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   24-JAN-2024, entry version 206.
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; DOI=10.1002/j.1460-2075.1991.tb07664.x;
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; 10090-ENSMUSP00000021016; -.
DR   PeptideAtlas; P27889; -.
DR   ProteomicsDB; 273154; -. [P27889-1]
DR   ProteomicsDB; 273155; -. [P27889-2]
DR   ProteomicsDB; 273156; -. [P27889-3]
DR   ProteomicsDB; 273157; -. [P27889-4]
DR   Antibodypedia; 72795; 585 antibodies from 38 providers.
DR   DNASU; 21410; -.
DR   Ensembl; ENSMUST00000021016.10; ENSMUSP00000021016.3; ENSMUSG00000020679.12. [P27889-1]
DR   Ensembl; ENSMUST00000108113.3; ENSMUSP00000103748.2; ENSMUSG00000020679.12. [P27889-3]
DR   Ensembl; ENSMUST00000108114.9; ENSMUSP00000103749.3; ENSMUSG00000020679.12. [P27889-2]
DR   GeneID; 21410; -.
DR   KEGG; mmu:21410; -.
DR   UCSC; uc007kpx.2; mouse. [P27889-1]
DR   UCSC; uc007kpy.2; mouse. [P27889-2]
DR   AGR; MGI:98505; -.
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; GQSDDTC; -.
DR   OrthoDB; 5398560at2759; -.
DR   PhylomeDB; P27889; -.
DR   TreeFam; TF320327; -.
DR   BioGRID-ORCS; 21410; 5 hits in 79 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 139 other cell types or tissues.
DR   ExpressionAtlas; P27889; baseline and differential.
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: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:0045893; P:positive regulation of DNA-templated transcription; 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 by RNA polymerase II; ISO: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:0060677; P:ureteric bud elongation; IMP:MGI.
DR   CDD; cd00086; homeodomain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 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; HEPATOCYTE NUCLEAR FACTOR 1; 1.
DR   PANTHER; PTHR11568:SF2; HEPATOCYTE NUCLEAR FACTOR 1-BETA; 1.
DR   Pfam; PF04814; HNF-1_N; 1.
DR   Pfam; PF04812; HNF-1B_C; 1.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF100957; Dimerization cofactor of HNF-1 alpha; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 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.
DR   Genevisible; P27889; MM.
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
//