ID   STPAP_MOUSE             Reviewed;         869 AA.
AC   Q8R3F9; Q3UUH3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 148.
DE   RecName: Full=Speckle targeted PIP5K1A-regulated poly(A) polymerase;
DE            Short=Star-PAP;
DE            EC=2.7.7.19 {ECO:0000250|UniProtKB:Q9H6E5};
DE   AltName: Full=RNA-binding motif protein 21;
DE            Short=RNA-binding protein 21;
DE   AltName: Full=U6 snRNA-specific terminal uridylyltransferase 1;
DE            Short=U6-TUTase;
DE            EC=2.7.7.52 {ECO:0000250|UniProtKB:Q9H6E5};
GN   Name=Tut1; Synonyms=Rbm21;
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 MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver, Spleen, and Testis;
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).
CC   -!- FUNCTION: Poly(A) polymerase that creates the 3'-poly(A) tail of
CC       specific pre-mRNAs. Localizes to nuclear speckles together with PIP5K1A
CC       and mediates polyadenylation of a select set of mRNAs, such as HMOX1.
CC       In addition to polyadenylation, it is also required for the 3'-end
CC       cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and
CC       promotes the recruitment and assembly of the CPSF complex on the 3'UTR
CC       of pre-mRNAs. In addition to adenylyltransferase activity, also has
CC       uridylyltransferase activity. However, the ATP ratio is higher than UTP
CC       in cells, suggesting that it functions primarily as a poly(A)
CC       polymerase. Acts as a specific terminal uridylyltransferase for U6
CC       snRNA in vitro: responsible for a controlled elongation reaction that
CC       results in the restoration of the four 3'-terminal UMP-residues found
CC       in newly transcribed U6 snRNA. Not involved in replication-dependent
CC       histone mRNA degradation. {ECO:0000250|UniProtKB:Q9H6E5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide;
CC         Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17348,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:140395,
CC         ChEBI:CHEBI:173116; EC=2.7.7.52;
CC         Evidence={ECO:0000250|UniProtKB:Q9H6E5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC         Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC         ChEBI:CHEBI:173115; EC=2.7.7.19;
CC         Evidence={ECO:0000250|UniProtKB:Q9H6E5};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9H6E5};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q9NVV4};
CC       Note=Binds 1 divalent cation per subunit.
CC       {ECO:0000250|UniProtKB:Q9H6E5};
CC   -!- ACTIVITY REGULATION: Adenylyltransferase activity is specifically
CC       phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2).
CC       {ECO:0000250|UniProtKB:Q9H6E5}.
CC   -!- SUBUNIT: Associates with the cleavage and polyadenylation specificity
CC       factor (CPSF) complex. Interacts with CPSF1 and CPSF3; the interaction
CC       is direct. Interacts with PIP5K1A. {ECO:0000250|UniProtKB:Q9H6E5}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q9H6E5}. Nucleus speckle
CC       {ECO:0000250|UniProtKB:Q9H6E5}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R3F9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R3F9-2; Sequence=VSP_021201, VSP_021202;
CC   -!- DOMAIN: The zinc-finger domain is required for terminal
CC       uridylyltransferase activity. Together with the RRM domain, binds the
CC       5'-area of U6 snRNA. {ECO:0000250|UniProtKB:Q9H6E5}.
CC   -!- DOMAIN: The RRM domain is required for terminal uridylyltransferase
CC       activity. Together with the zinc-finger domain, binds the 5'-area of U6
CC       snRNA. {ECO:0000250|UniProtKB:Q9H6E5}.
CC   -!- DOMAIN: The proline-rich region is dispensable for terminal
CC       uridylyltransferase activity. {ECO:0000250|UniProtKB:Q9H6E5}.
CC   -!- PTM: Phosphorylated by CK1 in the proline-rich (Pro-rich) region.
CC       {ECO:0000250|UniProtKB:Q9H6E5}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC       {ECO:0000305}.
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DR   EMBL; AK138418; BAE23652.1; -; mRNA.
DR   EMBL; BC023900; AAH23900.1; -; mRNA.
DR   EMBL; BC025499; AAH25499.1; -; mRNA.
DR   CCDS; CCDS29562.1; -. [Q8R3F9-1]
DR   RefSeq; NP_932110.1; NM_197993.3. [Q8R3F9-1]
DR   AlphaFoldDB; Q8R3F9; -.
DR   SMR; Q8R3F9; -.
DR   BioGRID; 213834; 4.
DR   STRING; 10090.ENSMUSP00000093958; -.
DR   iPTMnet; Q8R3F9; -.
DR   PhosphoSitePlus; Q8R3F9; -.
DR   SwissPalm; Q8R3F9; -.
DR   EPD; Q8R3F9; -.
DR   jPOST; Q8R3F9; -.
DR   MaxQB; Q8R3F9; -.
DR   PaxDb; 10090-ENSMUSP00000093958; -.
DR   PeptideAtlas; Q8R3F9; -.
DR   ProteomicsDB; 257462; -. [Q8R3F9-1]
DR   ProteomicsDB; 257463; -. [Q8R3F9-2]
DR   Pumba; Q8R3F9; -.
DR   Ensembl; ENSMUST00000096239.7; ENSMUSP00000093958.6; ENSMUSG00000071645.7. [Q8R3F9-1]
DR   GeneID; 70044; -.
DR   KEGG; mmu:70044; -.
DR   UCSC; uc008gog.1; mouse. [Q8R3F9-2]
DR   UCSC; uc008goh.1; mouse. [Q8R3F9-1]
DR   AGR; MGI:1917294; -.
DR   CTD; 64852; -.
DR   MGI; MGI:1917294; Tut1.
