JIP4_MOUSE
ID JIP4_MOUSE Reviewed; 1321 AA.
AC Q58A65; Q3UH77; Q3UHF0; Q58VQ4; Q5NC70; Q5NC78; Q6A057; Q6PAS3; Q8CJC2;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=C-Jun-amino-terminal kinase-interacting protein 4;
DE Short=JIP-4;
DE Short=JNK-interacting protein 4;
DE AltName: Full=JNK-associated leucine-zipper protein;
DE Short=JLP;
DE AltName: Full=JNK/SAPK-associated protein 2;
DE Short=JSAP2;
DE AltName: Full=Mitogen-activated protein kinase 8-interacting protein 4;
DE AltName: Full=Sperm-associated antigen 9;
GN Name=Spag9 {ECO:0000312|MGI:MGI:1918084};
GN Synonyms=Jip4, Jsap2, Kiaa0516, Mapk8ip4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH MAX;
RP MAPK8; MAPK14; MAP3K3; MYC AND MAP2K4, AND SUBCELLULAR LOCATION.
RX PubMed=12391307; DOI=10.1073/pnas.232310199;
RA Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.;
RT "JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules and
RT transcription factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), FUNCTION, INTERACTION WITH KNS2 AND
RP MAPK8, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=15767678; DOI=10.1128/mcb.25.7.2733-2743.2005;
RA Kelkar N., Standen C.L., Davis R.J.;
RT "Role of the JIP4 scaffold protein in the regulation of mitogen-activated
RT protein kinase signaling pathways.";
RL Mol. Cell. Biol. 25:2733-2743(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RA Takamatsu N., Tochigi M., Ito M., Odama Y., Xu P., Nakabeppu Y.,
RA Yoshioka K., Shiba T.;
RT "JSAP2, a novel member of the JSAP1 JNK scaffold protein family.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH KNS2, AND INDUCTION.
RX PubMed=15987681; DOI=10.1074/jbc.m505499200;
RA Nguyen Q., Lee C.M., Le A., Reddy E.P.;
RT "JLP associates with kinesin light chain 1 through a novel leucine zipper-
RT like domain.";
RL J. Biol. Chem. 280:30185-30191(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [10]
RP FUNCTION, INTERACTION WITH PIKFYVE, AND SUBCELLULAR LOCATION.
RX PubMed=19056739; DOI=10.1074/jbc.m806539200;
RA Ikonomov O.C., Fligger J., Sbrissa D., Dondapati R., Mlak K., Deeb R.,
RA Shisheva A.;
RT "Kinesin adapter JLP links PIKfyve to microtubule-based endosome-to-trans-
RT Golgi network traffic of furin.";
RL J. Biol. Chem. 284:3750-3761(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-217 AND THR-365, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; THR-217; THR-292 AND
RP SER-733, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: The JNK-interacting protein (JIP) group of scaffold proteins
CC selectively mediates JNK signaling by aggregating specific components
CC of the MAPK cascade to form a functional JNK signaling module
CC (PubMed:12391307, PubMed:15767678). Regulates lysosomal positioning by
CC acting as an adapter protein which links PIP4P1-positive lysosomes to
CC the dynein-dynactin complex (By similarity). Assists PIKFYVE selective
CC functionality in microtubule-based endosome-to-TGN trafficking
CC (PubMed:19056739). {ECO:0000250|UniProtKB:O60271,
CC ECO:0000269|PubMed:12391307, ECO:0000269|PubMed:15767678,
CC ECO:0000269|PubMed:19056739}.
CC -!- SUBUNIT: Homodimer (By similarity). The homodimer interacts with ARF6,
CC forming a heterotetramer (By similarity). Homooligomer (By similarity).
CC Interacts with MAX, MAPK8, MAPK14, MAP3K3, MYC, and MAP2K4
CC (PubMed:12391307). Interacts with KNS2 (PubMed:15987681). Interaction
CC with KNS2 is important in the formation of ternary complex with MAPK8
CC (PubMed:15767678). Interacts with PIP4P1 (By similarity). Interacts
CC with PIKFYVE (PubMed:19056739). {ECO:0000250|UniProtKB:O60271,
CC ECO:0000269|PubMed:12391307, ECO:0000269|PubMed:15767678,
CC ECO:0000269|PubMed:15987681, ECO:0000269|PubMed:19056739}.
