ZC12A_RAT
ID ZC12A_RAT Reviewed; 596 AA.
AC A0JPN4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Endoribonuclease ZC3H12A {ECO:0000305};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q5D1E7};
DE AltName: Full=Monocyte chemotactic protein-induced protein 1 {ECO:0000250|UniProtKB:Q5D1E7};
DE Short=MCP-induced protein 1 {ECO:0000250|UniProtKB:Q5D1E7};
DE Short=MCPIP-1 {ECO:0000250|UniProtKB:Q5D1E7};
DE AltName: Full=Regnase-1 {ECO:0000250|UniProtKB:Q5D1E7};
DE Short=Reg1 {ECO:0000250|UniProtKB:Q5D1E7};
DE AltName: Full=Zinc finger CCCH domain-containing protein 12A {ECO:0000312|RGD:1306776};
GN Name=Zc3h12a {ECO:0000312|RGD:1306776};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAI27517.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart {ECO:0000312|EMBL:AAI27517.1};
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).
CC -!- FUNCTION: Endoribonuclease involved in various biological functions
CC such as cellular inflammatory response and immune homeostasis, glial
CC differentiation of neuroprogenitor cells, cell death of cardiomyocytes,
CC adipogenesis and angiogenesis. Functions as an endoribonuclease
CC involved in mRNA decay. Modulates the inflammatory response by
CC promoting the degradation of a set of translationally active cytokine-
CC induced inflammation-related mRNAs, such as IL6 and IL12B, during the
CC early phase of inflammation. Prevents aberrant T-cell-mediated immune
CC reaction by degradation of multiple mRNAs controlling T-cell
CC activation, such as those encoding cytokines (IL6 and IL2), cell
CC surface receptors (ICOS, TNFRSF4 and TNFR2) and transcription factor
CC (REL). Inhibits cooperatively with ZC3H12A the differentiation of
CC helper T cells Th17 in lungs. They repress target mRNA encoding the
CC Th17 cell-promoting factors IL6, ICOS, REL, IRF4, NFKBID and NFKBIZ.
CC The cooperation requires RNA-binding by RC3H1 and the nuclease activity
CC of ZC3H12A (By similarity). Together with RC3H1, destabilizes
CC TNFRSF4/OX40 mRNA by binding to the conserved stem loop structure in
CC its 3'UTR (By similarity). Self regulates by destabilizing its own
CC mRNA. Cleaves mRNA harboring a stem-loop (SL), often located in their
CC 3'-UTRs, during the early phase of inflammation in a helicase UPF1-
CC dependent manner (By similarity). Plays a role in the inhibition of
CC microRNAs (miRNAs) biogenesis (By similarity). Cleaves the terminal
CC loop of a set of precursor miRNAs (pre-miRNAs) important for the
CC regulation of the inflammatory response leading to their degradation,
CC and thus preventing the biosynthesis of mature miRNAs (By similarity).
CC Also plays a role in promoting angiogenesis in response to inflammatory
CC cytokines by inhibiting the production of antiangiogenic microRNAs via
CC its anti-dicer RNase activity (By similarity). Affects the overall
CC ubiquitination of cellular proteins. Positively regulates
CC deubiquitinase activity promoting the cleavage at 'Lys-48'- and 'Lys-
CC 63'-linked polyubiquitin chains on TNF receptor-associated factors
CC (TRAFs), preventing JNK and NF-kappa-B signaling pathway activation,
CC and hence negatively regulating macrophage-mediated inflammatory
CC response and immune homeostasis (By similarity). Induces also
CC deubiquitination of the transcription factor HIF1A, probably leading to
CC its stabilization and nuclear import, thereby positively regulating the
CC expression of proangiogenic HIF1A-targeted genes. Involved in a TANK-
CC dependent negative feedback response to attenuate NF-kappaB activation
CC through the deubiquitination of IKBKG or TRAF6 in response to
CC interleukin-1-beta (IL1B) stimulation or upon DNA damage (By
CC similarity). Prevents stress granules (SGs) formation and promotes
CC macrophage apoptosis under stress conditions, including arsenite-
CC induced oxidative stress, heat shock, and energy deprivation. Plays a
CC role in the regulation of macrophage polarization; promotes IL4-induced
CC polarization of macrophages M1 into anti-inflammatory M2 state. May
CC also act as a transcription factor that regulates the expression of
CC multiple genes involved in inflammatory response, angiogenesis,
CC adipogenesis and apoptosis (By similarity). Functions as a positive
CC regulator of glial differentiation of neuroprogenitor cells through an
CC amyloid precursor protein (APP)-dependent signaling pathway (By
CC similarity). Attenuates septic myocardial contractile dysfunction in
CC response to lipopolysaccharide (LPS) by reducing I-kappa-B-kinase
CC (IKK)-mediated NF-kappa-B activation, and hence myocardial pro-
CC inflammatory cytokine production (By similarity).
