ID TUT7_MOUSE Reviewed; 1491 AA.
AC Q5BLK4; A1A4B1; Q3V3V7; Q8CIH3;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 3.
DT 24-JAN-2024, entry version 129.
DE RecName: Full=Terminal uridylyltransferase 7 {ECO:0000305};
DE Short=TUTase 7;
DE EC=2.7.7.52 {ECO:0000250|UniProtKB:Q5VYS8};
DE AltName: Full=Zinc finger CCHC domain-containing protein 6;
GN Name=Tut7 {ECO:0000312|MGI:MGI:2387179}; Synonyms=Kiaa1711, Zcchc6;
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].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary gland;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 110-1378.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-172; SER-747;
RP THR-865 AND SER-891, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, 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).
RN [4]
RP FUNCTION IN PRE-LET-7 REPRESSION.
RX PubMed=22898984; DOI=10.1261/rna.034538.112;
RA Thornton J.E., Chang H.M., Piskounova E., Gregory R.I.;
RT "Lin28-mediated control of let-7 microRNA expression by alternative TUTases
RT Zcchc11 (TUT4) and Zcchc6 (TUT7).";
RL RNA 18:1875-1885(2012).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28792939; DOI=10.1038/nature23318;
RA Morgan M., Much C., DiGiacomo M., Azzi C., Ivanova I., Vitsios D.M.,
RA Pistolic J., Collier P., Moreira P.N., Benes V., Enright A.J.,
RA O'Carroll D.;
RT "mRNA 3' uridylation and poly(A) tail length sculpt the mammalian maternal
RT transcriptome.";
RL Nature 548:347-351(2017).
CC -!- FUNCTION: Uridylyltransferase that mediates the terminal uridylation of
CC mRNAs with short (less than 25 nucleotides) poly(A) tails, hence
CC facilitating global mRNA decay (PubMed:28792939). Essential for both
CC oocyte maturation and fertility. Through 3' terminal uridylation of
CC mRNA, sculpts, with TUT7, the maternal transcriptome by eliminating
CC transcripts during oocyte growth (PubMed:28792939). Involved in
CC microRNA (miRNA)-induced gene silencing through uridylation of
CC deadenylated miRNA targets. Also acts as a suppressor of miRNA
CC biogenesis by mediating the terminal uridylation of miRNA precursors,
CC including that of let-7 (pre-let-7) (PubMed:22898984). Uridylated pre-
CC let-7 RNA is not processed by Dicer and undergo degradation. Pre-let-7
CC uridylation is strongly enhanced in the presence of LIN28A. Due to
CC functional redundancy between ZCCHC6 and ZCCHC11, the identification of
CC the specific role of each of these proteins is difficult (By
CC similarity) (PubMed:22898984). Involved in microRNA (miRNA)-induced
CC gene silencing through uridylation of deadenylated miRNA targets (By
CC similarity). Also functions as an integral regulator of microRNA
CC biogenesiS using 3 different uridylation mechanisms (By similarity).
CC Acts as a suppressor of miRNA biogenesis by mediating the terminal
CC uridylation of some miRNA precursors, including that of let-7 (pre-let-
CC 7). Uridylated pre-let-7 RNA is not processed by Dicer and undergo
CC degradation. Pre-let-7 oligouridylation is strongly enhanced in the
CC presence of LIN28A (PubMed:22898984). In the absence of LIN28A, TUT7
CC and TUT4 monouridylate group II pre-miRNAs, which includes most of pre-
CC let7 members, that shapes an optimal 3' end overhang for efficient
CC processing (By similarity). Add oligo-U tails to truncated pre-miRNAS
CC with a 5' overhang which may promote rapid degradation of non-
CC functional pre-miRNA species (By similarity). Does not play a role in
CC replication-dependent histone mRNA degradation (By similarity). Due to
CC functional redundancy between TUT4 and TUT7, the identification of the
CC specific role of each of these proteins is difficult (PubMed:28792939,
CC PubMed:22898984). TUT4 and TUT7 restrict retrotransposition of long
CC interspersed element-1 (LINE-1) in cooperation with MOV10 counteracting
CC the RNA chaperonne activity of L1RE1. TUT7 uridylates LINE-1 mRNAs in
CC the cytoplasm which inhibits initiation of reverse transcription once
CC in the nucleus, whereas uridylation by TUT4 destabilizes mRNAs in
CC cytoplasmic ribonucleoprotein granules (By similarity).
CC {ECO:0000250|UniProtKB:Q5VYS8, ECO:0000269|PubMed:22898984,
CC ECO:0000269|PubMed:28792939}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5VYS8}.
