HNF1B_MOUSE
ID HNF1B_MOUSE Reviewed; 558 AA.
AC P27889; Q5NC37; Q8R162; Q9CS26; Q9R1W1; Q9R1W2; Q9WTL5; Q9WTL6;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Hepatocyte nuclear factor 1-beta;
DE Short=HNF-1-beta;
DE Short=HNF-1B;
DE AltName: Full=Homeoprotein LFB3;
DE AltName: Full=Transcription factor 2;
DE Short=TCF-2;
GN Name=Hnf1b; Synonyms=Hnf-1b, Tcf2;
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).
RX PubMed=1673925;
RA de Simone V., de Magistris L., Lazzaro L., Gerstner J., Monaci P.,
RA Nicosia A., Cortese R.;
RT "LFB3, a heterodimer-forming homeoprotein of the LFB1 family, is expressed
RT in specialized epithelia.";
RL EMBO J. 10:1435-1443(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT ALA-222.
RC STRAIN=C3H/HeJ, and NSY; TISSUE=Kidney;
RX PubMed=10331425; DOI=10.2337/diabetes.48.5.1168;
RA Ueda H., Ikegami H., Kawaguchi Y., Fujisawa T., Yamato E., Shibata M.,
RA Ogihara T.;
RT "Genetic analysis of late-onset type 2 diabetes in a mouse model of human
RT complex trait.";
RL Diabetes 48:1168-1174(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-222.
RC STRAIN=C3H/HeJ, NOD, and NSY;
RX PubMed=11456274; DOI=10.1507/endocrj.48.241;
RA Yamada K., Ikegami H., Kawaguchi Y., Fujisawa T., Hotta M., Ueda H.,
RA Shintani M., Nojima K., Kawabata Y., Ono M., Nishino M., Itoi M.,
RA Babaya N., Shibata M., Makino S., Ogihara T.;
RT "Sequence analysis of candidate genes for common susceptibility to type 1
RT and type 2 diabetes in mice.";
RL Endocr. J. 48:241-247(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Liver;
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]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Kidney;
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-52; SER-75 AND
RP SER-80, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Pancreas;
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: Transcription factor that binds to the inverted palindrome
CC 5'-GTTAATNATTAAC-3' (By similarity). Binds to the FPC element in the
CC cAMP regulatory unit of the PLAU gene (By similarity). Transcriptional
CC activity is increased by coactivator PCBD1 (By similarity).
CC {ECO:0000250|UniProtKB:P35680, ECO:0000250|UniProtKB:Q03365}.
CC -!- SUBUNIT: Binds DNA as a dimer. Can form homodimer or heterodimer with
CC HNF1-alpha (By similarity). Interacts (via HNF-p1 domain) with PCBD1;
CC the interaction increases its transactivation activity (By similarity).
CC {ECO:0000250|UniProtKB:P35680}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P27889-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P27889-2; Sequence=VSP_007100;
CC Name=3;
CC IsoId=P27889-3; Sequence=VSP_007099;
CC Name=4;
CC IsoId=P27889-4; Sequence=VSP_007099, VSP_007100;
CC -!- SIMILARITY: Belongs to the HNF1 homeobox family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB31632.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X55842; CAA39358.1; -; mRNA.
DR EMBL; AB008174; BAA77718.1; -; mRNA.
DR EMBL; AB008175; BAA77719.1; -; mRNA.
DR EMBL; AB008176; BAA77720.1; -; mRNA.
DR EMBL; AB008177; BAA77721.1; -; mRNA.
DR EMBL; AB052659; BAB60814.1; -; mRNA.
DR EMBL; AK004837; BAB23604.1; -; mRNA.
DR EMBL; AK019258; BAB31632.2; ALT_INIT; mRNA.
DR EMBL; AL669868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025189; AAH25189.1; -; mRNA.
DR CCDS; CCDS25179.1; -. [P27889-1]
DR CCDS; CCDS70271.1; -. [P27889-2]
DR CCDS; CCDS70272.1; -. [P27889-3]
DR PIR; A39633; A39633.
