SYF1_YEAST
ID SYF1_YEAST Reviewed; 859 AA.
AC Q04048; D6VT47;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Pre-mRNA-splicing factor SYF1;
DE AltName: Full=PRP19-associated complex protein 90;
DE AltName: Full=Synthetic lethal with CDC40 protein 1;
GN Name=SYF1; Synonyms=NTC90; OrderedLocusNames=YDR416W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP PROTEIN SEQUENCE OF 6-23, AND IDENTIFICATION IN THE PRP19-ASSOCIATED
RP COMPLEX.
RX PubMed=11842115; DOI=10.1093/nar/30.4.1029;
RA Chen C.-H., Yu W.-C., Tsao T.Y., Wang L.-Y., Chen H.-R., Lin J.-Y.,
RA Tsai W.-Y., Cheng S.-C.;
RT "Functional and physical interactions between components of the Prp19p-
RT associated complex.";
RL Nucleic Acids Res. 30:1029-1037(2002).
RN [4]
RP FUNCTION, AND INTERACTION WITH CEF1; ISY1; NTC20; PRP22 AND SYF2.
RX PubMed=11102353; DOI=10.1093/genetics/156.4.1503;
RA Ben-Yehuda S., Dix I., Russell C.S., McGarvey M., Beggs J.D., Kupiec M.;
RT "Genetic and physical interactions between factors involved in both cell
RT cycle progression and pre-mRNA splicing in Saccharomyces cerevisiae.";
RL Genetics 156:1503-1517(2000).
RN [5]
RP FUNCTION, AND IDENTIFICATION IN THE SPLICEOSOME.
RX PubMed=11105756; DOI=10.1017/s1355838200000984;
RA Russell C.S., Ben-Yehuda S., Dix I., Kupiec M., Beggs J.D.;
RT "Functional analyses of interacting factors involved in both pre-mRNA
RT splicing and cell cycle progression in Saccharomyces cerevisiae.";
RL RNA 6:1565-1572(2000).
RN [6]
RP IDENTIFICATION IN THE CWC COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11884590; DOI=10.1128/mcb.22.7.2011-2024.2002;
RA Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
RT "Proteomics analysis reveals stable multiprotein complexes in both fission
RT and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA
RT splicing factors, and snRNAs.";
RL Mol. Cell. Biol. 22:2011-2024(2002).
RN [7]
RP INTERACTION WITH CEF1; CLF1; ISY1; NTC20 AND PRP46.
RX PubMed=12088152; DOI=10.1017/s1355838202025050;
RA Ohi M.D., Gould K.L.;
RT "Characterization of interactions among the Cef1p-Prp19p-associated
RT splicing complex.";
RL RNA 8:798-815(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in pre-mRNA splicing and cell cycle control. As a
CC component of the NTC complex (or PRP19-associated complex), associates
CC to the spliceosome to mediate conformational rearrangement or to
CC stabilize the structure of the spliceosome after U4 snRNA dissociation,
CC which leads to spliceosome maturation. {ECO:0000269|PubMed:11102353,
CC ECO:0000269|PubMed:11105756}.
CC -!- SUBUNIT: Belongs to the NTC complex (or PRP19-associated complex),
CC composed of at least CEF1, CLF1, ISY1, NTC20, SNT309, SYF1, SYF2, and
CC PRP19. The NTC complex associates with the spliceosome after the
CC release of the U1 and U4 snRNAs and forms the CWC spliceosome
CC subcomplex (or CEF1-associated complex) reminiscent of a late-stage
CC spliceosome composed also of the U2, U5 and U6 snRNAs and at least
CC BUD13, BUD31, BRR2, CDC40, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23,
CC CWC24, CWC25, CWC27, ECM2, HSH155, IST3, LEA1, MSL1, PRP8, PRP9, PRP11,
CC PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3,
CC SNU114, SPP2, RSE1 and YJU2. Interacts with CEF1, CLF1, ISY1, NTC20,
CC PRP22, PRP46 and SYF2. {ECO:0000269|PubMed:11102353,
CC ECO:0000269|PubMed:11105756, ECO:0000269|PubMed:11842115,
CC ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:12088152}.
