ID SF3B3_MOUSE Reviewed; 1217 AA.
AC Q921M3; Q3UGI3; Q6ZQL0; Q8BUD9; Q8K2J8;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 162.
DE RecName: Full=Splicing factor 3B subunit 3;
DE AltName: Full=Pre-mRNA-splicing factor SF3b 130 kDa subunit;
DE Short=SF3b130;
DE AltName: Full=Spliceosome-associated protein 130;
DE Short=SAP 130;
GN Name=Sf3b3; Synonyms=Kiaa0017;
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=C57BL/6J, and NOD; TISSUE=Mammary gland, and Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N, and FVB/N-3; TISSUE=Eye, 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 [4]
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Component of the 17S U2 SnRNP complex of the spliceosome, a
CC large ribonucleoprotein complex that removes introns from transcribed
CC pre-mRNAs. The 17S U2 SnRNP complex (1) directly participates in early
CC spliceosome assembly and (2) mediates recognition of the intron branch
CC site during pre-mRNA splicing by promoting the selection of the pre-
CC mRNA branch-site adenosine, the nucleophile for the first step of
CC splicing. Within the 17S U2 SnRNP complex, SF3B3 is part of the SF3B
CC subcomplex, which is required for 'A' complex assembly formed by the
CC stable binding of U2 snRNP to the branchpoint sequence in pre-mRNA.
CC Sequence independent binding of SF3A and SF3B subcomplexes upstream of
CC the branch site is essential, it may anchor U2 snRNP to the pre-mRNA.
CC May also be involved in the assembly of the 'E' complex. Also acts as a
CC component of the minor spliceosome, which is involved in the splicing
CC of U12-type introns in pre-mRNAs. {ECO:0000250|UniProtKB:Q15393}.
CC -!- SUBUNIT: Component of the 17S U2 SnRNP complex, a ribonucleoprotein
CC complex that contains small nuclear RNA (snRNA) U2 and a number of
CC specific proteins. Part of the SF3B subcomplex of the 17S U2 SnRNP
CC complex. SF3B associates with the splicing subcomplex SF3A and a 12S
CC RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2
CC snRNP). Within the SF3B subcomplex, interacts directly with SF3B1 (via
CC HEAT domain), SF3B5 and PHF5A. Identified in the spliceosome A complex;
CC remains associated with the spliceosome throughout the splicing
CC process. Component of the spliceosome B complex. Identified in the
CC spliceosome C complex. Identified in the spliceosome E complex.
CC Component of the minor (U12-type spliceosome) spliceosome. Within this
CC complex, interacts with SCNM1. Associates with the STAGA transcription
CC coactivator-HAT complex. Interacts with SUPT3H. Interacts with TAF3.
CC {ECO:0000250|UniProtKB:Q15393}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15393}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q921M3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q921M3-2; Sequence=VSP_022980;
CC -!- DOMAIN: The core of the protein consists of three beta-propeller
CC domains. {ECO:0000250|UniProtKB:Q15393}.
CC -!- SIMILARITY: Belongs to the RSE1 family. {ECO:0000305}.
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DR EMBL; AK085705; BAC39513.1; -; mRNA.
DR EMBL; AK088268; BAC40248.1; -; mRNA.
DR EMBL; AK129035; BAC97845.1; -; Transcribed_RNA.
DR EMBL; AK147914; BAE28225.1; -; mRNA.
DR EMBL; BC011412; AAH11412.1; -; mRNA.
DR EMBL; BC031197; AAH31197.2; -; mRNA.
DR EMBL; BC042580; AAH42580.1; -; mRNA.
DR CCDS; CCDS22665.1; -. [Q921M3-1]
DR RefSeq; NP_598714.1; NM_133953.2. [Q921M3-1]
DR RefSeq; XP_006530581.1; XM_006530518.3. [Q921M3-1]
DR PDB; 7B9C; X-ray; 2.40 A; A=1-442, A=768-915.
DR PDB; 7OPI; X-ray; 3.10 A; A=1-442, A=768-915.
DR PDBsum; 7B9C; -.
DR PDBsum; 7OPI; -.
DR AlphaFoldDB; Q921M3; -.
DR SMR; Q921M3; -.
