PARP4_MOUSE
ID PARP4_MOUSE Reviewed; 1969 AA.
AC E9PYK3; Q6A0B1; Q80UW6; Q8BW82; Q8R3A5;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Protein mono-ADP-ribosyltransferase PARP4 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q9UKK3};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 4 {ECO:0000250|UniProtKB:Q9UKK3};
DE Short=ARTD4 {ECO:0000250|UniProtKB:Q9UKK3};
DE AltName: Full=Poly [ADP-ribose] polymerase 4 {ECO:0000250|UniProtKB:Q9UKK3};
DE Short=PARP-4 {ECO:0000250|UniProtKB:Q9UKK3};
DE AltName: Full=Vault poly(ADP-ribose) polymerase {ECO:0000303|PubMed:15169895};
DE Short=VPARP {ECO:0000303|PubMed:15169895};
DE Short=mVparp {ECO:0000303|PubMed:15169895};
GN Name=Parp4 {ECO:0000312|MGI:MGI:2685589};
GN Synonyms=Kiaa0177 {ECO:0000303|PubMed:15368895};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1254.
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 623-1120 AND 1598-1961.
RC STRAIN=Czech II, and FVB/N;
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 1752-1969.
RC STRAIN=C57BL/6J; TISSUE=Oviduct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=15169895; DOI=10.1128/mcb.24.12.5314-5323.2004;
RA Liu Y., Snow B.E., Kickhoefer V.A., Erdmann N., Zhou W., Wakeham A.,
RA Gomez M., Rome L.H., Harrington L.;
RT "Vault poly(ADP-ribose) polymerase is associated with mammalian telomerase
RT and is dispensable for telomerase function and vault structure in vivo.";
RL Mol. Cell. Biol. 24:5314-5323(2004).
CC -!- FUNCTION: Mono-ADP-ribosyltransferase that mediates mono-ADP-
CC ribosylation of target proteins. {ECO:0000250|UniProtKB:Q9UKK3}.
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:0000250|UniProtKB:Q9UKK3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-
CC glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA-
CC COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540;
CC Evidence={ECO:0000250|UniProtKB:Q9UKK3};
CC -!- SUBUNIT: Component of the vault ribonucleoprotein particle, at least
CC composed of MVP, PARP4 and one or more vault RNAs (vRNAs). Interacts
CC with TEP1. {ECO:0000250|UniProtKB:Q9UKK3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8K3Y6}. Nucleus
CC {ECO:0000250|UniProtKB:Q8K3Y6}. Note=Localizes in the cytoplasm at
CC steady state, but shuttles between nucleus and cytoplasm in a XPO1-
CC dependent manner. {ECO:0000250|UniProtKB:Q8K3Y6}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:15169895). Mice are
CC viable and fertile for up to five generations, with no apparent changes
CC in telomerase activity or telomere length (PubMed:15169895).
CC {ECO:0000269|PubMed:15169895}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32185.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC154731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK172907; BAD32185.1; ALT_INIT; mRNA.
DR EMBL; BC025847; AAH25847.1; -; mRNA.
DR EMBL; BC046397; AAH46397.1; -; mRNA.
DR EMBL; AK053992; BAC35611.1; -; mRNA.
DR CCDS; CCDS49503.1; -.
DR RefSeq; NP_001139450.2; NM_001145978.2.
DR AlphaFoldDB; E9PYK3; -.
DR SMR; E9PYK3; -.
DR STRING; 10090.ENSMUSP00000124258; -.
DR iPTMnet; E9PYK3; -.
DR PhosphoSitePlus; E9PYK3; -.
DR EPD; E9PYK3; -.
DR jPOST; E9PYK3; -.
DR MaxQB; E9PYK3; -.
DR PaxDb; E9PYK3; -.
DR PeptideAtlas; E9PYK3; -.
DR PRIDE; E9PYK3; -.
DR ProteomicsDB; 365736; -.
DR Antibodypedia; 1562; 203 antibodies from 27 providers.
DR Ensembl; ENSMUST00000161553; ENSMUSP00000124258; ENSMUSG00000054509.
