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JIP3 protein

 JIP3_RAT                Reviewed;        1322 AA.
E9PSK7; B0VXR4;
18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
03-APR-2013, sequence version 2.
10-OCT-2018, entry version 55.
RecName: Full=C-Jun-amino-terminal kinase-interacting protein 3;
Short=JIP-3;
Short=JNK-interacting protein 3;
AltName: Full=JNK MAP kinase scaffold protein 3;
Name=Mapk8ip3; Synonyms=Jip3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH MAPK10.
STRAIN=Sprague-Dawley; TISSUE=Heart;
PubMed=21076496; DOI=10.1139/y10-088;
Xu B., Zhou Y., Karmin O., Choy P.C., Pierce G.N., Siow Y.L.;
"Regulation of stress-associated scaffold proteins JIP1 and JIP3 on
the c-Jun NH2-terminal kinase in ischemia-reperfusion.";
Can. J. Physiol. Pharmacol. 88:1084-1092(2010).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[3]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NTRK2 AND KLC1.
PubMed=21775604; DOI=10.1523/JNEUROSCI.0436-11.2011;
Huang S.H., Duan S., Sun T., Wang J., Zhao L., Geng Z., Yan J.,
Sun H.J., Chen Z.Y.;
"JIP3 mediates TrkB axonal anterograde transport and enhances BDNF
signaling by directly bridging TrkB with kinesin-1.";
J. Neurosci. 31:10602-10614(2011).
[4]
INTERACTION WITH SH3RF2.
PubMed=22128169; DOI=10.1074/jbc.M111.269431;
Wilhelm M., Kukekov N.V., Schmit T.L., Biagas K.V., Sproul A.A.,
Gire S., Maes M.E., Xu Z., Greene L.A.;
"Sh3rf2/POSHER protein promotes cell survival by RING-mediated
proteasomal degradation of the c-Jun N-terminal kinase scaffold POSH
(Plenty of SH3s) protein.";
J. Biol. Chem. 287:2247-2256(2012).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23576431; DOI=10.1074/jbc.M113.464453;
Sun T., Yu N., Zhai L.K., Li N., Zhang C., Zhou L., Huang Z.,
Jiang X.Y., Shen Y., Chen Z.Y.;
"c-Jun NH2-terminal kinase (JNK)-interacting protein-3 (JIP3)
regulates neuronal axon elongation in a kinesin- and JNK-dependent
manner.";
J. Biol. Chem. 288:14531-14543(2013).
[7]
FUNCTION.
PubMed=25944905; DOI=10.1074/jbc.M115.651885;
Watt D., Dixit R., Cavalli V.;
"JIP3 activates kinesin-1 motility to promote axon elongation.";
J. Biol. Chem. 290:15512-15525(2015).
-!- FUNCTION: The JNK-interacting protein (JIP) group of scaffold
proteins selectively mediates JNK signaling by aggregating
specific components of the MAPK cascade to form a functional JNK
signaling module. May function as a regulator of vesicle
transport, through interactions with the JNK-signaling components
and motor proteins (By similarity). Promotes neuronal axon
elongation in a kinesin- and JNK-dependent manner. Activates
cofilin at axon tips via local activation of JNK, thereby
regulating filopodial dynamics and enhancing axon elongation. Its
binding to kinesin heavy chains (KHC), promotes kinesin-1 motility
along microtubules and is essential for axon elongation and
regeneration. Regulates cortical neuronal migration by mediating
NTRK2/TRKB anterograde axonal transport during brain development.
Acts as an adapter that bridges the interaction between NTRK2/TRKB
and KLC1 and drives NTRK2/TRKB axonal but not dendritic
anterograde transport, which is essential for subsequent BDNF-
triggered signaling and filopodia formation.
{ECO:0000250|UniProtKB:Q9ESN9, ECO:0000269|PubMed:21076496,
ECO:0000269|PubMed:21775604, ECO:0000269|PubMed:23576431,
ECO:0000269|PubMed:25944905}.
-!- SUBUNIT: Forms homo- or heterooligomeric complexes. The central
region of MAPK8IP3 interacts with the C-terminal of MAPK8IP2 but
not MAPK8IP1. Binds specific components of the JNK signaling
pathway namely MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3 to the N-
terminal region, MAP2K4/MKK4 and MAP2K7/MKK7 to the central region
and MAP3K11 to the C-terminal region. Binds the TPR motif-
containing C-terminal of kinesin light chain, KLC1. Pre-assembled
MAPK8IP1 scaffolding complexes are then transported as a cargo of
kinesin, to the required subcellular location. Interacts with
ROCK1 and this interaction is enhanced by ultraviolet-B (UVB)
radiation (By similarity). Interacts with SH3RF2
(PubMed:22128169). Interacts with NTRK3/TRKC (By similarity).
