ID A0A151X2H0_9HYME Unreviewed; 1260 AA.
AC A0A151X2H0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 22-FEB-2023, entry version 20.
DE SubName: Full=JNK-interacting protein 3 {ECO:0000313|EMBL:KYQ54505.1};
GN ORFNames=ALC60_06652 {ECO:0000313|EMBL:KYQ54505.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ54505.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ54505.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ54505.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ54505.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the JIP scaffold family.
CC {ECO:0000256|ARBA:ARBA00009866}.
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DR EMBL; KQ982580; KYQ54505.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151X2H0; -.
DR STRING; 64791.A0A151X2H0; -.
DR Proteomes; UP000075809; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000075809}.
FT DOMAIN 4..92
FT /note="RH1"
FT /evidence="ECO:0000259|PROSITE:PS51776"
FT DOMAIN 455..526
FT /note="RH2"
FT /evidence="ECO:0000259|PROSITE:PS51777"
FT REGION 246..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 65..159
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 386..483
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 634..671
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 246..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1260 AA; 140715 MW; 084CEA4C4491AD7A CRC64;
MDQETVYGTH EDSHVVMSEK VQSLAGSIYQ EFEKMIARYD EDVVKDLMPL LVNVLECLDI
SYTENQEREV ELELLREDNE QLVTQYEREK QLRKASDQKL LELEDVSEDE RKELLSKIDS
LESIVRMLEL KTKNSHDHVG RLEEKEAELK REYSRLHDRY TELFKTHVDY MERTKMLVGS
TERLESVSTS RAPSRLPSLG LAHMSRSSGP LSYGFQSLEA SINAEDVQED IVPNVVNLRT
EMLDSSSEAA IETSDKSQLT DQPVQENKTT AISRHESPET EVPPSLITPT TPTASIEKLA
TTPSGRSRTE REQRSGNTLY QELSFQDADA LGEMDEGADI TGSLVHPGEY ASSVNDNFFG
MGKEVENLIM ENNELLATKN ALNVVKDDLI VKVDELTSEQ EILREEVRGL QQARERLRQR
IVALEEELKK VKEEAEAAAK ATKSDDEEDV PLSQRKRFTR VEMARVLMER NQYKERFMEL
QEAVRWTEMI RASKTDPSSI SGGKGSVWKF FSNLFTGPAD RGTLVRSTHT LPHVRSSEKL
VARRASERRE QYRQVRAHVK KEDGRLQAYG WSLPGKPSAP VRQPPVPVPV YCRPLQETEP
GMKIWCGAGV NLSSGKTRDG RCMVGGSVFY AAEAQETSNV KTEAEDAVEH LDKELQESEN
RRLEAERWEQ QLSSLVWICT STQKMSKVTV IDANNPADVL EVFNVCQGHL LCIASVPGAK
ESDYAQFSNE NSIRNSNGTI NDSENNNGAC EDVTNGNENT EQNGQKNHQD TETAVDKNKS
EFDNQSEDQA NENTEKSAET DQNSTNEPQS LESIDSETAN LGKVNFIRCN AEASLRSNDK
DAVNEEAKEE VVEETPIEKM SSIQPTMWLG AQNGAVFVHS AVAKWSMCLH SVKLRDAALS
IVHVQGRVLV ALADGTVTIF RRGIDGQWDL SQYHVITLGS PQHSIRCMTA VSGKTVWCGY
RNKIHVIDPI SMTLECTVDA HPRKESQVRQ LAWLGDGVWV SIRLDSTLRL YHAHTYQHLQ
DVDIEPYVSK MLGTGKLGFS FVRITALLIS SNRLWIGTGN GVIISVPLSE SAGGSMAVAR
AQTGNNKSDA PGVGVRIFAS ERGVTPGSFV PYCSMAHAQL SFHGHRDAVK MFVAVPGHGG
QSAVTDGTQP AMLVLSGGEG YIDFRVADEA EDESDVATHL IVWQMVRYAP REKQEVCRFL
YLDLNEHFSV LTKSLLIGDG EETEESMDRS NTAVSNEEHG EQSHLIVWQV QCPLPMPVNG
//