PAR12_HUMAN
ID PAR12_HUMAN Reviewed; 701 AA.
AC Q9H0J9; Q9H610; Q9NP36; Q9NTI3;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Protein mono-ADP-ribosyltransferase PARP12 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000269|PubMed:25043379};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 12 {ECO:0000303|PubMed:20106667};
DE Short=ARTD12 {ECO:0000303|PubMed:20106667};
DE AltName: Full=Poly [ADP-ribose] polymerase 12 {ECO:0000303|PubMed:20106667};
DE Short=PARP-12 {ECO:0000303|PubMed:20106667};
DE AltName: Full=Zinc finger CCCH domain-containing protein 1;
GN Name=PARP12 {ECO:0000303|PubMed:20106667, ECO:0000312|HGNC:HGNC:21919};
GN Synonyms=ZC3HDC1;
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 [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 444-701.
RC TISSUE=Small intestine;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP NOMENCLATURE.
RX PubMed=20106667; DOI=10.1016/j.tibs.2009.12.003;
RA Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.;
RT "Toward a unified nomenclature for mammalian ADP-ribosyltransferases.";
RL Trends Biochem. Sci. 35:208-219(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND ADP-RIBOSYLATION AT CYS-474; ASP-600 AND
RP ASP-611.
RX PubMed=25043379; DOI=10.1038/ncomms5426;
RA Vyas S., Matic I., Uchima L., Rood J., Zaja R., Hay R.T., Ahel I.,
RA Chang P.;
RT "Family-wide analysis of poly(ADP-ribose) polymerase activity.";
RL Nat. Commun. 5:4426-4426(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 489-684.
RX PubMed=25635049; DOI=10.1074/jbc.m114.630160;
RA Karlberg T., Klepsch M., Thorsell A.G., Andersson C.D., Linusson A.,
RA Schuler H.;
RT "Structural basis for lack of ADP-ribosyltransferase activity in poly(ADP-
RT ribose) polymerase-13/zinc finger antiviral protein.";
RL J. Biol. Chem. 290:7336-7344(2015).
CC -!- FUNCTION: Mono-ADP-ribosyltransferase that mediates mono-ADP-
CC ribosylation of target proteins. {ECO:0000269|PubMed:25043379}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-
CC aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-
CC COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102;
CC Evidence={ECO:0000269|PubMed:25043379};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54425;
CC Evidence={ECO:0000269|PubMed:25043379};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + NAD(+) = H(+) + nicotinamide + S-(ADP-
CC D-ribosyl)-L-cysteinyl-[protein]; Xref=Rhea:RHEA:56612, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:14624, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29950, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:140607; Evidence={ECO:0000269|PubMed:25043379};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56613;
CC Evidence={ECO:0000269|PubMed:25043379};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- PTM: Auto-mono-ADP-ribosylated. {ECO:0000269|PubMed:25043379}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
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DR EMBL; AL136766; CAB66700.1; -; mRNA.
DR EMBL; AL137255; CAB70657.1; -; mRNA.
DR EMBL; AC004849; AAS00360.1; -; Genomic_DNA.
DR EMBL; AC025816; AAF66161.1; -; Genomic_DNA.
DR EMBL; AC004961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC081541; AAH81541.1; -; mRNA.
DR EMBL; AK026346; BAB15457.1; -; mRNA.
DR CCDS; CCDS5857.1; -.
DR PIR; T46327; T46327.
DR RefSeq; NP_073587.1; NM_022750.3.
DR PDB; 2PQF; X-ray; 2.20 A; A/B/C/D/E/F=489-684.
DR PDB; 6V3W; X-ray; 2.04 A; A=489-684.
DR PDBsum; 2PQF; -.
DR PDBsum; 6V3W; -.
DR AlphaFoldDB; Q9H0J9; -.
DR SMR; Q9H0J9; -.
DR BioGRID; 122274; 43.
DR IntAct; Q9H0J9; 14.
DR MINT; Q9H0J9; -.
DR STRING; 9606.ENSP00000263549; -.
