JIP1_DROME
ID JIP1_DROME Reviewed; 490 AA.
AC Q9W0K0; Q8IGG5; Q9NH69;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=JNK-interacting protein 1;
DE Short=JIP-1;
DE AltName: Full=APP-like-interacting protein 1;
DE Short=APLIP1;
DE AltName: Full=Protein eye developmental SP512;
GN Name=Aplip1; Synonyms=SP512; ORFNames=CG1200;
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 [MRNA] (ISOFORM B), TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INTERACTION WITH APPL; HEP AND KLC.
RC TISSUE=Embryo;
RX PubMed=11912189; DOI=10.1074/jbc.m108372200;
RA Taru H., Iijima K., Hase M., Kirino Y., Yagi Y., Suzuki T.;
RT "Interaction of Alzheimer's beta-amyloid precursor family proteins with
RT scaffold proteins of the JNK signaling cascade.";
RL J. Biol. Chem. 277:20070-20078(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM B).
RA Serano T.L., Pendleton J.D., Rubin G.M.;
RT "A reverse genetic screen for genes involved in Drosophila eye
RT development.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: The JNK-interacting protein (JIP) group of scaffold proteins
CC selectively mediates JNK signaling by aggregating specific components
CC of the MAPK cascade to form a functional JNK signaling module. May
CC function as a regulator of vesicle transport, through interactions with
CC the JNK-signaling components and motor proteins (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Forms homo- and heterooligomeric complexes. Binds Hep, a dual
CC specificity protein kinase in the JNK pathway, but not its downstream
CC target bsk. The C-terminal region interacts with the kinesin light
CC chain protein, Klc, and the C-terminal PTY motif of amyloid-beta
CC protein precursor-like protein, Appl. {ECO:0000269|PubMed:11912189}.
CC -!- INTERACTION:
CC Q9W0K0; Q9W0K0: Aplip1; NbExp=2; IntAct=EBI-74120, EBI-74120;
CC Q9W0K0; P14599: Appl; NbExp=6; IntAct=EBI-74120, EBI-74135;
CC Q9W0K0; Q23977: hep; NbExp=2; IntAct=EBI-74120, EBI-74214;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B;
CC IsoId=Q9W0K0-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q9W0K0-2; Sequence=VSP_009507;
CC -!- TISSUE SPECIFICITY: Expressed in the brain, CNS, PNS and cells
CC posterior to the morphogenetic furrow in the eye imaginal disk of late
CC embryos. {ECO:0000269|PubMed:11912189}.
CC -!- DEVELOPMENTAL STAGE: Expressed from embryonic stage 12 through to
CC adulthood. {ECO:0000269|PubMed:11912189}.
CC -!- SIMILARITY: Belongs to the JIP scaffold family. {ECO:0000305}.
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DR EMBL; AF220194; AAL50332.1; -; mRNA.
DR EMBL; AF231037; AAF34806.1; -; mRNA.
DR EMBL; AE014296; AAF47446.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11462.1; -; Genomic_DNA.
DR EMBL; AY051495; AAK92919.1; -; mRNA.
DR EMBL; BT001795; AAN71550.1; -; mRNA.
DR RefSeq; NP_728573.1; NM_167856.3. [Q9W0K0-1]
DR RefSeq; NP_728574.1; NM_167857.4. [Q9W0K0-2]
DR PDB; 4Z88; X-ray; 2.09 A; M/N/O/P/Q/R/S/T/U/V/W/X=149-163.
DR PDBsum; 4Z88; -.
DR AlphaFoldDB; Q9W0K0; -.
DR SMR; Q9W0K0; -.
DR BioGRID; 72744; 13.
DR DIP; DIP-20311N; -.
DR IntAct; Q9W0K0; 3.
DR STRING; 7227.FBpp0072523; -.
DR PaxDb; Q9W0K0; -.
DR DNASU; 53472; -.
DR EnsemblMetazoa; FBtr0072626; FBpp0072522; FBgn0040281. [Q9W0K0-2]
DR EnsemblMetazoa; FBtr0072627; FBpp0072523; FBgn0040281. [Q9W0K0-1]
DR GeneID; 53472; -.
DR KEGG; dme:Dmel_CG1200; -.
DR CTD; 53472; -.
DR FlyBase; FBgn0040281; Aplip1.
DR VEuPathDB; VectorBase:FBgn0040281; -.
DR eggNOG; KOG3775; Eukaryota.
DR GeneTree; ENSGT00940000169182; -.
DR InParanoid; Q9W0K0; -.
DR OMA; GPCIDYF; -.
DR PhylomeDB; Q9W0K0; -.
DR SignaLink; Q9W0K0; -.
DR BioGRID-ORCS; 53472; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 53472; -.
DR PRO; PR:Q9W0K0; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0040281; Expressed in brain and 25 other tissues.
DR Genevisible; Q9W0K0; DM.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019894; F:kinesin binding; IPI:UniProtKB.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; IMP:FlyBase.
DR GO; GO:0019896; P:axonal transport of mitochondrion; IMP:FlyBase.
DR GO; GO:0007254; P:JNK cascade; ISA:FlyBase.
DR GO; GO:0046328; P:regulation of JNK cascade; IPI:FlyBase.
DR GO; GO:2000331; P:regulation of terminal button organization; IMP:FlyBase.
DR GO; GO:0048491; P:retrograde synaptic vesicle transport; IMP:FlyBase.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00640; PID; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW Reference proteome; SH3 domain.
FT CHAIN 1..490
FT /note="JNK-interacting protein 1"
FT /id="PRO_0000220635"
FT DOMAIN 271..332
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 344..479
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 164..171
FT /note="SSILHLLG -> C (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_009507"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:4Z88"
SQ SEQUENCE 490 AA; 53816 MW; 2744E85790EE043F CRC64;
MADSEFEEFH RPIFEPHTIA GFGSGAGSKK NNPHAFYSLI PNDDLEDSHS SKSDGDGSDQ
EDGIGLVDHE PKMRQVEDDE LGDGLKVTLS SDGSLDTNDS FNSHRHHPLN HQDAIGGFLG
MDTSGLGGNS APVTIGASTD LLAPNTAATR RRRKLPEIPK NKKSSILHLL GGSNFGSLAD
EFRNGGGGGI PPAVRSGQQR SFLSLKCGYL MDEDSSPDSE RMQSLGDVDS GHSTAHSPND
FKSMSPQITS PVSQSPFPPP FGGVPFGQLE MLEATHRGLH KFVPRHHDEI ELEIGDAIYV
QKEAEDLWCE GVNLRTGRQG IFPSAYAVDL DYNEFDPTVQ LVKKERYLLG YLGSVETLAH
KGTGVVCQAV RKIVGEYGNS PTGQTCILEV SDQGLRMVDR SGPNQNKKDK KPCIDYFYSL
KNVSFCAFHP RDHRFIGFIT KHPTVQRFAC HVFKGSESTR PVAEAVGRAF QRFYQKFIET
AYPIEDIYIE
