SPT7_YEAST
ID SPT7_YEAST Reviewed; 1332 AA.
AC P35177; D6VQ80;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Transcriptional activator SPT7;
GN Name=SPT7; OrderedLocusNames=YBR081C; ORFNames=YBR0739;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7713415; DOI=10.1093/genetics/139.2.523;
RA Gansheroff L.J., Dollard C., Tan P., Winston F.;
RT "The Saccharomyces cerevisiae SPT7 gene encodes a very acidic protein
RT important for transcription in vivo.";
RL Genetics 139:523-536(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7985423; DOI=10.1002/yea.320100711;
RA van der Aart Q.J.M., Barthe C., Doignon F., Aigle M., Crouzet M.,
RA Steensma H.Y.;
RT "Sequence analysis of a 31 kb DNA fragment from the right arm of
RT Saccharomyces cerevisiae chromosome II.";
RL Yeast 10:959-964(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 463-523.
RX PubMed=1350857; DOI=10.1093/nar/20.10.2603;
RA Haynes S.R., Dollard C., Winston F., Beck S., Trowsdale J., Dawid I.B.;
RT "The bromodomain: a conserved sequence found in human, Drosophila and yeast
RT proteins.";
RL Nucleic Acids Res. 20:2603-2603(1992).
RN [6]
RP IDENTIFICATION IN THE SAGA COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=9674426; DOI=10.1016/s0092-8674(00)81220-9;
RA Grant P.A., Schieltz D., Pray-Grant M.G., Steger D.J., Reese J.C.,
RA Yates J.R. III, Workman J.L.;
RT "A subset of TAF(II)s are integral components of the SAGA complex required
RT for nucleosome acetylation and transcriptional stimulation.";
RL Cell 94:45-53(1998).
RN [7]
RP IDENTIFICATION IN A SAGA COMPLEX WITH SPT2; HFI1; SPT8; GCN5; SPT20; ADA2;
RP ADA3 AND TRA1.
RX PubMed=9885573; DOI=10.1016/s1097-2765(00)80300-7;
RA Grant P.A., Schieltz D., Pray-Grant M.G., Yates J.R. III, Workman J.L.;
RT "The ATM-related cofactor Tra1 is a component of the purified SAGA
RT complex.";
RL Mol. Cell 2:863-867(1998).
RN [8]
RP FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX.
RX PubMed=10026213; DOI=10.1074/jbc.274.9.5895;
RA Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M., Workman J.L.;
RT "Expanded lysine acetylation specificity of Gcn5 in native complexes.";
RL J. Biol. Chem. 274:5895-5900(1999).
RN [9]
RP IDENTIFICATION IN THE SLIK COMPLEX.
RX PubMed=12446794; DOI=10.1128/mcb.22.24.8774-8786.2002;
RA Pray-Grant M.G., Schieltz D., McMahon S.J., Wood J.M., Kennedy E.L.,
RA Cook R.G., Workman J.L., Yates J.R. III, Grant P.A.;
RT "The novel SLIK histone acetyltransferase complex functions in the yeast
RT retrograde response pathway.";
RL Mol. Cell. Biol. 22:8774-8786(2002).
RN [10]
RP IDENTIFICATION IN THE SALSA COMPLEX.
RX PubMed=12186975; DOI=10.1073/pnas.182021199;
RA Sterner D.E., Belotserkovskaya R., Berger S.L.;
RT "SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates
RT with activated transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11622-11627(2002).
RN [11]
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 [12]
RP IDENTIFICATION IN THE SLIK COMPLEX.
RX PubMed=15647753; DOI=10.1038/nature03242;
RA Pray-Grant M.G., Daniel J.A., Schieltz D., Yates J.R. III, Grant P.A.;
RT "Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-
RT dependent acetylation.";
RL Nature 433:434-438(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-78 AND SER-88, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1293, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [16]
RP 3D-STRUCTURE MODELING OF THE SAGA COMPLEX.
RX PubMed=15260971; DOI=10.1016/j.molcel.2004.06.005;
RA Wu P.Y., Ruhlmann C., Winston F., Schultz P.;
RT "Molecular architecture of the S. cerevisiae SAGA complex.";
RL Mol. Cell 15:199-208(2004).
