GANP_MOUSE
ID GANP_MOUSE Reviewed; 1971 AA.
AC Q9WUU9; Q7TS87;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Germinal-center associated nuclear protein;
DE Short=GANP;
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:O60318};
DE AltName: Full=GC-associated DNA primase {ECO:0000303|PubMed:11526238};
GN Name=Mcm3ap; Synonyms=Ganp, Map80;
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], INTERACTION WITH MCM3, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INDUCTION BY CD40 STIMULATION.
RC STRAIN=BALB/c X NZB;
RX PubMed=10733502;
RA Kuwahara K., Yoshida M., Kondo E., Sakata A., Watanabe Y., Abe E.,
RA Kouno Y., Tomiyasu S., Fujimura S., Tokuhisa T., Kimura H., Ezaki T.,
RA Sakaguchi N.;
RT "A novel nuclear phosphoprotein, GANP, is up-regulated in centrocytes of
RT the germinal center and associated with MCM3, a protein essential for DNA
RT replication.";
RL Blood 95:2321-2328(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 INDUCTION BY CD40 STIMULATION AND LPS, AND PHOSPHORYLATION AT SER-502.
RX PubMed=11526238; DOI=10.1073/pnas.181335698;
RA Kuwahara K., Tomiyasu S., Fujimura S., Nomura K., Xing Y., Nishiyama N.,
RA Ogawa M., Imajoh-Ohmi S., Izuta S., Sakaguchi N.;
RT "Germinal center-associated nuclear protein (GANP) has a phosphorylation-
RT dependent DNA-primase activity that is up-regulated in germinal center
RT regions.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:10279-10283(2001).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=17903179; DOI=10.1111/j.1365-2443.2007.01119.x;
RA Yoshida M., Kuwahara K., Shimasaki T., Nakagata N., Matsuoka M.,
RA Sakaguchi N.;
RT "GANP suppresses DNA recombination, measured by direct-repeat beta-
RT galactosidase gene construct, but does not suppress the type of
RT recombination applying to immunoglobulin genes in mammalian cells.";
RL Genes Cells 12:1205-1213(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [7]
RP INTERACTION WITH AICDA, AND SUBCELLULAR LOCATION.
RX PubMed=20507984; DOI=10.1074/jbc.m110.131441;
RA Maeda K., Singh S.K., Eda K., Kitabatake M., Pham P., Goodman M.F.,
RA Sakaguchi N.;
RT "GANP-mediated recruitment of activation-induced cytidine deaminase to cell
RT nuclei and to immunoglobulin variable region DNA.";
RL J. Biol. Chem. 285:23945-23953(2010).
RN [8]
RP FUNCTION.
RX PubMed=23652018; DOI=10.1038/ncomms2823;
RA Singh S.K., Maeda K., Eid M.M., Almofty S.A., Ono M., Pham P.,
RA Goodman M.F., Sakaguchi N.;
RT "GANP regulates recruitment of AID to immunoglobulin variable regions by
RT modulating transcription and nucleosome occupancy.";
RL Nat. Commun. 4:1830-1830(2013).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-483 AND LYS-484, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-32, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: As a component of the TREX-2 complex, involved in the export
CC of mRNAs to the cytoplasm through the nuclear pores (By similarity).
CC Through the acetylation of histones, affects the assembly of
CC nucleosomes at immunoglobulin variable region genes and promotes the
CC recruitment and positioning of transcription complex to favor DNA
CC cytosine deaminase AICDA/AID targeting, hence promoting somatic
CC hypermutations (PubMed:23652018). {ECO:0000250|UniProtKB:O60318,
CC ECO:0000269|PubMed:23652018}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845,
CC Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000250|UniProtKB:O60318};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993;
CC Evidence={ECO:0000250|UniProtKB:O60318};
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC)-associated TREX-2
CC complex (transcription and export complex 2), composed of at least
CC GANP, 2 copies of ENY2, PCID2, SEM1/DSS1, and either centrin CETN2 or
CC centrin CETN3. The TREX-2 complex also associates with ALYREF/ALY (By
CC similarity). Interacts with RNA polymerase II subunit POLR2A and with
CC the transcription elongation factor SUPT5H/SPT5 (By similarity).