CC -!- DOMAIN: Utilizes two multidomain functional modules during the switch
CC from monouridylation to oligouridylation. The catalytic module
CC (containing the 3 CCHC-type Zinc finger domains) is essential for both
CC activities while the Lin28-interacting module (LIM) at the N-termail
CC part is indispensable for oligouridylation.
CC {ECO:0000250|UniProtKB:Q5VYS8}.
CC -!- DISRUPTION PHENOTYPE: Double conditional knockouts that have deleted
CC both TUT4 and TUT7 at the secondary oocyte stage are infertile. Females
CC ovulate normal numbers of oocytes with normal morphology of antral
CC follicles but with a slight decrease in the frequency of surrounded
CC nucleolus state oocytes. Mutant oocytes are unable to support early
CC embryonic development, they fail to complete meiosis I properly.
CC {ECO:0000269|PubMed:28792939}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH23438.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH23880.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE20473.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC023880; AAH23880.1; ALT_INIT; mRNA.
DR EMBL; BC043111; AAH43111.1; -; mRNA.
DR EMBL; BC023438; AAH23438.1; ALT_SEQ; mRNA.
DR EMBL; AK031043; BAE20473.1; ALT_INIT; mRNA.
DR RefSeq; NP_705766.3; NM_153538.3.
DR RefSeq; XP_006517271.1; XM_006517208.1.
DR RefSeq; XP_017170969.1; XM_017315480.1.
DR AlphaFoldDB; Q5BLK4; -.
DR SMR; Q5BLK4; -.
DR BioGRID; 229511; 1.
DR DIP; DIP-60223N; -.
DR IntAct; Q5BLK4; 1.
DR STRING; 10090.ENSMUSP00000071623; -.
DR iPTMnet; Q5BLK4; -.
DR PhosphoSitePlus; Q5BLK4; -.
DR SwissPalm; Q5BLK4; -.
DR EPD; Q5BLK4; -.
DR jPOST; Q5BLK4; -.
DR MaxQB; Q5BLK4; -.
DR PaxDb; 10090-ENSMUSP00000071623; -.
DR ProteomicsDB; 298387; -.
DR Pumba; Q5BLK4; -.
DR DNASU; 214290; -.
DR GeneID; 214290; -.
DR KEGG; mmu:214290; -.
DR UCSC; uc007qvf.1; mouse.
DR AGR; MGI:2387179; -.
DR CTD; 79670; -.
DR MGI; MGI:2387179; Tut7.
DR eggNOG; KOG2277; Eukaryota.
DR InParanoid; Q5BLK4; -.
DR OrthoDB; 170176at2759; -.
DR PhylomeDB; Q5BLK4; -.
DR BioGRID-ORCS; 214290; 2 hits in 76 CRISPR screens.
DR PRO; PR:Q5BLK4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q5BLK4; Protein.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR GO; GO:0050265; F:RNA uridylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0070569; F:uridylyltransferase activity; IMP:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0010586; P:miRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0001556; P:oocyte maturation; IMP:UniProtKB.
DR GO; GO:1990074; P:polyuridylation-dependent mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0031054; P:pre-miRNA processing; ISS:UniProtKB.
DR GO; GO:0141008; P:retrotransposon silencing by mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0071076; P:RNA 3' uridylation; IMP:UniProtKB.
DR GO; GO:0031123; P:RNA 3'-end processing; ISS:UniProtKB.
DR CDD; cd05402; NT_PAP_TUTase; 2.
DR Gene3D; 1.10.1410.10; -; 2.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 2.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR045100; TUTase_dom.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR12271; POLY A POLYMERASE CID PAP -RELATED; 1.
DR PANTHER; PTHR12271:SF34; TERMINAL URIDYLYLTRANSFERASE 7; 1.
DR Pfam; PF03828; PAP_assoc; 2.
DR Pfam; PF19088; TUTase; 2.
DR Pfam; PF16631; TUTF7_u4; 1.
DR Pfam; PF00098; zf-CCHC; 3.
DR SMART; SM00343; ZnF_C2HC; 3.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 2.
DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 2.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 3.