CC -!- FUNCTION: Functions as component of the transcription regulatory
CC histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is
CC involved in RNA polymerase II-dependent transcriptional regulation of
CC approximately 10% of yeast genes. At the promoters, SAGA is required
CC for recruitment of the basal transcription machinery. It influences RNA
CC polymerase II transcriptional activity through different activities
CC such as TBP interaction (SPT3, SPT8 and SPT20) and promoter
CC selectivity, interaction with transcription activators (GCN5, ADA2,
CC ADA3 and TRA1), and chromatin modification through histone acetylation
CC (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone
CC H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA
CC interacts with DNA via upstream activating sequences (UASs). SALSA an
CC altered form of SAGA, may be involved in positive transcriptional
CC regulation. SLIK is proposed to have partly overlapping functions with
CC SAGA. It preferentially acetylates methylated histone H3, at least
CC after activation at the GAL1-10 locus. SPT7 is transcriptional
CC activator of TY elements and other genes.
CC {ECO:0000269|PubMed:10026213}.
CC -!- SUBUNIT: Component of the 1.8 MDa SAGA complex, which consists of at
CC least TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12,
CC TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and
CC SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2
CC copies. SAGA is built of 5 distinct domains with specialized functions.
CC Domain I (containing TRA1) probably represents the activator
CC interaction surface. Domain II (containing TAF5 and TAF6, and probably
CC TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and
CC ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing
CC HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily
CC an architectural role. Domain III also harbors the HAT activity. Domain
CC V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-
CC interacting module, which may be associated transiently with SAGA.
CC Component of the SALSA complex, which consists of at least TRA1, SPT7
CC (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1,
CC GCN5, ADA2 and SPT3. Component of the SLIK complex, which consists of
CC at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1,
CC UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9.
CC {ECO:0000269|PubMed:12186975, ECO:0000269|PubMed:12446794,
CC ECO:0000269|PubMed:15647753, ECO:0000269|PubMed:9674426,
CC ECO:0000269|PubMed:9885573}.
CC -!- INTERACTION:
CC P35177; Q12060: HFI1; NbExp=15; IntAct=EBI-17958, EBI-8287;
CC P35177; P32608: RTG2; NbExp=2; IntAct=EBI-17958, EBI-16322;
CC P35177; P38915: SPT8; NbExp=13; IntAct=EBI-17958, EBI-17964;
CC P35177; P38811: TRA1; NbExp=10; IntAct=EBI-17958, EBI-24638;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 2360 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; L22537; AAC37424.1; -; Genomic_DNA.
DR EMBL; X76294; CAA53940.1; -; Genomic_DNA.
DR EMBL; Z35950; CAA85026.1; -; Genomic_DNA.
DR EMBL; M87651; AAA35087.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07200.1; -; Genomic_DNA.
DR PIR; S41552; S41552.
DR RefSeq; NP_009637.1; NM_001178429.1.
DR PDB; 6T9I; EM; 3.90 A; K=1-1332.
DR PDB; 6T9K; EM; 3.30 A; K=1-1332.
DR PDBsum; 6T9I; -.
DR PDBsum; 6T9K; -.
DR AlphaFoldDB; P35177; -.
DR SMR; P35177; -.
DR BioGRID; 32783; 245.
DR ComplexPortal; CPX-656; SAGA complex.
DR ComplexPortal; CPX-675; SLIK (SAGA-like) complex.
DR DIP; DIP-771N; -.
DR IntAct; P35177; 200.
DR MINT; P35177; -.
DR STRING; 4932.YBR081C; -.
DR iPTMnet; P35177; -.
DR MaxQB; P35177; -.
DR PaxDb; P35177; -.
DR PRIDE; P35177; -.
DR EnsemblFungi; YBR081C_mRNA; YBR081C; YBR081C.
DR GeneID; 852373; -.
DR KEGG; sce:YBR081C; -.
DR SGD; S000000285; SPT7.
DR VEuPathDB; FungiDB:YBR081C; -.
DR eggNOG; KOG1472; Eukaryota.
DR HOGENOM; CLU_006198_0_1_1; -.
DR InParanoid; P35177; -.
DR OMA; CHKISLI; -.
DR BioCyc; YEAST:G3O-29049-MON; -.
DR ChiTaRS; SPT7; yeast.
DR PRO; PR:P35177; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P35177; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0000124; C:SAGA complex; IDA:SGD.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IDA:SGD.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IDA:SGD.
DR GO; GO:0006325; P:chromatin organization; IDA:SGD.
DR GO; GO:0000747; P:conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0016573; P:histone acetylation; IDA:SGD.