CC -!- INTERACTION:
CC Q04048; Q03654: CEF1; NbExp=5; IntAct=EBI-540, EBI-476;
CC Q04048; Q12309: CLF1; NbExp=4; IntAct=EBI-540, EBI-484;
CC Q04048; P21374: ISY1; NbExp=4; IntAct=EBI-540, EBI-9382;
CC Q04048; P38302: NTC20; NbExp=6; IntAct=EBI-540, EBI-20921;
CC Q04048; P32523: PRP19; NbExp=6; IntAct=EBI-540, EBI-493;
CC Q04048; P28004: PRP45; NbExp=3; IntAct=EBI-540, EBI-20640;
CC Q04048; P53277: SYF2; NbExp=3; IntAct=EBI-540, EBI-23308;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2170 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the crooked-neck family. {ECO:0000305}.
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DR EMBL; U33007; AAB64862.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12257.1; -; Genomic_DNA.
DR PIR; S69700; S69700.
DR RefSeq; NP_010704.1; NM_001180724.1.
DR PDB; 5GM6; EM; 3.50 A; v=569-734.
DR PDB; 5GMK; EM; 3.40 A; v=569-734.
DR PDB; 5LJ3; EM; 3.80 A; T=1-859.
DR PDB; 5LJ5; EM; 3.80 A; T=1-859.
DR PDB; 5LQW; EM; 5.80 A; P=1-859.
DR PDB; 5MPS; EM; 3.85 A; T=1-859.
DR PDB; 5MQ0; EM; 4.17 A; T=1-859.
DR PDB; 5WSG; EM; 4.00 A; v=569-734.
DR PDB; 5Y88; EM; 3.70 A; H=1-859.
DR PDB; 5YLZ; EM; 3.60 A; H=1-859.
DR PDB; 6BK8; EM; 3.30 A; U=1-859.
DR PDB; 6EXN; EM; 3.70 A; T=1-859.
DR PDB; 6J6G; EM; 3.20 A; v=1-859.
DR PDB; 6J6H; EM; 3.60 A; v=1-859.
DR PDB; 6J6N; EM; 3.86 A; v=1-859.
DR PDB; 6J6Q; EM; 3.70 A; v=1-859.
DR PDBsum; 5GM6; -.
DR PDBsum; 5GMK; -.
DR PDBsum; 5LJ3; -.
DR PDBsum; 5LJ5; -.
DR PDBsum; 5LQW; -.
DR PDBsum; 5MPS; -.
DR PDBsum; 5MQ0; -.
DR PDBsum; 5WSG; -.
DR PDBsum; 5Y88; -.
DR PDBsum; 5YLZ; -.
DR PDBsum; 6BK8; -.
DR PDBsum; 6EXN; -.
DR PDBsum; 6J6G; -.
DR PDBsum; 6J6H; -.
DR PDBsum; 6J6N; -.
DR PDBsum; 6J6Q; -.
DR AlphaFoldDB; Q04048; -.
DR SMR; Q04048; -.
DR BioGRID; 32475; 250.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR ComplexPortal; CPX-1885; NineTeen complex.
DR DIP; DIP-1681N; -.
DR IntAct; Q04048; 28.
DR MINT; Q04048; -.
DR STRING; 4932.YDR416W; -.
DR MaxQB; Q04048; -.
DR PaxDb; Q04048; -.
DR PRIDE; Q04048; -.
DR EnsemblFungi; YDR416W_mRNA; YDR416W; YDR416W.
DR GeneID; 852025; -.
DR KEGG; sce:YDR416W; -.
DR SGD; S000002824; SYF1.
DR VEuPathDB; FungiDB:YDR416W; -.
DR eggNOG; KOG2047; Eukaryota.
DR GeneTree; ENSGT00940000175925; -.
DR HOGENOM; CLU_007736_0_0_1; -.
DR InParanoid; Q04048; -.
DR OMA; FLMQQPL; -.
DR BioCyc; YEAST:G3O-29958-MON; -.
DR Reactome; R-SCE-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR PRO; PR:Q04048; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04048; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IBA:GO_Central.
DR GO; GO:0000974; C:Prp19 complex; IDA:SGD.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IDA:SGD.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:SGD.
DR GO; GO:0071008; C:U2-type post-mRNA release spliceosomal complex; IDA:SGD.
DR GO; GO:0071004; C:U2-type prespliceosome; IDA:SGD.
DR GO; GO:0000349; P:generation of catalytic spliceosome for first transesterification step; IDA:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR045075; Syf1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR11246; PTHR11246; 1.
