ZC12D_HUMAN
ID ZC12D_HUMAN Reviewed; 527 AA.
AC A2A288; A1L178; B2RXF4; B7WNU7; B9ZZP9; B9ZZQ0; Q6ZRW2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Probable ribonuclease ZC3H12D;
DE EC=3.1.-.-;
DE AltName: Full=MCP-induced protein 4 {ECO:0000303|PubMed:18178554};
DE AltName: Full=Transformed follicular lymphoma;
DE AltName: Full=Zinc finger CCCH domain-containing protein 12D;
DE AltName: Full=p34 {ECO:0000303|PubMed:17210687};
GN Name=ZC3H12D; Synonyms=C6orf95, MCPIP4 {ECO:0000303|PubMed:18178554}, TFL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND VARIANT LEU-53.
RX PubMed=19531561; DOI=10.1158/1541-7786.mcr-08-0511;
RA Minagawa K., Katayama Y., Nishikawa S., Yamamoto K., Sada A., Okamura A.,
RA Shimoyama M., Matsui T.;
RT "Inhibition of G(1) to S phase progression by a novel zinc finger protein
RT P58(TFL) at P-bodies.";
RL Mol. Cancer Res. 7:880-889(2009).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC87196.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT LEU-53.
RC TISSUE=Spleen {ECO:0000312|EMBL:BAC87196.1};
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAI27763.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex {ECO:0000305};
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).
RN [5] {ECO:0000305}
RP CHROMOSOMAL TRANSLOCATION, AND INVOLVEMENT IN DIFFUSE LARGE B-CELL
RP LYMPHOMA.
RX PubMed=17854321; DOI=10.1111/j.1365-2141.2007.06752.x;
RA Minagawa K., Yamamoto K., Nishikawa S., Ito M., Sada A., Yakushijin K.,
RA Okamura A., Shimoyama M., Katayama Y., Matsui T.;
RT "Deregulation of a possible tumour suppressor gene, ZC3H12D, by
RT translocation of IGK@ in transformed follicular lymphoma with
RT t(2;6)(p12;q25).";
RL Br. J. Haematol. 139:161-163(2007).
RN [6] {ECO:0000305}
RP FUNCTION, AND VARIANT ARG-106.
RX PubMed=17210687; DOI=10.1158/0008-5472.can-06-2723;
RA Wang M., Vikis H.G., Wang Y., Jia D., Wang D., Bierut L.J.,
RA Bailey-Wilson J.E., Amos C.I., Pinney S.M., Petersen G.M., de Andrade M.,
RA Yang P., Wiest J.S., Fain P.R., Schwartz A.G., Gazdar A., Minna J.,
RA Gaba C., Rothschild H., Mandal D., Kupert E., Seminara D., Liu Y.,
RA Viswanathan A., Govindan R., Anderson M.W., You M.;
RT "Identification of a novel tumor suppressor gene p34 on human chromosome
RT 6q25.1.";
RL Cancer Res. 67:93-99(2007).
RN [7] {ECO:0000305}
RP INDUCTION.
RX PubMed=18178554; DOI=10.1074/jbc.m707861200;
RA Liang J., Wang J., Azfer A., Song W., Tromp G., Kolattukudy P.E., Fu M.;
RT "A novel CCCH-zinc finger protein family regulates proinflammatory
RT activation of macrophages.";
RL J. Biol. Chem. 283:6337-6346(2008).
RN [8]
RP FUNCTION, INTERACTION WITH ZC3H12A, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP ASP-95, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=26134560; DOI=10.1074/jbc.m114.635870;
RA Huang S., Liu S., Fu J.J., Tony Wang T., Yao X., Kumar A., Liu G., Fu M.;
RT "Monocyte chemotactic protein-induced protein 1 and 4 form a complex but
RT act independently in regulation of interleukin-6 mRNA degradation.";
RL J. Biol. Chem. 290:20782-20792(2015).
CC -!- FUNCTION: May regulate cell growth likely by suppressing RB1
CC phosphorylation (PubMed:19531561). May function as RNase and regulate
CC the levels of target RNA species (Potential). In association with
CC ZC3H12A enhances the degradation of interleukin IL-6 mRNA level in
CC activated macrophages (PubMed:26134560). Serve as a tumor suppressor in
CC certain leukemia cells (PubMed:17210687). Overexpression inhibits the
CC G1 to S phase progression through suppression of RB1 phosphorylation
CC (PubMed:19531561). {ECO:0000269|PubMed:17210687,
CC ECO:0000269|PubMed:19531561, ECO:0000269|PubMed:26134560, ECO:0000305}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts with ZC3H12A (PubMed:26134560).
