RBM19_MOUSE
ID RBM19_MOUSE Reviewed; 952 AA.
AC Q8R3C6; Q8BHR0; Q9CW63;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Probable RNA-binding protein 19;
DE AltName: Full=RNA-binding motif protein 19;
GN Name=Rbm19;
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] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary cancer;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 363-952 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Eye, and Lung;
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 SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=16027046; DOI=10.1016/j.modgep.2005.05.001;
RA Lorenzen J.A., Bonacci B.B., Palmer R.E., Wells C., Zhang J., Haber D.A.,
RA Goldstein A.M., Mayer A.N.;
RT "Rbm19 is a nucleolar protein expressed in crypt/progenitor cells of the
RT intestinal epithelium.";
RL Gene Expr. Patterns 6:45-56(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-693, AND IDENTIFICATION BY
RP 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 [5]
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19087264; DOI=10.1186/1471-213x-8-115;
RA Zhang J., Tomasini A.J., Mayer A.N.;
RT "RBM19 is essential for preimplantation development in the mouse.";
RL BMC Dev. Biol. 8:115-115(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-944, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [8]
RP STRUCTURE BY NMR OF 581-678.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the second RNA binding domain from hypothetical
RT protein BAB23448.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Plays a role in embryo pre-implantation development.
CC {ECO:0000269|PubMed:19087264}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm.
CC Cytoplasm. Chromosome. Note=Colocalizes with NPM1 during interphase. By
CC late prophase, metaphase, anaphase and telophase, associates with the
CC chromosome periphery. By telophase localizes to nucleolar precursor
CC body (NPB) (By similarity). In discrete foci distributed throughout the
CC cytoplasm and nucleoplasm during the 4 to 8 cell stages and the morula
CC stage, but not in the periphery of the NPB. During blastocyst
CC development, becomes increasingly localized to the nucleolus and less
CC to the cytoplasm. At the late blastocyst stage, localized predominantly
CC in the nucleolus. Localized in the nucleolus during interphase and to
CC the perichromosomal sheath during mitosis. Does not colocalize in the
CC cytoplasm with GW182 in P-bodies. May translocate to the nucleolus upon
CC early embryonic development. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R3C6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R3C6-2; Sequence=VSP_015005, VSP_015006;
CC -!- TISSUE SPECIFICITY: Expressed in the crypts of Lieberkuhn of the
CC intestine (at protein level). {ECO:0000269|PubMed:16027046}.
CC -!- DEVELOPMENTAL STAGE: Expressed during early development. Expressed in
CC the epithelium of the embryonic gut tube (at protein level).
CC {ECO:0000269|PubMed:16027046}.
CC -!- DISRUPTION PHENOTYPE: Arrests embryonic development prior to
CC implantation. Embryos at 3.5 dpc lack the mature, tripartite nucleoli,
CC but instead, contain spheres resembling nucleolar precursor body (NPB),
CC indicating arrest of nucleologenesis. {ECO:0000269|PubMed:19087264}.
CC -!- SIMILARITY: Belongs to the RRM MRD1 family. {ECO:0000305}.
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DR EMBL; BC025619; AAH25619.1; -; mRNA.
DR EMBL; BC034010; AAH34010.1; -; mRNA.
DR EMBL; AK004657; BAB23448.1; -; mRNA.
DR EMBL; AK053511; BAC35411.1; -; mRNA.
DR CCDS; CCDS19616.1; -. [Q8R3C6-1]
DR RefSeq; NP_083038.1; NM_028762.1. [Q8R3C6-1]
DR PDB; 1WHW; NMR; -; A=399-484.
DR PDB; 1WHX; NMR; -; A=581-678.
DR PDB; 2CPF; NMR; -; A=724-808.
DR PDB; 2CPH; NMR; -; A=816-909.
DR PDBsum; 1WHW; -.
DR PDBsum; 1WHX; -.
DR PDBsum; 2CPF; -.
DR PDBsum; 2CPH; -.
DR AlphaFoldDB; Q8R3C6; -.
DR SMR; Q8R3C6; -.
DR BioGRID; 216500; 3.
DR STRING; 10090.ENSMUSP00000031590; -.
DR iPTMnet; Q8R3C6; -.
DR PhosphoSitePlus; Q8R3C6; -.
DR EPD; Q8R3C6; -.
DR MaxQB; Q8R3C6; -.
DR PaxDb; Q8R3C6; -.
DR PeptideAtlas; Q8R3C6; -.