DR SMART; SM00386; HAT; 8.
DR SUPFAM; SSF48452; SSF48452; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; mRNA processing; mRNA splicing;
KW Nucleus; Reference proteome; Repeat; Spliceosome.
FT CHAIN 1..859
FT /note="Pre-mRNA-splicing factor SYF1"
FT /id="PRO_0000205737"
FT REPEAT 17..49
FT /note="HAT 1"
FT REPEAT 52..84
FT /note="HAT 2"
FT REPEAT 88..108
FT /note="HAT 3"
FT REPEAT 123..157
FT /note="HAT 4"
FT REPEAT 177..219
FT /note="HAT 5"
FT REPEAT 238..271
FT /note="HAT 6"
FT REPEAT 427..459
FT /note="HAT 7"
FT REPEAT 461..482
FT /note="HAT 8"
FT REPEAT 520..554
FT /note="HAT 9"
FT REPEAT 599..633
FT /note="HAT 10"
FT REPEAT 639..675
FT /note="HAT 11"
FT REPEAT 685..718
FT /note="HAT 12"
FT REPEAT 720..754
FT /note="HAT 13"
FT REPEAT 756..790
FT /note="HAT 14"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 72..83
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 137..148
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 168..182
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 186..198
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 236..247
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 267..279
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 283..294
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 304..315
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 319..331
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 337..346
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 350..363
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 370..381
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 386..398
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 405..413
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 420..434
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 436..439
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 445..458
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 466..474
FT /evidence="ECO:0007829|PDB:6J6G"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 482..498
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 501..509
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 518..527
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 534..537
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 538..540
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 542..555
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 561..563
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 565..580
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 585..597
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 601..611
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 612..614
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 617..619
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 620..633
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 641..658
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 663..676
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 682..690
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 706..714
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 716..720
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 722..724
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 725..732
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 741..755
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 762..771
FT /evidence="ECO:0007829|PDB:6J6G"
FT TURN 772..774
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 780..791
FT /evidence="ECO:0007829|PDB:6J6G"
FT HELIX 800..818
FT /evidence="ECO:0007829|PDB:6J6G"
SQ SEQUENCE 859 AA; 100229 MW; ED4368A624A40E7C CRC64;
MSAYIAMKGV ITNVDENIRN DEDVAFEYEI QKTPQNILTW KRYIEYWKEE GRTDKQIRWL
YERFCSQFVT DTSIWEDYIR WESTKEVVET SRIFWLFQRC LKSCVRDCDR ICLSYLELAI
EQYDLAMIRH ALASSLMKME REMHRKVWDP VIKFVEEKVL PLTQLDSTQE DEEESTDEAE
LINVLLVKGF TKGGFISEEI SENGSRGDIW SSHILERYLK VAPQQKRNES LATLALTRDN
ITIKSVYEKY LPQDENSGKY LPSSELPFEL NFNYLASLEK LGLDNQYEEF MRQMNGIYPD
KWLFLILSLA KYYISRGRLD SCGDLLKKSL QQTLRYSDFD RIYNFYLLFE QECSQFILGK
LKENDSKFFN QKDWTEKLQA HMATFESLIN LYDIYLNDVA LRQDSNLVET WMKRVSLQKS
AAEKCNVYSE AILKIDPRKV GTPGSFGRLW CSYGDLYWRS NAISTARELW TQSLKVPYPY
IEDLEEIYLN WADRELDKEG VERAFSILED ALHVPTNPEI LLEKYKNGHR KIPAQTVLFN
SLRIWSKYID YLEAYCPKDA NSSDKIFNKT KMAYNTVIDL RLITPAMAEN FALFLQNHYE
VMESFQVYEK TIPLFPPEIQ YELWIEYLEV ATSHQLSSLS PEHIRFLFEK ALKNLCSNGI
DCKTIFIAYS VFEERISGLI SKSIEILRRG AVIGTVSVST HLESRLQLWR MCISKAESTL
GPSVTRELYQ ECIQILPNSK AVEFVIKFSD FESSIGETIR AREILAYGAK LLPPSRNTEL
WDSFEIFELK HGDKETYKDM LKMKKVLESN MLIDSASVSH EEGNINFVAA ATSHAPNSHT
LTQSTSSYSI NPDEIELDI
