STP1_YEAST
ID STP1_YEAST Reviewed; 519 AA.
AC Q00947; D6VT88;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Transcription factor STP1;
DE Flags: Precursor;
GN Name=STP1; Synonyms=BAP1, SSY2; OrderedLocusNames=YDR463W;
GN ORFNames=D8035.7;
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], IDENTIFICATION OF INITIATION SITE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=1588961; DOI=10.1128/mcb.12.6.2633-2643.1992;
RA Wang S.S., Stanford D.R., Silvers C.D., Hopper A.K.;
RT "STP1, a gene involved in pre-tRNA processing, encodes a nuclear protein
RT containing zinc finger motifs.";
RL Mol. Cell. Biol. 12:2633-2643(1992).
RN [2]
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 [3]
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 [4]
RP FUNCTION IN TRNA MATURATION.
RX PubMed=3072476; DOI=10.1128/mcb.8.12.5140-5149.1988;
RA Wang S.S., Hopper A.K.;
RT "Isolation of a yeast gene involved in species-specific pre-tRNA
RT processing.";
RL Mol. Cell. Biol. 8:5140-5149(1988).
RN [5]
RP FUNCTION.
RX PubMed=1803818; DOI=10.1002/yea.320070905;
RA Tullin S., Gjermansen C., Kielland-Brandt M.C.;
RT "A high-affinity uptake system for branched-chain amino acids in
RT Saccharomyces cerevisiae.";
RL Yeast 7:933-941(1991).
RN [6]
RP FUNCTION IN TRANSCRIPTION REGULATION.
RX PubMed=9065387; DOI=10.1007/s002940050201;
RA Joergensen M.U., Gjermansen C., Andersen H.A., Kielland-Brandt M.C.;
RT "STP1, a gene involved in pre-tRNA processing in yeast, is important for
RT amino-acid uptake and transcription of the permease gene BAP2.";
RL Curr. Genet. 31:241-247(1997).
RN [7]
RP DOMAIN ATYPICAL ZINC-FINGER.
RX PubMed=9171100; DOI=10.1093/nar/25.12.2464;
RA Boehm S., Frishman D., Mewes H.-W.;
RT "Variations of the C2H2 zinc finger motif in the yeast genome and
RT classification of yeast zinc finger proteins.";
RL Nucleic Acids Res. 25:2464-2469(1997).
RN [8]
RP FUNCTION IN TRANSCRIPTION REGULATION.
RX PubMed=10648791; DOI=10.1093/nar/28.4.974;
RA de Boer M., Nielsen P.S., Bebelman J.-P., Heerikhuizen H., Andersen H.A.,
RA Planta R.J.;
RT "Stp1p, Stp2p and Abf1p are involved in regulation of expression of the
RT amino acid transporter gene BAP3 of Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 28:974-981(2000).
RN [9]
RP DNA-BINDING.
RX PubMed=11212916; DOI=10.1007/s004380000347;
RA Nielsen P.S., van den Hazel B., Didion T., de Boer M., Joergensen M.U.,
RA Planta R.J., Kielland-Brandt M.C., Andersen H.A.;
RT "Transcriptional regulation of the Saccharomyces cerevisiae amino acid
RT permease gene BAP2.";
RL Mol. Gen. Genet. 264:613-622(2001).
RN [10]
RP PROTEOLYTIC PROCESSING, IDENTIFICATION OF INITIATION SITE, MUTAGENESIS OF
RP 9-PRO--PHE-66, AND SUBCELLULAR LOCATION.
RX PubMed=12502738; DOI=10.1101/gad.239202;
RA Andreasson C., Ljungdahl P.O.;
RT "Receptor-mediated endoproteolytic activation of two transcription factors
RT in yeast.";
RL Genes Dev. 16:3158-3172(2002).
RN [11]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [12]
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 [13]
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 [14]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12775844; DOI=10.1126/science.1084337;
RA Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA Waterston R., Cohen B.A., Johnston M.;
RT "Finding functional features in Saccharomyces genomes by phylogenetic
RT footprinting.";
RL Science 301:71-76(2003).
