PROX1_MOUSE
ID PROX1_MOUSE Reviewed; 737 AA.
AC P48437; O88478; Q3UPV1; Q543D8;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Prospero homeobox protein 1;
DE AltName: Full=Homeobox prospero-like protein PROX1;
DE Short=PROX-1;
GN Name=Prox1;
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.
RX PubMed=9703987; DOI=10.1006/bbrc.1998.8989;
RA Tomarev S.I., Zinovieva R.D., Chang B., Hawes N.L.;
RT "Characterization of the mouse Prox1 gene.";
RL Biochem. Biophys. Res. Commun. 248:684-689(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye, and Heart;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 573-737, AND TISSUE SPECIFICITY.
RX PubMed=7908825; DOI=10.1016/0925-4773(93)90012-m;
RA Oliver G., Sosa-Pineda B., Geisendorf S., Spana E.P., Doe C.Q., Gruss P.;
RT "Prox 1, a prospero-related homeobox gene expressed during mouse
RT development.";
RL Mech. Dev. 44:3-16(1993).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179; SER-511 AND SER-514, AND
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179; SER-291; SER-295;
RP SER-511 AND SER-514, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Pancreas, and Spleen;
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 [8]
RP REVIEW.
RX PubMed=22733308; DOI=10.1007/s10555-012-9390-8;
RA Elsir T., Smits A., Lindstroem M.S., Nister M.;
RT "Transcription factor PROX1: its role in development and cancer.";
RL Cancer Metastasis Rev. 31:793-805(2012).
RN [9]
RP FUNCTION, INDUCTION, SUBCELLULAR LOCATION, INTERACTION WITH RORA AND RORG,
RP AND DOMAIN.
RX PubMed=23723244; DOI=10.1093/nar/gkt447;
RA Takeda Y., Jetten A.M.;
RT "Prospero-related homeobox 1 (Prox1) functions as a novel modulator of
RT retinoic acid-related orphan receptors alpha- and gamma-mediated
RT transactivation.";
RL Nucleic Acids Res. 41:6992-7008(2013).
CC -!- FUNCTION: Transcription factor involved in developmental processes such
CC as cell fate determination, gene transcriptional regulation and
CC progenitor cell regulation in a number of organs. Plays a critical role
CC in embryonic development and functions as a key regulatory protein in
CC neurogenesis and the development of the heart, eye lens, liver,
CC pancreas and the lymphatic system. Involved in the regulation of the
CC circadian rhythm. Represses: transcription of the retinoid-related
CC orphan receptor RORG, transcriptional activator activity of RORA and
CC RORG and the expression of RORA/G-target genes including core clock
CC components: ARNTL/BMAL1, NPAS2 and CRY1 and metabolic genes: AVPR1A and
CC ELOVL3. {ECO:0000269|PubMed:23723244, ECO:0000303|PubMed:22733308}.
CC -!- SUBUNIT: Interacts with RORA and RORG (via AF-2 motif).
CC {ECO:0000269|PubMed:23723244}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23723244}. Note=RORG
CC promotes its nuclear localization. {ECO:0000269|PubMed:23723244}.
CC -!- TISSUE SPECIFICITY: Expressed in the young neurons of the
CC subventricular region of the CNS, developing eye lens and pancreas. It
CC is also found in the developing liver, heart and skeletal muscle. In
CC the eye, expressed in the lens and retina at postnatal day 10. In the
CC retina, localized to the inner nuclear layer. In the lens, localized to
CC epithelial and fiber cells. {ECO:0000269|PubMed:7908825,
CC ECO:0000269|PubMed:9703987}.
CC -!- INDUCTION: Expressed in a circadian manner in the liver with a peak at
CC ZT4. {ECO:0000269|PubMed:23723244}.
CC -!- DOMAIN: The Prospero-type homeodomain and the adjacent Prospero domain
CC act as a single structural unit, the Homeo-Prospero domain (Potential).
CC The Prospero-type homeodomain is essential for repression of RORG
CC transcriptional activator activity (PubMed:23723244).
CC {ECO:0000255|PROSITE-ProRule:PRU01162, ECO:0000269|PubMed:23723244}.
CC -!- SIMILARITY: Belongs to the Prospero homeodomain family.
CC {ECO:0000255|PROSITE-ProRule:PRU01162}.
