ZFHX4_MOUSE
ID ZFHX4_MOUSE Reviewed; 3550 AA.
AC Q9JJN2;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 29-SEP-2021, entry version 149.
DE RecName: Full=Zinc finger homeobox protein 4;
DE AltName: Full=Zinc finger homeodomain protein 4;
DE Short=ZFH-4;
GN Name=Zfhx4; Synonyms=Zfh4;
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], AND TISSUE SPECIFICITY.
RC STRAIN=Swiss Webster / NIH;
RX PubMed=10873665; DOI=10.1006/bbrc.2000.2990;
RA Sakata N., Hemmi K., Kawaguchi M., Miura Y., Noguchi S., Ma D.,
RA Sasahara M., Kato T., Hori M., Tamaoki T.;
RT "The mouse ZFH-4 protein contains four homeodomains and twenty-two zinc
RT fingers.";
RL Biochem. Biophys. Res. Commun. 273:686-693(2000).
RN [2]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16946494; DOI=10.1248/bpb.29.1830;
RA Hemmi K., Ma D., Miura Y., Kawaguchi M., Sasahara M., Hashimoto-Tamaoki T.,
RA Tamaoki T., Sakata N., Tsuchiya K.;
RT "A homeodomain-zinc finger protein, ZFHX4, is expressed in neuronal
RT differentiation manner and suppressed in muscle differentiation manner.";
RL Biol. Pharm. Bull. 29:1830-1835(2006).
RN [3]
RP STRUCTURE BY NMR OF 2937-2984.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ZF-C2H2 domain in zinc finger homeodomain 4.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: May play a role in neural and muscle differentiation. May be
CC involved in transcriptional regulation. {ECO:0000269|PubMed:16946494}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, lung, muscle and small
CC intestine. No expression detected in undifferentiated P19 cells,
CC however, expression was seen following retinoic acid treatment to
CC induce neuronal differentiation. Expressed in undifferentiated C2C12
CC cells, following induction of muscle differentiation in a low-serum
CC medium, expression levels were decreased. {ECO:0000269|PubMed:10873665,
CC ECO:0000269|PubMed:16946494}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed at day 7.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AB024499; BAB03600.1; -; mRNA.
DR PDB; 2YRK; NMR; -; A=2937-2984.
DR PDBsum; 2YRK; -.
DR SMR; Q9JJN2; -.
DR IntAct; Q9JJN2; 1.
DR MINT; Q9JJN2; -.
DR STRING; 10090.ENSMUSP00000135827; -.
DR iPTMnet; Q9JJN2; -.
DR PhosphoSitePlus; Q9JJN2; -.
DR MaxQB; Q9JJN2; -.
DR PaxDb; Q9JJN2; -.
DR PeptideAtlas; Q9JJN2; -.
DR PRIDE; Q9JJN2; -.
DR ProteomicsDB; 275349; -.
DR MGI; MGI:2137668; Zfhx4.
DR eggNOG; KOG1146; Eukaryota.
DR InParanoid; Q9JJN2; -.
DR PhylomeDB; Q9JJN2; -.
DR ChiTaRS; Zfhx4; mouse.
DR EvolutionaryTrace; Q9JJN2; -.
DR PRO; PR:Q9JJN2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9JJN2; protein.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00086; homeodomain; 4.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00046; Homeodomain; 4.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00389; HOX; 4.
DR SMART; SM00355; ZnF_C2H2; 23.
DR SMART; SM00451; ZnF_U1; 7.
DR SUPFAM; SSF46689; SSF46689; 4.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS00027; HOMEOBOX_1; 2.