CC Interacts (via FG-repeats) with NXF1; this interaction is not mediated
CC by RNA (By similarity). Interacts with nuclear envelope proteins NUP62,
CC NUP153 and RANBP2/NUP358; interaction with NUP153 is required for full
CC localization at the nuclear pore complex (By similarity). Interacts
CC with several RNA helicases, including DHX9, DDX21, and DDX39A/DDX39,
CC and with DNA topoisomerase TOP2A (By similarity). Directly interacts
CC with AICDA/AID (PubMed:20507984). Interacts with the glucocorticoid
CC receptor NR3C1 (By similarity). Interacts with MCM3 (PubMed:10733502).
CC {ECO:0000250|UniProtKB:O60318, ECO:0000269|PubMed:10733502,
CC ECO:0000269|PubMed:20507984}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10733502,
CC ECO:0000269|PubMed:20507984}. Nucleus {ECO:0000269|PubMed:10733502,
CC ECO:0000269|PubMed:20507984}. Nucleus envelope
CC {ECO:0000250|UniProtKB:O60318}. Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:O60318}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:O60318}. Chromosome
CC {ECO:0000250|UniProtKB:O60318}. Note=In stimulated B-cells, selectively
CC targeted to immunoglobulin gene variable regions (PubMed:20507984).
CC Predominantly located at the nuclear envelope, facing the nucleus
CC interior (By similarity). Localization at the nuclear pore complex
CC requires NUP153, TPR and ALYREF/ALY (By similarity). Also found
CC associated with chromatin (PubMed:23652018). In B-cells, targeted to
CC the immunoglobulin variable region genes (PubMed:20507984,
CC PubMed:23652018). {ECO:0000250|UniProtKB:O60318,
CC ECO:0000269|PubMed:20507984, ECO:0000269|PubMed:23652018}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in lymphoid organs,
CC including thymus, spleen and lymph nodes (PubMed:10733502). Up-
CC regulated in stimulated B-cells in spleen and Peyer's patch germinal
CC centers (at protein level) (PubMed:11526238).
CC {ECO:0000269|PubMed:10733502, ECO:0000269|PubMed:11526238}.
CC -!- INDUCTION: Up-regulated in B-cells by CD40 stimulation and bacterial
CC lipopolysaccharide (LPS) (at protein level).
CC {ECO:0000269|PubMed:10733502, ECO:0000269|PubMed:11526238}.
CC -!- PTM: Phosphorylation at Ser-502 is induced in B-cells by CD40-
CC stimulation, but not by bacterial lipopolysaccharide (LPS).
CC {ECO:0000269|PubMed:11526238}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal at 11.5 dpc.
CC {ECO:0000269|PubMed:17903179}.
CC -!- SIMILARITY: Belongs to the SAC3 family. {ECO:0000305}.
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DR EMBL; AJ006590; CAB44241.1; -; mRNA.
DR EMBL; CH466553; EDL31849.1; -; Genomic_DNA.
DR EMBL; BC052452; AAH52452.1; -; mRNA.
DR CCDS; CCDS23947.1; -.
DR RefSeq; NP_062307.2; NM_019434.2.
DR AlphaFoldDB; Q9WUU9; -.
DR SMR; Q9WUU9; -.
DR BioGRID; 207638; 4.
DR IntAct; Q9WUU9; 1.
DR STRING; 10090.ENSMUSP00000125960; -.
DR iPTMnet; Q9WUU9; -.
DR PhosphoSitePlus; Q9WUU9; -.
DR EPD; Q9WUU9; -.
DR jPOST; Q9WUU9; -.
DR MaxQB; Q9WUU9; -.
DR PaxDb; Q9WUU9; -.
DR PeptideAtlas; Q9WUU9; -.
DR PRIDE; Q9WUU9; -.
DR ProteomicsDB; 268847; -.
DR Antibodypedia; 10636; 250 antibodies from 33 providers.
DR DNASU; 54387; -.
DR Ensembl; ENSMUST00000170795; ENSMUSP00000125960; ENSMUSG00000001150.
DR GeneID; 54387; -.
DR KEGG; mmu:54387; -.
