ZN608_MOUSE
ID ZN608_MOUSE Reviewed; 1511 AA.
AC Q56A10; Q6ZPU8; Q8BIG5; Q8BJ06;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Zinc finger protein 608;
GN Name=Znf608; Synonyms=Kiaa1281, Zfp608;
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 [LARGE SCALE MRNA] OF 861-1511 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Head;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N-3; 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1260-1511 (ISOFORM 2).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
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. 10:167-180(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420; SER-423; THR-480;
RP SER-492; SER-626 AND SER-781, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC 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).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23076336; DOI=10.1038/gene.2012.47;
RA Reed N.P., Henderson M.A., Oltz E.M., Aune T.M.;
RT "Reciprocal regulation of Rag expression in thymocytes by the zinc-finger
RT proteins, Zfp608 and Zfp609.";
RL Genes Immun. 14:7-12(2013).
CC -!- FUNCTION: Transcription factor, which represses ZNF609 transcription.
CC {ECO:0000269|PubMed:23076336}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q56A10-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q56A10-2; Sequence=VSP_023667, VSP_023668;
CC Name=3;
CC IsoId=Q56A10-3; Sequence=VSP_023665, VSP_023666;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in thymocytes.
CC {ECO:0000269|PubMed:23076336}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC36234.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK047979; BAC33204.1; -; mRNA.
DR EMBL; AK076178; BAC36234.1; ALT_INIT; mRNA.
DR EMBL; BC092219; AAH92219.1; -; mRNA.
DR EMBL; AK129321; BAC98131.1; -; mRNA.
DR CCDS; CCDS37824.1; -. [Q56A10-1]
DR RefSeq; NP_786927.2; NM_175751.4. [Q56A10-1]
DR RefSeq; XP_006526020.1; XM_006525957.3. [Q56A10-1]
DR AlphaFoldDB; Q56A10; -.
DR BioGRID; 234596; 1.
DR STRING; 10090.ENSMUSP00000068192; -.
DR iPTMnet; Q56A10; -.
DR PhosphoSitePlus; Q56A10; -.
DR EPD; Q56A10; -.
DR MaxQB; Q56A10; -.
DR PaxDb; Q56A10; -.
DR PeptideAtlas; Q56A10; -.
DR PRIDE; Q56A10; -.
DR ProteomicsDB; 275086; -. [Q56A10-1]
DR ProteomicsDB; 275087; -. [Q56A10-2]
DR ProteomicsDB; 275088; -. [Q56A10-3]
DR Antibodypedia; 1014; 90 antibodies from 25 providers.
DR Ensembl; ENSMUST00000064763; ENSMUSP00000068192; ENSMUSG00000052713. [Q56A10-1]
DR GeneID; 269023; -.
DR KEGG; mmu:269023; -.
DR UCSC; uc008eyc.2; mouse. [Q56A10-1]
DR UCSC; uc008eyg.1; mouse. [Q56A10-3]
DR CTD; 269023; -.
DR MGI; MGI:2442338; Zfp608.
DR VEuPathDB; HostDB:ENSMUSG00000052713; -.
DR eggNOG; ENOG502QSUK; Eukaryota.
DR GeneTree; ENSGT00390000008748; -.
DR HOGENOM; CLU_004142_1_0_1; -.
DR InParanoid; Q56A10; -.
DR OMA; PSGHLYG; -.
DR PhylomeDB; Q56A10; -.
DR TreeFam; TF329775; -.
DR BioGRID-ORCS; 269023; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Zfp608; mouse.
DR PRO; PR:Q56A10; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q56A10; protein.
DR Bgee; ENSMUSG00000052713; Expressed in rostral migratory stream and 223 other tissues.
DR ExpressionAtlas; Q56A10; baseline and differential.