DR BindingDB; Q9H0J9; -.
DR ChEMBL; CHEMBL2429709; -.
DR DrugCentral; Q9H0J9; -.
DR iPTMnet; Q9H0J9; -.
DR PhosphoSitePlus; Q9H0J9; -.
DR BioMuta; PARP12; -.
DR DMDM; 47117630; -.
DR EPD; Q9H0J9; -.
DR jPOST; Q9H0J9; -.
DR MassIVE; Q9H0J9; -.
DR MaxQB; Q9H0J9; -.
DR PaxDb; Q9H0J9; -.
DR PeptideAtlas; Q9H0J9; -.
DR PRIDE; Q9H0J9; -.
DR ProteomicsDB; 80289; -.
DR Antibodypedia; 1226; 99 antibodies from 24 providers.
DR DNASU; 64761; -.
DR Ensembl; ENST00000263549.8; ENSP00000263549.3; ENSG00000059378.13.
DR GeneID; 64761; -.
DR KEGG; hsa:64761; -.
DR MANE-Select; ENST00000263549.8; ENSP00000263549.3; NM_022750.4; NP_073587.1.
DR UCSC; uc003vvl.2; human.
DR CTD; 64761; -.
DR DisGeNET; 64761; -.
DR GeneCards; PARP12; -.
DR HGNC; HGNC:21919; PARP12.
DR HPA; ENSG00000059378; Low tissue specificity.
DR MIM; 612481; gene.
DR neXtProt; NX_Q9H0J9; -.
DR OpenTargets; ENSG00000059378; -.
DR PharmGKB; PA134953063; -.
DR VEuPathDB; HostDB:ENSG00000059378; -.
DR eggNOG; ENOG502QSC4; Eukaryota.
DR GeneTree; ENSGT00940000154649; -.
DR HOGENOM; CLU_014825_2_1_1; -.
DR InParanoid; Q9H0J9; -.
DR OMA; YSKSDTH; -.
DR OrthoDB; 782733at2759; -.
DR PhylomeDB; Q9H0J9; -.
DR TreeFam; TF338389; -.
DR PathwayCommons; Q9H0J9; -.
DR SignaLink; Q9H0J9; -.
DR BioGRID-ORCS; 64761; 13 hits in 1085 CRISPR screens.
DR ChiTaRS; PARP12; human.
DR EvolutionaryTrace; Q9H0J9; -.
DR GeneWiki; PARP12; -.
DR GenomeRNAi; 64761; -.
DR Pharos; Q9H0J9; Tchem.
DR PRO; PR:Q9H0J9; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9H0J9; protein.
DR Bgee; ENSG00000059378; Expressed in secondary oocyte and 165 other tissues.
DR ExpressionAtlas; Q9H0J9; baseline and differential.
DR Genevisible; Q9H0J9; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IBA:GO_Central.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0070213; P:protein auto-ADP-ribosylation; IDA:UniProtKB.
DR GO; GO:0140289; P:protein mono-ADP-ribosylation; IDA:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.720.50; -; 1.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR037197; WWE_dom_sf.
DR InterPro; IPR000571; Znf_CCCH.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02825; WWE; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 3.
DR SUPFAM; SSF117839; SSF117839; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50918; WWE; 2.