DR GeneID; 328417; -.
DR KEGG; mmu:328417; -.
DR UCSC; uc007ucd.2; mouse.
DR CTD; 143; -.
DR MGI; MGI:2685589; Parp4.
DR VEuPathDB; HostDB:ENSMUSG00000054509; -.
DR eggNOG; KOG1037; Eukaryota.
DR GeneTree; ENSGT00940000160555; -.
DR HOGENOM; CLU_001437_0_0_1; -.
DR InParanoid; E9PYK3; -.
DR OMA; CFVVNKQ; -.
DR OrthoDB; 955432at2759; -.
DR PhylomeDB; E9PYK3; -.
DR TreeFam; TF329720; -.
DR Reactome; R-MMU-197264; Nicotinamide salvaging.
DR BioGRID-ORCS; 328417; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Parp4; mouse.
DR PRO; PR:E9PYK3; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; E9PYK3; protein.
DR Bgee; ENSMUSG00000054509; Expressed in lumbar dorsal root ganglion and 169 other tissues.
DR Genevisible; E9PYK3; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; TAS:MGI.
DR GO; GO:0005819; C:spindle; TAS:MGI.
DR GO; GO:0005876; C:spindle microtubule; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; ISO:MGI.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008219; P:cell death; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; ISO:MGI.
DR GO; GO:0036211; P:protein modification process; ISO:MGI.
DR GO; GO:0140289; P:protein mono-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0051972; P:regulation of telomerase activity; ISO:MGI.
DR Gene3D; 3.40.50.10190; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR031273; PARP4.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR004102; Poly(ADP-ribose)pol_reg_dom.
DR InterPro; IPR036616; Poly(ADP-ribose)pol_reg_dom_sf.
DR InterPro; IPR013694; VIT.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR46530; PTHR46530; 1.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF08487; VIT; 1.
DR Pfam; PF13768; VWA_3; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00609; VIT; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF47587; SSF47587; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS51468; VIT; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycosyltransferase; Methylation; NAD; Nucleotidyltransferase;
KW Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Transferase.
FT CHAIN 1..1969
FT /note="Protein mono-ADP-ribosyltransferase PARP4"
FT /id="PRO_0000446171"
FT DOMAIN 1..94
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 235..363
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 362..566
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT DOMAIN 600..728
FT /note="VIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00801"
FT DOMAIN 869..1039
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1443..1541
FT /note="FH1"
FT /evidence="ECO:0000255"
FT REGION 92..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1808..1969
FT /note="Interaction with the major vault protein"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK3"
FT MOTIF 19..25
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 1230..1242
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1372..1391