DR UCSC; uc007fup.1; mouse.
DR CTD; 8888; -.
DR MGI; MGI:1930089; Mcm3ap.
DR VEuPathDB; HostDB:ENSMUSG00000001150; -.
DR eggNOG; KOG1860; Eukaryota.
DR GeneTree; ENSGT00940000156322; -.
DR HOGENOM; CLU_001842_1_0_1; -.
DR InParanoid; Q9WUU9; -.
DR OMA; RRHGHET; -.
DR OrthoDB; 1593971at2759; -.
DR TreeFam; TF105948; -.
DR BioGRID-ORCS; 54387; 23 hits in 77 CRISPR screens.
DR ChiTaRS; Mcm3ap; mouse.
DR PRO; PR:Q9WUU9; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9WUU9; protein.
DR Bgee; ENSMUSG00000001150; Expressed in saccule of membranous labyrinth and 268 other tissues.
DR ExpressionAtlas; Q9WUU9; baseline and differential.
DR Genevisible; Q9WUU9; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0044615; C:nuclear pore nuclear basket; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0070390; C:transcription export complex 2; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0010484; F:H3 histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004402; F:histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0034728; P:nucleosome organization; ISS:UniProtKB.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; ISS:UniProtKB.
DR CDD; cd12443; RRM_MCM3A_like; 1.
DR InterPro; IPR031910; GANP_CID_dom.
DR InterPro; IPR031907; MCM3AP_GANP.
DR InterPro; IPR034265; MCM3AP_RRM.
DR InterPro; IPR031908; NupH_GANP.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR045107; SAC3/GANP/THP3.
DR InterPro; IPR005062; SAC3/GANP/THP3_conserved.
DR PANTHER; PTHR12436; PTHR12436; 1.
DR Pfam; PF16766; CID_GANP; 1.
DR Pfam; PF16769; MCM3AP_GANP; 1.
DR Pfam; PF16768; NupH_GANP; 1.
DR Pfam; PF03399; SAC3_GANP; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Chromosome; Coiled coil; Cytoplasm; Immunity;
KW Methylation; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transferase; Translocation;
KW Transport.
FT CHAIN 1..1971
FT /note="Germinal-center associated nuclear protein"
FT /id="PRO_0000096285"
FT DOMAIN 768..951
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..335
FT /note="FG-repeats"
FT REGION 214..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..550
FT /note="DNA primase"
FT REGION 1793..1840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1124..1162
FT /evidence="ECO:0000255"
FT COMPBIAS 11..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1793..1818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1822..1837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 32
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60318"
FT MOD_RES 483
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 484
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11526238"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60318"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60318"