CC {ECO:0000269|PubMed:26134560}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:26134560}.
CC Note=Colocalizes with ZC3H12A in GW bodies (GWBs) (PubMed:26134560).
CC {ECO:0000269|PubMed:26134560}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Note=Localized as
CC discrete granules. Colocalized with mRNA-processing body markers, AGO2
CC and DCP1A, but not with a stress granule maker, TIA1, in the cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:14574404}; Synonyms=P58TFL, TFL1;
CC IsoId=A2A288-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2A288-3; Sequence=VSP_052853;
CC Name=3; Synonyms=P36TFL, TFL2;
CC IsoId=A2A288-4; Sequence=VSP_040794, VSP_040795;
CC -!- TISSUE SPECIFICITY: Expressed in normal human lymphocytes but defective
CC in some leukemia/lymphoma cell lines. {ECO:0000269|PubMed:19531561}.
CC -!- INDUCTION: By prolonged exposure to bacterial lipopolysaccharides (LPS)
CC in acute monocytic leukemia cell line THP-1 cells.
CC {ECO:0000269|PubMed:18178554}.
CC -!- DISEASE: Note=A chromosomal aberration involving ZC3H12D may be the
CC cause of the transformation of follicular lymphoma (FL) to diffuse
CC large B-cell lymphoma (DLBCL). Translocation t(2;6)(p12;q25) with IGK.
CC Resulting protein may not be expressed.
CC -!- SIMILARITY: Belongs to the ZC3H12 family.
CC {ECO:0000250|UniProtKB:A6QQJ8}.
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DR EMBL; AB458221; BAH28268.1; -; mRNA.
DR EMBL; AB458222; BAH28269.1; -; mRNA.
DR EMBL; AK127932; BAC87196.1; -; mRNA.
DR EMBL; AL031133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC127762; AAI27763.1; -; mRNA.
DR EMBL; BC157832; AAI57833.1; -; mRNA.
DR CCDS; CCDS47500.2; -. [A2A288-1]
DR RefSeq; NP_997243.2; NM_207360.2. [A2A288-1]
DR AlphaFoldDB; A2A288; -.
DR SMR; A2A288; -.
DR BioGRID; 131004; 32.
DR CORUM; A2A288; -.
DR STRING; 9606.ENSP00000386616; -.
DR iPTMnet; A2A288; -.
DR PhosphoSitePlus; A2A288; -.
DR BioMuta; ZC3H12D; -.
DR jPOST; A2A288; -.
DR MassIVE; A2A288; -.
DR MaxQB; A2A288; -.
DR PaxDb; A2A288; -.
DR PeptideAtlas; A2A288; -.
DR PRIDE; A2A288; -.
DR ProteomicsDB; 178; -. [A2A288-1]
DR ProteomicsDB; 179; -. [A2A288-3]
DR ProteomicsDB; 180; -. [A2A288-4]
DR Antibodypedia; 51365; 57 antibodies from 22 providers.
DR DNASU; 340152; -.
DR Ensembl; ENST00000409806.8; ENSP00000386616.3; ENSG00000178199.14. [A2A288-1]
DR GeneID; 340152; -.
DR KEGG; hsa:340152; -.
DR MANE-Select; ENST00000409806.8; ENSP00000386616.3; NM_207360.3; NP_997243.2.
DR UCSC; uc010kid.4; human. [A2A288-1]
DR CTD; 340152; -.
DR DisGeNET; 340152; -.
DR GeneCards; ZC3H12D; -.
DR HGNC; HGNC:21175; ZC3H12D.
DR HPA; ENSG00000178199; Group enriched (bone marrow, intestine, lymphoid tissue).
DR MIM; 611106; gene.
DR neXtProt; NX_A2A288; -.
DR OpenTargets; ENSG00000178199; -.
DR PharmGKB; PA134867170; -.
DR VEuPathDB; HostDB:ENSG00000178199; -.
DR eggNOG; KOG3777; Eukaryota.
DR GeneTree; ENSGT00940000161388; -.
DR HOGENOM; CLU_013020_2_1_1; -.
DR InParanoid; A2A288; -.
DR OrthoDB; 771251at2759; -.
DR PhylomeDB; A2A288; -.
DR TreeFam; TF315783; -.
DR PathwayCommons; A2A288; -.