DR PROSITE; PS50103; ZF_C3H1; 4.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Glycosyltransferase; Metal-binding; NAD;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..701
FT /note="Protein mono-ADP-ribosyltransferase PARP12"
FT /id="PRO_0000211341"
FT DOMAIN 298..361
FT /note="WWE 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT DOMAIN 364..458
FT /note="WWE 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT DOMAIN 484..698
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT ZN_FING 94..119
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 150..179
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 180..202
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 270..297
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 271..296
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 234..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 474
FT /note="ADP-ribosylcysteine"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 600
FT /note="ADP-ribosyl aspartic acid"
FT /evidence="ECO:0000269|PubMed:25043379"
FT MOD_RES 611
FT /note="ADP-ribosyl aspartic acid"
FT /evidence="ECO:0000269|PubMed:25043379"
FT VARIANT 293
FT /note="V -> I (in dbSNP:rs34111764)"
FT /id="VAR_050463"
FT VARIANT 463
FT /note="V -> M (in dbSNP:rs35456446)"
FT /id="VAR_050464"
FT VARIANT 620
FT /note="A -> V (in dbSNP:rs17161356)"
FT /id="VAR_050465"
FT CONFLICT 462
FT /note="Y -> C (in Ref. 4; BAB15457)"
FT /evidence="ECO:0000305"
FT STRAND 498..502
FT /evidence="ECO:0007829|PDB:6V3W"
FT HELIX 508..518
FT /evidence="ECO:0007829|PDB:6V3W"
FT STRAND 524..534
FT /evidence="ECO:0007829|PDB:6V3W"
FT HELIX 535..551
FT /evidence="ECO:0007829|PDB:6V3W"
FT TURN 552..554
FT /evidence="ECO:0007829|PDB:6V3W"
FT STRAND 560..566
FT /evidence="ECO:0007829|PDB:6V3W"
FT HELIX 568..570
FT /evidence="ECO:0007829|PDB:6V3W"
FT HELIX 571..577
FT /evidence="ECO:0007829|PDB:6V3W"
FT HELIX 581..583
FT /evidence="ECO:0007829|PDB:6V3W"
FT STRAND 592..599
FT /evidence="ECO:0007829|PDB:6V3W"
FT HELIX 601..604
FT /evidence="ECO:0007829|PDB:6V3W"
FT HELIX 605..607
FT /evidence="ECO:0007829|PDB:6V3W"
FT STRAND 611..622
FT /evidence="ECO:0007829|PDB:6V3W"
FT STRAND 626..629
FT /evidence="ECO:0007829|PDB:6V3W"
FT STRAND 649..653
FT /evidence="ECO:0007829|PDB:6V3W"
FT STRAND 655..657
FT /evidence="ECO:0007829|PDB:6V3W"
FT STRAND 660..663
FT /evidence="ECO:0007829|PDB:6V3W"
FT HELIX 666..668
FT /evidence="ECO:0007829|PDB:6V3W"
FT STRAND 669..678
FT /evidence="ECO:0007829|PDB:6V3W"
SQ SEQUENCE 701 AA; 79064 MW; 35152182F24CD215 CRC64;
MAQAGVVGEV TQVLCAAGGA LELPELRRRL RMGLSADALE RLLRQRGRFV VAVRAGGAAA
APERVVLAAS PLRLCRAHQG SKPGCVGLCA QLHLCRFMVY GACKFLRAGK NCRNSHSLTT
EHNLSVLRTH GVDHLSYNEL CQLLFQNDPW LLPEICQHYN KGDGPHGSCA FQKQCIKLHI
CQYFLQGECK FGTSCKRSHD FSNSENLEKL EKLGMSSDLV SRLPTIYRNA HDIKNKSSAP
SRVPPLFVPQ GTSERKDSSG SVSPNTLSQE EGDQICLYHI RKSCSFQDKC HRVHFHLPYR
WQFLDRGKWE DLDNMELIEE AYCNPKIERI LCSESASTFH SHCLNFNAMT YGATQARRLS
TASSVTKPPH FILTTDWIWY WSDEFGSWQE YGRQGTVHPV TTVSSSDVEK AYLAYCTPGS
DGQAATLKFQ AGKHNYELDF KAFVQKNLVY GTTKKVCRRP KYVSPQDVTT MQTCNTKFPG
PKSIPDYWDS SALPDPGFQK ITLSSSSEEY QKVWNLFNRT LPFYFVQKIE RVQNLALWEV
YQWQKGQMQK QNGGKAVDER QLFHGTSAIF VDAICQQNFD WRVCGVHGTS YGKGSYFARD
AAYSHHYSKS DTQTHTMFLA RVLVGEFVRG NASFVRPPAK EGWSNAFYDS CVNSVSDPSI
FVIFEKHQVY PEYVIQYTTS SKPSVTPSIL LALGSLFSSR Q
