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Database: UniProt
Entry: A0A2U3VKG0_ODORO
LinkDB: A0A2U3VKG0_ODORO
Original site: A0A2U3VKG0_ODORO 
ID   A0A2U3VKG0_ODORO        Unreviewed;      1177 AA.
AC   A0A2U3VKG0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=C-Jun-amino-terminal kinase-interacting protein 4 isoform X5 {ECO:0000313|RefSeq:XP_004395262.1};
GN   Name=SPAG9 {ECO:0000313|RefSeq:XP_004395262.1};
OS   Odobenus rosmarus divergens (Pacific walrus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC   Odobenus.
OX   NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004395262.1};
RN   [1] {ECO:0000313|RefSeq:XP_004395262.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_004395262.1; XM_004395205.1.
DR   AlphaFoldDB; A0A2U3VKG0; -.
DR   GeneID; 101380648; -.
DR   CTD; 9043; -.
DR   OrthoDB; 3685563at2759; -.
DR   Proteomes; UP000245340; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; 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; 1.20.5.1000; 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; 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; PF19056; WD40_2; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS51777; RH2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Kinase {ECO:0000313|RefSeq:XP_004395262.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245340};
KW   Transferase {ECO:0000313|RefSeq:XP_004395262.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          343..414
FT                   /note="RH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51777"
FT   REGION          94..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          319..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          646..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          697..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1093..1122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          570..597
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        106..127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..443
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        658..675
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1093..1120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1177 AA;  128636 MW;  7BC4B877FDA777BD CRC64;
     MSPGCMLLFV FGFVGGAVVI NSAILVSLSV LLLVHFSIST GVPALTQNLP RILRKERPIS
     LGIFPLPAGD GLLTPDTQKG GETPGSEQWK FQELSQPRSH TSLKDELSDV SQGGSKATTP
     ASTAASDVAT LPTDTPLKED NEGFVKVADT PNKSEISKHI EVQVAQETRN VSTGSAENEE
     KSEVQAIIES TPELDMDKDL SGYKGSSTPT KGIENKAFDR NTESLFEELS SAGSGLIGDV
     DEGADLLGMG REVENLILEN TQLLETKHAL NVVKNDLIAK VDELTCEKDV LQGELEAVKL
     AKLKLEEKNK ELEEELRKAR AEAEDARQKA KDDDDSDIPT AQRKRFTRVE MARVLMERNQ
     YKERLMELQE AVRWTEMIRA SRENPAMQEK KRSSIWQFFS RLFSSSSNTT KKPEPPVNLK
     YNAPTSHVTP SVKKRSSTLS QLPGDKSKAF DFLSEETEAS LASRREQKRE QYRQVKAHVQ
     KEDGRVQAFG WSLPQKYKQV TNGQGENKMK NLPVPVYLRP LDEKDTSMKL WCAVGVNLSG
     GKTRDGGSVV GASVFYKDVA GLDTEGSKQR SASQSSLDKL DQELKEQQKE LKNQEELSSL
     VWICTSTHSA TKVIIIDAIQ PGNILDSFTV CNSHVLCIAS VPGARETDYP AGEESSESGQ
     VDKASLCGSM TSNSSAETDS LLGGITVVGC STESVTAAAT SPSTNGASPV MEKPPEKEAE
     NSEVDENIPT AEEATEATEG NAGSAEDTVD ISQPGVYTEH VFTDPLGVQI PEDLSPVYQS
     SNDSDAYKDQ LSVLPNEQDL VREEAQKMSS LLPTMWLGAQ NGCLYVHSSV AQWRKCLHSI
     KLKDSILSIV HVKGIVLVAL ADGTLAIFHR GVDGQWDLSN YHLLDLGRPH HSIRCMTVVH
     DKVWCGYRNK IYVVQPKAMK IEKSFDAHPR KESQVRQLAW VGDGVWVSIR LDSTLRLYHA
     HTYQHLQDVD IEPYVSKMLG TGKLGFSFVR ITALMVSCNR LWVGTGNGVI ISIPLTETVI
     LHQGRLLGLR ANKTSGATGN RPGSVIRVYG DENSDKVTPG TFIPYCSMAH AQLCFHGHRD
     AVKFFVAVPG QVVSPQSGSS DTDLTGDKAG PSTQEPGSQM PLKSMLVISG GEGYIDFRMG
     DEGGESELLG EDLPLEPSVA KAERSHLIVW QVMYGSE
//
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