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DR EMBL; AF061576; AAC32824.1; -; mRNA.
DR EMBL; AK052889; BAC35190.1; -; mRNA.
DR EMBL; AK143179; BAE25293.1; -; mRNA.
DR EMBL; BC051411; AAH51411.1; -; mRNA.
DR CCDS; CCDS35822.1; -.
DR PIR; JE0269; JE0269.
DR RefSeq; NP_032963.1; NM_008937.2.
DR RefSeq; XP_006497191.1; XM_006497128.3.
DR AlphaFoldDB; P48437; -.
DR BMRB; P48437; -.
DR SMR; P48437; -.
DR BioGRID; 202396; 5.
DR DIP; DIP-58960N; -.
DR IntAct; P48437; 2.
DR STRING; 10090.ENSMUSP00000135703; -.
DR iPTMnet; P48437; -.
DR PhosphoSitePlus; P48437; -.
DR MaxQB; P48437; -.
DR PaxDb; P48437; -.
DR PeptideAtlas; P48437; -.
DR PRIDE; P48437; -.
DR ProteomicsDB; 291888; -.
DR Antibodypedia; 34616; 648 antibodies from 44 providers.
DR DNASU; 19130; -.
DR Ensembl; ENSMUST00000010319; ENSMUSP00000010319; ENSMUSG00000010175.
DR Ensembl; ENSMUST00000175916; ENSMUSP00000135703; ENSMUSG00000010175.
DR Ensembl; ENSMUST00000177288; ENSMUSP00000135066; ENSMUSG00000010175.
DR GeneID; 19130; -.
DR KEGG; mmu:19130; -.
DR UCSC; uc007ebc.2; mouse.
DR CTD; 5629; -.
DR MGI; MGI:97772; Prox1.
DR VEuPathDB; HostDB:ENSMUSG00000010175; -.
DR eggNOG; KOG3779; Eukaryota.
DR GeneTree; ENSGT00940000154790; -.
DR HOGENOM; CLU_016051_0_0_1; -.
DR InParanoid; P48437; -.
DR OMA; NGDNHNF; -.
DR OrthoDB; 373478at2759; -.
DR PhylomeDB; P48437; -.
DR TreeFam; TF316638; -.
DR BioGRID-ORCS; 19130; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Prox1; mouse.
DR PRO; PR:P48437; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P48437; protein.
DR Bgee; ENSMUSG00000010175; Expressed in lens of camera-type eye and 178 other tissues.
DR Genevisible; P48437; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0050692; F:DNA binding domain binding; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0050693; F:LBD domain binding; ISO:MGI.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0090425; P:acinar cell differentiation; IMP:MGI.
DR GO; GO:0060414; P:aorta smooth muscle tissue morphogenesis; IMP:BHF-UCL.
DR GO; GO:0055009; P:atrial cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
DR GO; GO:0060837; P:blood vessel endothelial cell differentiation; IMP:MGI.
DR GO; GO:0061114; P:branching involved in pancreas morphogenesis; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0021707; P:cerebellar granule cell differentiation; IMP:BHF-UCL.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0021542; P:dentate gyrus development; IMP:BHF-UCL.
DR GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IEP:BHF-UCL.
DR GO; GO:0060214; P:endocardium formation; IMP:BHF-UCL.
DR GO; GO:0010631; P:epithelial cell migration; IMP:MGI.
DR GO; GO:0002194; P:hepatocyte cell migration; IMP:MGI.
DR GO; GO:0070365; P:hepatocyte differentiation; IEP:BHF-UCL.
DR GO; GO:0072574; P:hepatocyte proliferation; IMP:MGI.
DR GO; GO:0048839; P:inner ear development; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0070309; P:lens fiber cell morphogenesis; IMP:BHF-UCL.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:BHF-UCL.
DR GO; GO:0046619; P:lens placode formation involved in camera-type eye formation; IEP:BHF-UCL.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0001945; P:lymph vessel development; IMP:MGI.
DR GO; GO:0001946; P:lymphangiogenesis; ISO:MGI.
DR GO; GO:0060836; P:lymphatic endothelial cell differentiation; IMP:MGI.
DR GO; GO:0060838; P:lymphatic endothelial cell fate commitment; ISO:MGI.
DR GO; GO:0070858; P:negative regulation of bile acid biosynthetic process; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; ISO:MGI.
