C8AP2_MOUSE
ID C8AP2_MOUSE Reviewed; 1962 AA.
AC Q9WUF3; B1AX74; Q9CSW2;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=CASP8-associated protein 2;
DE AltName: Full=FLICE-associated huge protein;
GN Name=Casp8ap2 {ECO:0000312|MGI:MGI:1349399};
GN Synonyms=Flash {ECO:0000312|EMBL:AAD29045.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAD29045.1}
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN DISC COMPLEX WITH CASP8; FADD
RP AND FAS, AND TISSUE SPECIFICITY.
RC TISSUE=T-cell lymphoma {ECO:0000312|EMBL:AAD29045.1};
RX PubMed=10235259; DOI=10.1038/19709;
RA Imai Y., Kimura T., Murakami A., Yajima N., Sakamaki K., Yonehara S.;
RT "The CED-4-homologous protein FLASH is involved in Fas-mediated activation
RT of caspase-8 during apoptosis.";
RL Nature 398:777-785(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4] {ECO:0000305, ECO:0000312|EMBL:BAB27860.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1766-1962.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB27860.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAB27860.1};
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 [5] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH TRAF2.
RX PubMed=11340079; DOI=10.1074/jbc.m102941200;
RA Choi Y.-H., Kim K.-B., Kim H.-H., Hong G.-S., Kwon Y.-K., Chung C.-W.,
RA Park Y.-M., Shen Z.-J., Kim B.J., Lee S.-Y., Jung Y.-K.;
RT "FLASH coordinates NF-kappa B activity via TRAF2.";
RL J. Biol. Chem. 276:25073-25077(2001).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=15592525; DOI=10.1038/sj.onc.1208186;
RA Jun J.-I., Chung C.-W., Lee H.-J., Pyo J.-O., Lee K.N., Kim N.-S.,
RA Kim Y.S., Yoo H.-S., Lee T.-H., Kim E., Jung Y.-K.;
RT "Role of FLASH in caspase-8-mediated activation of NF-kappaB: dominant-
RT negative function of FLASH mutant in NF-kappaB signaling pathway.";
RL Oncogene 24:688-696(2005).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=17003125; DOI=10.1073/pnas.0604227103;
RA Barcaroli D., Bongiorno-Borbone L., Terrinoni A., Hofmann T.G., Rossi M.,
RA Knight R.A., Matera A.G., Melino G., De Laurenzi V.;
RT "FLASH is required for histone transcription and S-phase progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14808-14812(2006).
RN [8]
RP INTERACTION WITH CASP8.
RX PubMed=17245429; DOI=10.1038/sj.emboj.7601504;
RA Milovic-Holm K., Krieghoff E., Jensen K., Will H., Hofmann T.G.;
RT "FLASH links the CD95 signaling pathway to the cell nucleus and nuclear
RT bodies.";
RL EMBO J. 26:391-401(2007).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1323, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Participates in TNF-alpha-induced blockade of glucocorticoid
CC receptor (GR) transactivation at the nuclear receptor coactivator
CC level, upstream and independently of NF-kappa-B. Suppresses both
CC NCOA2- and NCOA3-induced enhancement of GR transactivation (By
CC similarity). Required for histone gene transcription and progression
CC through S phase (By similarity). Required for histone gene
CC transcription and S phase progression (By similarity). Involved in TNF-
CC alpha-induced activation of NF-kappa-B via a TRAF2-dependent pathway.
CC Acts as a downstream mediator for CASP8-induced activation of NF-kappa-
CC B. Required for the activation of CASP8 in FAS-mediated apoptosis.
CC {ECO:0000250, ECO:0000269|PubMed:11340079,
CC ECO:0000269|PubMed:15592525}.
CC -!- SUBUNIT: Self-associates. Interacts with NPAT (By similarity).
CC Interacts with SRRT (By similarity). Interacts (via SIM domains) with
CC SUMO1 and SUMO2 (By similarity). Interacts with SP100; may negatively
CC regulate CASP8AP2 export from the nucleus to the cytoplasm (By
CC similarity). Interacts with NCOA2 and NCOA3 (By similarity). Component
CC of the death-inducing signaling complex (DISC) with CASP8, FADD and
CC FAS. Interacts with TRAF2. {ECO:0000250, ECO:0000269|PubMed:10235259,
CC ECO:0000269|PubMed:11340079, ECO:0000269|PubMed:17245429}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000269|PubMed:17003125}. Nucleus, PML body {ECO:0000250}.