DR PRIDE; Q8R3C6; -.
DR ProteomicsDB; 255121; -. [Q8R3C6-1]
DR ProteomicsDB; 255122; -. [Q8R3C6-2]
DR Antibodypedia; 31281; 55 antibodies from 16 providers.
DR DNASU; 74111; -.
DR Ensembl; ENSMUST00000031590; ENSMUSP00000031590; ENSMUSG00000029594. [Q8R3C6-1]
DR GeneID; 74111; -.
DR KEGG; mmu:74111; -.
DR UCSC; uc008zha.1; mouse. [Q8R3C6-1]
DR CTD; 9904; -.
DR MGI; MGI:1921361; Rbm19.
DR VEuPathDB; HostDB:ENSMUSG00000029594; -.
DR eggNOG; KOG0110; Eukaryota.
DR GeneTree; ENSGT00840000129953; -.
DR HOGENOM; CLU_008479_1_0_1; -.
DR InParanoid; Q8R3C6; -.
DR OMA; TALIEYC; -.
DR OrthoDB; 1428854at2759; -.
DR PhylomeDB; Q8R3C6; -.
DR TreeFam; TF105725; -.
DR BioGRID-ORCS; 74111; 24 hits in 74 CRISPR screens.
DR ChiTaRS; Rbm19; mouse.
DR EvolutionaryTrace; Q8R3C6; -.
DR PRO; PR:Q8R3C6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8R3C6; protein.
DR Bgee; ENSMUSG00000029594; Expressed in ectoplacental cone and 219 other tissues.
DR ExpressionAtlas; Q8R3C6; baseline and differential.
DR Genevisible; Q8R3C6; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0040019; P:positive regulation of embryonic development; IMP:UniProtKB.
DR CDD; cd12564; RRM1_RBM19; 1.
DR CDD; cd12502; RRM2_RMB19; 1.
DR CDD; cd12567; RRM3_RBM19; 1.
DR CDD; cd12569; RRM4_RBM19; 1.
DR CDD; cd12318; RRM5_RBM19_like; 1.
DR CDD; cd12571; RRM6_RBM19; 1.
DR Gene3D; 3.30.70.330; -; 6.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034419; RBM19_RRM3.
DR InterPro; IPR034420; RBM19_RRM4.
DR InterPro; IPR034423; RBM19_RRM5.
DR InterPro; IPR034421; RBM19_RRM6.
DR InterPro; IPR034418; RMB19_RRM1.
DR InterPro; IPR034417; RMB19_RRM2.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF00076; RRM_1; 5.
DR SMART; SM00360; RRM; 6.
DR SMART; SM00361; RRM_1; 2.
DR SUPFAM; SSF54928; SSF54928; 5.
DR PROSITE; PS50102; RRM; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome; Cytoplasm;
KW Developmental protein; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Ubl conjugation.
FT CHAIN 1..952
FT /note="Probable RNA-binding protein 19"
FT /id="PRO_0000081782"
FT DOMAIN 2..79
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 293..368
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 400..478
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 584..656
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 722..803
FT /note="RRM 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 824..904
FT /note="RRM 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 85..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..192
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..250
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..719
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4C8"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4C8"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4C8"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 928
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4C8"
FT MOD_RES 944
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CROSSLNK 479
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4C8"
FT VAR_SEQ 485..521
FT /note="EANAPGSSYKKKKEAMDKANSSSSHNWNTLFMGPNAV -> APAALSPPQQD
