ID   PR40A_MOUSE             Reviewed;         953 AA.
AC   Q9R1C7; Q61049; Q8BQ76; Q8BRW4; Q8C2U1;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 182.
DE   RecName: Full=Pre-mRNA-processing factor 40 homolog A;
DE   AltName: Full=Formin-binding protein 11;
DE            Short=FBP-11;
DE   AltName: Full=Formin-binding protein 3;
GN   Name=Prpf40a; Synonyms=Fbp11, Fnbp3;
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).
RA   Bedford M.T., Das R., Reed R., Leder P.;
RT   "FBP11, a mammalian ortholog of the essential yeast splicing factor
RT   PRP40.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-380 (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 647-953.
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Aorta, Embryonic spinal ganglion, Thymus, and Vein;
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 [MRNA] OF 146-212, AND INTERACTION WITH FORMIN.
RC   STRAIN=FVB/NJ;
RX   PubMed=8605874; DOI=10.1002/j.1460-2075.1996.tb00442.x;
RA   Chan D.C., Bedford M.T., Leder P.;
RT   "Formin binding proteins bear WWP/WW domains that bind proline-rich
RT   peptides and functionally resemble SH3 domains.";
RL   EMBO J. 15:1045-1054(1996).
RN   [4]
RP   INTERACTION WITH SF1; SRPK1; ENAH; ATBF1 AND MECP2.
RX   PubMed=9171351; DOI=10.1093/emboj/16.9.2376;
RA   Bedford M.T., Chan D.C., Leder P.;
RT   "FBP WW domains and the Abl SH3 domain bind to a specific class of proline-
RT   rich ligands.";
RL   EMBO J. 16:2376-2383(1997).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH WASL.
RX   PubMed=14697212; DOI=10.1016/j.bbrc.2003.11.139;
RA   Mizutani K., Suetsugu S., Takenawa T.;
RT   "FBP11 regulates nuclear localization of N-WASP and inhibits N-WASP-
RT   dependent microspike formation.";
RL   Biochem. Biophys. Res. Commun. 313:468-474(2004).
RN   [6]
RP   INTERACTION WITH AKAP8L, AND SUBCELLULAR LOCATION.
RX   PubMed=16391387; DOI=10.1385/nmm:7:4:297;
RA   Sayer J.A., Manczak M., Akileswaran L., Reddy P.H., Coghlan V.M.;
RT   "Interaction of the nuclear matrix protein NAKAP with HypA and huntingtin:
RT   implications for nuclear toxicity in Huntington's disease pathogenesis.";
RL   NeuroMolecular Med. 7:297-310(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-928; SER-929; SER-931 AND
RP   SER-934, AND IDENTIFICATION BY 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; THR-928; SER-929; SER-931
RP   AND SER-934, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC   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   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-196, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [10]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-9, 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: Binds to WASL/N-WASP and suppresses its translocation from
CC       the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic
CC       function. Plays a role in the regulation of cell morphology and
CC       cytoskeletal organization. Required in the control of cell shape and
CC       migration. May play a role in cytokinesis. May be involved in pre-mRNA
CC       splicing. {ECO:0000269|PubMed:14697212}.
CC   -!- SUBUNIT: Interacts with the N-terminus of HTT and with the
CC       phosphorylated C-terminal domain of POLR2A (By similarity). Interacts
CC       with AKAP8L, SF1, SRPK1, ENAH, ATBF1 and MECP2. Interacts through the
CC       WW domains with formin proline-rich regions and with WASL/N-WASP.
CC       {ECO:0000250, ECO:0000269|PubMed:14697212, ECO:0000269|PubMed:16391387,
CC       ECO:0000269|PubMed:8605874, ECO:0000269|PubMed:9171351}.
CC   -!- INTERACTION:
CC       Q9R1C7; Q9ULX6: AKAP8L; Xeno; NbExp=3; IntAct=EBI-645554, EBI-357530;
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle. Nucleus matrix. Note=Colocalizes
CC       with AKAP8L in the nuclear matrix.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9R1C7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9R1C7-2; Sequence=VSP_008049;
CC   -!- DOMAIN: The WW domains are essential for localization to nuclear
CC       speckles.