DR GO; GO:0016578; P:histone deubiquitination; IC:ComplexPortal.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR Gene3D; 1.10.20.10; -; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR037782; Spt7.
DR PANTHER; PTHR47343; PTHR47343; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Bromodomain; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..1332
FT /note="Transcriptional activator SPT7"
FT /id="PRO_0000211214"
FT DOMAIN 458..528
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 80..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1286..1332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..250
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..717
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1314..1332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphothreonine; by ATM or ATR"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 1293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 153..162
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 168..184
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 732..740
FT /evidence="ECO:0007829|PDB:6T9K"
FT TURN 741..743
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 744..752
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 854..856
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 869..883
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 899..901
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 902..915
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 918..928
FT /evidence="ECO:0007829|PDB:6T9K"
FT TURN 963..966
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 976..988
FT /evidence="ECO:0007829|PDB:6T9K"
FT TURN 992..995
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 1001..1026
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 1036..1045
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 1050..1052
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 1054..1063
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 1066..1084
FT /evidence="ECO:0007829|PDB:6T9K"
SQ SEQUENCE 1332 AA; 152617 MW; 083B63624669244F CRC64;
MTERIPIKNY QRTNAKALLK LTEKLFNKNF FDLYLTSQQL VVLEYLLSIS SEEDKLKAWD
YFLKGNIALN VEKSFPLTQE EEHHGAVSPA VDTRSDDVSS QTIKDNNNTN TNTSISNENH
VENEIEDKGD NAIANEDNFV NNDESDNVEE DLFKLDLEDL KQQISGTRFI GNLSLKIRYV
LWQCAIDYIY CDRNEFGDEN DTEYTLLDVE EKEEEEIGKN EKPQNKEGIS KFAEDEDYDD
EDENYDEDST DVKNVDDPPK NLDSISSSNI EIDDERRLVL NISISKETLS KLKTNNVEEI
MGNWNKIYHS FEYDKETMIK RLKLEESDKM IEKGKKKRSR SDLEAATDEQ DRENTNDEPD
TNQKLPTPEG STFSDTGNKR PKQSNLDLTV NLGIENLSLK HLLSSIQQKK SQLGISDYEL
KHLIMDVRKN RSKWTSDERI GQEELYEACE KVVLELRNYT EHSTPFLNKV SKREAPNYHQ
IIKKSMDLNT VLKKLKSFQY DSKQEFVDDI MLIWKNCLTY NSDPSHFLRG HAIAMQKKSL
QLIRMIPNIT IRNRADLEKE IEDMEKDKDY ELDEEEEVAG SGRKGLNMGA HMLAKENGKV
SEKDSSKTVK DEAPTNDDKL TSVIPEGEKE KDKTASSTVT VHENVNKNEI KENGKNEEQD
MVEESSKTED SSKDADAAKK DTEDGLQDKT AENKEAGENN EEEEDDDDED EDEDMVDSQS
YLLEKDDDRD DLEISVWKTV TAKVRAEICL KRTEYFKNGK LNSDSEAFLK NPQRMKRFDQ
LFLEYKEQKA LESYRQKIEQ NSIMKNGFGT VLKQEDDDQL QFHNDHSLNG NEAFEKQPND
IELDDTRFLQ EYDISNAIPD IVYEGVNTKT LDKMEDASVD RMLQNGINKQ SRFLANKDLG
LTPKMNQNIT LIQQIRHICH KISLIRMLQS PLSAQNSRSN PNAFLNNHIY NYTIIDDSLD
IDPVSQLPTH DYKNNRELIW KFMHKNISKV AMANGFETAH PSAINMLTEI AGDYLSNLIK
TLKLHHETNS LNRGTNVEML QTTLLENGIN RPDDLFSYVE SEFGKKTKKL QDIKQKLESF
LRALLRPTLQ ELSERNFEDE SQSFFTGDFA SELTGEDFFG FRELGLEKEF GVLSSSVPLQ
LLTTQFQTVD GETKVQAKKI QPEESDSIVY KKITKGMLDA GSFWNTLLPL LQKDYERSKA
YIAKQSKSSA NDKTSMTSTE DNSFALLEED QFVSKKTATK ARLPPTGKIS TTYKKKPIAS
AFILPEEDLE NDVKADPTTT VNAKVGAEND GDSSLFLRTP QPLDPLDMDD AFDDTNMGSN
SSFSLSLPRL NQ
