ID E2AJX5_CAMFO Unreviewed; 1284 AA.
AC E2AJX5;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 03-MAY-2023, entry version 43.
DE SubName: Full=C-jun-amino-terminal kinase-interacting protein 3 {ECO:0000313|EMBL:EFN66291.1};
GN ORFNames=EAG_13771 {ECO:0000313|EMBL:EFN66291.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN66291.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
CC -!- SIMILARITY: Belongs to the JIP scaffold family.
CC {ECO:0000256|ARBA:ARBA00009866}.
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DR EMBL; GL440100; EFN66291.1; -; Genomic_DNA.
DR STRING; 104421.E2AJX5; -.
DR InParanoid; E2AJX5; -.
DR OMA; VPTYCSN; -.
DR Proteomes; UP000000311; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.1770; -; 1.
DR Gene3D; 1.20.5.1000; arf6 gtpase in complex with a specific effector, jip4; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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:SF4; JNK-INTERACTING PROTEIN 3; 1.
DR PANTHER; PTHR13886; JNK/SAPK-ASSOCIATED PROTEIN; 1.
DR Pfam; PF16471; JIP_LZII; 1.
DR Pfam; PF09744; Jnk-SapK_ap_N; 1.
DR Pfam; PF19056; WD40_2; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS51776; RH1; 1.
DR PROSITE; PS51777; RH2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000313|EMBL:EFN66291.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW Transferase {ECO:0000313|EMBL:EFN66291.1}.
FT DOMAIN 4..92
FT /note="RH1"
FT /evidence="ECO:0000259|PROSITE:PS51776"
FT DOMAIN 455..527
FT /note="RH2"
FT /evidence="ECO:0000259|PROSITE:PS51777"
FT REGION 243..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1234..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 65..159
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 386..445
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 679..709
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 243..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1234..1250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1284 AA; 142935 MW; E8504F33BA47AC84 CRC64;
MDQETVYGTH EDSHVVMSEK VQSLAGSIYQ EFEKMIARYD EDVVKDLMPL LVNVLECLDI
SYTENQEREV ELELLREDNE QLVTQYEREK QLRKASDQKL LELEDISEDE RKELLSKIDS
LESIVRMLEL KTKNSHDHVG RLEEKEAELK REYSRLHDRY TELFKTHVDY MERTKMLVGS
TERLESVSTS RAPSRLPSLG LAHMSRSSGP LSYGFQSLEA SMNSEDVHED IIPNAANLRT
EMLDSSSEAA IETSDKSQLT DQPVQENKTT AISRHESPET EVPPTLMTPT TPTAGMEKLA
TTPGGRSRTE REQRSGNTLY QELSFQDADA LGEMDEGADI TGSLVHPGEY ASSVNDNFFG
MGKEVENLIM ENNELLATKN ALNVVKDDLI VKVDELTSEQ EILREEVRGL QQARERLRQR
IAALEEELKK AKEEAEAAAK ATKSDDEEDV PLSQRKRFTR VEMARVLMER NQYKERFIEL
QDAVRWTEMI RASKTVPSSI SGGKGGSVWK FFSNLFTGPA DRGTLVRSAH TLPHVRYSAP
ANQVVPAPPL DAMRRRTLKS RQDFLDQGDT ISSEKLVARR ASERREQYRQ VRAHVKKEDG
RLQAYGWSLP GKPSAPVRQP PVPVPVYCRP LQETEPGMKI WCGAGVNLSG GKTRDGGCMI
GGSVFYAAEA QETTSGNAKT EAEDAVEHLD KELQESENRR LEAERWEQQL SSLVWICTST
QKMSKVTVID ANNPADILEV FNVCQGHLLC IASVPGAKES DYAQSSNENS VRNSVNGSTT
NDNENNNGAY EDVTNANENA EQSNDRKNHQ DIDAAVDKNK NESDNQSEDQ ANENTEKTAE
TDQNSTTNEP QSLESIDSET ANLGKVHFVR NVEAHPSRLN DKDIVNEETK EEVVEEETPI
EKMSSIQPTM WLGAQNGAVF VHSAVAKWSV CLHSVKLKDA ALAIVHVQGR VLVALADGTV
TIFRRGADGQ WDLSQYHVIT LGSPQHSIRC MTAVSGKTVW CGYRNKIHVI DPISMTLECT
VDAHPRRESQ VRQLAWLGDG VWISIRLDST LRLYHAHTYQ HLQDVDIEPY VSKMLGTGKL
GFSFVRITAL LISSNRLWIG TGNGVIISVP LSESAGGSMA VSRIQTSGNK GDAPGVGVRI
FASERGVTPG SFIPYCSMAH AQLSFHGHRD AVKMFVAVPG HGGQSAVTDG TQPAMLVLSG
GEGYIDFRVA DEAEDESDVA THLIVWQMVR YAPRERSKQS DGEETEESMD RSNATVNNGT
EEHGEQSHLI VWQVQCPLPI PMNG
//