CC   -!- SIMILARITY: Belongs to the PRPF40 family. {ECO:0000305}.
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DR   EMBL; AF135439; AAD39463.1; -; mRNA.
DR   EMBL; AK041205; BAC30863.1; -; mRNA.
DR   EMBL; AK051375; BAC34617.1; -; mRNA.
DR   EMBL; AK087963; BAC40061.2; -; mRNA.
DR   EMBL; U40747; AAC52475.1; -; mRNA.
DR   PIR; S64713; S64713.
DR   RefSeq; NP_061255.1; NM_018785.2.
DR   AlphaFoldDB; Q9R1C7; -.
DR   BMRB; Q9R1C7; -.
DR   SMR; Q9R1C7; -.
DR   BioGRID; 207833; 28.
DR   ELM; Q9R1C7; -.
DR   IntAct; Q9R1C7; 5.
DR   MINT; Q9R1C7; -.
DR   STRING; 10090.ENSMUSP00000075655; -.
DR   GlyGen; Q9R1C7; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9R1C7; -.
DR   PhosphoSitePlus; Q9R1C7; -.
DR   SwissPalm; Q9R1C7; -.
DR   EPD; Q9R1C7; -.
DR   jPOST; Q9R1C7; -.
DR   MaxQB; Q9R1C7; -.
DR   PaxDb; 10090-ENSMUSP00000075655; -.
DR   PeptideAtlas; Q9R1C7; -.
DR   ProteomicsDB; 289391; -. [Q9R1C7-1]
DR   ProteomicsDB; 289392; -. [Q9R1C7-2]
DR   Pumba; Q9R1C7; -.
DR   Antibodypedia; 33687; 116 antibodies from 18 providers.
DR   DNASU; 56194; -.
DR   Ensembl; ENSMUST00000239398.2; ENSMUSP00000159339.2; ENSMUSG00000061136.17. [Q9R1C7-1]
DR   GeneID; 56194; -.
DR   KEGG; mmu:56194; -.
DR   UCSC; uc008jrk.2; mouse. [Q9R1C7-1]
DR   AGR; MGI:1860512; -.
DR   CTD; 55660; -.
DR   MGI; MGI:1860512; Prpf40a.
DR   VEuPathDB; HostDB:ENSMUSG00000061136; -.
DR   eggNOG; KOG0152; Eukaryota.
DR   GeneTree; ENSGT00930000150980; -.
DR   HOGENOM; CLU_005825_0_0_1; -.
DR   InParanoid; Q9R1C7; -.
DR   OrthoDB; 25674at2759; -.
DR   PhylomeDB; Q9R1C7; -.
DR   TreeFam; TF318732; -.
DR   Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR   BioGRID-ORCS; 56194; 22 hits in 79 CRISPR screens.
DR   ChiTaRS; Prpf40a; mouse.
DR   PRO; PR:Q9R1C7; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q9R1C7; Protein.
DR   Bgee; ENSMUSG00000061136; Expressed in embryonic post-anal tail and 271 other cell types or tissues.
DR   ExpressionAtlas; Q9R1C7; baseline and differential.
DR   GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005685; C:U1 snRNP; IBA:GO_Central.
DR   GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
DR   GO; GO:0070064; F:proline-rich region binding; IDA:MGI.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR   GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR   GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR   GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR   CDD; cd00201; WW; 2.
DR   Gene3D; 2.20.70.10; -; 2.
DR   Gene3D; 1.10.10.440; FF domain; 5.
DR   InterPro; IPR002713; FF_domain.
DR   InterPro; IPR036517; FF_domain_sf.
DR   InterPro; IPR039726; Prp40-like.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR11864:SF20; PRE-MRNA-PROCESSING FACTOR 40 HOMOLOG A; 1.
DR   PANTHER; PTHR11864; PRE-MRNA-PROCESSING PROTEIN PRP40; 1.
DR   Pfam; PF01846; FF; 4.
DR   Pfam; PF00397; WW; 2.
DR   SMART; SM00441; FF; 5.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF81698; FF domain; 5.
DR   SUPFAM; SSF51045; WW domain; 2.
DR   PROSITE; PS51676; FF; 6.
