JMY_MOUSE
ID JMY_MOUSE Reviewed; 983 AA.
AC Q9QXM1; Q3UQZ0; Q5BL16; Q6NST0; Q8CBP9; Q8VDZ3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Junction-mediating and -regulatory protein;
GN Name=Jmy;
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 1), FUNCTION, INTERACTION WITH EP300,
RP AND TISSUE SPECIFICITY.
RX PubMed=10518217; DOI=10.1016/s1097-2765(00)80338-x;
RA Shikama N., Lee C.-W., France S., Delavaine L., Lyon J.,
RA Krstic-Demonacos M., La Thangue N.B.;
RT "A novel cofactor for p300 that regulates the p53 response.";
RL Mol. Cell 4:365-376(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-555 AND 940-983 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion, and Urinary bladder;
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 [4]
RP FUNCTION, ALTERNATIVE SPLICING (ISOFORM 3), AND INTERACTION WITH TTC5 AND
RP EP300.
RX PubMed=11511361; DOI=10.1016/s1097-2765(01)00277-5;
RA Demonacos C., Krstic-Demonacos M., La Thangue N.B.;
RT "A TPR motif cofactor contributes to p300 activity in the p53 response.";
RL Mol. Cell 8:71-84(2001).
RN [5]
RP UBIQUITINATION, AND INDUCTION.
RX PubMed=17170761; DOI=10.1038/sj.embor.7400855;
RA Coutts A.S., Boulahbel H., Graham A., La Thangue N.B.;
RT "Mdm2 targets the p53 transcription cofactor JMY for degradation.";
RL EMBO Rep. 8:84-90(2007).
RN [6]
RP IDENTIFICATION BY 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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-981.
RX PubMed=19287377; DOI=10.1038/ncb1852;
RA Zuchero J.B., Coutts A.S., Quinlan M.E., Thangue N.B., Mullins R.D.;
RT "p53-cofactor JMY is a multifunctional actin nucleation factor.";
RL Nat. Cell Biol. 11:451-459(2009).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19897726; DOI=10.1073/pnas.0906785106;
RA Coutts A.S., Weston L., La Thangue N.B.;
RT "A transcription co-factor integrates cell adhesion and motility with the
RT p53 response.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19872-19877(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-883 AND SER-969, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, 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: Acts both as a nuclear p53/TP53-cofactor and a cytoplasmic
CC regulator of actin dynamics depending on conditions. In nucleus, acts
CC as a cofactor that increases p53/TP53 response via its interaction with
CC p300/EP300. Increases p53/TP53-dependent transcription and apoptosis,
CC suggesting an important role in p53/TP53 stress response such as DNA
CC damage. In cytoplasm, acts as a nucleation-promoting factor for both
CC branched and unbranched actin filaments. Activates the Arp2/3 complex
CC to induce branched actin filament networks. Also catalyzes actin
CC polymerization in the absence of Arp2/3, creating unbranched filaments.
CC Contributes to cell motility by controlling actin dynamics. May promote
CC the rapid formation of a branched actin network by first nucleating new
CC mother filaments and then activating Arp2/3 to branch off these
CC filaments. Upon nutrient stress, directly recruited by MAP1LC3B to the
CC phagophore membrane surfaces to promote actin assembly during autophagy
CC (By similarity). The p53/TP53-cofactor and actin activator activities
CC are regulated via its subcellular location.
CC {ECO:0000250|UniProtKB:Q8N9B5, ECO:0000269|PubMed:10518217,
CC ECO:0000269|PubMed:11511361, ECO:0000269|PubMed:19287377,
CC ECO:0000269|PubMed:19897726}.
CC -!- SUBUNIT: Interacts with p300/EP300, the complex activates p53/TP53
CC transcriptional activity (PubMed:11511361, PubMed:10518217). Interacts
CC with TTC5/STRAP; the interaction takes place in the nucleus and
CC facilitates the association between JMY and p300/EP300
CC (PubMed:11511361). Interacts with TTC5/STRAP; the interaction takes
CC place in the cytoplasm and results in the inhibition of JYM's
CC nucleation activity (By similarity). Interacts with MAP1LC3B; the
CC interaction results in the activation of JYM's nucleation activity in
CC the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q8N9B5,
CC ECO:0000269|PubMed:10518217, ECO:0000269|PubMed:11511361}.
CC -!- INTERACTION:
CC Q9QXM1; Q09472: EP300; Xeno; NbExp=16; IntAct=EBI-866001, EBI-447295;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19287377,
CC ECO:0000269|PubMed:19897726}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q8N9B5}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q8N9B5}. Endomembrane system; Lipid-anchor.
