JIP3_DROME
ID JIP3_DROME Reviewed; 1227 AA.
AC Q9GQF1; Q5U182; Q8IGL6; Q95SK0; Q9VSC0;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=JNK-interacting protein 3;
DE AltName: Full=Protein sunday driver;
GN Name=syd; ORFNames=CG8110;
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 {ECO:0000312|EMBL:AAG36930.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND INTERACTION WITH KLC.
RX PubMed=11106729; DOI=10.1016/s0092-8674(00)00162-8;
RA Bowman A.B., Kamal A., Ritchings B.W., Philp A.V., McGrail M.,
RA Gindhart J.G., Goldstein L.S.B.;
RT "Kinesin-dependent axonal transport is mediated by the Sunday Driver (SYD)
RT protein.";
RL Cell 103:583-594(2000).
RN [2] {ECO:0000305}
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 937-1227.
RC STRAIN=Berkeley; TISSUE=Embryo, and 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).
RN [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP RNA EDITING OF POSITION 983.
RX PubMed=17018572; DOI=10.1261/rna.254306;
RA Stapleton M., Carlson J.W., Celniker S.E.;
RT "RNA editing in Drosophila melanogaster: new targets and functional
RT consequences.";
RL RNA 12:1922-1932(2006).
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. Syd is required for
CC efficient kinesin-I mediated axonal transport.
CC -!- SUBUNIT: Forms homo- and heterooligomeric complexes. Binds the TPR
CC motif-containing C-terminal of kinesin light chain, Klc. Pre-assembled
CC syd scaffolding complexes are then transported as a cargo of kinesin,
CC to the required subcellular location.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q9GQF1-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9GQF1-2; Sequence=VSP_002780;
CC -!- RNA EDITING: Modified_positions=983 {ECO:0000269|PubMed:17018572};
CC Note=Partially edited. Target of Adar.;
CC -!- SIMILARITY: Belongs to the JIP scaffold family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28296.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAN71473.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAN71473.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAV36895.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAV36895.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF262045; AAG36930.1; -; mRNA.
DR EMBL; AE014296; AAF50505.2; -; Genomic_DNA.
DR EMBL; AE014296; AAN12032.2; -; Genomic_DNA.
DR EMBL; AY060748; AAL28296.1; ALT_INIT; mRNA.
DR EMBL; BT001718; AAN71473.1; ALT_SEQ; mRNA.
DR EMBL; BT016010; AAV36895.1; ALT_SEQ; mRNA.
DR RefSeq; NP_524652.1; NM_079913.3. [Q9GQF1-1]
DR RefSeq; NP_729311.2; NM_168245.3. [Q9GQF1-2]
DR AlphaFoldDB; Q9GQF1; -.
DR BioGRID; 68706; 1.
DR IntAct; Q9GQF1; 4.
DR STRING; 7227.FBpp0076483; -.
DR PaxDb; Q9GQF1; -.
DR EnsemblMetazoa; FBtr0076768; FBpp0076483; FBgn0024187. [Q9GQF1-1]
DR EnsemblMetazoa; FBtr0076769; FBpp0076484; FBgn0024187. [Q9GQF1-2]
DR GeneID; 43905; -.
DR KEGG; dme:Dmel_CG8110; -.
DR CTD; 43905; -.
DR FlyBase; FBgn0024187; syd.
DR VEuPathDB; VectorBase:FBgn0024187; -.
DR eggNOG; KOG2077; Eukaryota.
DR GeneTree; ENSGT00940000153496; -.
DR InParanoid; Q9GQF1; -.
DR PhylomeDB; Q9GQF1; -.
DR Reactome; R-DME-525793; Myogenesis.
DR BioGRID-ORCS; 43905; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Sdc; fly.
DR GenomeRNAi; 43905; -.
DR PRO; PR:Q9GQF1; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0024187; Expressed in central nervous system and 29 other tissues.
DR ExpressionAtlas; Q9GQF1; baseline and differential.
DR Genevisible; Q9GQF1; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:FlyBase.
DR GO; GO:0043005; C:neuron projection; IEA:GOC.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IDA:FlyBase.
DR GO; GO:0008432; F:JUN kinase binding; IBA:GO_Central.
DR GO; GO:0019894; F:kinesin binding; IPI:UniProtKB.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; ISS:UniProtKB.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central.
DR GO; GO:0008088; P:axo-dendritic transport; IMP:FlyBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:0050821; P:protein stabilization; IMP:FlyBase.
DR GO; GO:0046328; P:regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IEP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR039911; JIP3/JIP4.
DR InterPro; IPR032486; JIP_LZII.
