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Database: UniProt
Entry: A0A1S3R6E6_SALSA
LinkDB: A0A1S3R6E6_SALSA
Original site: A0A1S3R6E6_SALSA 
ID   A0A1S3R6E6_SALSA        Unreviewed;      1351 AA.
AC   A0A1S3R6E6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=C-Jun-amino-terminal kinase-interacting protein 3 isoform X12 {ECO:0000313|RefSeq:XP_014047696.1};
GN   Name=mapk8ip3 {ECO:0000313|RefSeq:XP_014047696.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014047696.1};
RN   [1] {ECO:0000313|RefSeq:XP_014047696.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014047696.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the JIP scaffold family.
CC       {ECO:0000256|ARBA:ARBA00009866}.
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DR   RefSeq; XP_014047696.1; XM_014192221.1.
DR   OrthoDB; 3685563at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa03.
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:SF3; C-JUN-AMINO-TERMINAL KINASE-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|RefSeq:XP_014047696.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Transferase {ECO:0000313|RefSeq:XP_014047696.1}.
FT   DOMAIN          6..94
FT                   /note="RH1"
FT                   /evidence="ECO:0000259|PROSITE:PS51776"
FT   DOMAIN          516..587
FT                   /note="RH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51777"
FT   REGION          178..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          241..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          489..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          739..781
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          876..983
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1308..1329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          60..161
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        178..192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..280
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        757..780
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1351 AA;  149108 MW;  BBE12413A0DD3E25 CRC64;
     MMEIDEVVYQ DDYGSVSVMS ERVSGLANSI YREFERLISS YDEEVVKELM PLVVNVLENL
     DSVLTENQEH EVELELLKED NEQLITQYER EKALRKQAEE KFIEFEDALE GEKKDLQTHV
     ESLELQGKQL ELKTKNYSDQ ITRLEERESD MKKEYNALHQ RHTEMIQTYV EHIERSKMQQ
     AGNNSQSEGP GSGRTKVERP PSLSLYPSGE GMGMVRGGLG GARMPGSGTN VWQVSELSQS
     RYTSGYQEDG SESDSVAATP SSTGSKSNTP TSSVPSATVT PLNEGFLPPG EFDPIHAVSR
     GRKSAKRLSR NMEVQVSQET RNVSIGMGSS DEWSEFQEII DSTPELDMCV DPRLYGGGNS
     PSQGIVNEAF GINTDSLYHE IKDAKSDIIG DVDAGAELLG EFSVRDDFFG MGKEVENLLT
     ENKHLLETKN ALNIVKNDLI AKVDELSGEH EVLREELEAL RTAKKKVDTK VKELEEELKR
     LRAEALTLGA SQDSKDEGGE DYSSPMVDGD VTMTQRRRFT RVEMARVLME RNQYKERLME
     LQEAVRWTEM IRASRESPQM QEKKKSTIWQ FFARLFSSSA SPPPVKRPYY SVNIHYKSPS
     PAGFPQRRSH TMCQISTSNR TLEFFPEDDS ALSARREQRR EQYRQVREHM RRDDGIMQAC
     GWSVPPRFKQ TGAQLDSALE GPLKKQQANE KEDNRMKNVP VPVYCRPLVE KDPNRKLWCA
     AGVDLTGWKT CTQEIMTVKA GPGNSVTNPL AIEEGEGGDG KSNHSSPEKR KSKELHETDT
     MSSRVWILTS THSASKVVII DANQPGSLVD QFNVCNAHVL CISSVPAASE SDYPAGEIVL
     DSGEGGGEET GGVEGMLAGI TLVGCATNCS VVRSNCSSRT DTPVLDRGQA PTAPPLSGKL
     HPTQSAEEAT EATEVAEPAA SETDDTLGPP GPFMEHVFTD PQPPVVDAGQ YDRCAGQSKE
     ESNSPPQETE DGSDDPKAGT SVAPTMWLGA QNGWLYVHSA VANWKKCLHS IKLKDSVLSL
     VHVKGRVLVA LADGTLAIFH RSEDGQWDLS NYHLMDLGRP HHSIRCMAMV HDKVWCGYKN
     KIHVIQPKSM QIEKSFDAHP RRESQVRQLA WIGDGVWVSI RLDSTLRLYH ALTHQHLQDV
     DIEPYVSKML GTGKLGFSFV RITALLIGGN RLWVGTGNGV VISIPLTETV VLHRGQLLGL
     RANKVSPTSS GGVAGGVIHV YADDNPEKSS GSFIPYCSMA QAQLCFHGHR DAVKFFVSVP
     GNVLATLNGS VLDSPSEGQG SSAQPEAETQ SVHNVLVLSG GEGYIDFRIG DGEDDETEEG
     EVPGGAPQMK PAVCKAERSH IIVWQVSYVP E
//
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