DR PROSITE; PS50071; HOMEOBOX_2; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; DNA-binding; Homeobox;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..3550
FT /note="Zinc finger homeobox protein 4"
FT /id="PRO_0000278466"
FT ZN_FING 611..634
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 642..665
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 697..721
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 765..787
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 915..939
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 971..993
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1019..1043
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1188..1211
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1217..1240
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1368..1390
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1396..1419
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1512..1538
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1564..1588
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1916..1939
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 2069..2128
FT /note="Homeobox 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT DNA_BIND 2166..2225
FT /note="Homeobox 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT ZN_FING 2252..2276
FT /note="C2H2-type 15; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2430..2452
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 2542..2601
FT /note="Homeobox 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT ZN_FING 2612..2635
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 2865..2924
FT /note="Homeobox 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT ZN_FING 2943..2967
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 3337..3361
FT /note="C2H2-type 19; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 3381..3405
FT /note="C2H2-type 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1467..1492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1779..1873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1973..2006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2318..2412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2490..2545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2746..2791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2810..2866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3051..3156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3261..3318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3424..3445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 3248..3277
FT /evidence="ECO:0000255"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1796..1817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1822..1860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1991..2005
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2353..2381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2382..2396
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2397..2412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2490..2509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2515..2545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2811..2836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2837..2858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3053..3093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3094..3112
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3119..3156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3261..3279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3296..3318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3429..3445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q86UP3"
FT MOD_RES 2645
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UP3"
FT CROSSLNK 1165
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86UP3"
FT CROSSLNK 1315
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86UP3"
FT CROSSLNK 1562
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86UP3"
FT CROSSLNK 1805
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86UP3"
FT CROSSLNK 3137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86UP3"
FT TURN 2946..2948
