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Database: UniProt
Entry: A0A2Y9KFJ6_ENHLU
LinkDB: A0A2Y9KFJ6_ENHLU
Original site: A0A2Y9KFJ6_ENHLU 
ID   A0A2Y9KFJ6_ENHLU        Unreviewed;      1315 AA.
AC   A0A2Y9KFJ6;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=C-Jun-amino-terminal kinase-interacting protein 3 isoform X7 {ECO:0000313|RefSeq:XP_022372286.1};
GN   Name=LOC111156025 {ECO:0000313|RefSeq:XP_022372286.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022372286.1};
RN   [1] {ECO:0000313|RefSeq:XP_022372286.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022372286.1};
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_022372286.1; XM_022516578.1.
DR   Proteomes; UP000248482; Unplaced.
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; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR034743; RH1.
DR   InterPro; IPR034744; RH2.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_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; SSF50998; Quinoprotein alcohol dehydrogenase-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_022372286.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW   Transferase {ECO:0000313|RefSeq:XP_022372286.1}.
FT   DOMAIN          12..100
FT                   /note="RH1"
FT                   /evidence="ECO:0000259|PROSITE:PS51776"
FT   DOMAIN          500..574
FT                   /note="RH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51777"
FT   REGION          183..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          699..747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          858..947
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1275..1294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          66..167
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          437..528
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        246..288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..316
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        716..745
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        861..877
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1315 AA;  144742 MW;  B68ABCAF6A5A4FEF CRC64;
     MMEIQMDEGG GVVVYQDDYC SGSVMSERVS GLAGSIYREF ERLIHCYDEE VVKELMPLVV
     NVLENLDSVL SENQEHEVEL ELLREDNEQL LTQYEREKAL RKQAEEKFIE FEDALEQEKK
     ELQTQVEHYE FQTRQLELKA KNYADQISRL EERESEMKKE YNALHQRHTE MIQTYVEHIE
     RSKMQQVGGN SQTEGSLPGR SRKERPTSLN VFPLADGMVR AQMGGKLVPA GDHWHLSDLG
     QFSSSYQCPQ DDMSESGQSS AAATPSTTGT KSNTPTSSVP SAAVTPLNES LQPLGDYGAG
     TKGSKRAREK RNSRNMEVQV TQEMRNVSIG MGSSDEWSDV QDIIESTPEL DMSREPRLDR
     MGNSPTQGIV NKAFGINTDS LYHELSTAGS EVIGDVDEGA DLLGMGKEVG NLLLENSQLL
     ETKNALNVVK NDLIAKVDQL SGEQEVLKGD LEAARQAKLR LEGRVKDLEE ELRRVKSEAI
     VARREPKEEV EDDKVPLAQR RRFTRVEMAR VLMERNQYKE RLMELQEAVR WTEMIRASRE
     HPSVQEKKKS TIWQFFSRLF SSSSSPPPAK RPYPSVNIHY KSPTTAGFSQ RRGHAMCPMS
     AGSRPLEFFP DDDCTSSARR EQKREQYRQV REHVRNDDGR LQACGWSLPA KYKQLSPNGG
     QEDTRMKNVP VPVYCRPLVE KDPTMKLWCA AGVNLSGWKP GEDDSGNGVK PVPGRDPLTC
     DREVEGETKS DHTSPEKKAK ELPEPDAASS RVWILTSTLT TSKVVIIDAN QPGTVVDQFT
     VCNAHVLCIS SIPAASDSDY PPGEIFLDGD VNPEDSSADG VLAGITLVGC ATRCNVPRSN
     CSSRGDTPVL DKGQGEVATV ANGKVNPSQS TEEATEATEV PDSGPSEAEA AAVRPGPLTE
     HVFTDLAPSP APTAQPGSEN GPEADTGGAQ PEPEPSADPA GASSSAAPTM WLGAQNGWLY
     VHSAVANWKK CLHSIKLKDS VLSLVHVKGR VLVALADGTL AIFHRGEDGQ WDLSNYHLMD
     LGHPHHSIRC MAVVCDRVWC GYKNKVHVIQ PKTMQIEKSF DAHPRRESQV RQLAWIGDGV
     WVSIRLDSTL RLYHAHTHQH LQDVDIEPYV SKMLGTGKLG FSFVRITALL IAGNRLWVGT
     GNGVVISIPL TETVVLHRGQ LLGLRANKTS PTAGEGARPG GVIHVYGDDS CDKSASSFIP
     YCSMAQAQLC FHGHRDAVKF FVSVPGNVLA TLNGSVLDSP SESPGPAAPA SDAEGQKLKN
     VLVLSGGEGY IDFRIGDGED DDTEENNGDM SQVKPLLSKA ERSHIIVWQV SYSPE
//
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