CC Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000250|UniProtKB:Q8N9B5}. Note=Localizes to the nucleus in most
CC cell types. In primary neutrophils, it colocalizes with actin filaments
CC at the leading edge and is excluded from the nucleus. Localization
CC correlates with motility, because it moves from the nucleus to the
CC cytoplasmic compartment when cells are differentiated from nonmotile
CC cells into highly motile neutrophil-like cells (By similarity).
CC Accumulates in nucleus under DNA damage conditions, increasing p53/TP53
CC transcription response and reducing its influence on cell motility.
CC Localizes to cytoplasmic vesicles which associate with actin filament
CC and autophagosomal membranes upon starvation-induced autophagy (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q8N9B5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9QXM1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QXM1-2; Sequence=VSP_032311, VSP_032312;
CC Name=3; Synonyms=DeltaP;
CC IsoId=Q9QXM1-3; Sequence=VSP_032313;
CC -!- TISSUE SPECIFICITY: Widely expressed, except in testis where it is
CC expressed at low level. {ECO:0000269|PubMed:10518217}.
CC -!- INDUCTION: Accumulates in DNA-damaged cells (at protein level).
CC {ECO:0000269|PubMed:17170761}.
CC -!- DOMAIN: The N-terminal region is involved in actin binding and actin
CC nucleation activity. {ECO:0000250|UniProtKB:Q8N9B5}.
CC -!- PTM: Ubiquitinated by MDM2, leading to its subsequent degradation by
CC the proteasome. In case of DNA damage, the interaction with MDM2 is
CC altered, preventing degradation and allowing interaction with
CC p300/EP300 and its function in p53/TP53 stress response.
CC {ECO:0000269|PubMed:17170761}.
CC -!- MISCELLANEOUS: [Isoform 3]: Alters the p53/TP53 response.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the JMY family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH69906.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AF201390; AAF17555.1; -; mRNA.
DR EMBL; BC020052; AAH20052.1; -; mRNA.
DR EMBL; BC069906; AAH69906.1; ALT_SEQ; mRNA.
DR EMBL; BC090835; AAH90835.1; -; mRNA.
DR EMBL; AK035559; BAC29105.1; -; mRNA.
DR EMBL; AK141957; BAE24898.1; -; mRNA.
DR CCDS; CCDS26688.1; -. [Q9QXM1-1]
DR RefSeq; NP_067285.2; NM_021310.3.
DR AlphaFoldDB; Q9QXM1; -.
DR BioGRID; 208310; 3.
DR IntAct; Q9QXM1; 23.
DR MINT; Q9QXM1; -.
DR STRING; 10090.ENSMUSP00000070339; -.
DR iPTMnet; Q9QXM1; -.
DR PhosphoSitePlus; Q9QXM1; -.
DR EPD; Q9QXM1; -.
DR jPOST; Q9QXM1; -.
DR MaxQB; Q9QXM1; -.
DR PaxDb; Q9QXM1; -.
DR PeptideAtlas; Q9QXM1; -.
DR PRIDE; Q9QXM1; -.
DR ProteomicsDB; 269369; -. [Q9QXM1-1]
DR ProteomicsDB; 269370; -. [Q9QXM1-2]
DR ProteomicsDB; 269371; -. [Q9QXM1-3]
DR DNASU; 57748; -.
DR GeneID; 57748; -.
DR KEGG; mmu:57748; -.
DR UCSC; uc007rlf.2; mouse. [Q9QXM1-1]
DR CTD; 133746; -.
DR MGI; MGI:1913096; Jmy.
DR eggNOG; ENOG502QRHU; Eukaryota.
DR InParanoid; Q9QXM1; -.
DR OrthoDB; 183925at2759; -.
DR PhylomeDB; Q9QXM1; -.
DR TreeFam; TF331023; -.
DR Reactome; R-MMU-6804760; Regulation of TP53 Activity through Methylation.
DR BioGRID-ORCS; 57748; 7 hits in 110 CRISPR screens.
DR ChiTaRS; Jmy; mouse.
DR PRO; PR:Q9QXM1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9QXM1; protein.
DR GO; GO:0000421; C:autophagosome membrane; ISS:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0071933; F:Arp2/3 complex binding; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR GO; GO:0070060; P:'de novo' actin filament nucleation; IDA:UniProtKB.
DR GO; GO:0070358; P:actin polymerization-dependent cell motility; IDA:UniProtKB.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IDA:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0043620; P:regulation of DNA-templated transcription in response to stress; TAS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR InterPro; IPR033324; Jmy.
