TTP_SHEEP
ID TTP_SHEEP Reviewed; 325 AA.
AC Q6S9E0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=mRNA decay activator protein ZFP36 {ECO:0000305};
DE AltName: Full=Tristetraprolin {ECO:0000250|UniProtKB:P26651};
DE Short=TTP {ECO:0000250|UniProtKB:P26651};
DE AltName: Full=Zinc finger protein 36 {ECO:0000250|UniProtKB:P26651};
DE Short=Zfp-36 {ECO:0000250|UniProtKB:P22893};
GN Name=ZFP36 {ECO:0000250|UniProtKB:P26651};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=14679154; DOI=10.1093/jnci/djg118;
RA Twizere J.-C., Kruys V., Lefebvre L., Vanderplasschen A., Collete D.,
RA Debacq C., Lai W.S., Jauniaux J.-C., Bernstein L.R., Semmes J.O., Burny A.,
RA Blackshear P.J., Kettmann R., Willems L.;
RT "Interaction of retroviral Tax oncoproteins with tristetraprolin and
RT regulation of tumor necrosis factor-alpha expression.";
RL J. Natl. Cancer Inst. 95:1846-1859(2003).
CC -!- FUNCTION: Zinc-finger RNA-binding protein that destabilizes numerous
CC cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by
CC promoting their poly(A) tail removal or deadenylation, and hence
CC provide a mechanism for attenuating protein synthesis. Acts as an 3'-
CC untranslated region (UTR) ARE mRNA-binding adapter protein to
CC communicate signaling events to the mRNA decay machinery. Recruits
CC deadenylase CNOT7 (and probably the CCR4-NOT complex) via association
CC with CNOT1, and hence promotes ARE-mediated mRNA deadenylation.
CC Functions also by recruiting components of the cytoplasmic RNA decay
CC machinery to the bound ARE-containing mRNAs. Self regulates by
CC destabilizing its own mRNA. Binds to 3'-UTR ARE of numerous mRNAs.
CC Binds also to ARE of its own mRNA. Plays a role in anti-inflammatory
CC responses; suppresses tumor necrosis factor (TNF)-alpha production by
CC stimulating ARE-mediated TNF-alpha mRNA decay and several other
CC inflammatory ARE-containing mRNAs in interferon (IFN)- and/or
CC lipopolysaccharide (LPS)-induced macrophages. Also plays a role in the
CC regulation of dendritic cell maturation at the post-transcriptional
CC level, and hence operates as part of a negative feedback loop to limit
CC the inflammatory response. Promotes ARE-mediated mRNA decay of hypoxia-
CC inducible factor HIF1A mRNA during the response of endothelial cells to
CC hypoxia. Positively regulates early adipogenesis of preadipocytes by
CC promoting ARE-mediated mRNA decay of immediate early genes (IEGs).
CC Negatively regulates hematopoietic/erythroid cell differentiation by
CC promoting ARE-mediated mRNA decay of the transcription factor STAT5B
CC mRNA. Plays a role in maintaining skeletal muscle satellite cell
CC quiescence by promoting ARE-mediated mRNA decay of the myogenic
CC determination factor MYOD1 mRNA. Associates also with and regulates the
CC expression of non-ARE-containing target mRNAs at the post-
CC transcriptional level, such as MHC class I mRNAs. Participates in
CC association with argonaute RISC catalytic components in the ARE-
CC mediated mRNA decay mechanism; assists microRNA (miRNA) targeting ARE-
CC containing mRNAs. May also play a role in the regulation of cytoplasmic
CC mRNA decapping; enhances decapping of ARE-containing RNAs, in vitro.
CC Involved in the delivery of target ARE-mRNAs to processing bodies
CC (PBs). In addition to its cytosolic mRNA-decay function, affects
CC nuclear pre-mRNA processing. Negatively regulates nuclear poly(A)-
CC binding protein PABPN1-stimulated polyadenylation activity on ARE-
CC containing pre-mRNA during LPS-stimulated macrophages. Also involved in
CC the regulation of stress granule (SG) and P-body (PB) formation and
CC fusion. Plays a role in the regulation of keratinocyte proliferation,
CC differentiation and apoptosis. Plays a role as a tumor suppressor by
CC inhibiting cell proliferation in breast cancer cells.
CC {ECO:0000250|UniProtKB:P22893, ECO:0000250|UniProtKB:P26651}.