CC -!- INTERACTION:
CC Q58A65; P62331: Arf6; NbExp=10; IntAct=EBI-6530207, EBI-988682;
CC Q58A65; Q5S007: LRRK2; Xeno; NbExp=2; IntAct=EBI-6530207, EBI-5323863;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12391307,
CC ECO:0000269|PubMed:15767678, ECO:0000269|PubMed:19056739}. Cytoplasm,
CC perinuclear region {ECO:0000269|PubMed:12391307,
CC ECO:0000269|PubMed:19056739}. Lysosome membrane
CC {ECO:0000250|UniProtKB:O60271}. Note=Perinuclear distribution in
CC response to stress signals such as UV radiation.
CC {ECO:0000269|PubMed:12391307}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=JLP(L) {ECO:0000303|PubMed:19056739};
CC IsoId=Q58A65-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q58A65-2; Sequence=VSP_018228;
CC Name=3;
CC IsoId=Q58A65-3; Sequence=VSP_018226, VSP_018227, VSP_018228,
CC VSP_018229;
CC Name=4;
CC IsoId=Q58A65-4; Sequence=VSP_018226, VSP_018227, VSP_018228,
CC VSP_018230;
CC Name=5;
CC IsoId=Q58A65-5; Sequence=VSP_018227, VSP_018228;
CC Name=6;
CC IsoId=Q58A65-6; Sequence=VSP_018225, VSP_018228;
CC -!- TISSUE SPECIFICITY: [Isoform 6]: Highly expressed in brain, kidney,
CC liver, heart. {ECO:0000269|PubMed:15767678}.
CC -!- INDUCTION: Up-regulated during neuronal differentiation.
CC {ECO:0000269|PubMed:15987681}.
CC -!- PTM: Phosphorylated by MAPK8 and MAPK14. {ECO:0000269|PubMed:15767678}.
CC -!- SIMILARITY: Belongs to the JIP scaffold family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32239.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAI35376.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF327451; AAN61564.1; -; mRNA.
DR EMBL; AY823270; AAX19462.1; -; mRNA.
DR EMBL; AB047782; BAD93176.1; -; mRNA.
DR EMBL; AK172961; BAD32239.1; ALT_INIT; mRNA.
DR EMBL; AK147431; BAE27907.1; -; mRNA.
DR EMBL; AK147537; BAE27980.1; -; mRNA.
DR EMBL; AL662838; CAI35367.1; -; Genomic_DNA.
DR EMBL; AL662838; CAI35375.1; -; Genomic_DNA.
DR EMBL; AL662838; CAI35376.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC060100; AAH60100.1; -; mRNA.
DR EMBL; BC094670; AAH94670.1; -; mRNA.
DR CCDS; CCDS25248.1; -. [Q58A65-2]
DR CCDS; CCDS56797.1; -. [Q58A65-3]
DR RefSeq; NP_001020599.1; NM_001025428.1.
DR RefSeq; NP_001020600.1; NM_001025429.1. [Q58A65-3]
DR RefSeq; NP_001020601.1; NM_001025430.1.
DR RefSeq; NP_001186132.1; NM_001199203.1.
DR RefSeq; NP_001186133.1; NM_001199204.1.
DR RefSeq; NP_001186134.1; NM_001199205.1. [Q58A65-4]
DR RefSeq; NP_081845.2; NM_027569.2. [Q58A65-2]
DR RefSeq; XP_006534282.1; XM_006534219.2.
DR AlphaFoldDB; Q58A65; -.
DR BioGRID; 214283; 15.
DR IntAct; Q58A65; 2.
DR MINT; Q58A65; -.
DR STRING; 10090.ENSMUSP00000042271; -.
DR iPTMnet; Q58A65; -.
DR PhosphoSitePlus; Q58A65; -.
DR EPD; Q58A65; -.
DR jPOST; Q58A65; -.