DR BioGRID-ORCS; 340152; 1 hit in 245 CRISPR screens.
DR ChiTaRS; ZC3H12D; human.
DR GenomeRNAi; 340152; -.
DR Pharos; A2A288; Tbio.
DR PRO; PR:A2A288; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; A2A288; protein.
DR Bgee; ENSG00000178199; Expressed in epithelium of nasopharynx and 143 other tissues.
DR ExpressionAtlas; A2A288; baseline and differential.
DR Genevisible; A2A288; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GO_Central.
DR InterPro; IPR040546; Rege-1_UBA-like.
DR InterPro; IPR021869; RNase_Zc3h12_NYN.
DR InterPro; IPR000571; Znf_CCCH.
DR Pfam; PF11977; RNase_Zc3h12a; 1.
DR Pfam; PF18039; UBA_6; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosomal rearrangement; Cytoplasm; Endonuclease;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Nucleus; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..527
FT /note="Probable ribonuclease ZC3H12D"
FT /id="PRO_0000348931"
FT DOMAIN 88..243
FT /note="RNase NYN"
FT /evidence="ECO:0000255"
FT ZN_FING 248..279
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 48..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..356
FT /note="Necessary for interaction with ZC3H12A"
FT /evidence="ECO:0000269|PubMed:26134560"
FT REGION 296..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..412
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 228..527
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052853"
FT VAR_SEQ 300..321
FT /note="GAGAEEQRPPRAPGGSAGARAA -> VLPGRPPASARPAAPAAGRTPP (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:19531561"
FT /id="VSP_040794"
FT VAR_SEQ 322..527
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:19531561"
FT /id="VSP_040795"
FT VARIANT 53
FT /note="P -> L (in dbSNP:rs7747948)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:19531561"
FT /id="VAR_046199"
FT VARIANT 106
FT /note="K -> R (in some sporadic lung cancer sample; appears
FT to cause loss of tumor suppressor activity;
FT dbSNP:rs61997220)"
FT /evidence="ECO:0000269|PubMed:17210687"
FT /id="VAR_046200"
FT MUTAGEN 95
FT /note="D->N: Inhibits interleukin IL6 mRNA instability."
FT /evidence="ECO:0000269|PubMed:26134560"
FT CONFLICT 135
FT /note="S -> F (in Ref. 1; BAH28269)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="P -> S (in Ref. 1; BAH28269 and 2; BAC87196)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="P -> L (in Ref. 1; BAH28269 and 2; BAC87196)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="P -> S (in Ref. 4; AAI57833)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="A -> T (in Ref. 4; AAI57833)"
FT /evidence="ECO:0000305"
FT CONFLICT A2A288-4:300
FT /note="V -> G (in Ref. 1; BAH28269 and 2; BAC87196)"
FT /evidence="ECO:0000305"
FT CONFLICT A2A288-4:301
FT /note="L -> V (in Ref. 1; BAH28269 and 2; BAC87196)"
FT /evidence="ECO:0000305"
FT CONFLICT A2A288-4:302
FT /note="P -> R (in Ref. 1; BAH28269 and 2; BAC87196)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 527 AA; 58078 MW; E330D92548D49DD7 CRC64;
MEHPSKMEFF QKLGYDREDV LRVLGKLGEG ALVNDVLQEL IRTGSRPGAL EHPAAPRLVP
RGSCGVPDSA QRGPGTALEE DFRTLASSLR PIVIDGSNVA MSHGNKETFS CRGIKLAVDW
FRDRGHTYIK VFVPSWRKDP PRADTPIREQ HVLAELERQA VLVYTPSRKV HGKRLVCYDD
RYIVKVAYEQ DGVIVSNDNY RDLQSENPEW KWFIEQRLLM FSFVNDRFMP PDDPLGRHGP
SLSNFLSRKP KPPEPSWQHC PYGKKCTYGI KCKFYHPERP HHAQLAVADE LRAKTGARPG
AGAEEQRPPR APGGSAGARA APREPFAHSL PPARGSPDLA ALRGSFSRLA FSDDLGPLGP
PLPVPACSLT PRLGGPDWVS AGGRVPGPLS LPSPESQFSP GDLPPPPGLQ LQPRGEHRPR
DLHGDLLSPR RPPDDPWARP PRSDRFPGRS VWAEPAWGDG ATGGLSVYAT EDDEGDARAR
ARIALYSVFP RDQVDRVMAA FPELSDLARL ILLVQRCQSA GAPLGKP
