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Database: UniProt
Entry: A0A1S3A203_ERIEU
LinkDB: A0A1S3A203_ERIEU
Original site: A0A1S3A203_ERIEU 
ID   A0A1S3A203_ERIEU        Unreviewed;      1325 AA.
AC   A0A1S3A203;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=C-Jun-amino-terminal kinase-interacting protein 3 isoform X3 {ECO:0000313|RefSeq:XP_007528073.1};
GN   Name=MAPK8IP3 {ECO:0000313|RefSeq:XP_007528073.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007528073.1};
RN   [1] {ECO:0000313|RefSeq:XP_007528073.1}
RP   IDENTIFICATION.
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_007528073.1; XM_007528011.2.
DR   CTD; 23162; -.
DR   OrthoDB; 3685563at2759; -.
DR   Proteomes; UP000079721; 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; 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_007528073.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW   Transferase {ECO:0000313|RefSeq:XP_007528073.1}.
FT   DOMAIN          11..99
FT                   /note="RH1"
FT                   /evidence="ECO:0000259|PROSITE:PS51776"
FT   DOMAIN          513..587
FT                   /note="RH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51777"
FT   REGION          181..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          718..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          872..954
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1245..1266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          65..166
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          441..489
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        243..285
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        728..751
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        876..897
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1325 AA;  146074 MW;  C2181325B0B95D43 CRC64;
     MMEIQMDESG VAVYQDDYGP GSVMSERVSG LAGSIYREFE RLIRCYDEEV VKELMPLVVT
     VLENLDAVLG ENQEHEVELE LLREDNEQLL TQYEREKALR KQAEEKFIEF EDALEQEKKE
     LQVQVEHYEL QTRQLELKAK NYADQISRLE EREAEMKKEY NALHQRHTEM IQTYVEHIER
     SKMQQVGGNS QTESSLPGRR KERPTSLNVF PLADGMVRAQ MGGQLVPAGD HWHLSDLGQL
     QFSSSYQGPN DEMSESGQSS AAATPSTTGT KSNTPTSSVP SAAVTPLNEC LQPPGDYAGG
     PKNGRRAREK RNSRNMEVQV TQEMRNVSIG MGSSDEWSDV QDIIDSTPEL DVVREPRLDR
     TGNSPTQGIV NKAFGINTDS LYHELSTAGS EVIGDVDEGA DLLGEFSGMG KEVGNLLLEN
     SQLLETKNAL NVVKNDLIAK VDQLSGEQEV LKGDLEAARQ AKLRLESRIK DLEEELRRVK
     SEAITARREP KEEVEDVSSS LCTELDKIPM AQRRRFTRVE MARVLMERNQ YKERLMELQE
     AVRWTEMIRA SREHPSVQEK KKSTIWQFFS RLFSSSSSPP PAKRSYPSVN IHYKSPTTAG
     FSQRRNHAMC QIAGSRPLEF FPDDDCTSSA RREQKREQYR QVREHVRNDD GRLQACGWSL
     PAKYKQLSPN GGQEDTRMKN VPVPVYCRPL VEKDPTMKLW CAAGVNLSGW RPIEEDPAAT
     VKSVPGRDPL TCDREAEGEP KSSHTSPEKK VKELVEADAT CSRVWVLTST LTTSKVVIID
     ANQPGTVVDQ FTVCNAHVLC ISSIPAASDS DYPPGEIFLD SDVNPEDSGA DGVLAGITLV
     GCATRCNVPR SNCSSRGDTP VLDKSRGEVA AVANGKVNPA QSTEEATEAT EVPDSGSSEA
     DTAAVRPGPL TEHVFTDPTP TPTPSAPPGS EPEVEMSGAP PEQEPSAEPA GPCSSAAPTM
     WLGAQNGWLY VHSAVANWNK CLHSIKLKDS VLSLVHVKGR VLVALADGTL AIFHRGEDGQ
     WDLSNYHLMD LGHPHHSIRC MAVVYDRVWC GYKNKVHVIQ PKTMQIEKSF DAHPRRESQV
     RQLAWIGDGV WVSIRLDSTL RLYHAHTHQH LQDVDIEPYV SKMLGTGKLG FSFVRITALL
     IAGNRLWVGT GNGVVISIPL TETVVLHRGQ LLGLRANKTS PTSGEGARPG GVIHVYGDDP
     SDKSASSFIP YCSMAQAQLC FHGHRDAVKF FVSVPGNVLA TLNGSVLDSP SEGPGPAAPA
     SDPESQKLKS ALVLSGGEGY IDFRIGDGED DEAEESVGDI GQVKPVLSKA ERSHIIVWQV
     SYAPE
//
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