DR GO; GO:0007405; P:neuroblast proliferation; IMP:MGI.
DR GO; GO:0048664; P:neuron fate determination; IMP:MGI.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; IMP:BHF-UCL.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:BHF-UCL.
DR GO; GO:1901978; P:positive regulation of cell cycle checkpoint; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:BHF-UCL.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:2000979; P:positive regulation of forebrain neuron differentiation; IMP:BHF-UCL.
DR GO; GO:0060421; P:positive regulation of heart growth; IMP:BHF-UCL.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IMP:BHF-UCL.
DR GO; GO:0060298; P:positive regulation of sarcomere organization; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
DR GO; GO:0030240; P:skeletal muscle thin filament assembly; IMP:BHF-UCL.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0048845; P:venous blood vessel morphogenesis; IMP:BHF-UCL.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
DR GO; GO:0055005; P:ventricular cardiac myofibril assembly; IMP:BHF-UCL.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL.
DR Gene3D; 1.10.10.500; -; 1.
DR InterPro; IPR023082; Homeo_prospero_dom.
DR InterPro; IPR037131; Homeo_prospero_dom_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR039350; Prospero_homeodomain.
DR InterPro; IPR007738; Prox1.
DR PANTHER; PTHR12198; PTHR12198; 1.
DR PANTHER; PTHR12198:SF6; PTHR12198:SF6; 1.
DR Pfam; PF05044; HPD; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51818; HOMEO_PROSPERO; 1.
PE 1: Evidence at protein level;
KW Biological rhythms; Developmental protein; DNA-binding; Homeobox;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..737
FT /note="Prospero homeobox protein 1"
FT /id="PRO_0000208881"
FT DOMAIN 577..635
FT /note="Prospero-type homeo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01162"
FT DOMAIN 636..735
FT /note="Prospero"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01162"
FT REGION 1..28
FT /note="Interaction with RORG"
FT /evidence="ECO:0000269|PubMed:23723244"
FT REGION 103..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..735
FT /note="Homeo-Prospero"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01162"
FT REGION 723..729
FT /note="Essential for nuclear localization, interaction with
FT RORG, repression of RORG transcriptional activator
FT activity"
FT /evidence="ECO:0000269|PubMed:23723244"
FT COMPBIAS 103..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92786"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92786"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92786"
FT CROSSLNK 324
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92786"
FT CONFLICT 685
FT /note="A -> V (in Ref. 2; BAC35190)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 737 AA; 83126 MW; 834DF6963FF5C9B5 CRC64;
MPDHDSTALL SRQTKRRRVD IGVKRTVGTA SAFFAKARAT FFSAMNPQGS EQDVEYSVVQ
HADGEKSNVL RKLLKRANSY EDAMMPFPGA TIISQLLKNN MNKNGGTEPS FQASGLSSTG
SEVHQEDICS NSSRDSPPEC LSPFGRPTMS QFDVDRLCDE HLRAKRARVE NIIRGMSHSP
SVALRGNENE REMAPQSVSP RESYRENKRK QKLPQQQQQS FQQLVSARKE QKREERRQLK
QQLEDMQKQL RQLQEKFYQV YDSTDSENDE DGDLSEDSMR SEILDARAQD SVGRSDNEMC
ELDPGQFIDR ARALIREQEM AENKPKREGS NKERDHGPNS LQPEGKHLAE TLKQELNTAM
SQVVDTVVKV FSAKPSRQVP QVFPPLQIPQ ARFAVNGENH NFHTANQRLQ CFGDVIIPNP
LDTFGSVQMP SSTDQTEALP LVVRKNSSEQ SASGPATGGH HQPLHQSPLS ATAGFTTPSF
RHPFPLPLMA YPFQSPLGAP SGSFSGKDRA SPESLDLTRD TTSLRTKMSS HHLSHHPCSP
AHPPSTAEGL SLSLIKSECG DLQDMSDISP YSGSAMQEGL SPNHLKKAKL MFFYTRYPSS
NMLKTYFSDV KFNRCITSQL IKWFSNFREF YYIQMEKYAR QAINDGVTST EELSITRDCE
LYRALNMHYN KANDFEVPER FLEVAQITLR EFFNAIIAGK DVDPSWKKAI YKVICKLDSE
VPEIFKSPNC LQELLHE
