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Terminal uridylyltransferase 4 (TUTase 4) (EC 2.7.7.52) (Zinc finger CCHC domain-containing protein 11)

 TUT4_MOUSE              Reviewed;        1644 AA.
B2RX14; A2A8R8; Q3UYT6; Q5DU43;
22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
22-SEP-2009, sequence version 2.
05-DEC-2018, entry version 85.
RecName: Full=Terminal uridylyltransferase 4 {ECO:0000305};
Short=TUTase 4;
EC=2.7.7.52 {ECO:0000269|PubMed:19701194};
AltName: Full=Zinc finger CCHC domain-containing protein 11;
Name=Tut4 {ECO:0000312|MGI:MGI:2445126};
Synonyms=Kiaa0191, Zcchc11 {ECO:0000312|MGI:MGI:2445126};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-1644.
TISSUE=Brain;
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene.
The complete nucleotide sequences of mouse KIAA-homologous cDNAs
identified by screening of terminal sequences of cDNA clones randomly
sampled from size-fractionated libraries.";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 753-1644.
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
FUNCTION IN PRE-LET-7 URIDYLATION AND MAINTENANCE OF EMBRYONIC STEM
CELL PLURIPOTENCY, AND SUBCELLULAR LOCATION.
PubMed=19703396; DOI=10.1016/j.cell.2009.08.002;
Heo I., Joo C., Kim Y.-K., Ha M., Yoon M.-J., Cho J., Yeom K.-H.,
Han J., Kim V.N.;
"TUT4 in concert with Lin28 suppresses MicroRNA biogenesis through
pre-microRNA uridylation.";
Cell 138:696-708(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[7]
FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF
ASP-1026 AND ASP-1028.
PubMed=19701194; DOI=10.1038/ncb1931;
Jones M.R., Quinton L.J., Blahna M.T., Neilson J.R., Fu S.,
Ivanov A.R., Wolf D.A., Mizgerd J.P.;
"Zcchc11-dependent uridylation of microRNA directs cytokine
expression.";
Nat. Cell Biol. 11:1157-1163(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION IN PRE-LET-7 URIDYLATION, AND MUTAGENESIS OF CYS-326 AND
CYS-329.
PubMed=22898984; DOI=10.1261/rna.034538.112;
Thornton J.E., Chang H.M., Piskounova E., Gregory R.I.;
"Lin28-mediated control of let-7 microRNA expression by alternative
TUTases Zcchc11 (TUT4) and Zcchc6 (TUT7).";
RNA 18:1875-1885(2012).
[10]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1624, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[11]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-1026 AND
ASP-1028.
PubMed=28792939; DOI=10.1038/nature23318;
Morgan M., Much C., DiGiacomo M., Azzi C., Ivanova I., Vitsios D.M.,
Pistolic J., Collier P., Moreira P.N., Benes V., Enright A.J.,
O'Carroll D.;
"mRNA 3' uridylation and poly(A) tail length sculpt the mammalian
maternal transcriptome.";
Nature 548:347-351(2017).
[12]
FUNCTION, DOMAIN, INTERACTION WITH LIN28A, AND RNA-BINDING.
PubMed=28671666; DOI=10.1038/nsmb.3428;
Faehnle C.R., Walleshauser J., Joshua-Tor L.;
"Multi-domain utilization by TUT4 and TUT7 in control of let-7
biogenesis.";
Nat. Struct. Mol. Biol. 24:658-665(2017).
-!- FUNCTION: Uridylyltransferase that mediates the terminal
uridylation of mRNAs with short (less than 25 nucleotides) poly(A)
tails, hence facilitating global mRNA decay (PubMed:28792939).
Essential for both oocyte maturation and fertility. Through 3'
terminal uridylation of mRNA, sculpts, with TUT7, the maternal
transcriptome by eliminating transcripts during oocyte growth
(PubMed:28792939). Involved in microRNA (miRNA)-induced gene
silencing through uridylation of deadenylated miRNA targets. Also
functions as an integral regulator of microRNA biogenesiS using 3
different uridylation mechanisms (By similarity). Acts as a
suppressor of miRNA biogenesis by mediating the terminal
uridylation of some miRNA precursors, including that of let-7
(pre-let-7), miR107, miR-143 and miR-200c. Uridylated miRNAs are
not processed by Dicer and undergo degradation. Degradation of
pre-let-7 contributes to the maintenance of embryonic stem (ES)
cell pluripotency (By similarity). Also catalyzes the 3'
uridylation of miR-26A, a miRNA that targets IL6 transcript. This
abrogates the silencing of IL6 transcript, hence promoting
cytokine expression (PubMed:19703396). In the absence of LIN28A,
TUT7 and TUT4 monouridylate group II pre-miRNAs, which includes
most of pre-let7 members, that shapes an optimal 3' end overhang
for efficient processing (PubMed:28671666). Add oligo-U tails to
truncated pre-miRNAS with a 5' overhang which may promote rapid
degradation of non-functional pre-miRNA species (By similarity).