RN [15]
RP FUNCTION.
RX PubMed=15126393; DOI=10.1534/genetics.166.4.1727;
RA Abdel-Sater F., Iraqui I., Urrestarazu A., Andre B.;
RT "The external amino acid signaling pathway promotes activation of Stp1 and
RT Uga35/Dal81 transcription factors for induction of the AGP1 gene in
RT Saccharomyces cerevisiae.";
RL Genetics 166:1727-1739(2004).
RN [16]
RP FUNCTION, AND MUTAGENESIS OF 27-LEU--ILE-32; LEU-65; PHE-66 AND PRO-67.
RX PubMed=15314160; DOI=10.1128/mcb.24.17.7503-7513.2004;
RA Andreasson C., Ljungdahl P.O.;
RT "The N-terminal regulatory domain of Stp1p is modular and, fused to an
RT artificial transcription factor, confers full Ssy1p-Ptr3p-Ssy5p sensor
RT control.";
RL Mol. Cell. Biol. 24:7503-7513(2004).
RN [17]
RP PROTEOLYTIC CLEAVAGE BY SSY5, AND PHOSPHORYLATION BY CKI.
RX PubMed=15509782; DOI=10.1128/mcb.24.22.9771-9785.2004;
RA Abdel-Sater F., El Bakkoury M., Urrestarazu A., Vissers S., Andre B.;
RT "Amino acid signaling in yeast: casein kinase I and the Ssy5 endoprotease
RT are key determinants of endoproteolytic activation of the membrane-bound
RT Stp1 transcription factor.";
RL Mol. Cell. Biol. 24:9771-9785(2004).
RN [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15197729; DOI=10.1002/yea.1120;
RA Eckert-Boulet N., Nielsen P.S., Friis C., dos Santos M.M., Nielsen J.,
RA Kielland-Brandt M.C., Regenberg B.;
RT "Transcriptional profiling of extracellular amino acid sensing in
RT Saccharomyces cerevisiae and the role of Stp1p and Stp2p.";
RL Yeast 21:635-648(2004).
RN [19]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16977312; DOI=10.1038/sj.emboj.7601330;
RA Menant A., Barbey R., Thomas D.;
RT "Substrate-mediated remodeling of methionine transport by multiple
RT ubiquitin-dependent mechanisms in yeast cells.";
RL EMBO J. 25:4436-4447(2006).
RN [20]
RP FUNCTION.
RX PubMed=16400180; DOI=10.1128/ec.5.1.174-179.2006;
RA Eckert-Boulet N., Larsson K., Wu B., Poulsen P., Regenberg B., Nielsen J.,
RA Kielland-Brandt M.C.;
RT "Deletion of RTS1, encoding a regulatory subunit of protein phosphatase 2A,
RT results in constitutive amino acid signaling via increased Stp1p
RT processing.";
RL Eukaryot. Cell 5:174-179(2006).
RN [21]
RP INTERACTION WITH SSY5.
RX PubMed=16778074; DOI=10.1101/gad.374206;
RA Andreasson C., Heessen S., Ljungdahl P.O.;
RT "Regulation of transcription factor latency by receptor-activated
RT proteolysis.";
RL Genes Dev. 20:1563-1568(2006).
RN [22]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16735580; DOI=10.1083/jcb.200601011;
RA Boban M., Zargari A., Andreasson C., Heessen S., Thyberg J.,
RA Ljungdahl P.O.;
RT "Asi1 is an inner nuclear membrane protein that restricts promoter access
RT of two latent transcription factors.";
RL J. Cell Biol. 173:695-707(2006).
RN [23]
RP DNA-BINDING, AND SUBCELLULAR LOCATION OF MUTANT STP1-133.
RX PubMed=17603098; DOI=10.1534/genetics.107.075077;
RA Boban M., Ljungdahl P.O.;
RT "Dal81 enhances Stp1- and Stp2-dependent transcription necessitating
RT negative modulation by inner nuclear membrane protein Asi1 in Saccharomyces
RT cerevisiae.";
RL Genetics 176:2087-2097(2007).