DR InterPro; IPR031738; JMY/WHAMM.
DR InterPro; IPR031808; JMY/WHAMM_N.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR23330:SF8; PTHR23330:SF8; 1.
DR Pfam; PF15871; JMY; 1.
DR Pfam; PF15920; WHAMM-JMY_N; 1.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; DNA damage; DNA repair; Lipoprotein;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..983
FT /note="Junction-mediating and -regulatory protein"
FT /id="PRO_0000324612"
FT DOMAIN 916..933
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..119
FT /note="Interaction with p300/EP300"
FT /evidence="ECO:0000269|PubMed:10518217"
FT REGION 50..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..558
FT /note="Interaction with p300/EP300"
FT /evidence="ECO:0000269|PubMed:10518217"
FT REGION 723..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 315..351
FT /evidence="ECO:0000255"
FT COILED 480..528
FT /evidence="ECO:0000255"
FT COILED 571..612
FT /evidence="ECO:0000255"
FT COMPBIAS 50..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..820
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..983
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9B5"
FT MOD_RES 704
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N9B5"
FT MOD_RES 883
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 969
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 445..446
FT /note="VY -> FP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032311"
FT VAR_SEQ 447..983
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032312"
FT VAR_SEQ 794..812
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_032313"
FT MUTAGEN 981
FT /note="W->A: Decreases the activation of Arp2/3 without
FT affecting the intrinsic nucleation activity."
FT /evidence="ECO:0000269|PubMed:19287377"
FT CONFLICT 54
FT /note="Q -> H (in Ref. 3; BAE24898)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="G -> V (in Ref. 2; AAH20052)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="S -> R (in Ref. 3; BAE24898)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="I -> T (in Ref. 2; AAH20052/AAH90835 and 3;
FT BAE24898)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="V -> A (in Ref. 2; AAH20052/AAH90835 and 3;
FT BAE24898)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="M -> I (in Ref. 2; AAH20052)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="S -> P (in Ref. 2; AAH20052/AAH90835 and 3;
FT BAE24898)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="R -> K (in Ref. 2; AAH20052)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 983 AA; 110586 MW; EC58500CC05B8BAA CRC64;
MSFALEETLE SDWVAVRPHV FDEREKHKFV FIVAWNEIEG KFAITCHNRT AQRQRSGSRE
QAGTPASDGS RGPGSPAARG RSEAAASATA ALRSPGPRKS QAWAEGGSPR SARSLKGDPP
RGPAGRGPES PLRSPARAKA SPLRRSAESR DAIASATPVP PAPPVPPVSS VRVVSASGAV
SEEIEVLEMV REDEAPQPLP DSEQPPSAAE LESSAEECSW AGLFSFQDLR AVHQQLCSVN
SQLEPCLPVF PEEPSGMWTV LFGGAPEMTE QEIDALCYQL QVYLGHGLDT CGWKILSQVL
FTETDDPEEY YESLSELRQK GYEEVLQRAR RRIQELLDKH KTIESMVELL DLYQMEDEAY
SSLAEATTEL YQYLLQPFRD MRELAMLRRQ QIKISMENDY LGPRRIESLQ KEDADWQRKA
HMAVLSIQDL TVKYFEITAK AQKAVYDRMR ADQKKFGKAS WAAAAERMEK LQYAVSKETL
QMMRAKEICL EQKKHALKEE MQSLQGGTEA IARLDQLESD YYDLQLQLYE VQFEILKCEE
LLLTAQLESI KRLISEKRDE VVYYDTYESM EAMLEKEEMA ASVHAQREEL QKLQQKARQL
EARRGRVSAK KAYLRNKKEI CIAKHHEKFQ QRFQSEDEYR AHHTIQIKRD KLHDEEERKS
AWVSQERQRT LDRLRTFKQR YPGQVILKST RLRVAHSRRK STASPVPCEE QCHSLPTVLQ
GQEKTEVGGG GSQLGPSQTA EPQSLVQLED TSSEQLESTS LPPRAVVSSE LPPPQSAPLL
TSIDPKPCSV TIDPLPPPLP PTPPPPPPPP PPPPPPLPVA KDNGASTTAE TLEKDALRTE
GNERSIPKSA SAPAAHLFDS SQLVSARKKL RKTVEGLQRR RVSSPMDEVL ASLKRGSFHL
KKVEQRTLPP FPDEDDSNNI LAQIRKGVKL KKVQKEVLRE SFTLLPDTDP LTRSIHEALR
RIKEASPESE DEEEALPCTD WEN