DR RefSeq; NP_001278197.1; NM_001291268.1. [P27889-2]
DR RefSeq; NP_001278198.1; NM_001291269.1. [P27889-3]
DR RefSeq; NP_033356.2; NM_009330.3. [P27889-1]
DR RefSeq; XP_006532859.1; XM_006532796.3. [P27889-3]
DR AlphaFoldDB; P27889; -.
DR BMRB; P27889; -.
DR SMR; P27889; -.
DR BioGRID; 204003; 5.
DR IntAct; P27889; 1.
DR STRING; 10090.ENSMUSP00000021016; -.
DR iPTMnet; P27889; -.
DR PhosphoSitePlus; P27889; -.
DR MaxQB; P27889; -.
DR PaxDb; P27889; -.
DR PeptideAtlas; P27889; -.
DR PRIDE; P27889; -.
DR ProteomicsDB; 273154; -. [P27889-1]
DR ProteomicsDB; 273155; -. [P27889-2]
DR ProteomicsDB; 273156; -. [P27889-3]
DR ProteomicsDB; 273157; -. [P27889-4]
DR Antibodypedia; 72795; 530 antibodies from 38 providers.
DR DNASU; 21410; -.
DR Ensembl; ENSMUST00000021016; ENSMUSP00000021016; ENSMUSG00000020679. [P27889-1]
DR Ensembl; ENSMUST00000108113; ENSMUSP00000103748; ENSMUSG00000020679. [P27889-3]
DR Ensembl; ENSMUST00000108114; ENSMUSP00000103749; ENSMUSG00000020679. [P27889-2]
DR GeneID; 21410; -.
DR KEGG; mmu:21410; -.
DR UCSC; uc007kpx.2; mouse. [P27889-1]
DR UCSC; uc007kpy.2; mouse. [P27889-2]
DR CTD; 6928; -.
DR MGI; MGI:98505; Hnf1b.
DR VEuPathDB; HostDB:ENSMUSG00000020679; -.
DR eggNOG; ENOG502QRPW; Eukaryota.
DR GeneTree; ENSGT00940000153818; -.
DR HOGENOM; CLU_035503_0_0_1; -.
DR InParanoid; P27889; -.
DR OMA; DDTCSEP; -.
DR OrthoDB; 409935at2759; -.
DR PhylomeDB; P27889; -.
DR TreeFam; TF320327; -.
DR BioGRID-ORCS; 21410; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Hnf1b; mouse.
DR PRO; PR:P27889; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P27889; protein.
DR Bgee; ENSMUSG00000020679; Expressed in right kidney and 136 other tissues.
DR ExpressionAtlas; P27889; baseline and differential.
DR Genevisible; P27889; MM.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IPI:MGI.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:MGI.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:MGI.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISO:MGI.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IMP:MGI.
DR GO; GO:0048598; P:embryonic morphogenesis; ISO:MGI.
DR GO; GO:0031018; P:endocrine pancreas development; ISS:UniProtKB.
DR GO; GO:0007492; P:endoderm development; IMP:MGI.
DR GO; GO:0001706; P:endoderm formation; ISO:MGI.
DR GO; GO:0001714; P:endodermal cell fate specification; IMP:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0060429; P:epithelium development; IMP:MGI.
DR GO; GO:0048806; P:genitalia development; ISS:UniProtKB.
DR GO; GO:0061017; P:hepatoblast differentiation; IMP:MGI.
DR GO; GO:0070365; P:hepatocyte differentiation; IEA:Ensembl.
DR GO; GO:0030902; P:hindbrain development; IMP:MGI.
DR GO; GO:0001826; P:inner cell mass cell differentiation; IMP:MGI.
DR GO; GO:0030073; P:insulin secretion; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0060993; P:kidney morphogenesis; IGI:MGI.
DR GO; GO:0001889; P:liver development; IMP:MGI.
DR GO; GO:1900200; P:mesenchymal cell apoptotic process involved in metanephros development; IMP:MGI.
DR GO; GO:0072177; P:mesonephric duct development; IMP:MGI.
DR GO; GO:0072181; P:mesonephric duct formation; IMP:MGI.
DR GO; GO:0072164; P:mesonephric tubule development; IGI:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0061296; P:negative regulation of mesenchymal cell apoptotic process involved in mesonephric nephron morphogenesis; IMP:MGI.