DR BioGRID; 221759; 67.
DR ComplexPortal; CPX-6803; SAGA complex, KAT2B variant.
DR ComplexPortal; CPX-920; SAGA complex, KAT2A variant.
DR IntAct; Q921M3; 4.
DR MINT; Q921M3; -.
DR STRING; 10090.ENSMUSP00000045073; -.
DR GlyGen; Q921M3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q921M3; -.
DR PhosphoSitePlus; Q921M3; -.
DR SwissPalm; Q921M3; -.
DR EPD; Q921M3; -.
DR jPOST; Q921M3; -.
DR MaxQB; Q921M3; -.
DR PaxDb; 10090-ENSMUSP00000045073; -.
DR PeptideAtlas; Q921M3; -.
DR ProteomicsDB; 261505; -. [Q921M3-1]
DR ProteomicsDB; 261506; -. [Q921M3-2]
DR Pumba; Q921M3; -.
DR Antibodypedia; 30001; 378 antibodies from 38 providers.
DR DNASU; 101943; -.
DR Ensembl; ENSMUST00000042012.7; ENSMUSP00000045073.6; ENSMUSG00000033732.11. [Q921M3-1]
DR GeneID; 101943; -.
DR KEGG; mmu:101943; -.
DR UCSC; uc009nlb.1; mouse. [Q921M3-1]
DR UCSC; uc009nlc.1; mouse. [Q921M3-2]
DR AGR; MGI:1289341; -.
DR CTD; 23450; -.
DR MGI; MGI:1289341; Sf3b3.
DR VEuPathDB; HostDB:ENSMUSG00000033732; -.
DR eggNOG; KOG1898; Eukaryota.
DR GeneTree; ENSGT00950000183151; -.
DR HOGENOM; CLU_003246_0_0_1; -.
DR InParanoid; Q921M3; -.
DR OMA; PRATGHW; -.
DR OrthoDB; 101343at2759; -.
DR PhylomeDB; Q921M3; -.
DR TreeFam; TF105685; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72165; mRNA Splicing - Minor Pathway.
DR BioGRID-ORCS; 101943; 25 hits in 116 CRISPR screens.
DR ChiTaRS; Sf3b3; mouse.
DR PRO; PR:Q921M3; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q921M3; Protein.
DR Bgee; ENSMUSG00000033732; Expressed in frontonasal prominence and 262 other cell types or tissues.
DR ExpressionAtlas; Q921M3; baseline and differential.
DR Genevisible; Q921M3; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000124; C:SAGA complex; NAS:ComplexPortal.
DR GO; GO:0005689; C:U12-type spliceosomal complex; ISO:MGI.
DR GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0005684; C:U2-type spliceosomal complex; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030620; F:U2 snRNA binding; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; NAS:ComplexPortal.
DR GO; GO:0006282; P:regulation of DNA repair; NAS:ComplexPortal.
DR GO; GO:0043484; P:regulation of RNA splicing; NAS:ComplexPortal.
DR Gene3D; 1.10.150.910; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR10644; DNA REPAIR/RNA PROCESSING CPSF FAMILY; 1.
DR PANTHER; PTHR10644:SF1; SPLICING FACTOR 3B SUBUNIT 3; 1.
DR Pfam; PF03178; CPSF_A; 1.
DR Pfam; PF10433; MMS1_N; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Spliceosome.