FT CWPVDRAGDSTSSSGPLPCPCDAARF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015005"
FT VAR_SEQ 522..952
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015006"
FT STRAND 400..405
FT /evidence="ECO:0007829|PDB:1WHW"
FT HELIX 413..421
FT /evidence="ECO:0007829|PDB:1WHW"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:1WHW"
FT TURN 435..437
FT /evidence="ECO:0007829|PDB:1WHW"
FT STRAND 442..450
FT /evidence="ECO:0007829|PDB:1WHW"
FT HELIX 451..460
FT /evidence="ECO:0007829|PDB:1WHW"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:1WHW"
FT STRAND 464..468
FT /evidence="ECO:0007829|PDB:1WHW"
FT STRAND 470..475
FT /evidence="ECO:0007829|PDB:1WHW"
FT STRAND 581..590
FT /evidence="ECO:0007829|PDB:1WHX"
FT HELIX 597..605
FT /evidence="ECO:0007829|PDB:1WHX"
FT STRAND 610..614
FT /evidence="ECO:0007829|PDB:1WHX"
FT STRAND 617..620
FT /evidence="ECO:0007829|PDB:1WHX"
FT STRAND 622..627
FT /evidence="ECO:0007829|PDB:1WHX"
FT HELIX 629..639
FT /evidence="ECO:0007829|PDB:1WHX"
FT STRAND 643..648
FT /evidence="ECO:0007829|PDB:1WHX"
FT STRAND 650..655
FT /evidence="ECO:0007829|PDB:1WHX"
FT TURN 656..659
FT /evidence="ECO:0007829|PDB:1WHX"
FT HELIX 666..670
FT /evidence="ECO:0007829|PDB:1WHX"
FT HELIX 675..677
FT /evidence="ECO:0007829|PDB:1WHX"
FT STRAND 724..728
FT /evidence="ECO:0007829|PDB:2CPF"
FT HELIX 735..743
FT /evidence="ECO:0007829|PDB:2CPF"
FT STRAND 748..757
FT /evidence="ECO:0007829|PDB:2CPF"
FT STRAND 763..775
FT /evidence="ECO:0007829|PDB:2CPF"
FT HELIX 776..785
FT /evidence="ECO:0007829|PDB:2CPF"
FT STRAND 797..799
FT /evidence="ECO:0007829|PDB:2CPF"
FT STRAND 826..830
FT /evidence="ECO:0007829|PDB:2CPH"
FT HELIX 837..845
FT /evidence="ECO:0007829|PDB:2CPH"
FT STRAND 850..854
FT /evidence="ECO:0007829|PDB:2CPH"
FT STRAND 860..862
FT /evidence="ECO:0007829|PDB:2CPH"
FT STRAND 867..875
FT /evidence="ECO:0007829|PDB:2CPH"
FT HELIX 876..887
FT /evidence="ECO:0007829|PDB:2CPH"
FT STRAND 891..894
FT /evidence="ECO:0007829|PDB:2CPH"
FT STRAND 898..901
FT /evidence="ECO:0007829|PDB:2CPH"
SQ SEQUENCE 952 AA; 106083 MW; 91C45ADB66F8CDB2 CRC64;
MSRLIVKNLP NGMKEERFRQ LFAAFGTLTD CSLKFTKDGK FRKFGFIGFK SEEEAQAALN
HFHRSFIDTT RITVEFCKSF GDPSKPRAWS KHAQKSSQPK QPSQDSVPSD TKKDKKKKGP
SDLEKLKEDA KFQEFLSIHQ KRTQVATWAN DALEAKLPKA KTKASSDYLN FDSDSNSDSG
QESEEEPARE DPEEEQGLQP KAAVQKELSD MDYLKSKMVR AEVSSEDEDE EDSEDEAVNC
EEGSEEEEEE GSPASPAKQG GVSRGAVPGV LRPQEAAGKV EKPVSQKEPT TPYTVKLRGA
PFNVTEKNVI EFLAPLKPVA IRIVRNAHGN KTGYVFVDLS SEEEVKKALK CNRDYMGGRY
IEVFREKQAP TARGPPKSTT PWQGRTLGEN EEEEDLADSG RLFVRNLSYT SSEEDLEKLF
SAYGPLSELH YPIDSLTKKP KGFAFVTFMF PEHAVKAYAE VDGQVFQGRM LHVLPSTIKK
EASQEANAPG SSYKKKKEAM DKANSSSSHN WNTLFMGPNA VADAIAQKYN ATKSQVFDHE
TRGSVAVRVA LGETQLVQEV RSFLIDNGVC LDSFSQAAAE RSKTVILAKN LPAGTLAAEI
QETFSRFGSL GRVLLPEGGI TAIVEFLEPL EARKAFRHLA YSKFHHVPLY LEWAPIGVFG
AAPQKKDSQH EQPAEKAEVE QETVLDPEGE KASVEGAEAS TGKMEEEEEE EEEEEEESIP
GCTLFIKNLN FSTTEETLKG VFSKVGAIKS CTISKKKNKA GVLLSMGFGF VEYKKPEQAQ
KALKQLQGHT VDGHKLEVRI SERATKPALT STRKKQVPKK QTTSKILVRN IPFQANQREI
RELFSTFGEL KTVRLPKKMT GTGAHRGFGF VDFITKQDAK KAFNALCHST HLYGRRLVLE
WADSEVTVQT LRRKTARHFQ EPPKKKRSAV LDGILEQLED EDNSDGEQAL QL