RN [24]
RP FUNCTION.
RX PubMed=17085444; DOI=10.1074/jbc.m609201200;
RA Zargari A., Boban M., Heessen S., Andreasson C., Thyberg J.,
RA Ljungdahl P.O.;
RT "Inner nuclear membrane proteins Asi1, Asi2, and Asi3 function in concert
RT to maintain the latent properties of transcription factors Stp1 and Stp2.";
RL J. Biol. Chem. 282:594-605(2007).
CC -!- FUNCTION: Transcription factor involved in the regulation of gene
CC expression in response to extracellular amino acid levels. Synthesized
CC as latent cytoplasmic precursor, which, upon a signal initiated by the
CC plasma membrane SPS (SSY1-PTR3-SSY5) amino acid sensor system, becomes
CC proteolytically activated and relocates to the nucleus, where it
CC induces the expression of SPS-sensor-regulated genes, including the
CC amino-acid permeases AGP1, BAP2, BAP3 and GNP1. Binding to promoters is
CC facilitated by DAL81. Involved in the repression of genes subject to
CC nitrogen catabolite repression and genes involved in stress response.
CC Negatively regulated by inner nuclear membrane proteins ASI1, ASI2 and
CC ASI3, which prevent unprocessed precursor forms that escape cytoplasmic
CC anchoring from inducing SPS-sensor-regulated genes. May be involved in
CC pre-tRNA splicing. {ECO:0000269|PubMed:10648791,
CC ECO:0000269|PubMed:15126393, ECO:0000269|PubMed:15197729,
CC ECO:0000269|PubMed:15314160, ECO:0000269|PubMed:16400180,
CC ECO:0000269|PubMed:16735580, ECO:0000269|PubMed:16977312,
CC ECO:0000269|PubMed:17085444, ECO:0000269|PubMed:1803818,
CC ECO:0000269|PubMed:3072476, ECO:0000269|PubMed:9065387}.
CC -!- SUBUNIT: Interacts (via Region II) with SSY5; protease component of the
CC SPS-sensor. {ECO:0000269|PubMed:16778074}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Nucleus. Note=Localizes to the cytoplasm in its
CC unprocessed form and is targeted to the nucleus after proteolytic
CC processing upon induction by amino acids. The SCF(MET30) ubiquitin
CC ligase complex negatively regulates nuclear accumulation of the
CC processed form in the absence of high extracellular methionine levels.
CC -!- DOMAIN: The N-terminal inhibitory domain contains conserved sequence
CC elements important for cytoplasmic retention (Region I) and proteolytic
CC processing (Region II) of the protein. Region I is also required for
CC ASI1/2/3-mediated negative regulation of transcription.
CC {ECO:0000269|PubMed:9171100}.
CC -!- PTM: Phosphorylated by casein kinase I. Phosphorylation is not
CC dependent on the extracellular amino acid levels, but is a prerequisite
CC for proteolytic processing. {ECO:0000269|PubMed:12502738,
CC ECO:0000269|PubMed:15509782}.
CC -!- PTM: Activated by the amino acid-induced proteolytic removal of an N-
CC terminal inhibitory domain by serine protease SSY5, an intrinsic
CC component of the SPS-sensor. Processing requires at least 2 components
CC of the SCF(GRR1) ubiquitin ligase complex, namely the F-box protein
CC GRR1 and the E2 enzyme CDC34, but does not depend on the proteasome.
CC Processing is negatively regulated by the protein phosphatase 2A
CC regulatory subunit RTS1.
CC -!- MISCELLANEOUS: Present with 1310 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- CAUTION: Was originally thought to be an amino-acid permease.
CC {ECO:0000305|PubMed:1803818}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB64913.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M88597; AAA35124.1; -; Genomic_DNA.
DR EMBL; U33050; AAB64913.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006938; DAA12298.1; -; Genomic_DNA.