CC -!- SUBUNIT: Associates with cytoplasmic CCR4-NOT and PAN2-PAN3 deadenylase
CC complexes to trigger ARE-containing mRNA deadenylation and decay
CC processes. Part of a mRNA decay activation complex at least composed of
CC poly(A)-specific exoribonucleases CNOT6, EXOSC2 and XRN1 and mRNA-
CC decapping enzymes DCP1A and DCP2. Associates with the RNA exosome
CC complex. Interacts (via phosphorylated form) with 14-3-3 proteins;
CC these interactions promote exclusion of ZFP36 from cytoplasmic stress
CC granules in response to arsenite treatment in a MAPKAPK2-dependent
CC manner and does not prevent CCR4-NOT deadenylase complex recruitment or
CC ZFP36-induced ARE-containing mRNA deadenylation and decay processes.
CC Interacts with 14-3-3 proteins; these interactions occur in response to
CC rapamycin in an Akt-dependent manner. Interacts with AGO2 and AGO4.
CC Interacts (via C-terminus) with CNOT1; this interaction occurs in a
CC RNA-independent manner and induces mRNA deadenylation. Interacts (via
CC N-terminus) with CNOT6. Interacts with CNOT6L. Interacts (via C-
CC terminus) with CNOT7; this interaction occurs in a RNA-independent
CC manner, induces mRNA deadenylation and is inhibited in a
CC phosphorylation MAPKAPK2-dependent manner. Interacts (via
CC unphosphorylated form) with CNOT8; this interaction occurs in a RNA-
CC independent manner and is inhibited in a phosphorylation MAPKAPK2-
CC dependent manner. Interacts with DCP1A. Interacts (via N-terminus) with
CC DCP2. Interacts with EDC3. Interacts (via N-terminus) with EXOSC2.
CC Interacts with heat shock 70 kDa proteins. Interacts with KHSRP; this
CC interaction increases upon cytokine-induced treatment. Interacts with
CC MAP3K4; this interaction enhances the association with SH3KBP1/CIN85.
CC Interacts with MAPKAPK2; this interaction occurs upon skeletal muscle
CC satellite cell activation. Interacts with NCL. Interacts with NUP214;
CC this interaction increases upon lipopolysaccharide (LPS) stimulation.
CC Interacts with PABPC1; this interaction occurs in a RNA-dependent
CC manner. Interacts (via hypophosphorylated form) with PABPN1 (via RRM
CC domain and C-terminal arginine-rich region); this interaction occurs in
CC the nucleus in a RNA-independent manner, decreases in presence of
CC single-stranded poly(A) RNA-oligomer and in a p38 MAPK-dependent-manner
CC and inhibits nuclear poly(A) tail synthesis. Interacts with PAN2.
CC Interacts (via C3H1-type zinc finger domains) with PKM. Interacts (via
CC C3H1-type zinc finger domains) with nuclear RNA poly(A) polymerase.
CC Interacts with PPP2CA; this interaction occurs in LPS-stimulated cells
CC and induces ZFP36 dephosphorylation, and hence may promote ARE-
CC containing mRNAs decay. Interacts (via C-terminus) with PRR5L (via C-
CC terminus); this interaction may accelerate ZFP36-mediated mRNA decay
CC during stress. Interacts (via C-terminus) with SFN; this interaction
CC occurs in a phosphorylation-dependent manner. Interacts (via extreme C-
CC terminal region) with SH3KBP1/CIN85 (via SH3 domains); this interaction
CC enhances MAP3K4-induced phosphorylation of ZFP36 at Ser-64 and Ser-91
CC and does not alter neither ZFP36 binding to ARE-containing transcripts
CC nor TNF-alpha mRNA decay. Interacts with XRN1. Interacts (via C-
CC terminus and Ser-184 phosphorylated form) with YWHAB; this interaction
CC occurs in a p38/MAPKAPK2-dependent manner, increases cytoplasmic
CC localization of ZFP36 and protects ZFP36 from Ser-184 dephosphorylation
CC by serine/threonine phosphatase 2A, and hence may be crucial for
CC stabilizing ARE-containing mRNAs. Interacts (via phosphorylated form)
CC with YWHAE. Interacts (via C-terminus) with YWHAG; this interaction
CC occurs in a phosphorylation-dependent manner. Interacts with YWHAH;
CC this interaction occurs in a phosphorylation-dependent manner.