Interacts with NTRK2/TRKB (PubMed:21775604).
{ECO:0000250|UniProtKB:Q9ESN9, ECO:0000250|UniProtKB:Q9UPT6,
ECO:0000269|PubMed:21076496, ECO:0000269|PubMed:21775604,
ECO:0000269|PubMed:22128169}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ESN9}.
Golgi apparatus {ECO:0000250|UniProtKB:Q9ESN9}. Cytoplasmic
vesicle {ECO:0000250|UniProtKB:Q9ESN9}. Cell projection, growth
cone {ECO:0000250|UniProtKB:Q9ESN9}. Cell projection, axon
{ECO:0000269|PubMed:21775604, ECO:0000269|PubMed:23576431}. Cell
projection, dendrite {ECO:0000269|PubMed:21775604}. Cytoplasm,
perinuclear region {ECO:0000269|PubMed:21775604}. Note=Localized
in the soma and growth cones of differentiated neurites and the
Golgi and vesicles of the early secretory compartment of
epithelial cells. KIF5A/B/C-mediated transportation to axon tips
is essential for its function in enhancing neuronal axon
elongation. {ECO:0000250|UniProtKB:Q9ESN9,
ECO:0000269|PubMed:23576431}.
-!- PTM: Phosphorylation by ROCK1 is crucial for the recruitment of
JNK. {ECO:0000250|UniProtKB:Q9UPT6}.
-!- SIMILARITY: Belongs to the JIP scaffold family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; DQ377222; ABD24061.1; -; mRNA.
EMBL; AC130925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_001094143.1; NM_001100673.1.
UniGene; Rn.16158; -.
STRING; 10116.ENSRNOP00000039682; -.
PaxDb; E9PSK7; -.
PeptideAtlas; E9PSK7; -.
Ensembl; ENSRNOT00000042066; ENSRNOP00000039682; ENSRNOG00000033568.
GeneID; 302983; -.
KEGG; rno:302983; -.
CTD; 23162; -.
RGD; 1563691; Mapk8ip3.
eggNOG; KOG2077; Eukaryota.
eggNOG; ENOG410XQ19; LUCA.
GeneTree; ENSGT00670000097546; -.
HOGENOM; HOG000290716; -.
HOVERGEN; HBG024110; -.
InParanoid; E9PSK7; -.
KO; K04436; -.
OMA; TRCNVPR; -.
OrthoDB; EOG091G016S; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000033568; Expressed in 9 organ(s), highest expression level in brain.
GO; GO:0030673; C:axolemma; IEA:Ensembl.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0044297; C:cell body; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl.
GO; GO:0008432; F:JUN kinase binding; IBA:GO_Central.
GO; GO:0019894; F:kinesin binding; ISS:UniProtKB.
GO; GO:0005078; F:MAP-kinase scaffold activity; IBA:GO_Central.
GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IPI:RGD.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IEA:Ensembl.
GO; GO:0030159; F:receptor signaling complex scaffold activity; IBA:GO_Central.
GO; GO:0007257; P:activation of JUN kinase activity; IMP:UniProtKB.
GO; GO:0099641; P:anterograde axonal protein transport; IMP:UniProtKB.
GO; GO:0061564; P:axon development; IMP:UniProtKB.
GO; GO:0007411; P:axon guidance; IEA:Ensembl.
GO; GO:0031103; P:axon regeneration; IMP:UniProtKB.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
GO; GO:0060425; P:lung morphogenesis; IEA:Ensembl.
GO; GO:0031175; P:neuron projection development; IEP:RGD.
GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:RGD.
GO; GO:2001224; P:positive regulation of neuron migration; IEA:Ensembl.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
GO; GO:0007585; P:respiratory gaseous exchange; IEA:Ensembl.
GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR032486; JIP_LZII.
InterPro; IPR019143; JNK/Rab-associated_protein-1_N.
InterPro; IPR034743; RH1.
InterPro; IPR034744; RH2.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF16471; JIP_LZII; 1.
Pfam; PF09744; Jnk-SapK_ap_N; 1.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS51776; RH1; 1.
PROSITE; PS51777; RH2; 1.
1: Evidence at protein level;
Cell projection; Coiled coil; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Golgi apparatus; Phosphoprotein;
Reference proteome.
CHAIN 1 1322 C-Jun-amino-terminal kinase-interacting
protein 3.
/FTId=PRO_0000444893.
DOMAIN 12 100 RH1. {ECO:0000255|PROSITE-
ProRule:PRU01112}.
DOMAIN 506 580 RH2. {ECO:0000255|PROSITE-
ProRule:PRU01113}.
