ERK7_DROME
ID ERK7_DROME Reviewed; 916 AA.
AC Q9W354; M9MSN4;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Extracellular signal-regulated kinase 7 {ECO:0000305};
DE EC=2.7.11.24 {ECO:0000255|PROSITE-ProRule:PRU00159};
GN Name=Erk7 {ECO:0000312|FlyBase:FBgn0052703};
GN ORFNames=CG32703 {ECO:0000312|FlyBase:FBgn0052703};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Berkeley; TISSUE=Testis;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP MUTAGENESIS OF LYS-54; THR-190 AND TYR-192, FUNCTION, AND INDUCTION.
RX PubMed=21847093; DOI=10.1038/emboj.2011.253;
RA Zacharogianni M., Kondylis V., Tang Y., Farhan H., Xanthakis D., Fuchs F.,
RA Boutros M., Rabouille C.;
RT "ERK7 is a negative regulator of protein secretion in response to amino-
RT acid starvation by modulating Sec16 membrane association.";
RL EMBO J. 30:3684-3700(2011).
RN [5]
RP INDUCTION, AND FUNCTION.
RX PubMed=25393288; DOI=10.1371/journal.pgen.1004764;
RA Hasygar K., Hietakangas V.;
RT "p53- and ERK7-dependent ribosome surveillance response regulates
RT Drosophila insulin-like peptide secretion.";
RL PLoS Genet. 10:E1004764-E1004764(2014).
CC -!- FUNCTION: Atypical MAPK protein that regulates protein secretion in a
CC kinase activity-dependent manner (PubMed:21847093, PubMed:25393288). In
CC response to starvation regulates protein secretion by mediating
CC transitional endoplasmic reticulum site disassembly (PubMed:21847093).
CC Mediates inhibition of insulin-like peptide secretion upon disturbed
CC ribosome biogenesis and acts as a downstream effector of TP53
CC (PubMed:25393288). {ECO:0000269|PubMed:21847093,
CC ECO:0000269|PubMed:25393288}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.24;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9W354-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9W354-2; Sequence=VSP_059618, VSP_059619;
CC -!- INDUCTION: Amino-acid starvation stabilizes protein level
CC (PubMed:21847093). Up-regulated upon impaired ribosome biogenesis and
CC starvation (PubMed:25393288). {ECO:0000269|PubMed:21847093,
CC ECO:0000269|PubMed:25393288}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AE014298; AAF46481.2; -; Genomic_DNA.
DR EMBL; AE014298; ADV37650.1; -; Genomic_DNA.
DR EMBL; AE014298; ADV37651.1; -; Genomic_DNA.
DR EMBL; BT003639; AAO39643.1; -; mRNA.
DR RefSeq; NP_001188568.1; NM_001201639.1. [Q9W354-1]
DR RefSeq; NP_001188569.1; NM_001201640.2. [Q9W354-2]
DR RefSeq; NP_727335.1; NM_167188.2. [Q9W354-1]
DR AlphaFoldDB; Q9W354; -.
DR SMR; Q9W354; -.
DR IntAct; Q9W354; 4.
DR STRING; 7227.FBpp0071264; -.
DR PaxDb; Q9W354; -.
DR DNASU; 31877; -.
DR EnsemblMetazoa; FBtr0071329; FBpp0071264; FBgn0052703. [Q9W354-1]
DR EnsemblMetazoa; FBtr0302965; FBpp0292090; FBgn0052703. [Q9W354-1]
DR EnsemblMetazoa; FBtr0302966; FBpp0292091; FBgn0052703. [Q9W354-2]
DR GeneID; 31877; -.
DR KEGG; dme:Dmel_CG32703; -.
DR UCSC; CG32703-RA; d. melanogaster. [Q9W354-1]
DR CTD; 31877; -.
DR FlyBase; FBgn0052703; Erk7.
DR VEuPathDB; VectorBase:FBgn0052703; -.
DR eggNOG; KOG0660; Eukaryota.
DR GeneTree; ENSGT00940000159758; -.
DR HOGENOM; CLU_000288_181_14_1; -.
DR InParanoid; Q9W354; -.
DR OMA; PDQEWTR; -.
DR OrthoDB; 741207at2759; -.
DR PhylomeDB; Q9W354; -.
DR SignaLink; Q9W354; -.
DR BioGRID-ORCS; 31877; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 31877; -.