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1412
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1448
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1479..1544
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1553..1602
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKK3"
FT CONFLICT 611
FT /note="A -> T (in Ref. 2; BAD32185)"
FT /evidence="ECO:0000305"
FT CONFLICT 1634
FT /note="D -> N (in Ref. 3; AAH25847)"
FT /evidence="ECO:0000305"
FT CONFLICT 1691
FT /note="V -> A (in Ref. 3; AAH25847)"
FT /evidence="ECO:0000305"
FT CONFLICT 1754
FT /note="D -> H (in Ref. 4; BAC35611)"
FT /evidence="ECO:0000305"
FT CONFLICT 1918
FT /note="A -> T (in Ref. 3; AAH25847)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1969 AA; 216133 MW; B1EDC5481653F93A CRC64;
MTLGIFANCI FCLKVKYLPR QQKKKLQTDI KENGGKFSFL LNPQCTHVIV DSADVLSRCH
LNSIQKNDVQ IANPAFIQDS VRQRRLLDVR NYDPLSPAPA APPAERSRSE VQSEYLPSDN
TPEKENTEVT EVSAENVEIP PFLQDFEVVK YNILEKVGGP ETVVVELQSS QDPESCPFVI
TAHFLLADQK TRRESTGKQT SEGAIEYYES YVEDLKRQGF LLQEHFTAEA TQLASEKLQA
LLLEEVISSG ALSQEVSDLL EVIWTEALGH LENTLLKPVN SMSLNDVSKA EGILLLVKTA
LKNGDSPGQL QKTMAEFYRL LPHRHPASEE VNLRLLAQKE DLCQLVRDMV NVCETNLSKP
NPPSLAKYRA LRCKIEHVDQ NTEEFSRVRK EVLQNNRSEQ PVDILQIFRV GRVNEATEFL
SKLGNVRLLF HGSPVRNILG ILSRGLLLPK VAEDRGVQRT DVGNLGSGIY FSDSLSTSIK
YAHAGETDGS RLLVVCDVAL GKCVNLFKKD FSLTEAPPGY DSVHGVSETT SVPTDFQDDE
FVVYKTNQVK MKYIVKFCTP GDQIKEFHPH ENTEVEEQRA EPSSVPEAGD FQLPDIKPFT
NIKAGLQDAS ANPVPLDSVH IKGRVIDFVA QVIVFQTYTN QSHVPIEAKY IFPLDDKAAV
CGFEAFINGK HIVGEIKEKE EARQEYREAV SQGHGAYLMD QDTPDVFTVS VGNLPPRAKV
LIKITYITEL SIQSPVAIFF IPGTVAPWQQ DKALNENLQD TVETIRIKEI GAEQSFSLAM
SIEMPYMIEF ISSDTHELRQ KSTDCKAVVS TVEGSSLDSG GFSLHIGLRD AYLPRMWVEK
HPEKESEACM LVFQPELADV LPDLRGKNEV IICLDCSSSM EGVTFTQAKQ VALYALSLLG
EEQKVNIMQF GTGYKELFSY PKCITDSKMA TEFIMSAAPS MGNTDFWKVL RYLSLLYPSE
GFRNILLISD GHLQSESLTL QLVKRNIQHT RVFTCAVGST ANRHILRTLS QCGAGVFEYF
NSKSKHSWKK QIEAQMTRIR SPSCHSVSVK WQQLSRDAPE PLQAPAWVPS LFHNDRLLVY
GFIPHCTQAT LQAFIQEKEF CTMVSTTELQ KTTGTMIHKL AARALIRDYE DGILHDDETN
HEMKKNIMKS LIIELSKENS LITQFTSFVA VEKRDVNEIP FANVPNISEL VAKEDVDFLP
YVSWQEKQPE ASISQTEIDS SRLKHNKLSD GHGVLQPVSV SSEVNEKPSL LLAAKKRKIK
TIKKCSLDIS EDFEDRTAVA QSPATAQSLN FHLPLSVRPQ LKAVEQQLHG NRLEPKQRGG
FRKLLMAKKC RNVPDSLVSS APAVTAEFSY LSACSSSSAF LSPLCDIPSS LPPHPLGGTH
PPPPLPLPDG THLPSPLFGS THPPPPLFGG TLIPPPSSLF GGTHLPPPPP LPGGTHIPPP
PPIPGGTLIP PSSSLFGGTH LPPPPLLSAG THIPPPPLLS AGTHLPPPPL LPAGTHIPPP
PPITGSTHPP PPSSLFGGTH LPPPPPLPGG THIPPPPPIP GGTLIPSPSS LFGGTHLPPP
PLLPAGTHIP PPPPITGSTH PPPPSSLFGG THLPPPPPAG TQFSLSPIGF IPPKLGPPKL
SHSHKLVGDT NIHDSEPPLL GFKDLCSRDM GFSCGTAFSG SFASSKDFDP GKFSQGPNNI
SFSPKAPEMG VLHQSPFCSP PKPPSAPPLV TNVLCSEAPQ SYFLNLQSAA VHQSPNNRVS
EIIMESVESS LPSDYSSRDA SSYLALEGAE DSLLGGSSFE TDTDEAAAFI ANDLLTSIET
SSDEECAFCD EDQESPVPWA SLFALQTENG FWKLTPELGL ILNLNVNALL TSLEEKGIRS
LGTKGRERLL DLIATLLVLQ FLYTKLEQEG MVAKSLIKMD DAFISRNIPW AFENIKKARE
WARKTEGQYP SICQRLELGK DWESATKQLL GIQPQANTSL HRILYYSQG