CC Mitochondrion {ECO:0000250}. Note=Exported from the nucleus to the
CC mitochondria upon FAS activation. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, brain, thymus, lung,
CC testis and spleen. {ECO:0000269|PubMed:10235259}.
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DR EMBL; AF132726; AAD29045.1; -; mRNA.
DR EMBL; AL805973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC138022; AAI38023.1; -; mRNA.
DR EMBL; BC138041; AAI38042.1; -; mRNA.
DR EMBL; AK011818; BAB27860.1; -; mRNA.
DR CCDS; CCDS18016.1; -.
DR RefSeq; NP_001116450.1; NM_001122978.2.
DR RefSeq; NP_036127.2; NM_011997.3.
DR AlphaFoldDB; Q9WUF3; -.
DR SMR; Q9WUF3; -.
DR BioGRID; 205038; 6.
DR IntAct; Q9WUF3; 2.
DR MINT; Q9WUF3; -.
DR STRING; 10090.ENSMUSP00000029950; -.
DR iPTMnet; Q9WUF3; -.
DR PhosphoSitePlus; Q9WUF3; -.
DR EPD; Q9WUF3; -.
DR jPOST; Q9WUF3; -.
DR MaxQB; Q9WUF3; -.
DR PaxDb; Q9WUF3; -.
DR PeptideAtlas; Q9WUF3; -.
DR PRIDE; Q9WUF3; -.
DR ProteomicsDB; 273810; -.
DR Antibodypedia; 4167; 165 antibodies from 21 providers.
DR DNASU; 26885; -.
DR Ensembl; ENSMUST00000029950; ENSMUSP00000029950; ENSMUSG00000028282.
DR Ensembl; ENSMUST00000178925; ENSMUSP00000136016; ENSMUSG00000028282.
DR GeneID; 26885; -.
DR KEGG; mmu:26885; -.
DR UCSC; uc008sew.2; mouse.
DR CTD; 9994; -.
DR MGI; MGI:1349399; Casp8ap2.
DR VEuPathDB; HostDB:ENSMUSG00000028282; -.
DR eggNOG; ENOG502QQGD; Eukaryota.
DR GeneTree; ENSGT00620000088063; -.
DR HOGENOM; CLU_001861_0_0_1; -.
DR InParanoid; Q9WUF3; -.
DR OMA; DENRHFR; -.
DR OrthoDB; 31356at2759; -.
DR TreeFam; TF332487; -.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR BioGRID-ORCS; 26885; 17 hits in 71 CRISPR screens.
DR ChiTaRS; Casp8ap2; mouse.
DR PRO; PR:Q9WUF3; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9WUF3; protein.
DR Bgee; ENSMUSG00000028282; Expressed in animal zygote and 263 other tissues.
DR ExpressionAtlas; Q9WUF3; baseline and differential.
DR Genevisible; Q9WUF3; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0032184; F:SUMO polymer binding; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IDA:MGI.
DR GO; GO:0036337; P:Fas signaling pathway; ISS:UniProtKB.
DR InterPro; IPR039674; FLASH.
DR PANTHER; PTHR15489; PTHR15489; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Apoptosis; Cell cycle; Cytoplasm; Mitochondrion;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UKL3"
FT CHAIN 2..1962
FT /note="CASP8-associated protein 2"
FT /id="PRO_0000076189"
FT REGION 141..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1152..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1238..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1688..1962
FT /note="NCOA2-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UKL3"
FT REGION 1784..1878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1716..1720
FT /note="SUMO interaction motif 1 (SIM); mediates the binding
FT to polysumoylated substrates"
FT /evidence="ECO:0000250"
FT COMPBIAS 160..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..901
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..940