DR MaxQB; Q58A65; -.
DR PaxDb; Q58A65; -.
DR PeptideAtlas; Q58A65; -.
DR PRIDE; Q58A65; -.
DR ProteomicsDB; 268911; -. [Q58A65-1]
DR ProteomicsDB; 268912; -. [Q58A65-2]
DR ProteomicsDB; 268913; -. [Q58A65-3]
DR ProteomicsDB; 268914; -. [Q58A65-4]
DR ProteomicsDB; 268915; -. [Q58A65-5]
DR ProteomicsDB; 268916; -. [Q58A65-6]
DR Antibodypedia; 30731; 223 antibodies from 36 providers.
DR DNASU; 70834; -.
DR Ensembl; ENSMUST00000041956; ENSMUSP00000042271; ENSMUSG00000020859. [Q58A65-2]
DR Ensembl; ENSMUST00000075695; ENSMUSP00000075115; ENSMUSG00000020859. [Q58A65-3]
DR GeneID; 70834; -.
DR KEGG; mmu:70834; -.
DR UCSC; uc007kxx.1; mouse. [Q58A65-2]
DR UCSC; uc007kxy.1; mouse. [Q58A65-1]
DR UCSC; uc007kxz.1; mouse. [Q58A65-6]
DR UCSC; uc007kya.1; mouse. [Q58A65-3]
DR UCSC; uc007kyc.1; mouse. [Q58A65-5]
DR UCSC; uc007kyd.1; mouse. [Q58A65-4]
DR CTD; 9043; -.
DR MGI; MGI:1918084; Spag9.
DR VEuPathDB; HostDB:ENSMUSG00000020859; -.
DR eggNOG; KOG2077; Eukaryota.
DR GeneTree; ENSGT00940000153496; -.
DR InParanoid; Q58A65; -.
DR OMA; KWTEMIR; -.
DR OrthoDB; 324912at2759; -.
DR PhylomeDB; Q58A65; -.
DR TreeFam; TF313096; -.
DR Reactome; R-MMU-525793; Myogenesis.
DR BioGRID-ORCS; 70834; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Spag9; mouse.
DR PRO; PR:Q58A65; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q58A65; protein.
DR Bgee; ENSMUSG00000020859; Expressed in otolith organ and 229 other tissues.
DR ExpressionAtlas; Q58A65; baseline and differential.
DR Genevisible; Q58A65; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0008432; F:JUN kinase binding; IDA:MGI.
DR GO; GO:0019894; F:kinesin binding; IDA:MGI.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; IDA:MGI.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central.
DR GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
DR GO; GO:1903860; P:negative regulation of dendrite extension; IEA:Ensembl.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:MGI.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
DR GO; GO:0051146; P:striated muscle cell differentiation; IGI:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 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; PTHR13886; 1.
DR Pfam; PF16471; JIP_LZII; 1.
DR Pfam; PF09744; Jnk-SapK_ap_N; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS51776; RH1; 1.