CC {ECO:0000250|UniProtKB:Q5D1E7, ECO:0000250|UniProtKB:Q5D1E8}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q5D1E7};
CC Note=Mg(2+) is required for RNase activity.
CC {ECO:0000250|UniProtKB:Q5D1E7};
CC -!- SUBUNIT: Oligomer. Found in a deubiquitination complex with TANK, USP10
CC and ZC3H12A; this complex inhibits genotoxic stress- or interleukin-1-
CC beta-mediated NF-kappaB activation by promoting IKBKG or TRAF6
CC deubiquitination. Interacts with IKBKG; this interaction increases in
CC response to DNA damage. Interacts with TANK; this interaction increases
CC in response to DNA damage and serves as a bridge to anchor both TANK
CC and USP10 into a deubiquitinating complex. Interacts with TRAF6; this
CC interaction increases in response to DNA damage and is stimulated by
CC TANK. Interacts with USP10; this interaction increases in response to
CC DNA damage and serves as a bridge to anchor both TANK and USP10 into a
CC deubiquitinating complex. Interacts with ZC3H12D. Interacts with
CC TNRC6A. Interacts with IKBKB/IKKB. Interacts with IKBKB/IKKB. Interacts
CC with IKBKB/IKKB. Interacts with BTRC; the interaction occurs when
CC ZC3H12A is phosphorylated in a IKBKB/IKKB-dependent manner. Interacts
CC with IRAK1; this interaction increases the interaction between ZC3H12A
CC and IKBKB/IKKB. Interacts with UPF1; this interaction occurs in a mRNA
CC translationally active- and termination-dependent manner and is
CC essential for ZC3H12A-mediated degradation of target mRNAs. Associates
CC with ribosomes. Interacts with ubiquitin.
CC {ECO:0000250|UniProtKB:Q5D1E7, ECO:0000250|UniProtKB:Q5D1E8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5D1E7}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q5D1E7}. Rough endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q5D1E7}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q5D1E7}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q5D1E7}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:Q5D1E7}. Cytoplasm, P-body
CC {ECO:0000250|UniProtKB:Q5D1E8}. Note=Predominantly localized in the
CC cytoplasm. Colocalizes with GW182 on many granule-like structures,
CC probably corresponding to cytoplasmic GW bodies (GWBs), also called
CC processing bodies (P bodies). Colocalizes with calnexin on the surface
CC of the rough endoplasmic reticulum (RER) membrane and with
CC translationally active polysomes. Colocalizes with ZC3H12D in
CC cytoplasmic mRNA processing P-body, also known as GW bodies (GWBs).
CC {ECO:0000250|UniProtKB:Q5D1E7, ECO:0000250|UniProtKB:Q5D1E8}.
CC -!- DOMAIN: The C3H1-type zinc finger domain and C-terminal region are
CC necessary for pre-miRNA binding. The C-terminal region and proline-rich
CC domain are necessary for oligomerization.
CC {ECO:0000250|UniProtKB:Q5D1E8}.
CC -!- PTM: Phosphorylated by IRAK1; phosphorylation is necessary for
CC subsequent phosphorylation by the I-kappa-B-kinase (IKK) complex.
