ID A0A6I8VBM7_DROPS Unreviewed; 1122 AA.
AC A0A6I8VBM7;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=PRKR-like endoplasmic reticulum kinase {ECO:0000256|ARBA:ARBA00041500};
GN Name=LOC4802443 {ECO:0000313|RefSeq:XP_015037811.2};
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245 {ECO:0000313|Proteomes:UP000001819, ECO:0000313|RefSeq:XP_015037811.2};
RN [1] {ECO:0000313|RefSeq:XP_015037811.2}
RP IDENTIFICATION.
RC STRAIN=MV2-25 {ECO:0000313|RefSeq:XP_015037811.2};
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_015037811.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR RefSeq; XP_015037811.2; XM_015182325.2.
DR AlphaFoldDB; A0A6I8VBM7; -.
DR Proteomes; UP000001819; Chromosome 2.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProt.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0070887; P:cellular response to chemical stimulus; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:UniProt.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR CDD; cd09768; Luminal_EIF2AK3; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR11042:SF91; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE; 1.
DR PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF01011; PQQ; 1.
DR SMART; SM00564; PQQ; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Initiation factor {ECO:0000313|RefSeq:XP_015037811.2};
KW Kinase {ECO:0000313|RefSeq:XP_015037811.2};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein biosynthesis {ECO:0000313|RefSeq:XP_015037811.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001819};
KW Signal {ECO:0000256|SAM:SignalP};
KW Stress response {ECO:0000256|ARBA:ARBA00023016};
KW Transferase {ECO:0000313|RefSeq:XP_015037811.2};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Unfolded protein response {ECO:0000256|ARBA:ARBA00023230}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1122
FT /note="PRKR-like endoplasmic reticulum kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5026287341"
FT DOMAIN 593..1081
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 426..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..781
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 622
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1122 AA; 126088 MW; 85A1232D2C17BE66 CRC64;
MNQLAIKLNL LFRLLYITTL DGRLSALDIA KSGKLRWSVP TGPGPLISSS IHRLELTNNG
QFVRMIPSLS GGIYKFDGDS IDPIPITAEH LLSSSAKFSD DLVISGGKET RTYGVSARTG
QLLYECSING CVNVTAEGRA INDTIEDVKE EPLPDDAADD DDHIRDEAGY IVAHDPLLDD
VIVVRRQTQT VRAVESRTGI ERWNFSVGQH ELDMVRASEC HMQPRDELEL AVLDVDIKVV
VPEGIICAFS KSNPHDMLWK YKFDHPIVSA WNTNADDELK AIDLFSSAQW LWDQDEDELL
NNRPTSAPSI YLGMYDKQLY IQESIRLRQE IMDQTQVYQQ LTGDTSLMPK IPWKPIAASS
HSLVIFQANQ IDPEVIGEEP PTQGNELVPY DDQNFAVAAQ SVLNASEFVN GNGYYFFTGS
TELEGPSECG TNETPTGLPA IEAPPSSGSN KTGGVDATGN HSINDDLGFS LDDIDAPVKV
VILSLWFWWK EIVVIAFTSA VILNIFMGQR NQRVEREYLV IERHVPVQTA IEATEASTQA
LLGPVVPMSH YHQQHQRPGN RFSFPGSGNT QRSLSESTTH SGEHYTSRFQ TDFDLMTCLG
RGGFGVVFEA KNKLDENHYA VKRITLPNKE SSRQRVLREA RTLASCEHHN IVRYFHSWTE
TPPIGWQEEE DRKLLAHELS TSIQIETPDE STFPSLADQF QEKRQQQLLS WVSDAANSTA
CSHDFHGNGD TGLRNIKEEY DDDEEEDSLI EFRSESRSAA LRAGVQQDDD DDEDDDDDDD
ESKREGPLHR SSVSIDIHSA SFDLKNINYS QHPLVSNSFQ IESVRSKGNV SDDAGDSDRL
RKKPLTLALA QNHNNNPHQP NGSHGTPPSA TMQNGVVAKP SKVYLYIQMQ LCRKESLRDW
LRENRTEARA SHIADIFHQI VDAVDYVHLK GLIHRDLKPS NIFFSQDGKI KIGDFGLVTD
MADIPNLVAK CGDQSGLPSC ARHTQQVGTH LYMSPEQLLG RHYDYRVDIY SLGLIFFELH
VYFCTEMERI KTMRALREGQ YPKDFANNYP GQYELLQQML SADPEQRPQT KQLKNQLHDI
LKLPVHLADG RSEQAALAEA ARRLSRSRTF SSSSDHQQHQ KH
//