FT CHAIN 1..1217
FT /note="Splicing factor 3B subunit 3"
FT /id="PRO_0000276755"
FT REGION 105..119
FT /note="Interaction with PHF5A, SF3B1 and SF3B5"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT REGION 145..168
FT /note="Interaction with PHF5A, SF3B1 and SF3B5"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT REGION 193..231
FT /note="Interaction with SF3B1 and SF3B5"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT REGION 786..804
FT /note="Interaction with SF3B1 and SF3B5"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT REGION 1028..1049
FT /note="Interaction with SF3B1"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT REGION 1100..1123
FT /note="Interaction with SF3B5"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT SITE 284
FT /note="Interaction with SF3B5"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT SITE 306
FT /note="Interaction with SF3B5"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT SITE 352
FT /note="Interaction with SF3B5"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT SITE 429
FT /note="Interaction with SF3B5"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT SITE 988
FT /note="Interaction with SF3B1"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT SITE 1171
FT /note="Interaction with SF3B1"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT MOD_RES 1200
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15393"
FT VAR_SEQ 819..913
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_022980"
FT CONFLICT 327
FT /note="L -> I (in Ref. 1; BAE28225)"
FT /evidence="ECO:0000305"
FT CONFLICT 870
FT /note="N -> S (in Ref. 1; BAE28225)"
FT /evidence="ECO:0000305"
FT CONFLICT 1135
FT /note="H -> Y (in Ref. 1; BAC97845)"
FT /evidence="ECO:0000305"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 35..43
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 165..173
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 219..227
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 248..259
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 287..294
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 308..318
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 321..332
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 336..342
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 346..354
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 393..401
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 406..413
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 422..427
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 430..432
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 434..440
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 774..780
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 782..790
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 792..794
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 797..805
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 809..825
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 829..831
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 832..844
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 849..852
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 862..869
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 871..873
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 876..881
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 886..894
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 897..899
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 903..912
FT /evidence="ECO:0007829|PDB:7B9C"
SQ SEQUENCE 1217 AA; 135550 MW; DD12A12EC8E8B23A CRC64;
MFLYNLTLQR ATGISFAIHG NFSGTKQQEI VVSRGKILEL LRPDPNTGKV HTLLTVEVFG
VIRSLMAFRL TGGTKDYIVV GSDSGRIVIL EYQPSKNMFE KIHQETFGKS GCRRIVPGQF
LAVDPKGRAV MISAIEKQKL VYILNRDAAA RLTISSPLEA HKANTLVYHV VGVDVGFENP
MFACLEMDYE EADNDPTGEA AANTQQTLTF YELDLGLNHV VRKYSEPLEE HGNFLITVPG
GSDGPSGVLI CSENYITYKN FGDQPDIRCP IPRRRNDLDD PERGMIFVCS ATHKTKSMFF
FLAQTEQGDI FKITLETDED MVTEIRLKYF DTVPVAAAMC VLKTGFLFVA SEFGNHYLYQ
IAHLGDDDEE PEFSSAMPLE EGDTFFFQPR PLKNLVLVDE LDSLSPILFC QIADLANEDT
PQLYVACGRG PRSSLRVLRH GLEVSEMAVS ELPGNPNAVW TVRRHIEDEF DAYIIVSFVN
ATLVLSIGET VEEVTDSGFL GTTPTLSCSL LGDDALVQVY PDGIRHIRAD KRVNEWKTPG
KKTIVKCAVN QRQVVIALTG GELVYFEMDP SGQLNEYTER KEMSADVVCM SLANVPPGEQ
RSRFLAVGLV DNTVRIISLD PSDCLQPLSM QALPAQPESL CIVEMGGTEK QDELGERGSI
GFLYLNIGLQ NGVLLRTVLD PVTGDLSDTR TRYLGSRPVK LFRVRMQGQE AVLAMSSRSW
LSYSYQSRFH LTPLSYETLE FASGFASEQC PEGIVAISTN TLRILALEKL GAVFNQVAFP
LQYTPRKFVI HPESNNLIII ETDHNAYTEA TKAQRKQQMA EEMVEAAGED ERELAAEMAA
AFLNENLPES IFGAPKAGNG QWASVIRVMN PIQGNTLDLV QLEQNEAAFS VAVCRFSNTG
EDWYVLVGVA KDLILSPRSV AGGFVYTYKL VNNGEKLEFL HKTPVEEVPA AIAPFQGRVL
IGVGKLLRVY DLGKKKLLRK CENKHIANYI SGIQTIGHRV IVSDVQESFI WVRYKRNENQ
LIIFADDTYP RWVTTASLLD YDTVAGADKF GNICVVRLPP NTNDEVDEDP TGNKALWDRG
LLNGASQKAE VIMNYHVGET VLSLQKTTLI PGGSESLVYT TLSGGIGILV PFTSHEDHDF
FQHVEMHLRS EHPPLCGRDH LSFRSYYFPV KNVIDGDLCE QFNSMEPNKQ KNVSEELDRT
PPEVSKKLED IRTRYAF
//
