SRRT_MOUSE
ID SRRT_MOUSE Reviewed; 875 AA.
AC Q99MR6; Q3UD04; Q5D042; Q8VEE6; Q99MR4; Q99MR5; Q99MR7;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Serrate RNA effector molecule homolog;
DE AltName: Full=Arsenite-resistance protein 2;
GN Name=Srrt; Synonyms=Ars2, Asr2;
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 [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS A; B;
RP C AND D).
RC STRAIN=129/Sv;
RX PubMed=11239002; DOI=10.1093/nar/29.6.1352;
RA Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P.,
RA Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., Miller W.,
RA Koop B.F.;
RT "Comparative analysis of the gene-dense ACHE/TFR2 region on human
RT chromosome 7q22 with the orthologous region on mouse chromosome 5.";
RL Nucleic Acids Res. 29:1352-1365(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Kidney, and Mammary tumor;
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 477-875 (ISOFORM C).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-543, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18086880; DOI=10.1128/mcb.01565-07;
RA Wilson M.D., Wang D., Wagner R., Breyssens H., Gertsenstein M., Lobe C.,
RA Lu X., Nagy A., Burke R.D., Koop B.F., Howard P.L.;
RT "ARS2 is a conserved eukaryotic gene essential for early mammalian
RT development.";
RL Mol. Cell. Biol. 28:1503-1514(2008).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, INTERACTION
RP WITH NCBP1 AND DROSHA, AND DISRUPTION PHENOTYPE.
RX PubMed=19632182; DOI=10.1016/j.cell.2009.04.046;
RA Gruber J.J., Zatechka D.S., Sabin L.R., Yong J., Lum J.J., Kong M.,
RA Zong W.-X., Zhang Z., Lau C.-K., Rawlings J., Cherry S., Ihle J.N.,
RA Dreyfuss G., Thompson C.B.;
RT "Ars2 links the nuclear cap-binding complex to RNA interference and cell
RT proliferation.";
RL Cell 138:328-339(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-543, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-543, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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 [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22198669; DOI=10.1038/nature10712;
RA Andreu-Agullo C., Maurin T., Thompson C.B., Lai E.C.;
RT "Ars2 maintains neural stem-cell identity through direct transcriptional
RT activation of Sox2.";
RL Nature 481:195-198(2012).
CC -!- FUNCTION: Acts as a mediator between the cap-binding complex (CBC) and
CC the primary microRNAs (miRNAs) processing machinery during cell
CC proliferation. Contributes to the stability and delivery of capped
CC primary miRNA transcripts to the primary miRNA processing complex
CC containing DGCR8 and DROSHA, thereby playing a role in RNA-mediated
CC gene silencing (RNAi) by miRNAs. Binds capped RNAs (m7GpppG-capped
CC RNA); however interaction is probably mediated via its interaction with
CC NCBP1/CBP80 component of the CBC complex. Involved in cell cycle
CC progression at S phase. Does not directly confer arsenite resistance
CC but rather modulates arsenic sensitivity. Independently of its activity
CC on miRNAs, necessary and sufficient to promote neural stem cell self-
CC renewal. Does so by directly binding SOX2 promoter and positively
CC regulating its transcription. {ECO:0000269|PubMed:19632182,
CC ECO:0000269|PubMed:22198669}.
CC -!- SUBUNIT: Interacts with CASP8AP2 and ERBB4 (By similarity). Interacts
CC with NCBP1/CBP80 and DROSHA (PubMed:19632182). Interacts with LUZP4 (By
CC similarity). Interacts with NCBP2/CBP20 and NCBP3 (By similarity).
CC Interacts with MTREX (By similarity). {ECO:0000250|UniProtKB:Q9BXP5,
CC ECO:0000269|PubMed:19632182}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Cytoplasm.