May also suppress Toll-like receptor-induced NF-kappa-B activation
via binding to T2BP (By similarity). Does not play a role in
replication-dependent histone mRNA degradation (By similarity).
Due to functional redundancy between TUT4 and TUT7, the
identification of the specific role of each of these proteins is
difficult (PubMed:28671666, PubMed:28792939, PubMed:22898984).
TUT4 and TUT7 restrict retrotransposition of long interspersed
element-1 (LINE-1) in cooperation with MOV10 counteracting the RNA
chaperonne activity of L1RE1. TUT7 uridylates LINE-1 mRNAs in the
cytoplasm which inhibits initiation of reverse transcription once
in the nucleus, whereas uridylation by TUT4 destabilizes mRNAs in
cytoplasmic ribonucleoprotein granules (By similarity).
{ECO:0000250|UniProtKB:Q5TAX3, ECO:0000269|PubMed:19703396,
ECO:0000269|PubMed:22898984, ECO:0000269|PubMed:28671666,
ECO:0000269|PubMed:28792939}.
-!- CATALYTIC ACTIVITY:
Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine
ribonucleotide; Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:11128,
Rhea:RHEA-COMP:14648, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
ChEBI:CHEBI:83400, ChEBI:CHEBI:140627; EC=2.7.7.52;
Evidence={ECO:0000269|PubMed:19701194};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- SUBUNIT: Interacts with LIN28A in the presence of pre-let-7 RNA
(PubMed:28671666). Interacts with T2BP. Interacts with MOV10; the
interaction is RNA-dependent. {ECO:0000250|UniProtKB:Q5TAX3}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5TAX3}.
Cytoplasm {ECO:0000269|PubMed:19703396}. Cytoplasm, Cytoplasmic
ribonucleoprotein granule {ECO:0000250|UniProtKB:Q5TAX3}.
Note=Mainly cytoplasmic (PubMed:19703396). Translocates into the
cytoplasm following treatment of the cell with LPS. Co-enriched in
cytoplasmic foci with MOV10. {ECO:0000250|UniProtKB:Q5TAX3,
ECO:0000269|PubMed:19703396}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:19701194}.
-!- DOMAIN: Utilizes two multidomain functional modules during the
switch from monouridylation to oligouridylation. The catalytic
module (containing the 3 CCHC-type Zinc finger domains) is
essential for both activites while the Lin28-interacting module
(LIM) at the N-termail part is indispensable for oligouridylation.
{ECO:0000269|PubMed:28671666}.
-!- DISRUPTION PHENOTYPE: Double conditional knockouts that have
deleted both TUT4 and TUT7 at the secondary oocyte stage are
infertile. Females ovulate normal numbers of oocytes with normal
morphology of antral follicles but with a slight decrease in the
frequency of surrounded nucleolus state oocytes. Mutant oocytes
are unable to support early embryonic development, they fail to
complete meiosis I properly. {ECO:0000269|PubMed:28792939}.
-!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAM23506.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAM25329.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AL626783; CAM23506.1; ALT_SEQ; Genomic_DNA.
EMBL; AL627238; CAM23506.1; JOINED; Genomic_DNA.
EMBL; AL627238; CAM25329.1; ALT_SEQ; Genomic_DNA.
EMBL; AL626783; CAM25329.1; JOINED; Genomic_DNA.
EMBL; BC150791; AAI50792.1; -; mRNA.
EMBL; AK220327; BAD90397.1; -; mRNA.
EMBL; AK134388; BAE22125.1; -; mRNA.
CCDS; CCDS18451.1; -.
RefSeq; NP_780681.2; NM_175472.3.
UniGene; Mm.25181; -.
UniGene; Mm.446602; -.
ProteinModelPortal; B2RX14; -.
SMR; B2RX14; -.
BioGrid; 230978; 1.
DIP; DIP-48571N; -.
IntAct; B2RX14; 1.
STRING; 10090.ENSMUSP00000044836; -.
iPTMnet; B2RX14; -.
PhosphoSitePlus; B2RX14; -.
EPD; B2RX14; -.
MaxQB; B2RX14; -.
PaxDb; B2RX14; -.
PRIDE; B2RX14; -.
Ensembl; ENSMUST00000043368; ENSMUSP00000044836; ENSMUSG00000034610.
GeneID; 230594; -.
KEGG; mmu:230594; -.
UCSC; uc008ubd.1; mouse.
CTD; 23318; -.