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..993
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1848..1863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1864..1878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKL3"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKL3"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKL3"
FT MOD_RES 798
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKL3"
FT MOD_RES 858
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKL3"
FT MOD_RES 923
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKL3"
FT MOD_RES 1323
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 152
FT /note="T -> A (in Ref. 1; AAD29045)"
FT /evidence="ECO:0000305"
FT CONFLICT 1062
FT /note="V -> I (in Ref. 1; AAD29045)"
FT /evidence="ECO:0000305"
FT CONFLICT 1766
FT /note="E -> K (in Ref. 4; BAB27860)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1962 AA; 219091 MW; 7B3FC637BB98D9EF CRC64;
MAADDDNGDG TGLFDVCPAS PLKNNDEGSL DIYAGLDSAV SDSTARSCVS FRNCLDLYEE
ILTEEGTAKE ATYNDLQIEY GKCQQQMKDL MKRFKEIQTQ NLNLKNENQS LKKNISALIK
TARVEINRKD EEINHLHQRL SEFPHFRNNH KTARTKDSQS TSPHLDDCSK TDHGVKSDVQ
KDVHPNTAQP NLEKEGKSHS EAQNPLHLST GVEKHCANNV WSRSPYQVGE GNSNEDNRRG
RSGTRHSQCS RGTDRTQKDL HSSCNDSEPR DKEANSRLQG HPEKHGNSEA RTESKISESK
SSTGMGYKSE RSASSWEKET SRERPHTRVE SQHDKNLEKQ NERLQNMHRK ELPSQDKTER
KVDVKFKPAG EEQGHRGRVD RALPPHPKND VKHYGFNKYH PEERRGREDC KRDRGMNSHG
FQDRRCSSFL SSNRNSKYPH SKEVSVAHQW ENTPFKAERH RTEDRRKRER ENKEESRHVK
SDKKSPPEHL QRTHKDTKKS TADGKRQTEP KHGKGAVSNS ELSKGTDSKE GATKVESGPN
EAKGKDLKLS FMEKLNLTLS PAKKQPACQD NPHQITGVPE PSGTCDSRSL ETTGTVACLP
SGSEHNREET KSELPEPKEA LLATSQLRIS IPENKMKEEK RLLFKSVENT VPCELLACGT
EISLPAPVEI EQARCLLGSV EVEETCGGAR TAASVVMHVL PEHASEDASQ ELDTKRHDGI
NACAISEGVK TKVILSPKAA AASESHLAPL VEEPSISLVN CSGDNNPKLE PSLEERPIVE
TKSCPLESCL PKETFVPSPQ KTELIDHKIE TGESNSVYQD DDNSVLSIDF NNLRPIPDPI
SPLNSPVRPV CKVVSMESSC AIPLYDSSHK DEFPSNSTLS TFKSQSDLNK ENEKPVPKFD
KCSEADSCKH LSLDELEEGE IRSDDEESVA QKRLEKSARP RVSAEVQPGK SSPGSRRSTV
HVHKDNGRTA VKLPRDRLTW SKRSSESRPS NTERKSKTMS ISSLEKILPL ILVPSSLWEV
MHMLRLLGKH VRKNYMKFKI KFSLTQFHRI IESAILSFTS LVKCLDLSKI CKSVSTLQKS
LCEVIESNLK QVKKNGIVDR LFEQQQTDMK KKLWKFVDEQ LDYLFEKLKK ILLKFCDSVN
FENENSEGKL GKKYKERTQH SNCQKKKMDN KEIRREKVLK SENTVNFKSS LGCEKSEEKH
QDQNKTNASI VKHDVKRTFS TCSDNTKNAE CKEQFLEKSC PSTPRPGKDE GHTEEEAQAA
QHASAKSERS FEILTEQQAS SLTFNLVSDA QMGEIFKSLL QGSDLLDTSG TEKAEWELKT
PEKQLLESLK CESAPACATE ELVSEGASLC PKVISDDNWS LLSSEKGPSL SSGLSLPVHP
DVLDENCMFE VSSNTALGKD NVYSSEKSKP CISSILLEDL AVSLTVPSPL KSDGHLSFLK
PEVLSTSTPE EVISAHFSED ALLEEEDASE QDIHLALESD NSSSKSSCSS WTSRSVASGF
QYHPNLPMHA VIMEKSNDHF IVKIRRATPS TSPGLKHGVV AEESLTSLPR TGKEAGVATE
KEPNLFQSTV LKPVKDLENT DKNIDKSKLT HEEQNSIVQT QVPDIYEFLK DASNKVVHCD
QVVDDCFKLH QVWEPKVSEN LQELPSMEKI PHSLDNHLPD THIDLTKDSA TETKSLGELM
EVTVLNVDHL ECSQTNLDQD AEITCSSLQP DTIDAFIDLT HDASSESKNE GSEPVLAVEG
MGCQVICIDE DTNKEGKMGR ANSPLESIVE ETCIDLTSES PGSCEIKRHN LKSEPPSKLD
CLELPETLGN GHKKRKNSPG VSHSSQKKQR KDIDLSSEKT QRLSPNSDRN GDAHRKQASK
KREPAVNETS LSSEASPEVK GSTAVLAASP ASLSAKNVIK KKGEIIVSWT RNDDREILLE
CQKRMPSLKT FTYLAVKLNK NPNQVSERFQ QLKKLFEKSK CR