DR PIR; S69631; S69631.
DR RefSeq; NP_010751.4; NM_001180771.3.
DR AlphaFoldDB; Q00947; -.
DR BioGRID; 32517; 211.
DR DIP; DIP-1272N; -.
DR IntAct; Q00947; 7.
DR MINT; Q00947; -.
DR STRING; 4932.YDR463W; -.
DR iPTMnet; Q00947; -.
DR MaxQB; Q00947; -.
DR PaxDb; Q00947; -.
DR PRIDE; Q00947; -.
DR EnsemblFungi; YDR463W_mRNA; YDR463W; YDR463W.
DR GeneID; 852074; -.
DR KEGG; sce:YDR463W; -.
DR SGD; S000002871; STP1.
DR VEuPathDB; FungiDB:YDR463W; -.
DR eggNOG; ENOG502S1NP; Eukaryota.
DR HOGENOM; CLU_025391_0_0_1; -.
DR InParanoid; Q00947; -.
DR OMA; LKMIKTS; -.
DR BioCyc; YEAST:G3O-29991-MON; -.
DR PRO; PR:Q00947; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q00947; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; DNA-binding; Membrane; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; tRNA processing; Zinc;
KW Zinc-finger; Zymogen.
FT PROPEP 1..?
FT /id="PRO_0000377642"
FT CHAIN ?..519
FT /note="Transcription factor STP1"
FT /id="PRO_0000046853"
FT ZN_FING 160..182
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 188..223
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 240..265
FT /note="C2H2-type 3; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 16..35
FT /note="I"
FT REGION 47..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..97
FT /note="II"
FT REGION 115..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 9..66
FT /note="Missing: In ASI13-1; dominant active and
FT constitutively nuclear localized transcription factor."
FT /evidence="ECO:0000269|PubMed:12502738"
FT MUTAGEN 27..32
FT /note="LVSGVI->AASGAA: In STP1-133; impairs cytoplasmic
FT retention, resulting in a dominant active transcription
FT factor. Activates transcription also in its unprocessed
FT form; when associated with A-66."
FT /evidence="ECO:0000269|PubMed:15314160"
FT MUTAGEN 65
FT /note="L->A: No effect."
FT /evidence="ECO:0000269|PubMed:15314160"
FT MUTAGEN 66
FT /note="F->A: In STP1-102; prevents proteolytic processing.
FT Activates transcription also in its unprocessed form; when
FT associated with 27-AASGAA-32."
FT /evidence="ECO:0000269|PubMed:15314160"
FT MUTAGEN 67
FT /note="P->A: No effect."
FT /evidence="ECO:0000269|PubMed:15314160"
SQ SEQUENCE 519 AA; 58088 MW; F95987994B74FA47 CRC64;
MPSTTLLFPQ KHIRAIPGKI YAFFRELVSG VIISKPDLSH HYSCENATKE EGKDAADEEK
TTTSLFPESN NIDRSLNGGC SVIPCSMDVS DLNTPISITL SPENRIKSEV NAKSLLGSRP
EQDTGAPIKM STGVTSSPLS PSGSTPEHST KVLNNGEEEF ICHYCDATFR IRGYLTRHIK
KHAIEKAYHC PFFNSATPPD LRCHNSGGFS RRDTYKTHLK ARHVLYPKGV KPQDRNKSSG
HCAQCGEYFS TIENFVENHI ESGDCKALPQ GYTKKNEKRS GKLRKIKTSN GHSRFISTSQ
SVVEPKVLFN KDAVEAMTIV ANNSSGNDII SKYGNNKLML NSENFKVDIP KRKRKYIKKK
QQQVSGSTVT TPEVATQNNQ EVAPDEISSA TIFSPFDTHL LEPVPSSSSE SSAEVMFHGK
QMKNFLIDIN SFTNQQQQAQ DNPSFLPLDI EQSSYDLSED AMSYPIISTQ SNRDCTQYDN
TKISQILQSQ LNPEYLSENH MRETQQYLNF YNDNFGSQF