MGI; MGI:2445126; Tut4.
eggNOG; KOG2277; Eukaryota.
eggNOG; COG5260; LUCA.
GeneTree; ENSGT00940000156988; -.
HOGENOM; HOG000231134; -.
InParanoid; B2RX14; -.
KO; K13291; -.
OMA; AFRYWAR; -.
Reactome; R-MMU-429947; Deadenylation of mRNA.
ChiTaRS; Zcchc11; mouse.
PRO; PR:B2RX14; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000034610; Expressed in 240 organ(s), highest expression level in dorsal pancreas.
ExpressionAtlas; B2RX14; baseline and differential.
Genevisible; B2RX14; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
GO; GO:0050265; F:RNA uridylyltransferase activity; IDA:UniProtKB.
GO; GO:0070569; F:uridylyltransferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0001816; P:cytokine production; IDA:MGI.
GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0010587; P:miRNA catabolic process; ISS:UniProtKB.
GO; GO:0010586; P:miRNA metabolic process; IMP:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:MGI.
GO; GO:0010526; P:negative regulation of transposition, RNA-mediated; ISS:UniProtKB.
GO; GO:0001556; P:oocyte maturation; IMP:UniProtKB.
GO; GO:1990074; P:polyuridylation-dependent mRNA catabolic process; IMP:UniProtKB.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:UniProtKB.
GO; GO:0031054; P:pre-miRNA processing; ISS:UniProtKB.
GO; GO:0031664; P:regulation of lipopolysaccharide-mediated signaling pathway; IDA:MGI.
GO; GO:0071076; P:RNA 3' uridylation; IDA:UniProtKB.
GO; GO:0031123; P:RNA 3'-end processing; IDA:UniProtKB.
GO; GO:0019827; P:stem cell population maintenance; ISS:UniProtKB.
InterPro; IPR002058; PAP_assoc.
InterPro; IPR002934; Polymerase_NTP_transf_dom.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF01909; NTP_transf_2; 1.
Pfam; PF03828; PAP_assoc; 2.
Pfam; PF00098; zf-CCHC; 2.
SMART; SM00343; ZnF_C2HC; 3.
SUPFAM; SSF57756; SSF57756; 2.
PROSITE; PS50158; ZF_CCHC; 3.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Magnesium; Manganese; Metal-binding;
Methylation; Nucleotidyltransferase; Nucleus; Phosphoprotein;
Reference proteome; Repeat; RNA-mediated gene silencing; Transferase;
Zinc; Zinc-finger.
CHAIN 1 1644 Terminal uridylyltransferase 4.
/FTId=PRO_0000385330.
DOMAIN 649 698 PAP-associated 1.
DOMAIN 1201 1254 PAP-associated 2.
ZN_FING 324 354 Matrin-type. {ECO:0000255|PROSITE-
ProRule:PRU00130}.
ZN_FING 930 947 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 1310 1327 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 1358 1375 CCHC-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
REGION 918 1634 Sufficient for monouridylation activity.
{ECO:0000250|UniProtKB:Q5VYS8}.
REGION 1015 1018 UTP binding.
{ECO:0000250|UniProtKB:Q5VYS8}.
REGION 1025 1028 UTP binding.
{ECO:0000250|UniProtKB:Q5VYS8}.
REGION 1138 1142 UTP binding.
{ECO:0000250|UniProtKB:Q5VYS8}.
COMPBIAS 1425 1598 Pro-rich.
METAL 1026 1026 Magnesium or manganese; catalytic.
{ECO:0000250}.
METAL 1028 1028 Magnesium or manganese; catalytic.
{ECO:0000250}.
BINDING 1098 1098 UTP. {ECO:0000250|UniProtKB:Q5VYS8}.
BINDING 1120 1120 UTP. {ECO:0000250|UniProtKB:Q5VYS8}.
BINDING 1254 1254 UTP. {ECO:0000250|UniProtKB:Q5VYS8}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000250|UniProtKB:Q5TAX3}.
MOD_RES 131 131 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 176 176 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1624 1624 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MUTAGEN 326 326 C->A: No effect on basal uridylation
activity, but loss of LIN28A-enhanced
uridylation; when associated with A-329.
{ECO:0000269|PubMed:22898984}.
MUTAGEN 329 329 C->A: No effect on basal uridylation
activity, but loss of LIN28A-enhanced
uridylation; when associated with A-326.
{ECO:0000269|PubMed:22898984}.
MUTAGEN 1026 1026 D->A: Loss of nucleotidyltransferase
activity and oocytes are unable to
support early embryonic development; when
associated with A-1028.
{ECO:0000269|PubMed:19701194,
ECO:0000269|PubMed:28792939}.