CC Interacts with YWHAQ; this interaction occurs in a phosphorylation-
CC dependent manner. Interacts with (via C-terminus) YWHAZ; this
CC interaction occurs in a phosphorylation-dependent manner. Does not
CC interact with SH3KBP1. Interacts (via P-P-P-P-G repeats) with GIGYF2;
CC the interaction is direct (By similarity).
CC {ECO:0000250|UniProtKB:P22893, ECO:0000250|UniProtKB:P26651}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P22893}. Cytoplasm
CC {ECO:0000250|UniProtKB:P22893}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:P22893}. Cytoplasm, P-body
CC {ECO:0000250|UniProtKB:P22893}. Note=Shuttles between nucleus and
CC cytoplasm in a CRM1-dependent manner. Localized predominantly in the
CC cytoplasm in a p38 MAPK- and YWHAB-dependent manner. Colocalizes with
CC SH3KBP1 and MAP3K4 in the cytoplasm. Component of cytoplasmic stress
CC granules (SGs). Localizes to cytoplasmic stress granules upon energy
CC starvation. Localizes in processing bodies (PBs). Excluded from stress
CC granules in a phosphorylation MAPKAPK2-dependent manner. Shuttles in
CC and out of both cytoplasmic P-body and SGs.
CC {ECO:0000250|UniProtKB:P22893, ECO:0000250|UniProtKB:P26651}.
CC -!- DOMAIN: The C3H1-type zinc finger domains are necessary for ARE-binding
CC activity. {ECO:0000250|UniProtKB:P26651}.
CC -!- PTM: Phosphorylated. Phosphorylation at serine and/or threonine
CC residues occurs in a p38 MAPK- and MAPKAPK2-dependent manner.
CC Phosphorylated by MAPKAPK2 at Ser-58 and Ser-184; phosphorylation
CC increases its stability and cytoplasmic localization, promotes binding
CC to 14-3-3 adapter proteins and inhibits the recruitment of cytoplasmic
CC CCR4-NOT and PAN2-PAN3 deadenylase complexes to the mRNA decay
CC machinery, thereby inhibiting ZFP36-induced ARE-containing mRNA
CC deadenylation and decay processes. Phosphorylation by MAPKAPK2 does not
CC impair ARE-containing RNA-binding. Phosphorylated in a MAPKAPK2- and
CC p38 MAPK-dependent manner upon skeletal muscle satellite cell
CC activation; this phosphorylation inhibits ZFP36-mediated mRNA decay
CC activity, and hence stabilizes MYOD1 mRNA. Phosphorylated by MAPK1 upon
CC mitogen stimulation. Phosphorylated at Ser-64 and Ser-91; these
CC phosphorylations increase in a SH3KBP1-dependent manner. Phosphorylated
CC at serine and threonine residues in a pyruvate kinase PKM- and p38
CC MAPK-dependent manner. Phosphorylation at Ser-58 may participate in the
CC PKM-mediated degradation of ZFP36 in a p38 MAPK-dependent manner.
CC Dephosphorylated by serine/threonine phosphatase 2A at Ser-184.
CC {ECO:0000250|UniProtKB:P22893, ECO:0000250|UniProtKB:P26651}.
CC -!- PTM: Ubiquitinated; pyruvate kinase (PKM)-dependent ubiquitination
CC leads to proteasomal degradation through a p38 MAPK signaling pathway.
CC {ECO:0000250|UniProtKB:P26651}.
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DR EMBL; AY462109; AAR31111.1; -; mRNA.
DR RefSeq; NP_001009765.1; NM_001009765.1.
DR AlphaFoldDB; Q6S9E0; -.
DR SMR; Q6S9E0; -.
DR STRING; 9940.ENSOARP00000006501; -.
DR PRIDE; Q6S9E0; -.
DR Ensembl; ENSOART00020039012; ENSOARP00020032319; ENSOARG00020024908.
DR GeneID; 443283; -.
DR KEGG; oas:443283; -.
DR CTD; 7538; -.
DR eggNOG; KOG1677; Eukaryota.
DR OrthoDB; 1541140at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0030014; C:CCR4-NOT complex; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0070578; C:RISC-loading complex; IEA:Ensembl.
DR GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
DR GO; GO:0019957; F:C-C chemokine binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0031072; F:heat shock protein binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0070063; F:RNA polymerase binding; ISS:UniProtKB.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISS:UniProtKB.
DR GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; ISS:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; IEA:Ensembl.