REGION 50 80 Kinesin-binding domain (KBD); essential
for its function in axon elongation.
{ECO:0000250|UniProtKB:Q9ESN9}.
REGION 210 226 JNK-binding domain (JBD); essential for
its function in axon elongation.
{ECO:0000250|UniProtKB:Q9ESN9}.
REGION 424 459 Leucine zipper-like domain (LZ);
essential for its function in axon
elongation.
{ECO:0000269|PubMed:21775604}.
REGION 459 515 Interaction with NTRK2.
{ECO:0000269|PubMed:21775604}.
COILED 66 167 {ECO:0000255}.
COILED 443 534 {ECO:0000255}.
MOD_RES 266 266 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9ESN9}.
MOD_RES 276 276 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9ESN9}.
MOD_RES 287 287 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9ESN9}.
MOD_RES 315 315 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UPT6}.
MOD_RES 365 365 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UPT6}.
MOD_RES 366 366 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ESN9}.
MOD_RES 588 588 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ESN9}.
MOD_RES 662 662 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ESN9}.
CONFLICT 440 440 I -> V (in Ref. 1; ABD24061).
{ECO:0000305}.
CONFLICT 940 940 V -> M (in Ref. 1; ABD24061).
{ECO:0000305}.
CONFLICT 1208 1208 Y -> N (in Ref. 1; ABD24061).
{ECO:0000305}.
SEQUENCE 1322 AA; 145650 MW; 01C4DAF1DFEDAA35 CRC64;
MMEIQMDEGG GVVVYQDDYC SGSVMSERVS GLAGSIYREF ERLIHCYDEE VVKELMPLVV
NVLENLDSVL SENQEHEVEL ELLREDNEQL LTQYEREKAL RKQAEEKFIE FEDALEQEKK
ELQIQVEHYE FQTRQLELKA KNYADQISRL EERESEMKKE YNALHQRHTE MIQTYVEHIE
RSKMQQVGGG GQTESSLPGR SRKERPTSLN VFPLADGMVR AQMGGKLVPA GDHWHLSDLG
QLQSSSSYQC PNDEMSESGQ SSAAATPSTT GTKSNTPTSS VPSAAVTPLN ESLQPLGDYG
SVTKNNKRAR EKRNSRNMEV QVTQEMRNVS IGMGSSDEWS DVQDIIDSTP ELDVCPETRL
DRTGSSPTQG IVNKAFGINT DSLYHELSTA GSEVIGDVDE GADLLGEFSG MGKEVGNLLL
ENSQLLETKN ALNVVKNDLI AKVDQLSGEQ EVLKGELEAA KQAKVKLENR IKELEEELKR
VKSEAVTARR EPREEVEDDK IPMAQRRRFT RVEMARVLME RNQYKERLME LQEAVRWTEM
IRASREHPSV QEKKKSTIWQ FFSRLFSSSS SPPPAKRSYP SVNIHYKSPT TAGFSQRRNH
ALCQISAGSR PLEFFPDDDC TSSARREQKR EQYRQVREHV RNDDGRLQAC GWSLPAKYKQ
LSPNGGQEDT RMKNVPVPVY CRPLVEKDPS TKLWCAAGVN LSGWKPNEED SSNGPKPAPG
RDPLTCDREG EGEPKSTHPS PEKKKAKEVP EADATSSRVW ILTSTLTTSK VVIIDANQPG
TVVDQFTVCN AHVLCISSIP AASDSDYPPG DMFLDSDVNP EDSGADGVLA GITLVGCATR
CNVPRSNCSS RGDTPVLDKG QGDVAATANG KVNPSQSTEE ATEATEVPDP GPSESEATTV
RPGPLTEHVF TDPAPTQSSS TQPASENGSE SDGSIVQPQV EPSGESSATT SSAAPTMWLG
AQNGWLYVHS AVANWKKCLH SIKLKDSVLS LVHVKGRVLV ALADGTLAIF HRGEDGQWDL
SNYHLMDLGH PHHSIRCMAV VDDRVWCGYK NKVHVIQPKT MQIEKSFDAH PRRESQVRQL
AWIGDGVWVS IRLDSTLRLY HAHTHQHLQD VDIEPYVSKM LGTGKLGFSF VRITALLIAG
NRLWVGTGNG VVISIPLTET VVLHRGQLLG LRANKTSPTS GEGTRPGGII HVYGDDSSDK
TASSFIPYCS MAQAQLCFHG HRDAVKFFVS VPGNVLATLN GSVLDSPSEG PGPAAPAADA
EGQKLKNALV LSGGEGYIDF RIGDGEDDET EEGTGDVNQT KPSLSKAERS HIIVWQVSYT
PE


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