ID   A0A2U4C3D0_TURTR        Unreviewed;      1307 AA.
AC   A0A2U4C3D0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=C-Jun-amino-terminal kinase-interacting protein 4 isoform X6 {ECO:0000313|RefSeq:XP_019799919.1};
GN   Name=SPAG9 {ECO:0000313|RefSeq:XP_019799919.1};
OS   Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Delphinidae; Tursiops.
OX   NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019799919.1};
RN   [1] {ECO:0000313|RefSeq:XP_019799919.1}
RP   IDENTIFICATION.
RC   TISSUE=Spleen {ECO:0000313|RefSeq:XP_019799919.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the JIP scaffold family.
CC       {ECO:0000256|ARBA:ARBA00009866}.
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DR   RefSeq; XP_019799919.1; XM_019944360.2.
DR   GeneID; 101332661; -.
DR   OrthoDB; 3685563at2759; -.
DR   Proteomes; UP000245320; Chromosome 20.
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:SF2; C-JUN-AMINO-TERMINAL KINASE-INTERACTING PROTEIN 4; 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|RefSeq:XP_019799919.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245320};
KW   Transferase {ECO:0000313|RefSeq:XP_019799919.1}.
FT   DOMAIN          7..95
FT                   /note="RH1"
FT                   /evidence="ECO:0000259|PROSITE:PS51776"
FT   DOMAIN          486..557
FT                   /note="RH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51777"
FT   REGION          207..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          549..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          840..892
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1226..1250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          75..162
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          713..740
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        222..241
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..586
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1307 AA;  144839 MW;  F9779E7720322FE7 CRC64;
     MELEDGVVYQ EEPGGSGAVM SERVSGLAGS IYREFERLIG RYDEEVVKEL MPLVVAVLEN
     LDSVFAQDQE HQVELELLRD DNEQLITQYE REKALRKHAE EKFIEFEDSQ EQEKKDLQTR
     VESLESQTRQ LELKAKNYAD QISRLEEREA ELKKEYNALH QRHTEMIHNY MEHLERTKLH
     QLSGGDQLES TAHSRIRKER PISLGIFPLP AGDGLLTPDT QKGGETPGSE QWKFQELSQP
     RSHTSLKDEL SDVSQGGSKA TTPASTTASD VAAIPSDTPL HEENEGFVKV ADTPDKLERS
     KHIEVQVVQE TRNVSTDSAE NEEKSEVQAI IESTPELDMD KDLSGYKGSS TPTKGIENKA
     FDRNTESLFE ELSSAGSGLI GDVDEGADLL GMGREVENLI LENTQLLETK NALNVVKNDL
     IAKVDELTCE KDVLQGELEA VKQAKLKLEE KNRELEEELR KARAEAEDAR QKAKDDDDSD
     IPTAQRKRFT RVEMARVLME RNQYKERLME LQEAVRWTEM IRASRENPAM QEKKRSSIWQ
     FFSRLFSSSS NTTKKPEPPV NLKYNAPTSH VTPSVKKRSS TLSQLPGDKS KAFDFLSEET
     EASLASRREQ KREQYRQVKA HVQKEDGRVQ AFGWSLPQKY KQVTNGQGEN KMKNLPVPVY
     LRPLDEKDTS MKLWCAVGVS LSGGKTRDGG SVVGASVFYK DVAGLDAEGS EQRSASQSSL
     DKLDQELKEQ QKELKNQEEL SSLVWICTST HSATKVIIID AVQPGNILDS FTVCNSHVLC
     IASVPGARET DYPAGEELSE SGQVDKASLC GSMTSNSSAE TDSLLGGITV VGCSTEGVTA
     AATSPSTNGT SPVIEKPPEK ETENSEVDEN VPTAEEATEA TEGNAGSAED TVDISQTGVY
     TEHVFTDPLG VQIPEDLSPV YQSSNDSDAY KDQISVLQNE QDLMREEAQK MSSLLPTMWL
     GAQNGCLYVH SSVAQWRKCL HSIKLKDSIL SIVHVKGIVL VALADGTLAI FHRGVDGQWD
     LSNYHLLDLG RPHHSIRCMT VVHDKVWCGY RNKIYVVQPK AMKIEKSFDA HPRKESQVRQ
     LAWVGDGVWV SIRLDSTLRL YHAHTYQHLQ DVDIEPYVSK MLGTGKLGFS FVRITALMVS
     CNRLWVGTGN GVIISIPLTE TNKTSGASGN RPGSVIRVYG DENSDKVTPG TFIPYCSMAH
     AQLCFHGHRD AVKFFVAVPG QVISPQSGSS GTDLTVDRAG PSAQEPGSQT PLKSMLVISG
     GEGYIDFRMG DEGGESELLG EDLPLEPSVA KAERSHLIVW QVMYGSE
//