DR Genevisible; Q56A10; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033085; P:negative regulation of T cell differentiation in thymus; TAS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR040010; ZN608/ZN609.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR21564; PTHR21564; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Isopeptide bond; Metal-binding;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1511
FT /note="Zinc finger protein 608"
FT /id="PRO_0000280421"
FT ZN_FING 552..577
FT /note="C2H2-type"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1219..1334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1422..1468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 277..303
FT /evidence="ECO:0000255"
FT COMPBIAS 50..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1051
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1433..1454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 480
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 894
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD9"
FT MOD_RES 963
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD9"
FT MOD_RES 1097
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD9"
FT CROSSLNK 282
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD9"
FT CROSSLNK 879
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD9"
FT CROSSLNK 1117
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD9"
FT CROSSLNK 1175
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD9"
FT CROSSLNK 1181
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD9"
FT CROSSLNK 1198
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD9"
FT CROSSLNK 1215
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD9"
FT CROSSLNK 1233
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD9"
FT CROSSLNK 1249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD9"
FT CROSSLNK 1291
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD9"
FT CROSSLNK 1309
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD9"
FT CROSSLNK 1413
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD9"
FT VAR_SEQ 388..423
FT /note="VLVVNVTWRNKTYVGTLLDCTKHDWAPPRFCESPTS -> KYVLFLFISLCP
FT LLHDVSLSICEGNLFSLWFERIER (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023665"
FT VAR_SEQ 424..1511
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023666"
FT VAR_SEQ 1432..1455
FT /note="PVEKASTEREREAERERDRHSPFS -> VSLLLLVVKRPCLVGEGRQETEQS
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_023667"
FT VAR_SEQ 1456..1511
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_023668"
FT CONFLICT 931..932
FT /note="AK -> PN (in Ref. 1; BAC36234)"
FT /evidence="ECO:0000305"
FT CONFLICT 987
FT /note="Q -> H (in Ref. 1; BAC36234)"
FT /evidence="ECO:0000305"
FT CONFLICT 1039
FT /note="K -> N (in Ref. 1; BAC36234)"
FT /evidence="ECO:0000305"
FT CONFLICT 1436
FT /note="A -> G (in Ref. 1; BAC36234)"
FT /evidence="ECO:0000305"
FT CONFLICT 1449
FT /note="D -> G (in Ref. 1; BAC36234)"
FT /evidence="ECO:0000305"
FT CONFLICT 1490
FT /note="V -> G (in Ref. 1; BAC36234)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1511 AA; 162345 MW; 4331F1298053D5AC CRC64;
MSVNVSTAGK GVDPNTVDTY DSGDDWEIGV GNLIIDLDAD LEKDRQKFEM NNSTNTTTNT
TKDCGGPASN GTCSTSALAD GLKFASVQPS APQGNSHKET SKSKVKRAKT SKDANKSLPS
AALYGIPEIS STGKRQEVQG RPGEATGMNS ALGQSVSGGG SSNPNSNGTS TGTSAATAGA
GSCGKSKEEK PGKSHSSRGA KRDKDAARSR KEKHDLLQGH QNGGGGQAPS GGHLYGFGTK
SNGSGASPFH CGGAGSGSVG AAGEVSKTAP DSTLMGNSML VKKEEEEEES HRRIKKLKTE
KVDPLFTVPA PPPPIASSLA PQIPPSYFPP SSSNIAAPVE QLLVRTRSVG VNTCEVGVVT
EPECLGPCEP GTSVNLEGIV WHETEEGVLV VNVTWRNKTY VGTLLDCTKH DWAPPRFCES
PTSDLEMRGG RGRGKRARSA AAAPGSEVSF TESRGLQSKN RGGANGKGRR GSLNASGRRT
PPNCAAEDIK ASPSSTNKRK NKPPMELDLN SSSEDSKPGK RVRTNSRSTP TTPQGKPETT
FLDQGCSSPV LIDCPHPNCN KKYKHINGLR YHQAHAHLDP ENKLEFEPDS EDKISDCEEA
LSNVALECNE SSTSVSSYDQ TKAPGSPGAG NPPGTPKGKR EHVSNGPGPI IGSKTGKNSG
KKRGLNNELN NLPVISNMTA ALDICSATDS NLTAEMPKLE AEGLIDKKSL GDKEKGKKAN
NCKMDKNLSK LKSARPIAPA PAPTPPQLIA IPTAAFTSTT TGTIPGLPSL TTTVVQATPK
SPPLKPIQPK PTIMGEPITV NPALVSLKDR KKKEKRKLKD KEGKETGGPK MDAKLGKLEE
AKAASKDLSG HFLKDHLGKS EGLANGLSES QESRMASIKA EADKVYTFTD NAPSPSIGSA
SRMECSTLVN GQAPMAPLHV LTQNGAESAA AKTSSPAYSD ISDAADDGGS DSRSEGMRSK
ASSPSDTFSN KDGVVKGHPS TSAQPSQLKE SHSPYYHGYE PYYSPSYMHP GQVGAPAAGN
GGSTQGMKIK KESEEDAEKK DKAEQLESKK VDHTSAPLQP QHQSVITQRH PALAQSLYYG
QYAYGLYMDQ KSLMATSPAY RQQYEKYYED QRLAEQKMAQ SGRGDCERKA ELPLKELGKE
DNKQKNMPSA TISKAPSTPE PNKNHSKLGP SVPNKTEETG KSQLLSSHQQ QLQADSFKAK
QMENHQLIKE AVEMKSVMDS MKQTGVDPTS RFKQDPESRT WHHYVYQPKY LDQQKPEELD
REKKLKEDSP RKTPNKESGV SSLPVSLTNI KEEPKEGKRP DSQSVEENKL KNDDRKTPVN
WKDSRGTRVA VSSPMSQHQS YIQYLHAYPY PQMYDPSHPA YRAVSPVLMH SYPGAYLSPG
FHYPVYGKMS GREEAEKVNT SPSINTKTAS EAKALDLLQH HANQYRSKSP APVEKASTER
EREAERERDR HSPFSQRHLH THHHTHVGMG YPLIPGQYDP FQGLTSAALV ASQQVAAQAS
ASGMFPAQRR E