CC Phosphorylated by I-kappa-B-kinases (IKKs) at Ser-435 and Ser-439 upon
CC lipopolysaccharide (LPS) or IL1B stimulation in macrophages through the
CC MyD88-dependent signaling pathway; these phosphorylations promote rapid
CC ubiquitin proteasome-mediated degradation of ZC3H12A in macrophages and
CC hence allows its target mRNAs, such as IL6, to escape from degradation
CC and accumulate during the inflammatory response.
CC {ECO:0000250|UniProtKB:Q5D1E7}.
CC -!- PTM: Ubiquitinated; ubiquitination is induced in response to
CC interleukin IL1 receptor stimuli in a IKBKB/IKKB and IRAK1-dependent
CC manner, leading to proteasome-mediated degradation.
CC {ECO:0000250|UniProtKB:Q5D1E7}.
CC -!- PTM: Proteolytically cleaved between Arg-111 and Arg-214 by MALT1 in
CC activated T-cells; cleavage at Arg-111 is critical for promoting
CC ZC3H12A degradation in response to T-cell receptor (TCR) stimulation,
CC and hence is necessary for prolonging the stability of a set of mRNAs
CC controlling T-cell activation and Th17 cell differentiation.
CC {ECO:0000250|UniProtKB:Q5D1E7}.
CC -!- SIMILARITY: Belongs to the ZC3H12 family. {ECO:0000305}.
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DR EMBL; BC127516; AAI27517.1; -; mRNA.
DR RefSeq; NP_001071139.1; NM_001077671.1.
DR AlphaFoldDB; A0JPN4; -.
DR SMR; A0JPN4; -.
DR STRING; 10116.ENSRNOP00000012314; -.
DR iPTMnet; A0JPN4; -.
DR PhosphoSitePlus; A0JPN4; -.
DR PaxDb; A0JPN4; -.
DR PRIDE; A0JPN4; -.
DR Ensembl; ENSRNOT00000012314; ENSRNOP00000012314; ENSRNOG00000009131.
DR GeneID; 313587; -.
DR KEGG; rno:313587; -.
DR UCSC; RGD:1306776; rat.
DR CTD; 80149; -.
DR RGD; 1306776; Zc3h12a.
DR eggNOG; KOG3777; Eukaryota.
DR GeneTree; ENSGT00940000155107; -.
DR HOGENOM; CLU_013020_2_1_1; -.
DR InParanoid; A0JPN4; -.
DR OMA; CGIFHPH; -.
DR OrthoDB; 771251at2759; -.
DR PhylomeDB; A0JPN4; -.
DR PRO; PR:A0JPN4; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000009131; Expressed in duodenum and 18 other tissues.
DR Genevisible; A0JPN4; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0004532; F:exoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
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:0004518; F:nuclease activity; ISS:UniProtKB.
DR GO; GO:0004540; F:ribonuclease activity; ISO:RGD.
DR GO; GO:0043022; F:ribosome binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0035613; F:RNA stem-loop binding; ISS:UniProtKB.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:1990869; P:cellular response to chemokine; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISO:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISO:RGD.
DR GO; GO:1904637; P:cellular response to ionomycin; ISS:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD.
DR GO; GO:1903936; P:cellular response to sodium arsenite; ISO:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
DR GO; GO:0098586; P:cellular response to virus; ISO:RGD.
DR GO; GO:0002757; P:immune response-activating signal transduction; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0010587; P:miRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0044828; P:negative regulation by host of viral genome replication; ISO:RGD.
DR GO; GO:0055118; P:negative regulation of cardiac muscle contraction; ISS:UniProtKB.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; ISS:UniProtKB.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; ISS:UniProtKB.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISS:UniProtKB.
DR GO; GO:1903799; P:negative regulation of miRNA maturation; ISS:UniProtKB.
DR GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:2000320; P:negative regulation of T-helper 17 cell differentiation; ISS:UniProtKB.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0000294; P:nuclear-transcribed mRNA catabolic process, endonucleolytic cleavage-dependent decay; ISO:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; ISO:RGD.
