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Database: UniProt
Entry: A0A2D0S859_ICTPU
LinkDB: A0A2D0S859_ICTPU
Original site: A0A2D0S859_ICTPU 
ID   A0A2D0S859_ICTPU        Unreviewed;      1294 AA.
AC   A0A2D0S859;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=C-Jun-amino-terminal kinase-interacting protein 4 isoform X3 {ECO:0000313|RefSeq:XP_017338929.1};
GN   Name=spag9b {ECO:0000313|RefSeq:XP_017338929.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017338929.1};
RN   [1] {ECO:0000313|RefSeq:XP_017338929.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017338929.1};
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_017338929.1; XM_017483440.3.
DR   STRING; 7998.ENSIPUP00000008624; -.
DR   GeneID; 108273832; -.
DR   KEGG; ipu:108273832; -.
DR   CTD; 100333761; -.
DR   OrthoDB; 3685563at2759; -.
DR   Proteomes; UP000221080; Chromosome 13.
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_017338929.1};
KW   Transferase {ECO:0000313|RefSeq:XP_017338929.1}.
FT   DOMAIN          6..94
FT                   /note="RH1"
FT                   /evidence="ECO:0000259|PROSITE:PS51776"
FT   DOMAIN          483..554
FT                   /note="RH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51777"
FT   REGION          209..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          792..822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          864..890
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1217..1237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          60..161
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          428..511
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          713..740
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        227..242
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..298
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        804..822
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..888
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1294 AA;  143305 MW;  BA48B8515F537899 CRC64;
     MELEDGVLYQ EDSGSSSMMS ERVSGLASSI YREFERLIRK YDEDVVKELM PLVVAVLENL
     DSVFAENQEH EVELELLKED NEQLVTQYER EKALRKGVEE RYMEIEDLQD QERKELQSKV
     TTLEGLTRQL ELKTKNYADQ IGRVEEREAE LKKEYNALHH RHTEMIHSYM EHLERTKMQQ
     LAGGEPTDTS TMSRHRKERP VSLGIFQLQG DVRTPELQRE QAATPGTDAW RFNNLSHPHS
     NTSLKDELSD ANRGGSKSAL PMSTAPSDAA SASVAVSQAE ESEGLNRNLN SSSRKPDSSK
     NIKVQEAVAT EVLPKDVLEN TEKSEVQAII ESTPELDMDL SGCKGSSTPA KGIENMAFDR
     NTDSLFEELS SAGTDLIGDV DEGADLLGMG REVEHLIQEN AQLLETKNTL NIVKNDLLGR
     VDQLTCDKEV LHGEMEVLKQ AKDKLEEKNK ELEEEIKRVR AELEVAKQKT KEEDDSDVPT
     AQRKRFTRVE MARVLMERNQ YKERLMELQE AVRWTEMIRA SRENPTLTEK KKSSIWQFFS
     RLFSSSSSSA AKKPEAPVNV KYNAPTSHIV PSVKKRSSTL AQLPSDKSKA FDFLNDDPEV
     ENIVSRREQK RAQYQQVKAH VQKEDGRIQA CGWSLPQKYK VSNAQADSKV KNLPVPVYLR
     PLDEKDASMK LWCAAGVNLS GGKTRDGGSI VGASVFYRDV SAPESGGLSP RLARGSRSSL
     DKLEQELKEQ EKELRQQDEL SSLVWICTST HTTSKVIVID ANQPGKILES FFVCNSHLLC
     ITSVPGARET DYPAGEEVSA NSQAGGAEGA SHTGTAANSS VAGSERVLDG ITVVGCSVEG
     AVAVSQTAGT DSVDADVLEQ RRQPGVAAAE EALEATESSN TTPAEESQPG IYTEHVFTDP
     LGVQNNRDPL SSYTQRECDL VKDGVSLIPE EQDLMREEAN KMSSVLPTMW LGAQNGCIYV
     HSSVAQWKKC LHSIKLKDSI LGIVHVKGRV LVALADGTLA IFHRGVDGQW DLTNYHLLDL
     GRPHHSIRCM TVVHDKVWCG YRNKIYVIQP KAMKIEKSFD AHPRKESQVR QLAWDGDGIW
     VSIRLDSTLR LFHAHTFQHL QDVDIEPYVS KMLGTGKLGF SFVRITALMV SCNRLWVGTG
     NGVIISIPLT ETKTVTQGTS NRPGSVIRVY GDENSDKVTA GTFVPFCSMA HAQLCFHGHR
     DAVKFFTAVP GHVVPSAGAG GEAGGDKPTA DSPTPEFSKS VLVMSGGEGY IDFRMGDEGG
     EGEDLSEPAL KLQPFLAKAE RSHLIVWQVM VNGD
//
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