DR GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; ISS:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; ISS:UniProtKB.
DR GO; GO:0030099; P:myeloid cell differentiation; IEA:Ensembl.
DR GO; GO:0045647; P:negative regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:1902037; P:negative regulation of hematopoietic stem cell differentiation; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; ISS:UniProtKB.
DR GO; GO:1904246; P:negative regulation of polynucleotide adenylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0032897; P:negative regulation of viral transcription; ISS:UniProtKB.
DR GO; GO:0031086; P:nuclear-transcribed mRNA catabolic process, deadenylation-independent decay; ISS:UniProtKB.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IEA:Ensembl.
DR GO; GO:0038066; P:p38MAPK cascade; ISS:UniProtKB.
DR GO; GO:1901835; P:positive regulation of deadenylation-independent decapping of nuclear-transcribed mRNA; ISS:UniProtKB.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:1904582; P:positive regulation of intracellular mRNA localization; ISS:UniProtKB.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; ISS:UniProtKB.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
DR GO; GO:1902172; P:regulation of keratinocyte apoptotic process; ISS:UniProtKB.
DR GO; GO:0045616; P:regulation of keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0010837; P:regulation of keratinocyte proliferation; ISS:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
DR GO; GO:0032680; P:regulation of tumor necrosis factor production; ISS:UniProtKB.
DR GO; GO:0042594; P:response to starvation; ISS:UniProtKB.
DR GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
DR InterPro; IPR045877; ZFP36-like.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR12547; PTHR12547; 1.
DR Pfam; PF00642; zf-CCCH; 2.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; SSF90229; 2.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 2: Evidence at transcript level;
KW Cytoplasm; Developmental protein; DNA-binding; Exosome; Metal-binding;
KW mRNA transport; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; Transport; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..325
FT /note="mRNA decay activator protein ZFP36"
FT /id="PRO_0000089166"
FT REPEAT 69..73
FT /note="P-P-P-P-G"
FT REPEAT 196..200
FT /note="P-P-P-P-G"
FT REPEAT 217..222
FT /note="P-P-P-P-G"
FT ZN_FING 101..129
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 139..167
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..172
FT /note="Necessary for localization of ARE-containing mRNAs
FT to processing bodies (PBs)"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT REGION 1..98
FT /note="Necessary and sufficient for the association with
FT mRNA decay enzymes and mRNA decay activation"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT REGION 1..15
FT /note="Necessary for nuclear export"
FT /evidence="ECO:0000250|UniProtKB:P47973"
FT REGION 15..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..166
FT /note="Necessary for nuclear localization"
FT /evidence="ECO:0000250|UniProtKB:P47973"
FT REGION 95..171
FT /note="Necessary for RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT REGION 98..325
FT /note="Necessary for localization of ARE-containing mRNAs
FT to processing bodies (PBs)"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT REGION 101..192
FT /note="Necessary for interaction with PABPN1"
FT /evidence="ECO:0000250|UniProtKB:P22893"
FT REGION 172..325
FT /note="Necessary for mRNA decay activation"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT REGION 185..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..325
FT /note="Interaction with CNOT1"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT COMPBIAS 19..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..86
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..226
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 58
FT /note="Phosphoserine; by MAPKAPK2"
FT /evidence="ECO:0000250|UniProtKB:P22893"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22893"
FT MOD_RES 90
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT MOD_RES 184
FT /note="Phosphoserine; by MAPKAPK2"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT MOD_RES 227
FT /note="Phosphoserine; by MAPK1; in vitro"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26651"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26651"
SQ SEQUENCE 325 AA; 34037 MW; B00911E11417FC27 CRC64;
MDLAAIYKSL LSLSPELPSD LGETESSTSW ASSGPWSLSS SDSSLPEAAA RLPGRSTSLV
EGRSCGWVPP PPGFAPLAPR PSSELSPSPT SPTATPTTSS RYKTELCRTF SESGRCRYGA
KCQFAHGLGE LRQPSRHPKY KTELCHKFYL QGRCPYGSRC HFIHNPSEDL AAPGHPHVLR
QSISFSGLPS GRRTSPPPAS LAGPSVPSWS FSPSSSPPPP PGDLPLSPSA FSAAPGTPVS
RRDPTPACCP SCRRATPNSV WGPVGGLARS PSAHSLGSDP DEYASSGSSL GGSDSPVFEA
GVFGPPQPPA APRRLPIFNR ISVSE