CC Note=Predominantly nuclear. Shuttles between the nucleus and the
CC cytoplasm in a CRM1-dependent way.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=A;
CC IsoId=Q99MR6-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q99MR6-2; Sequence=VSP_000325;
CC Name=C;
CC IsoId=Q99MR6-3; Sequence=VSP_000325, VSP_000326;
CC Name=D;
CC IsoId=Q99MR6-4; Sequence=VSP_000326;
CC -!- TISSUE SPECIFICITY: Widely expressed, with a preference for
CC proliferating cells. Highly expressed in hematopoietic tissues and
CC reduced or absent expression in parenchymal organs like liver and
CC kidney. In the brain, expressed in the subventricular zone by niche
CC astrocytes, ependymal cells and neural stem cells. In this cerebral
CC context, expressed in slowly dividing cells.
CC {ECO:0000269|PubMed:18086880, ECO:0000269|PubMed:19632182,
CC ECO:0000269|PubMed:22198669}.
CC -!- INDUCTION: Upon cell proliferation. {ECO:0000269|PubMed:19632182}.
CC -!- DISRUPTION PHENOTYPE: Death around the time of implantation. Deletion
CC in adults leads to proliferative arrest and bone marrow hypoplasia
CC whereas parenchymal organs composed of nonproliferating cells are
CC unaffected. {ECO:0000269|PubMed:18086880, ECO:0000269|PubMed:19632182}.
CC -!- SIMILARITY: Belongs to the ARS2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH19117.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE29458.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF312033; AAK28817.1; -; Genomic_DNA.
DR EMBL; AF312033; AAK28818.1; -; Genomic_DNA.
DR EMBL; AF312033; AAK28819.1; -; Genomic_DNA.
DR EMBL; AF312033; AAK28820.1; -; Genomic_DNA.
DR EMBL; BC019117; AAH19117.1; ALT_INIT; mRNA.
DR EMBL; BC066831; AAH66831.1; -; mRNA.
DR EMBL; AK150310; BAE29458.1; ALT_INIT; mRNA.
DR CCDS; CCDS39331.1; -. [Q99MR6-1]
DR CCDS; CCDS80439.1; -. [Q99MR6-3]
DR CCDS; CCDS80440.1; -. [Q99MR6-4]
DR RefSeq; NP_001103379.1; NM_001109909.1. [Q99MR6-4]
DR RefSeq; NP_001103380.1; NM_001109910.1. [Q99MR6-3]
DR RefSeq; NP_113582.1; NM_031405.2. [Q99MR6-1]
DR RefSeq; XP_006504692.1; XM_006504629.1.
DR AlphaFoldDB; Q99MR6; -.
DR SMR; Q99MR6; -.
DR BioGRID; 219965; 17.
DR IntAct; Q99MR6; 2.
DR MINT; Q99MR6; -.
DR STRING; 10090.ENSMUSP00000043123; -.
DR iPTMnet; Q99MR6; -.
DR PhosphoSitePlus; Q99MR6; -.
DR SwissPalm; Q99MR6; -.
DR EPD; Q99MR6; -.
DR jPOST; Q99MR6; -.
DR MaxQB; Q99MR6; -.
DR PaxDb; Q99MR6; -.
DR PeptideAtlas; Q99MR6; -.
DR PRIDE; Q99MR6; -.
DR ProteomicsDB; 258608; -. [Q99MR6-1]
DR ProteomicsDB; 258609; -. [Q99MR6-2]
DR ProteomicsDB; 258610; -. [Q99MR6-3]
DR ProteomicsDB; 258611; -. [Q99MR6-4]
DR Antibodypedia; 30897; 153 antibodies from 27 providers.
DR DNASU; 83701; -.
DR Ensembl; ENSMUST00000040873; ENSMUSP00000043123; ENSMUSG00000037364. [Q99MR6-1]
DR Ensembl; ENSMUST00000197466; ENSMUSP00000142564; ENSMUSG00000037364. [Q99MR6-3]
DR Ensembl; ENSMUST00000199243; ENSMUSP00000143232; ENSMUSG00000037364. [Q99MR6-4]
DR GeneID; 83701; -.
DR KEGG; mmu:83701; -.
DR UCSC; uc009acb.2; mouse. [Q99MR6-1]
DR UCSC; uc009acc.2; mouse. [Q99MR6-3]
DR UCSC; uc012eew.1; mouse. [Q99MR6-4]
DR CTD; 51593; -.
DR MGI; MGI:1933527; Srrt.