DR PROSITE; PS50158; ZF_CCHC; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Magnesium; Manganese; Metal-binding; Nucleotidyltransferase;
KW Phosphoprotein; Reference proteome; Repeat; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1491
FT /note="Terminal uridylyltransferase 7"
FT /id="PRO_0000150958"
FT DOMAIN 551..600
FT /note="PAP-associated 1"
FT DOMAIN 1230..1282
FT /note="PAP-associated 2"
FT ZN_FING 244..274
FT /note="Matrin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT ZN_FING 959..976
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 1341..1358
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 1447..1464
FT /note="CCHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 165..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..1491
FT /note="Sufficient for monouridylation activity"
FT /evidence="ECO:0000250|UniProtKB:Q5VYS8"
FT REGION 1362..1399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1463..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..862
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..887
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1467..1491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1043..1046
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q5VYS8"
FT BINDING 1053..1056
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q5VYS8"
FT BINDING 1054
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 1056
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 1126
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q5VYS8"
FT BINDING 1148
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q5VYS8"
FT BINDING 1166..1170
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q5VYS8"
FT BINDING 1282
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q5VYS8"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5VYS8"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VYS8"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 865
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 891
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 960
FT /note="V -> L (in Ref. 1; AAH23438)"
FT /evidence="ECO:0000305"
FT CONFLICT 982
FT /note="Q -> R (in Ref. 2; BAE20473)"
FT /evidence="ECO:0000305"
FT CONFLICT 1338
FT /note="P -> L (in Ref. 1; AAH43111)"
FT /evidence="ECO:0000305"
FT CONFLICT 1343
FT /note="C -> Y (in Ref. 2; BAE20473)"
FT /evidence="ECO:0000305"
FT CONFLICT 1472..1491
FT /note="LSSKYMTQGRASVKRTQQES -> AFT (in Ref. 1; AAH43111)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1491 AA; 169103 MW; C574FCAC3781B3CC CRC64;
MGDTAKPYFV KRTKDRGIID DDDFRRGHPQ QDYLIMDDYA KGHSSKMEKG LPKKKISPGN
YGNTPRKGLY GVSSNPYAFK NPIYSQPAWM NDNHKDQNKK WLSDELAGNA DSWREFKPGP
RIPVISRSRK ESFQESDDAY RWQEGRGCRA VRRLFQKDLS SLEAMSEMEA GSPENKKQRS
RPRKPRRTRT EDSEQDGDLD GPVIDESVLS TKELLGLQQA EERLKRDCID RLKRRPRNCP
TAKYTCKLCD ALIDSIPFAH KHIKEKRHKK NLKEKQEEEL LTTLPPPAPS QIHAVGSAID
RVVQEFGLHS ENLDQRLEIK RVMESVFRHK LPDCSLRLYG SSCSRLGFRD SDVNIDVQFP
AVMSQPDVLL LVQECLKNSD SFIDVDADFH ARVPVVVCRD KQSGLLCKVS AGNENAWLTT
KHLTALGKLE PRLVPLVIAF RYWAKLCSID RPEEGGLPPY VFALMAVFFL QQRKEPLLPV
YLGSWIEEFS LNKLGNFSLK DVEKDSVVWE YTDNSTGDTS SAKEEAPKET AAKKGQVPLT
FNIKHQPSVP VGQLWVELLR FYALEFNLAD LVISIRVKEL ISRESKDWPK KRIAIEDPYS
VKRNVARTLN NQPVFEYILH CLRTTYKYFA LPHKVTKPNL TKPPSPVTCV SDPYREAKNG
GPEPQATNID KLGNAAVAQD PGVQTSGDCR AQLVTLKNTT EEVGSPAKEK TGGVHIPAHQ
ESSGCVQAEV SCEGLEDATA ELPETGSDNE EVRRKTKHPL STDDQGLSSS KHPELQNCGS
LCGLQADNTL ELVAEECNSC ASLDNKAEVN EERIEGAEEL EEAAALSCFS PSVQSRTSAA
MHFDDEEEEE EEEEEEEPRL SINLTEDEEG VANEHQVDSR YAGSGEEDAL SEEDDLAEPA
KGEDTGECGE NVGGTLLIDL NRITLKEESF PEEDLPGDQS EFFYEFRKLT FTKGKSPTVV
CSLCKREGHL KKDCPEDFKR VQLEPLPPLT PKFSNILDQV CVQCYKDFSP TIVEDQAREH
IRQNLESFIK QDFPGTKLSL FGSSKNGFGF KQSDLDVCMT INGHETAEGL DCVRTIEELA
RVLRKHSGLR NILPITTAKV PIVKFFHLRS GLEVDISLYN TLALHNTRLL SAYSAIDPRV
KYLCYTMKVF TKMCDIGDAS RGSLSSYAYT LMVLYFLQQR SPPVIPVLQE IYKGEKKPEI
LVDGWNIYFF DQINELPTCW PEYGKNTEPV GQLWLGLLRF YTEEFDFKEH VISIRRKSLL
TTFKKQWTSK YIVIEDPFDL NHNLGAGLSR KMTNFIMKAF INGRRVFGIP VKGFPKDNPS
KLAYFFDPDV LTEGELAPND RCCRICGKIG HFMKDCPMRR KVRRRRDQED TPNQRYSESK
EKRSKEDKEI QNKYTEKEVS TKEDKLTPCA AAKAKPVRAA VDLGREKLLR TPTEKWKRQD
DRDSREKRCF ICGREGHIKK ECPQFKGSPG SLSSKYMTQG RASVKRTQQE S
//