DR   PROSITE; PS01159; WW_DOMAIN_1; 2.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
DR   Genevisible; Q9R1C7; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Isopeptide bond; Methylation;
KW   mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Ubl conjugation.
FT   CHAIN           1..953
FT                   /note="Pre-mRNA-processing factor 40 homolog A"
FT                   /id="PRO_0000076086"
FT   DOMAIN          140..173
FT                   /note="WW 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   DOMAIN          181..214
FT                   /note="WW 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   DOMAIN          389..443
FT                   /note="FF 1"
FT   DOMAIN          456..510
FT                   /note="FF 2"
FT   DOMAIN          523..583
FT                   /note="FF 3"
FT   DOMAIN          603..663
FT                   /note="FF 4"
FT   DOMAIN          668..723
FT                   /note="FF 5"
FT   DOMAIN          738..795
FT                   /note="FF 6"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          799..953
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        348..362
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..382
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        803..823
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        824..862
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        863..877
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        878..923
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        933..953
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         9
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         151
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75400"
FT   MOD_RES         196
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         341
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O75400"
FT   MOD_RES         369
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O75400"
FT   MOD_RES         719
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75400"
FT   MOD_RES         783
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75400"
FT   MOD_RES         879
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75400"
FT   MOD_RES         881
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75400"
FT   MOD_RES         884
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75400"
FT   MOD_RES         928
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         929
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         931
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         934
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   CROSSLNK        191
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O75400"
FT   CROSSLNK        241
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O75400"
FT   CROSSLNK        371
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O75400"
FT   CROSSLNK        372
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O75400"
FT   VAR_SEQ         14..55
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_008049"
FT   CONFLICT        334
FT                   /note="E -> A (in Ref. 2; BAC40061)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        355
FT                   /note="T -> I (in Ref. 2; BAC40061)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   953 AA;  108481 MW;  3C627AB7404D2285 CRC64;
     MRPGTGAERG GLMVSEMESQ PPSRGPGDGE RRLSGSNLCS SSWVSADGFL RRRPSMGHPG
     MHYAPMGMHP MGQRANMPPV PHGMMPQMMP PMGGPPMGQM PGMMSSVMSG MMMSHMSQAS
     MQPALPPGVN SMDVAAGAAS GAKSMWTEHK SPDGRTYYYN TETKQSTWEK PDDLKTPAEQ
     LLSKCPWKEY KSDSGKPYYY NSQTKESRWA KPKELEDLEG YQNTIVAGGL ITKSNLHAMI
     KAEESSKQEE CTTASTAPVP TTEIPTTMST MAAAEAAAAV VAAAAAAAAA ANANTSTTPT
     NTVGSVPVAP EPEVTSIVAT AVDNENTVTV STEEQAQLAN TTAIQDLSGD ISSNTGEEPA
     KQETVSDFTP KKEEEESQPA KKTYTWNTKE EAKQAFKELL KEKRVPSNAS WEQAMKMIIN
     DPRYSALAKL SEKKQAFNAY KVQTEKEEKE EARSKYKEAK ESFQRFLENH EKMTSTTRYK
     KAEQMFGEME VWNAISERDR LEIYEDVLFF LSKKEKEQAK QLRKRNWEAL KNILDNMANV
     TYSTTWSEAQ QYLMDNPTFA EDEELQNMDK EDALICFEEH IRALEKEEEE EKQKTLLRER
     RRQRKNRESF QIFLDELHEH GQLHSMSSWM ELYPTISSDI RFTNMLGQPG STALDLFKFY
     VEDLKARYHD EKKIIKDILK DKGFVVEVNT TFEDFVAIIS STKRSTTLDA GNIKLAFNSL
     LEKAEARERE REKEEARKMK RKESAFKSML KQATPPIELD AVWEDIRERF VKEPAFEDIT
     LESERKRIFK DFMHVLEHEC QHHHSKNKKH SKKSKKHHRK RSRSRSGSES DDDDSHSKKK
     RQRSESHSAS ERSSSAESER SYKKSKKHKK KSKKRRHKSD SPESDTEREK DKKEKDRDSE
     KDRSRQRSES KHKSPKKKTG KDSGNWDTSG SELSEGELEK RRRTLLEQLD DDQ
//