FT CONFLICT 10..11
FT /note="QQ -> SS (in Ref. 1; CAB44241)"
FT /evidence="ECO:0000305"
FT CONFLICT 1017
FT /note="V -> L (in Ref. 1; CAB44241)"
FT /evidence="ECO:0000305"
FT CONFLICT 1190
FT /note="E -> K (in Ref. 1; CAB44241)"
FT /evidence="ECO:0000305"
FT CONFLICT 1552
FT /note="R -> G (in Ref. 1; CAB44241)"
FT /evidence="ECO:0000305"
FT CONFLICT 1702
FT /note="V -> A (in Ref. 1; CAB44241)"
FT /evidence="ECO:0000305"
FT CONFLICT 1782
FT /note="L -> S (in Ref. 1; CAB44241)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1971 AA; 217363 MW; FA9CDB20D1441B02 CRC64;
MHPVNPFGGQ QPSAFAVSSS TTGTYQTKSP FRFGQPSLFG QNSTPSKSLA FSQVPSFATP
SGGSHSSSLP AFGLTQTSSV GLFSSLESTP SFAATSSSSV PGNTAFSFKS TSSVGVFPSG
ATFGPETGEV AGSGFRKTEF KFKPLENAVF KPIPGPESEP EKTQSQISSG FFTFSHPVGS
GSGGLTPFSF PQVTNSSVTS SSFIFSKPVT SNTPAFASPL SNQNVEEEKR VSTSAFGSSN
SSFSTFPTAS PGSLGEPFPA NKPSLRQGCE EAISQVEPLP TLMKGLKRKE DQDRSPRRHC
HEAAEDPDPL SRGDHPPDKR PVRLNRPRGG TLFGRTIQEV FKSNKEAGRL GSKESKESGF
AEPGESDHAA VPGGSQSTMV PSRLPAVTKE EEESRDEKED SLRGKSVRQS KRREEWIYSL
GGVSSLELTA IQCKNIPDYL NDRAILEKHF SKIAKVQRVF TRRSKKLAVI HFFDHASAAL
ARKKGKGLHK DVVIFWHKKK ISPSKKLFPL KEKLGESEAS QGIEDSPFQH SPLSKPIVRP
AAGSLLSKSS PVKKPSLLKM HQFEADPFDS GSEGSEGLGS CVSSLSTLIG TVADTSEEKY
RLLDQRDRIM RQARVKRTDL DKARAFVGTC PDMCPEKERY LRETRSQLSV FEVVPGTDQV
DHAAAVKEYS RSSADQEEPL PHELRPSAVL SRTMDYLVTQ IMDQKEGSLR DWYDFVWNRT
RGIRKDITQQ HLCDPLTVSL IEKCTRFHIH CAHFMCEEPM SSFDAKINNE NMTKCLQSLK
EMYQDLRNKG VFCASEAEFQ GYNVLLNLNK GDILREVQQF HPDVRNSPEV NFAVQAFAAL
NSNNFVRFFK LVQSASYLNA CLLHCYFNQI RKDALRALNV AYTVSTQRST VFPLDGVVRM
LLFRDSEEAT NFLNYHGLTV ADGCVELNRS AFLEPEGLCK ARKSVFIGRK LTVSVGEVVN
GGPLPPVPRH TPVCSFNSQN KYVGESLATE LPISTQRAGG DPAGGGRGED CEAEVDVPTL
AVLPQPPPAS SATPALHVQP LAPAAAPSLL QASTQPEVLL PKPAPVYSDS DLVQVVDELI
QEALQVDCEE VSSAGAAYVA AALGVSNAAV EDLITAATTG ILRHVAAEEV SMERQRLEEE
KQRAEEERLK QERELMLTQL SEGLAAELTE LTVTECVWET CSQELQSAVE IDQKVRVARC
CEAVCAHLVD LFLAEEIFQT AKETLQELQC FCKYLQRWRE AVAARKKFRR QMRAFPAAPC
CVDVNDRLQA LVPSAECPIT EENLAKGLLD LGHAGKVGVS CTRLRRLRNK TAHQIKVQHF
HQQLLRNAAW APLDLPSIVS EHLPMKQKRR FWKLVLVLPD VEEQTPESPG RILENWLKVK
FTGDDSMVGD IGDNAGDIQT LSVFNTLSSK GDQTVSVNVC IKVAHGTLSD SALDAVETQK
DLLGTSGLML LLPPKVKSEE VAEEELSWLS ALLQLKQLLQ AKPFQPALPL VVLVPSSRGD
SAGRAVEDGL MLQDLVSAKL ISDYIVVEIP DSVNDLQGTV KVSGAVQWLI SRCPQALDLC
CQTLVQYVED GISREFSRRF FHDRRERRLA SLPSQEPSTI IELFNSVLQF LASVVSSEQL
CDISWPVMEF AEVGGSQLLP HLHWNSPEHL AWLKQAVLGF QLPQMDLPPP GAPWLPVCSM
VIQYTSQIPS SSQTQPVLQS QVENLLCRTY QKWKNKSLSP GQELGPSVAE IPWDDIITLC
INHKLRDWTP PRLPVTLEAL SEDGQICVYF FKNLLRKYHV PLSWEQARMQ TQRELQLSHG
RSGMRSIHPP TSTFPTPLLH VHQKGKKKEE SGREGSLSTE DLLRGASAEE LLAQSLSSSL
LEEKEENKRF EDQLQQWLSQ DSQAFTESTR LPLYLPQTLV SFPDSIKTQT MVKTSTSPQN
SGTGKQLRFS EASGSSLTEK LKLLERLIQS SRAEEAASEL HLSALLEMVD M