DR PRO; PR:Q9W354; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0052703; Expressed in testis and 7 other tissues.
DR ExpressionAtlas; Q9W354; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:FlyBase.
DR GO; GO:0005635; C:nuclear envelope; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IMP:FlyBase.
DR GO; GO:0009267; P:cellular response to starvation; IMP:FlyBase.
DR GO; GO:0007030; P:Golgi organization; IMP:FlyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0034389; P:lipid droplet organization; IMP:FlyBase.
DR GO; GO:0045792; P:negative regulation of cell size; IMP:FlyBase.
DR GO; GO:0050709; P:negative regulation of protein secretion; IMP:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; ISS:FlyBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01351; MAPK; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..916
FT /note="Extracellular signal-regulated kinase 7"
FT /id="PRO_0000444601"
FT DOMAIN 25..319
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 364..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 31..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 393..451
FT /note="TTSAKQPTTSPAERKKEPSSVEVTQSRKNIKLLGSAHKAQSKEINHMESAIT
FT QVSIASA -> LHRAITKVTSTSNHLQQETFKERKESVESITVQRPVKERLHRSMHRKA
FT HRMRLKKGHSQ (in isoform 2)"
FT /id="VSP_059618"
FT VAR_SEQ 452..916
FT /note="Missing (in isoform 2)"
FT /id="VSP_059619"
FT MUTAGEN 54
FT /note="K->R: Does not lead to transitional endoplasmic
FT reticulum sites disassembly. Partially rescue transitional
FT endoplasmic reticulum site disassembly induced by amino-
FT acid starvation."
FT /evidence="ECO:0000269|PubMed:21847093"
FT MUTAGEN 190
FT /note="T->A: Does not lead to transitional endoplasmic
FT reticulum sites disassembly; when associated with F-192."
FT /evidence="ECO:0000269|PubMed:21847093"
FT MUTAGEN 192
FT /note="Y->F: Does not lead to transitional endoplasmic
FT reticulum sites disassembly; when associated with A-190."
FT /evidence="ECO:0000269|PubMed:21847093"
SQ SEQUENCE 916 AA; 105715 MW; 68C9605B2E2AD292 CRC64;
MANYQTAHAQ ERRIQELDQT VESIFDVRKR MGKGAYGIVW KATDRRTKNT VALKKVFDAF
RDETDAQRTY REVIFLRAFR CHPNIVRLVD IFKASNNLDF YLVFEFMESD LHNVIKRGNV
LKDVHKRFVM YQLINAIKFI HSGNVIHRDL KPSNILIDSK CRLKVADFGL ARTLSSRRIY
DDLEQDGMLT DYVATRWYRA PEILVASRNY TKGIDMWGLG CILGEMIRQK PLFQGTSTVN
QIEKIVTSLP NVTKLDIASI GPSFGSVLLS RNIQRDRRYS LDEMMKNCCD DGISLVKALL
VLNPHNRLTA KEAIRHPYVS RFQYASAEMD LHMDVVPPLK DHVRYDVDQY RNSLYELIDR
ETSCSNRTVS NSTPSSNRDE LPKPVRVTKQ ARTTSAKQPT TSPAERKKEP SSVEVTQSRK
NIKLLGSAHK AQSKEINHME SAITQVSIAS APPAAAPPAP AATAPAVPRK SGDKSVPKCQ
HNNAAVQREL AAVAAAAAVA RRKKSSWQSQ AQSQGKFHTE AKAHVQTAIQ TQKDNIKDSP
PRMIQESQSL TEAKAPIPKN RYSNKMCQEK KYKKKHHSMS CITRDTFPSE TEHRQQREER
AYQRQMKREL QLKESYRRRI EAESEPLKET TEQESKTIKV IEQKVCEHTE KKADESLSKD
QQKDSITFGT CVRERIHHLE LEMEKCTEEL VDFVELNADV LNYANVSTHL KKLQRSKESD
EKDEDDRRAL PEGIGGPGSQ NYEIFRQEQE KERQRQVQEF LARDETNEYD NLDLDHAYRA
KYYTAYKEIG KELNPAPDSG GRDSGSEHSP GRDNYTTYAD YFLKYTTPQQ NWNDLERANG
LQREHDRIYG LFWLNDRRQE EKYRRKLAQN DQEELPVHHH KACRHRHHKP NHHAPYDHMR
PTEDDIQEAD SLPESN