DR VEuPathDB; HostDB:ENSMUSG00000037364; -.
DR eggNOG; KOG2295; Eukaryota.
DR GeneTree; ENSGT00390000005492; -.
DR InParanoid; Q99MR6; -.
DR OMA; QVGFNWF; -.
DR OrthoDB; 525905at2759; -.
DR PhylomeDB; Q99MR6; -.
DR TreeFam; TF317609; -.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 83701; 22 hits in 75 CRISPR screens.
DR ChiTaRS; Srrt; mouse.
DR PRO; PR:Q99MR6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q99MR6; protein.
DR Bgee; ENSMUSG00000037364; Expressed in retinal neural layer and 61 other tissues.
DR ExpressionAtlas; Q99MR6; baseline and differential.
DR Genevisible; Q99MR6; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0140262; F:mRNA cap binding complex binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; IMP:UniProtKB.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IMP:CACAO.
DR GO; GO:0031053; P:primary miRNA processing; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR039727; SE/Ars2.
DR InterPro; IPR007042; SERRATE/Ars2_C.
DR InterPro; IPR021933; SERRATE/Ars2_N.
DR PANTHER; PTHR13165; PTHR13165; 2.
DR Pfam; PF04959; ARS2; 1.
DR Pfam; PF12066; SERRATE_Ars2_N; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Cytoplasm; Isopeptide bond;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-mediated gene silencing; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT CHAIN 2..875
FT /note="Serrate RNA effector molecule homolog"
FT /id="PRO_0000220966"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..382
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 8
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 543
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 670
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 832
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 839
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT MOD_RES 849
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT CROSSLNK 150
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BXP5"
FT VAR_SEQ 775..779
FT /note="ILPPG -> S (in isoform B and isoform C)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_000325"
FT VAR_SEQ 809..815
FT /note="Missing (in isoform C and isoform D)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_000326"
FT CONFLICT 567
FT /note="E -> G (in Ref. 3; BAE29458)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 875 AA; 100452 MW; 9571445674452886 CRC64;
MGDSDDEYDR RRRDKFRRER SDYDRSRERD ERRRGDDWND REWDRGRERR SRGEYRDYDR
NRRERFSPPR HELSPPQKRM RRDWDEHSSD PYHSGYDMPY AGGGGGPTYG PPQPWGHPDV
HIMQHHVLPI QARLGSIAEI DLGVPPPIMK SFKEFLLSLD DSVDETEAVK RYNDYKLDFR
RQQMQDFFLA HKDEEWFRSK YHPDEVGKRR QEARGALQNR LKVFLSLMES GWFDNLLLDI
DKADAIVKML DAAVIKMEGG TENDLRILEQ EEEEEQAGKT GEASKKEEAR AGPALGEGER
KANDKDEKKE DGKQAENDSS NDDKTKKSEG DGDKEEKKEE AEKEAKKSKK RNRKQSGDDS
FDEGSVSESE SESEGGQAEE EKEEAEEALK EKEKPKEEEK EKPKDAAGLE CKPRPLHKTC
SLFMRNIAPN ISRAEIISLC KRYPGFMRVA LSEPQPERRF FRRGWVTFDR SVNIKEICWN
LQNIRLRECE LSPGVNRDLT RRVRNINGIT QHKQIVRNDI KLAAKLIHTL DDRTQLWASE
PGTPPVPTSL PSQNPILKNI TDYLIEEVSA EEEELLGSSG GPPPEEPPKE GNPAEINVER
DEKLIKVLDK LLLYLRIVHS LDYYNTCEYP NEDEMPNRCG IIHVRGPMPP NRISHGEVLE
WQKTFEEKLT PLLSVRESLS EEEAQKMGRK DPEQEVEKFV TSNTQELGKD KWLCPLSGKK
FKGPEFVRKH IFNKHAEKIE EVKKEVAFFN NFLTDAKRPA LPEIKPAQPP GPAQILPPGL
TPGLPYPHQT PQGLMPYGQP RPPILGYGAG AVRPAVPTGG PPYPHAPYGA GRGNYDAFRG
QGGYPGKPRN RMVRGDPRAI VEYRDLDAPD DVDFF