DR InterPro; IPR019143; JNK/Rab-associated_protein-1_N.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR InterPro; IPR034743; RH1.
DR InterPro; IPR034744; RH2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR13886; PTHR13886; 1.
DR Pfam; PF16471; JIP_LZII; 1.
DR Pfam; PF09744; Jnk-SapK_ap_N; 1.
DR SUPFAM; SSF50969; SSF50969; 1.
DR PROSITE; PS51776; RH1; 1.
DR PROSITE; PS51777; RH2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Reference proteome;
KW RNA editing.
FT CHAIN 1..1227
FT /note="JNK-interacting protein 3"
FT /id="PRO_0000220636"
FT DOMAIN 25..113
FT /note="RH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01112"
FT DOMAIN 453..524
FT /note="RH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01113"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 84..191
FT /evidence="ECO:0000255"
FT COILED 363..489
FT /evidence="ECO:0000255"
FT COILED 814..849
FT /evidence="ECO:0000255"
FT COMPBIAS 281..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..838
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..34
FT /note="MMDNDDALLNNGGPQSGAETVYGTEDNNMVMSEK -> M (in isoform
FT B)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_002780"
FT VARIANT 983
FT /note="S -> G (in RNA edited version)"
FT CONFLICT 355..360
FT /note="Missing (in Ref. 4; AAN71473)"
FT /evidence="ECO:0000305"
FT CONFLICT 792
FT /note="M -> I (in Ref. 4; AAN71473)"
FT /evidence="ECO:0000305"
FT CONFLICT 1124
FT /note="K -> R (in Ref. 4; AAN71473)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1227 AA; 136712 MW; 2162C18066A057B8 CRC64;
MMDNDDALLN NGGPQSGAET VYGTEDNNMV MSEKNEQVVS IVQQLAGSIY QEFERMINRY
DEDVVKNLMP LLVNVLECLD ASYRINQEQD VEVELLREDN EQLVTQYERE KSARKQSEQK
LLEAEDLAEQ ENKELATRLE SVESIVRMLE LKHKNSLEHA SRLEEREADL KKEYNKLHER
YTELFKNHVD YMERTKMLMG STHSQMSTAS ERMDVSRARL NPVARSSGPV SYGFASLENS
VMLDTETICS VGSQSDDSGP PSLQNELDNL SGTLERGAAT DALQQQHHAT SPQSPDSSPV
VPNVPTNVGR STTKKEQRSD NNLYQELSFQ DNEESEENEI VTGSWVHPGE YASSANDNYF
GMGKEVENLI MENNELLATK NALNIVKDDL IVKVDELTGE VEIVREELNA MQQSRTKLRQ
RISELEDELK KAKEQVKQQN TEQEENDVPL AQRKRFTRVE MAMVLMERNQ YKERLMELQE
AVRLTEILRA SRTVDNLDRK SKQSIWKYFS NLFTPSNRPT ERVADGLGGG PMFRHTGGGS
PAHSHGSPSR GSGGGDNRLA LTSGQPPVHP ASAGLANALI MPKDYAEEGS SERISARRRE
QYRQLRAHVQ KEDGRLHAYG WSLPINKASQ EANPNRHSGG VPVPVYCNPL AEASPHMKVF
CAAGVNLHGG FTKNGQSLIP ANSPYAPKST LKIAEITSPT ADQSMEALDR QMARVSLETL
EPETQLSSFV WICTSTHAAS TVSVVDANQS ATVLDAFPIC ASHLLCIASV QGAMESDYAL
LEQSEVVKAG EMLQRPGEGT ELLGKVEFVR VKPKSDDEQN SNEKQQQEEE EAKEATEKSN
EQLPAVSAEE PLGNVEAIKI RQPLPGAPQR LSTDGNQTNN NNNSSSSSNL LFATKSLNPI
LETKDRDEPA MSSVGPTMWL GAQDGWLYVH SSVGRWHECL HRVLLPDAVL AIVHVEARVV
VALANAQLAV FRRQTDGQWD LNSYHLVTLG DRNHSIRCLC VAGERIWAAH RNKIFIVDPV
SLNIVHSLDA HPRKESQVRQ MAATGAGVWV SIRLDSTLRL YNTHTFEHKQ DVDIEPYVSK
MLGTGKLGFS FVRITALMVS CNRLWIGTSN GVIISVPLAE VQPKSSSDPH GQMPLCCMAN
AQLSFHGHRD AVKFFVSVPM LQQPNLNGGL TFTNKRPDML VMCGGEGYID FRINDNDMEN
SIQLEPNQTI ENRGDKSYLI VWHVSQR