DR GO; GO:1900212; P:negative regulation of mesenchymal cell apoptotic process involved in metanephros development; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0072176; P:nephric duct development; IMP:MGI.
DR GO; GO:0072179; P:nephric duct formation; IMP:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0039020; P:pronephric nephron tubule development; ISO:MGI.
DR GO; GO:0048793; P:pronephros development; ISO:MGI.
DR GO; GO:0065004; P:protein-DNA complex assembly; ISO:MGI.
DR GO; GO:0072095; P:regulation of branch elongation involved in ureteric bud branching; IMP:MGI.
DR GO; GO:0035565; P:regulation of pronephros size; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0030111; P:regulation of Wnt signaling pathway; IMP:MGI.
DR GO; GO:0009749; P:response to glucose; IMP:MGI.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0060677; P:ureteric bud elongation; IMP:MGI.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR039066; HNF-1.
DR InterPro; IPR006899; HNF-1_N.
DR InterPro; IPR044869; HNF-1_POU.
DR InterPro; IPR023219; HNF1_dimer_N_dom_sf.
DR InterPro; IPR006897; HNF1b_C.
DR InterPro; IPR044866; HNF_P1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR PANTHER; PTHR11568; PTHR11568; 1.
DR Pfam; PF04814; HNF-1_N; 1.
DR Pfam; PF04812; HNF-1B_C; 1.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF100957; SSF100957; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS51937; HNF_P1; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS51936; POU_4; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Homeobox; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..558
FT /note="Hepatocyte nuclear factor 1-beta"
FT /id="PRO_0000049122"
FT DOMAIN 1..32
FT /note="HNF-p1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01286"
FT DOMAIN 93..188
FT /note="POU-specific atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01285"
FT DNA_BIND 231..311
FT /note="Homeobox; HNF1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..31
FT /note="Dimerization"
FT /evidence="ECO:0000250"
FT REGION 66..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..123
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_007099"
FT VAR_SEQ 183..208
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10331425,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_007100"
FT VARIANT 222
FT /note="T -> A (in strain: NSY)"
FT /evidence="ECO:0000269|PubMed:10331425,
FT ECO:0000269|PubMed:11456274"
FT CONFLICT 67
FT /note="N -> S (in Ref. 4; BAB31632)"
FT /evidence="ECO:0000305"
FT CONFLICT 423..429
FT /note="LSHHNPQ -> THSPPQSP (in Ref. 1; CAA39358)"
FT /evidence="ECO:0000305"
FT CONFLICT 520..521
FT /note="PP -> HT (in Ref. 1; CAA39358)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 558 AA; 61588 MW; D4F2BC92B64374A6 CRC64;
MVSKLTSLQQ ELLSALLSSG VTKEVLIQAL EELLPSPNFG VKLETLPLSP GSGADLDTKP
VFHTLTNGHA KGRLSGDEGS EDGDDYDTPP ILKELQALNT EEAAEQRAEV DRMLSEDPWR
AAKMIKGYMQ QHNIPQREVV DVTGLNQSHL SQHLNKGTPM KTQKRAALYT WYVRKQREIL
RQFNQTVQSS GNMTDKSSQD QLLFLFPEFS QQNQGPGQSE DTCSEPTNKK MRRNRFKWGP
ASQQILYQAY DRQKNPSKEE REALVEECNR AECLQRGVSP SKAHGLGSNL VTEVRVYNWF
ANRRKEEAFR QKLAMDAYSS NQTHNLNPLL THGSPHHQPS SSPPNKMSGV RYNQPGNNEV
TSSSTISHHG NSAMVTSQSV LQQVSPASLD PGHSLLSPDS KMQITVSGGG LPPVSTLTNI
HSLSHHNPQQ SQNLIMTPLS GVMAIAQSLN TSQAQGVPVI NSVASSLAAL QPVQFSQQLH
SPHQQPLMQQ SPGSHMAQQP FMAAVTQLQN SHMYAHKQEP PQYSHTSRFP SAMVVTDTSS
INTLTSMSSS KQCPLQAW
