ID A0A3P8QX19_ASTCA Unreviewed; 1297 AA.
AC A0A3P8QX19;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=C-Jun-amino-terminal kinase-interacting protein 4-like {ECO:0000313|Ensembl:ENSACLP00000034230.1};
GN Name=SPAG9 {ECO:0000313|Ensembl:ENSACLP00000034230.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000034230.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000034230.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000034230.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the JIP scaffold family.
CC {ECO:0000256|ARBA:ARBA00009866}.
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DR Ensembl; ENSACLT00000035043.1; ENSACLP00000034230.1; ENSACLG00000023098.1.
DR GeneTree; ENSGT00940000153496; -.
DR Proteomes; UP000265100; Chromosome 8.
DR Bgee; ENSACLG00000023098; Expressed in anal fin and 8 other cell types or tissues.
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: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}.
FT DOMAIN 6..94
FT /note="RH1"
FT /evidence="ECO:0000259|PROSITE:PS51776"
FT DOMAIN 563..669
FT /note="RH2"
FT /evidence="ECO:0000259|PROSITE:PS51777"
FT REGION 175..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 67..161
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 492..591
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 790..817
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 230..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..951
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1297 AA; 143035 MW; 38F5BE96F010A96E CRC64;
MELDDVVLYQ DDSGNSTMMS ERVSGLASSI YREFERLIEK YDEDVVKELM PLVVAVLENL
DSVFAVNQEH EVELELLKED NEQLVTQYER EKALRKNTEE RYIALEDSQD GEKKDLQCRL
VTLESHTRQL ELKTRNYADQ ISRLEEREAE LKKEYNALHQ RHTEMIHSYM EHLERTKHQH
AAMTAEPSDT GTSVRTRKER PVSMGLFQLP AAEGMTPDLH REPVDTPSEP WRFNNLSHPR
SNTSLKDELS QLNCGSSRSN TQTNQGSVSK NGTPVSLQDG GSKSTTPSLG GASKSNTPTS
NYSNNSQSTT PLSPFDGGST GMSPMSSLGR GSASDVAMES VDTPLKDQET SDGHNKNLDR
SSGKPESNKN IAAVQEGQQK GPESDTTPLK EDDGADSLEK SEVQAIIEST PELDMDLAGC
RGTSTPTKGG VENLAFDRNT DSLFEELSSA GNDLIGDVDE GADLLGMGRE VEHLIHENTQ
LLETKNALNV VKNDLISRVD ELSCEKEVLQ GELNAVTHAK TKLEEKNKEL EEELKKVRAE
LDEAKQKVKN DNEDDSDVPT AQRKRFTRVE MARVLMERNQ YKERLMELQE AVRWTEMIRA
SKENPTLPEK KKSSLWQFFS RLFSSSGGGA KKPAAEAPVN VKYNAPTSQI QPSVKKKSST
LQQLPSDKSK AFDFLNEEAP ADSVVSRREQ KRAQYQQVKA HVQKEDGRLQ AYGWSLPKKY
KANGGQAESK MKSLPVPVFL RPLDEKDASM KLWCATCVNL SGGKTRDGGS IVGASVFYSD
VSGPESPKKK VGSQSSLDKL DQELRDQQKE QRHQEELSSL VWICTTTKST TKAVVIDANQ
PGNILEGFFV CNSHILCIAS VPGARETDYP AGEEVPPNSE VGPVGDGNSS ATSTSSTGGD
SVLGGITVVG CEAEGVTAVP QTAGKDGEAE SRPAEEATEA TETSAESADQ RESLREIYTE
HVFTDPLGAQ HKVETPANYS QRESDLLKDG VSLNPSAEEQ DLMREEAQKM SSVLPTMWLG
AQNGYVYVHS SVAQWKKCLH SIKLKDSVLG IVHVKGRVLV GLSDGTLAIF HRGVDGQWDL
TNYHLLDLGR PHHSIRCMTV VHDKVWCGFR NKIYVVQPKA MKIEKSFDAH PRKDSQVRLL
AWDGDGIWVS IRLDSTLRLF HAHTYQHLQD VDIEPYVSKM LGTGKLGFSF VRITALMVSC
NRLWIGTGNG VIISIPLTEG HAAASASCAG EAAGDKAADA TTQEGTKCML VMSGGEGYID
FRMGDEDGEM EEAEDAPIKL QPKAERSHLI VWQVTQD
//