DR   VEuPathDB; HostDB:ENSMUSG00000071645; -.
DR   eggNOG; KOG2277; Eukaryota.
DR   GeneTree; ENSGT00940000159914; -.
DR   HOGENOM; CLU_018757_1_0_1; -.
DR   InParanoid; Q8R3F9; -.
DR   OMA; KSCEEGR; -.
DR   OrthoDB; 170176at2759; -.
DR   PhylomeDB; Q8R3F9; -.
DR   TreeFam; TF354308; -.
DR   BioGRID-ORCS; 70044; 24 hits in 76 CRISPR screens.
DR   ChiTaRS; Tut1; mouse.
DR   PRO; PR:Q8R3F9; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q8R3F9; Protein.
DR   Bgee; ENSMUSG00000071645; Expressed in ear vesicle and 169 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISS:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0140767; F:enzyme-substrate adaptor activity; ISS:UniProtKB.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR   GO; GO:1990817; F:poly(A) RNA polymerase activity; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0050265; F:RNA uridylyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0017070; F:U6 snRNA binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0180010; P:co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway; ISS:UniProtKB.
DR   GO; GO:0006378; P:mRNA polyadenylation; ISO:MGI.
DR   GO; GO:0016180; P:snRNA processing; ISS:UniProtKB.
DR   GO; GO:0034477; P:U6 snRNA 3'-end processing; ISS:UniProtKB.
DR   CDD; cd05402; NT_PAP_TUTase; 1.
DR   CDD; cd12279; RRM_TUT1; 1.
DR   Gene3D; 1.10.1410.10; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 2.
DR   InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR002058; PAP_assoc.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR034388; Star-PAP_RRM.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR12271; POLY A POLYMERASE CID PAP -RELATED; 1.
DR   PANTHER; PTHR12271:SF127; SPECKLE TARGETED PIP5K1A-REGULATED POLY(A) POLYMERASE; 1.
DR   Pfam; PF03828; PAP_assoc; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF12874; zf-met; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00451; ZnF_U1; 1.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   Genevisible; Q8R3F9; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Magnesium; Manganese; Metal-binding;
KW   mRNA processing; Nucleotide-binding; Nucleotidyltransferase; Nucleus;
KW   Phosphoprotein; Reference proteome; RNA-binding; Transferase; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..869
FT                   /note="Speckle targeted PIP5K1A-regulated poly(A)
FT                   polymerase"
FT                   /id="PRO_0000254187"
FT   DOMAIN          56..128
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          494..552
FT                   /note="PAP-associated"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         16..46
FT                   /note="Matrin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT   REGION          114..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          226..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          601..869
FT                   /note="KA1; binds the bulging loops of U6 snRNA but is
FT                   dispensable for terminal uridylyltransferase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT   REGION          640..689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          735..757
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          775..796
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          803..822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..310
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..335
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        667..689
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         205
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT   BINDING         216
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT   BINDING         216
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT   BINDING         218
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT   BINDING         218
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT   BINDING         395
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT   BINDING         395
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT   BINDING         417
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT   BINDING         435
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT   BINDING         552
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6E5"
FT   MOD_RES         688
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         744
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3MHT4"
FT   VAR_SEQ         391..405
FT                   /note="LALYNSRFLNLCSEM -> YFCVGLKAGSKVWGI (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_021201"
FT   VAR_SEQ         406..869
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_021202"
SQ   SEQUENCE   869 AA;  94603 MW;  0D0D2C73AAC78A25 CRC64;
     MAAVDSDVVS LPRGRFRCCL CDVTTANRPS LDAHLKGRKH RDLVQLRATR KAQGLRSVFV
     SGFPRDVGSA QLSEYFQTFG PVANIVMDKD KGVFAIVEMG DISAREAVLS QPKHSLGGHG
     LRVRPREQKE FQSPASKSPK GVDSSSHQLV QALAEAADVG AQMVKLVELR ELSEAERQLR
     NLVVALMQEV FTEFFPGCVV HPFGSTVNSF DVHGCDLDLF LDMGDMEETE PDPKAPKVPE
     TSSLDSALAS SLDPQALACT PASPLDSLSP TSVQESESLD FDTPSSLAPQ TPDSALGSDT
     VTSPQSLPPV SPLQEDRKEG KQGKELELAE EASKDEKEEA AAVLELVGSI LRGCVPGVYR
     VQTVPSARRP VVKFCHRPSG LHGDVSLSNR LALYNSRFLN LCSEMDGRVR PLVYTLRCWA
     QHNGLSGGGP LLNNYALTLL VIYFLQTRDP PVLPTVAQLT QRAGEGEQVE VDGWDCSFPK
     DASRLEPSTN VEPLSSLLAQ FFSCVSCLDL SGSLLSLREG RPLMVAEGLP SDLWEGLRLG
     PMNLQDPFDL SHNVAANVTG RVAKRLQSCC GAAASYCRSL QYQQRSSRGR DWGLLPLLQP
     SSPSSLLSAK LIPLPSAPFP QVIMALVDVL REALGCHIEQ GTKRRRSEGA RIKDSPLGGV
     NKRQRLGGQE KSFEEGKEEP QGCAGDHSEN EVEEMVIEVR ETPQDWALLH SGPPEEELPL
     MTANCLDKAA EHNPMKPEVA GEGSQGETGK EASHPSSVSW RCALWHQVWQ GRRRARRRLQ
     QQTKEEGRGG PTTGAEWLAM EARVTQELKG PNSEQERPPG EPLLSFVASA SQAEQTLTVA
     PLQDSQGLFP GLHHFLQGFI PQALKNLLK
//