MUTAGEN 1028 1028 D->A: Loss of nucleotidyltransferase
activity and oocytes are unable to
support early embryonic development; when
associated with A-1026.
{ECO:0000269|PubMed:19701194,
ECO:0000269|PubMed:28792939}.
CONFLICT 815 815 D -> A (in Ref. 2; AAI50792 and 3;
BAD90397). {ECO:0000305}.
CONFLICT 1336 1336 S -> R (in Ref. 4; BAE22125).
{ECO:0000305}.
CONFLICT 1422 1422 S -> C (in Ref. 4; BAE22125).
{ECO:0000305}.
SEQUENCE 1644 AA; 184650 MW; 5EE701412E6157A0 CRC64;
MEEPKTSKNE NHEPKKNIIC EESKAVKIIS NQTLKPRNDK SEIGTSSLNR NSSKKTKQND
ICIEKTEAKS CKVNAASVPG PKDLGLVHRD QSHCKMKKLP NSPMKAQKGS SQTKLEKTPS
LQTKAEKVPK SPNLPVKAEK APCTTAEATT EKALNSQRKE ENTPTSQMKL QKTPRSPLEP
ENVPSLLLKE NVKQTESQQT GKKLTSSFVS MDKRKSEALQ GEKSALENSS LSQKQQTQTD
NIADSDDSAS GIEDTADDLS KMKSEESNKE NSSEMDYLEN ATVIDESALT PEQRLGLKQA
EERLERDHIF RLEKRSPEYT NCRYLCKLCL IHIENIQGAH KHIKEKRHKK NILEKQEESE
LRSLPSPSSA HLAALSVAVV ELAKEQGITD DDLRIRQDIV EEMSKVIMTF LPECSLRLYG
SSLTKFALKS SDVNIDIKFP PKMNHPDLLI QVLGILKKSA LYIDVESDFH AKVPVVVCKD
RKSALLCRVS AGNDMACLTT DLLAALGKVE PVFTPLVLAF RYWAKLCYID SQTDGGIPSY
CFALMVMFFL QQRKPPLLPC LLGSWIEGFD PKRMDDFQLK GIVEEKFVKW EYNSSSATEK
NLIADENKAK ADEPKDDTKK TETDNQSNAA KAKHGKSPLT LEAPNQVPLG QLWLELLKFY
TLDFALEEYV ICVRIQDILT RENKNWPKRR IAIEDPFSVK RNVARSLNSQ LVYEYVVERF
RAAYRYFACP QKKGGNKSTM DPKKKEKGKL SSKKPVKSDC SATNCCILGE SAEKIHMERG
QPAKHDETEF TSQRCIVDND SLLVNELGLA NHGQDSSSLS TASGGSDLKQ KSAEKQGDLT
PSETSLKKEL SQCICIGTPD GAESAGTDCR SNLEMDSSHQ IVCNNVSATS CNCKATEVTS
DLVDEDNLPS QELYYVFDKF ILTSGKPPTI VCSICKKDGH SKNDCPEDFR KIDLKPLPPM
TNRFREILDL VCKRCFDELS PPCSEQHNRE QILIGLEKFI QKEYDEKARL CLFGSSKNGF
GFRDSDLDIC MTLEGHENAE KLNCKEIIEN LAKILKRHPG LRNILPITTA KVPIVKFEHR
RSGLEGDISL YNTLAQHNTR MLATYAAIDP RVQYLGYTMK VFAKRCDIGD ASRGSLSSYA
YILMVLYFLQ QRKPPVIPVL QEIFDGKQIP QRMVDGWNAF FFDKTEELKK RLPSLGKNTE
SLGELWLGLL RFYTEEFDFK EYVISIRQKK LLTTFEKQWT SKCIAIEDPF DLNHNLGAGV
SRKMTNFIMK AFINGRKLFG TPFYPLIGRE AEYFFDSRVL TDGELAPNDR CCRVCGKIGH
YMKDCPKRKR LKKKDSEEEK EGNEEEKDSR DLLDSRDLRC FICGDAGHVR RECPEVKMAR
QRNSSVAAAQ LVRNLVNAQQ VAGSAQQQSD QSIRTRQSSE CSDSPSYSPQ PQPFPQNSPQ
PSALPPPPSQ PGSQPKLGPP QQGGQPPHQV QMPLYNFPQS PPAHYSPMHS MGLLPMHPLQ
IPAPSWPIHG PMLHSAPGST PSNIGLNDPS IIFAQPAARP MAIPSPSHDG HWPRTVAPNS
LVNNGAVGNS EPRFRGLNPP IPWEHAPRHF PLVPASWPYG LHQNFMHQGN PRFQPKPFYA
QADRCATRRC RERCPHPPRG NVSE


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