPT RPTTLSLDFT RNTVDRLQPS SPKVYLYIQM QLCRKENLKD WMNRRCSMED
REHRVCLHIF LQIAEAVQFL HSKGLMHRDL KPSNIFFTMD DVVKVGDFGL VTAMDQDEEE
QTVLTPMPAY ATHTGQVGTK LYMSPEQIHG NNYSHKVDIF SLGLILFELL YPFSTQMERV
RTLTDVRNLK FPPLFTQKYP QEHMMVQDML SPSPMERPEA TDIIENAVFE NLEFPGKTVL
RQRSRSLSSS GTKHSRQPSS TFSPLPGN


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