DR GO; GO:0010942; P:positive regulation of cell death; ISS:UniProtKB.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; ISO:RGD.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:1900119; P:positive regulation of execution phase of apoptosis; ISO:RGD.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0010884; P:positive regulation of lipid storage; ISO:RGD.
DR GO; GO:2000627; P:positive regulation of miRNA catabolic process; ISO:RGD.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISO:RGD.
DR GO; GO:1903003; P:positive regulation of protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:RGD.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0051259; P:protein complex oligomerization; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; ISS:UniProtKB.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; ISS:UniProtKB.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
DR InterPro; IPR040546; Rege-1_UBA-like.
DR InterPro; IPR040757; Regnase_1/ZC3H12_C.
DR InterPro; IPR021869; RNase_Zc3h12_NYN.
DR Pfam; PF18561; Regnase_1_C; 1.
DR Pfam; PF11977; RNase_Zc3h12a; 1.
DR Pfam; PF18039; UBA_6; 1.
PE 2: Evidence at transcript level;
KW Angiogenesis; Apoptosis; Cytoplasm; Developmental protein; Differentiation;
KW DNA damage; DNA-binding; Endonuclease; Endoplasmic reticulum; Hydrolase;
KW Immunity; Inflammatory response; Magnesium; Membrane; Metal-binding;
KW Neurogenesis; Nuclease; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Stress response; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..596
FT /note="Endoribonuclease ZC3H12A"
FT /id="PRO_0000341514"
FT DOMAIN 135..290
FT /note="RNase NYN"
FT /evidence="ECO:0000255"
FT ZN_FING 301..324
FT /note="C3H1-type"
FT REGION 24..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..87
FT /note="Ubiquitin association domain"
FT /evidence="ECO:0000250|UniProtKB:Q5D1E7"
FT REGION 81..150
FT /note="Necessary for interaction with TANK"
FT /evidence="ECO:0000250|UniProtKB:Q5D1E8"
FT REGION 92..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..281
FT /note="RNase"
FT /evidence="ECO:0000250|UniProtKB:Q5D1E8"
FT REGION 214..220
FT /note="RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q5D1E8"
FT REGION 278..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..454
FT /note="Necessary for interaction with ZC3H12D"
FT /evidence="ECO:0000250|UniProtKB:Q5D1E8"
FT REGION 339..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q5D1E8"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5D1E8"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5D1E8"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5D1E7"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5D1E7"
SQ SEQUENCE 596 AA; 65927 MW; C2BBA6DF323432AE CRC64;
MSDPCGKKLV QEISPTMSLW GLEDRHSCQG QPQPDQDPVA KEASASELQM KVDFFRKLGY
SSSEIHSALQ KLGVQADTNT VLGELVKHGS ATERECQAST DPCPQPPLVP RGGSTPKPST
VEPSLPEEDK ESSDLRPVVI DGSNVAMSHG NKEVFSCRGI LLAVNWFLER GHTDITVFVP
SWRKEQPRPD VPITDQHILR ELEKKKILVF TPSRRVGGKR VVCYDDRFIV KLAYESDGVV
VSNDTYRDLQ GERQEWKRFI EERLLMYSFV NDKFMPPDDP LGRHGPSLDN FLRKKPLPSE
HRKQPCPYGR KCTYGIKCRF FHPERPSRPQ RSVADELRAN ALLSPPRTPV KDKSSQRPSP
ASQPNSMSLE AEPGSPDGKK LGTRSSPGPH QEGSTQTCAP AGRSLPVSGG SFGPTEWLPH
TLDSLPYTSQ ECLDSGIGSL ESQMSELWGL RGGSPGESGP TRGPYTGYQT YGSKLPAAPA
FSPFRQAIGT GHFSVPTDYV PPPPTYPARE YWSEPYPLPP PTPVLQEPQR PRPRASGDPW
GRVSDLAKER AGVYTKLCGV FPPHLVEAVM GRFPQLLDPQ QLAAEILSYK SQHLSE