DR PROSITE; PS51777; RH2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Lysosome;
KW Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..1321
FT /note="C-Jun-amino-terminal kinase-interacting protein 4"
FT /id="PRO_0000234077"
FT DOMAIN 7..95
FT /note="RH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01112"
FT DOMAIN 500..604
FT /note="RH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01113"
FT REGION 203..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 66..166
FT /evidence="ECO:0000255"
FT COILED 408..534
FT /evidence="ECO:0000250"
FT COILED 724..758
FT /evidence="ECO:0000255"
FT COMPBIAS 222..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 217
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 292
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 348
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 365
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 418
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 586
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 595
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 705
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 732
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT MOD_RES 1264
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60271"
FT VAR_SEQ 1..165
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15767678"
FT /id="VSP_018225"
FT VAR_SEQ 1..143
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15368895,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_018226"
FT VAR_SEQ 144..196
FT /note="RLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSGSDQLEATAHSR
FT I -> MNPGCMLLFVFGFVGGAVVINSAILVSLSVLLLVHFSISTGVPALTQNLPRIL
FT (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15368895,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_018227"
FT VAR_SEQ 248..261
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12391307,
FT ECO:0000303|PubMed:15368895, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15767678, ECO:0000303|PubMed:16141072"
FT /id="VSP_018228"
FT VAR_SEQ 405
FT /note="G -> GEYSG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_018229"
FT VAR_SEQ 1175
FT /note="T -> TVILHQGRLLGLRA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018230"
FT CONFLICT 241
FT /note="R -> C (in Ref. 1; AAN61564)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="E -> A (in Ref. 1; AAN61564)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="E -> G (in Ref. 5; BAE27980)"
FT /evidence="ECO:0000305"
FT CONFLICT 705
FT /note="S -> T (in Ref. 3; BAD93176)"
FT /evidence="ECO:0000305"
FT CONFLICT 1114
FT /note="L -> P (in Ref. 5; BAE27907)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1321 AA; 146219 MW; 93A6E97A62E0E92C CRC64;
MELEDGVVYQ EEPGGSGAVM SERVSGLAGS IYREFERLIG RYDEEVVKEL MPLVVAVLEN
LDSVFAQDQE HQVELELLRD DNEQLITQYE REKALRKHAE EKFIEFEDSQ EQEKKDLQTR
VESLESQTRQ LELKAKNYAD QISRLEEREA ELKKEYNALH QRHTEMIHNY MEHLERTKLH
QLSGSDQLEA TAHSRIRKER PISLGIFPLP AGDGLLTPDT QKGGETPGSE QWKFQELSQP
RSHTSLKVSH SPEPPKAVEQ EDELSDISQG GSKATTPAST ANSDVSAIPP DTPSKEDNEG
FVKGTDTSNK SEISKHIEVQ VAQETRNVST ESGENEEKSE VQAIIESTPE LDMDKDLSGY
KGSSTPTKGI ENKAFDRNTE SLFEELSSAG SGLIGDVDEG ADLLGMGREV ENLILENTQL
LETKNALNVV KNDLIAKVDE LTCEKDVLQG ELEAVKQAKL KLEDKNRELE EELRKARAEA
EDARQKAKDD DDSDIPTAQR KRFTRVEMAR VLMERNQYKE RLMELQEAVR WTEMIRASRE
NPAMQEKKRS SIWQFFSRLF SSSSNATKKP EPPVNLKYNA PTSHVTPSVK KRSSTLSQLP
GDKSKAFDFL SEETEASLAS RREQKREQYR QVKAHVQKED GRVQAFGWSL PQKYKQVANG
QGETKMKNLP VPVYLRPLDE KDASMKLWCA VGVNLSGGKT RDGGSVVGAS VFYKDIAGLD
TEGSKQRSAS QSSLDKLDQE LKEQQKEFKN QEELSSQVWI CTSTHSTTKV IIIDAVQPGN
ILDSFTVCNS HVLCIASVPG ARETDYPAGE ELSESGQVDK ASLCGSMTSN SSAEMDSLLG
GITVVGCSTE GLTGAATSPS TNGASPVIEK PPEMETENSE VDENIPTAEE ATEATEGNAG
STEDTVDISQ PGVYTEHVFT DPLGVQIPED LSPVFQSSND SDVYKDQISV LPNEQDLARE
EAQKMSSLLP TMWLGAQNGC LYVHSSVAQW RKCLHSIKLK DSILSIVHVK GIVLVALADG
TLAIFHRGVD GQWDLSNYHL LDLGRPHHSI RCMTVVHDKV WCGYRNKIYV VQPKAMKIEK
SFDAHPRKES QVRQLAWVGD GVWVSIRLDS TLRLYHAHTY QHLQDVDIEP YVSKMLGTGK
LGFSFVRITA LMVSCNRLWV GTGNGVIISI PLTETNKTSG TPGNRPGSVI RVYGDENSDK
VTPGTFIPYC SMAHAQLCFH GHRDAVKFFV AVPGQVISPQ SSSGGADLTA DKAGSSAQEP
SSQTPLKSML VISGGEGYID FRMGDEGGES ELLGEDLPLE PSVTKAERSH LIVWQVMCGN
E
