JIP3_DROPS
ID JIP3_DROPS Reviewed; 1235 AA.
AC Q29EP6;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=JNK-interacting protein 3;
DE AltName: Full=Protein sunday driver;
GN Name=syd {ECO:0000250|UniProtKB:Q9GQF1}; ORFNames=GA20831;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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 (By similarity).
CC {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q58A65}.
CC -!- SIMILARITY: Belongs to the JIP scaffold family. {ECO:0000255}.
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DR EMBL; CH379070; EAL30014.2; -; Genomic_DNA.
DR RefSeq; XP_001352517.2; XM_001352481.3.
DR AlphaFoldDB; Q29EP6; -.
DR STRING; 7237.FBpp0286706; -.
DR EnsemblMetazoa; FBtr0288268; FBpp0286706; FBgn0080821.
DR GeneID; 4812552; -.
DR KEGG; dpo:Dpse_GA20831; -.
DR eggNOG; KOG2077; Eukaryota.
DR HOGENOM; CLU_003841_0_0_1; -.
DR InParanoid; Q29EP6; -.
DR OMA; YVTKMLG; -.
DR ChiTaRS; Sdc; fly.
DR Proteomes; UP000001819; Chromosome X.
DR Bgee; FBgn0080821; Expressed in insect adult head and 2 other tissues.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IEA:GOC.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; ISS:UniProtKB.
DR GO; GO:0019894; F:kinesin binding; ISS:UniProtKB.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; ISS:UniProtKB.
DR GO; GO:0008088; P:axo-dendritic transport; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:EnsemblMetazoa.
DR GO; GO:0050821; P:protein stabilization; IEA:EnsemblMetazoa.
DR GO; GO:0046328; P:regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS: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; IPR034743; RH1.
DR InterPro; IPR034744; RH2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13886; PTHR13886; 1.
DR Pfam; PF16471; JIP_LZII; 1.
DR Pfam; PF09744; Jnk-SapK_ap_N; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS51776; RH1; 1.
DR PROSITE; PS51777; RH2; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Reference proteome.
FT CHAIN 1..1235
FT /note="JNK-interacting protein 3"
FT /id="PRO_0000284449"
FT DOMAIN 25..113
FT /note="RH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01112"
FT DOMAIN 456..526
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 278..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 84..184
FT /evidence="ECO:0000255"
FT COILED 366..493
FT /evidence="ECO:0000255"
FT COMPBIAS 278..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1235 AA; 137449 MW; 55CE2D02184A5465 CRC64;
MMDNDDALLN NGGPQSGAET VYGTEDNNMV MSEKNDQVVS IVQQLAGSIY QEFERMINRY
DEDVVKNLMP LLVNVLECLD ASYRINQEQD VELELLREDN EQLVTQYERE KSARKQSEQK
LLEAEDLAEQ ENKELATRLE SVESIVRMLE LKHKNSLEHA SRLEERETDL KKEYNKLHER
YTELFKNHVD YMERTKMLMG STHSQMSTAS DRMEVSRARL NPVARSSGPV SYGFASLENS
VMLDTETICS VGSQSDDSGP PSLQNELDMS LPSTAERGAA TDSLQQQHQA TSPQSPPDTS
PVVPNVPPAN VGRSTTKKEQ RSDNNLYQEL SFQDNEESEE NEIVTGCWVH PGEYASSAND
NYFGMGKEVE NLIMENNELL ATKNALNIVK DDLIVKVDEL TGEVEIVREE LSAMQQSRTK
LRQRISELEE ELKKTKEQVK QQNTEQEEND VPLAQRKRFT RVEMAMVLME RNQYKERLME
LQEAVRLTEI LRASRTVDNL DKKSKQSIWK YFSNLFTPSN RPTERIADGL GGGPMFRNTG
GGSPAHSHGS PSRGSGDNRL TLAGSQPPMH PASAGLANAL VMPKDYSEDG GSERISARRR
EQYRQLRAHV QKEDGRLHAY GWSLPINKAN QEANPSRHSG GVPVPVYCNP LAEASPHMKV
FCAAGVNLHG GFTKDGQSLI PADSPYAPKS TLKITEITSP TAEQSVEALD RQIARASLET
LEPETQLSSF VWICTSTHAA STVSVVDANQ SATVLDAFPI CSSHLLCIAS VQGAMESDYA
LLEQSEVVKA GEMLQRPGEG TELLGKVEFV RVKPKSEDEQ NSNSKPQQQQ QDEEEAKEAT
EKSNEPLPPV NAEEPLVNVE AIKIRQALPG APQRLSSGNS GSDGNQANNN NSSSTGSVLF
ATKSLNPILG TKEREDPPMT SVGPTMWMGA QDGWLYVHSG VGRWHECLHR VLLPDAVLAI
VHVEARVVVA LANAQLAVFR RQTDGQWDLN SYHLVTLGDR NHSIRCLCVA GERIWAAHRN
KIFIVDPISL NIVHSLDAHP RKESQVRQMA ATGAGVWVSI RLDSTLRLYN THTFEHKQDV
DIEPYVSKML GTGKLGFSFV RITALMVSCN RLWIGTSNGV IISVPLAEVQ QKTSSDPHGQ
MPLCCMANAQ LSFHGHRDAV KFFVSVPMLQ QPNLNGGLTF VNKRPDMLVM CGGEGYIDFR
INDNDMENSI QLEPNQTIEN RGDKSYLIVW HVSQR