FT /evidence="ECO:0007829|PDB:2YRK"
FT STRAND 2954..2956
FT /evidence="ECO:0007829|PDB:2YRK"
FT HELIX 2958..2962
FT /evidence="ECO:0007829|PDB:2YRK"
FT HELIX 2965..2973
FT /evidence="ECO:0007829|PDB:2YRK"
SQ SEQUENCE 3550 AA; 392323 MW; 5CCBC400C45AB443 CRC64;
METCDSPPIS RQENGQSTSK LCGMTQLDNE VPEKVAGIEP DRENSSSHDN LKTDERKSEV
LLGFSIENAA ATQVTSAKEI PCNECATSFP SLQKYMEHHC PNARLPVLKD DESETSELED
SDVENLTGEI VYQPDGSAYI IEDSKESGQN AQTGANSKLF STAMFLDSLA SAGEKSDQSS
TAPVSFYPQI INTFHIASSL GKPFTADPAF PNTSALAGVG PVLHSFRVYD LRHKREKDYL
TSDGSAKNSC VSKDVPNNVD LSKFDGCVSD GKRKPVLMCF LCKLSFGYIR SFVTHAVHDH
RMTLNDEERR LLSNKCVSAI IQGIGKDKEP LISFLEPKKS TSVYPNFSTT NLIGPDPTFR
GLWSAFHVEN GDSLQAGFAF LKGSASPSSS AEQPLGITHM PKAEVNLGGL SSLVVNTPIT
SVSLSHLSSE SSKMSESKDQ ENNCERPKES TILHPNVGCP VKSEPTEPGD EDEEDAYSNE
LDDEEVLGEL TDSIGNKDFP LLNQSISPLS SSVLKFIEKG TSSSSGTIAE DTEKKKQAAA
TGRSNGNVTN SYSIGGKDFA DGSISRDGTT AAPSETTHGD EDSSTTHQHG FTPSTPGTPG
PGGDGSPGNG IECPKCDTVL GSSRSLGGHM TMMHSRNSCK TLKCPKCNWH YKYQQTLEAH
MKEKHPEPGG SCVYCKTGQP HPRLARGESY TRGYKPFRCE VCNYSTTTKG NLSIHMQSDK
HLNNVQNLQN GNGEQVFGHS APTPNTSLSG CGTPSPSKPK QKPTRRCEVC DYETNVARNL
RIHMTSEKHM HNMMLLQQNM KQIQHNLHLG LAPAEAELYQ YYLAQNIGLT GMKLENPAET
QLLLNPFQFD SATAAALAPG LGELSPYISD PALKLFQCAV CNKFTSDSLE ALSVHVNSER
SLPEEEWRAV IGDIYQCKLC NYNTQLKANF QLHCKTDKHM QKYQLVAHIK EGGKSNEWRL
KCIAIGNPVH LKCNACDYYT NSVDKLRLHT TNHRHEAALK LYKHLQKQEG AVNSESCCYY
CAVCDYSSKI KLNLVQHVRS VKHQQTEGLR KLQLHQQGLP SEEDNLSEIF FVKECPANEL
ETASLGARNG EDELIEQQLK AASEEPSEDA GDPLKPPTVA EDDEKEAHKR DNSEGKISTK
DPEVIVPEKE PKVVTGATQP LLLAKEDSTG TKRSKPTEDN KFCPEQFYQY PCCNYNSRDQ
SRIQMHVLSQ HSVQPVICCP LCQDVLSNKM HLQLHLTHLH SVSPDCVEKL LMTVPVPDVM
MLNSMLLPAA APEKSEQDPP TALTAEGSGK CSGDGPVDDK SMSGLEDSKV GVEIKNEEQK
PAKEPVEASE WNKTSSKDVN ISDALQDQLN EQQKRQPLSV SDRHVYKYRC NHCSLAFKTM
QKLQIHSQYH AIRAATMCTL CQRSFRTFQA LKKHLEAGHP ELSEAELQQL YASLPMNGEL
WAESETMTQD DHGIDQEMER EYEVDHEGKA SPVESDGSSI PDDLGLEPKR TLPFRKGPNF
TMEKFLDPSR PYKCTVCKES FTQKNILLVH YNSVSHLHKL KKVLQEASSP VPQEANSSTD
NKPYKCSTCS VAYSQSSTLE IHMRSVLHQT KARAAKLEPS RHLPSGHSIT AAVNSPGQGM
LESMSLASVN SKDTHLDAKE LNKKQTPELI SAQPTHHPPP RSPAQIQMQL QHELQQQAAF
FQPQFLNPAF LPHFPMTPEA LLQFQQPQFL FPFYIPGAEF SLGPDLGLPT STTFGVPGMT
GMAGSLLEDL KQQIQTQHHV GQTQLQFLQQ AQQYQAVQPQ LQPQNQQPPL PQQQQPQQQP
SKLLKQEQGS LASTDCQLMK DMPSYKEAEE VTEKQEKPKQ EFINDTEGLK DSKDIKKQKS
LEPCIPPPRI ASGARGNAAK ALLENFGFEL VIQYNENRQK VQKKGKSGEG ENSDKLECGI
CGKLFSNVLI LKSHQEHVHG QFFPYGALEK FARQYREAYD KLIQFLLPPL PPAPPQPSTL
GPVKIPNTVS APLQAPPPTP PSAPQQVQLP VSLDLPLFPS IMMQPVQHPA LPPQLALQLP
QMDTLSADLT QLCQQQLGID PNFLRHSQFK RPRTRITDDQ LKILRAYFDI NNSPSEEQIQ
EMAEKSGLSQ KVVKHWFRNT LFKERQRNKD SPYNFSNPPI TVLEDIRIDP QPTSLEHYKS
DAAFSKRSSR TRFTDYQLRV LQDFFDTNAY PKDDEIEQLS TVLNLPTRVI VVWFQNARQK
ARKSYENQAE AKDNEKRELT NERYIRTSNM QYQCKKCNVV FPRIFDLITH QKKQCYKDED
DDAQDESQTE DSMDATDQVL YKHCMVSGQT DTAKSTATLV ASSGSGTSTP LIPSPKPEPE
KNSPKTEYPG EKTKQSDPSL PQGTKSAPSS VLTSSEPQQA SIPQPPTQPP KQPQLIGRPP
SASQTPIPSS PLQISMTSLQ NSLPPQLLQY PCDQCTLAFP TLELWKEHQH MHFLAAQNQF
LHSPFLERPM DMPYMIFDPN NPLMTGQLLG SSLTQMPPQT STAHTTAPAS VAASLKRKLE
DKEDNNCSEK EGGNSGEDQH RDKRLRTTIT PEQLEILYEK YLLDSNPTRK MLDHIAREVG
LKKRVVQVWF QNTRARERKG QFRAVGPAQS HKRCPFCRAL FKAKSALESH IRSRHWNEGK
QAGYSLPPSP LISTEDGGES PQKYIYFDYP SLPLTKIDLS TENELASTVS TPVSKTAELS
PKNLLSPSSF KAECPEDVEN LNAPSADAGY DQSKTDFDET SSINTAISDA TTGDEGAADM
ENTGGSGEVK PALSPKETKT LDSLQKPATT PTTEVCDDKF LFSLTSPSIH FNDKDGDHDQ
SFYITDDPDD NADRSETSSI ADPSSPNPFG SSNPFKSKSN DRPGHKRFRT QMSNLQLKVL
KACFSDYRTP TMQECEMLGN EIGLPKRVVQ VWFQNARAKE RKFKINIGKP FMINQSGTDG
TKPECTLCGV KYSARLSIRD HIFSKQHISK VRETVGSQLD REKDYLAPTT VRQLMAQQEL
DRIKKASDVL GLTVQQQGIT DNCSLHGISL QAAYPGLPGL PPVILPGMNG PSSLPGFPQN
SNTLTSPGTG MLGFPSSATS SPALSLSSGP TKSLLQTPPP PPPPPPPPSS LSGQQTEPQN
KESEKKQTKP NKVKKIKEEE SEAIKPEKHP KKEEKISSAL TVLGKVVGET HMDPTQLQAL
QNAIAGDPAS FIGGQFLPYF IPGFASYFSP QLPGTVQGGY LPPICGVESL FPYGPAVPQT
LAGLSPGALL QQYQQYQQSL QDSLQKQQKQ QQEQQQKPVP AKTAKGEGDQ PQSSNEASET
KEEKSTAPES TKEEVQLDSK SAEFSDTCIV PFVKYEFVCR KCQMMFTDED ATVNHQKSFC
YFGQPLIDPQ ETVLRIPVSK YQCLACDLAL SGNEALSQHL QSSLHKEKTI KQAMRNAKEH
VRLLPHSVCS PPPNTSSTSP SAASSNNTYP HLSCFSMKSW PNILFQASAR KAASSPSSPP
SLSLPSTVTS SLCSTSGVQT SLPTESCSDE SDSELSQKLQ DLDNSLEVKA KPASGLDGNF
NSVRMDMFSV
