RTF1_HUMAN
ID RTF1_HUMAN Reviewed; 710 AA.
AC Q92541; Q96BX6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 4.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=RNA polymerase-associated protein RTF1 homolog;
GN Name=RTF1; Synonyms=KIAA0252;
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 GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-710.
RC TISSUE=Brain;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-710.
RC TISSUE=Uterus;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-697, AND IDENTIFICATION BY
RP 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 [7]
RP FUNCTION.
RX PubMed=19345177; DOI=10.1016/j.stem.2009.03.009;
RA Ding L., Paszkowski-Rogacz M., Nitzsche A., Slabicki M.M., Heninger A.K.,
RA de Vries I., Kittler R., Junqueira M., Shevchenko A., Schulz H., Hubner N.,
RA Doss M.X., Sachinidis A., Hescheler J., Iacone R., Anastassiadis K.,
RA Stewart A.F., Pisabarro M.T., Caldarelli A., Poser I., Theis M.,
RA Buchholz F.;
RT "A genome-scale RNAi screen for Oct4 modulators defines a role of the Paf1
RT complex for embryonic stem cell identity.";
RL Cell Stem Cell 4:403-415(2009).
RN [8]
RP IDENTIFICATION IN THE PAF1 COMPLEX, COMPOSITION OF THE PAF1 COMPLEX, AND
RP FUNCTION OF THE PAF1 COMPLEX.
RX PubMed=20178742; DOI=10.1016/j.cell.2009.12.050;
RA Kim J., Guermah M., Roeder R.G.;
RT "The human PAF1 complex acts in chromatin transcription elongation both
RT independently and cooperatively with SII/TFIIS.";
RL Cell 140:491-503(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-650 AND SER-697, AND
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53 AND THR-55, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626; SER-650; SER-655 AND
RP SER-697, AND 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 [13]
RP STRUCTURE BY NMR OF 347-482.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the plus-3 domain of human KIAA0252 protein.";
RL Submitted (JUN-2006) to the PDB data bank.
RN [14]
RP STRUCTURE BY NMR OF 353-484, DOMAIN PLUS3, DNA-BINDING, AND MUTAGENESIS OF
RP ARG-401; GLU-410; ARG-429; GLN-434 AND ARG-435.
RX PubMed=18184592; DOI=10.1016/j.str.2007.10.018;
RA de Jong R.N., Truffault V., Diercks T., Ab E., Daniels M.A., Kaptein R.,
RA Folkers G.E.;
RT "Structure and DNA binding of the human Rtf1 Plus3 domain.";
RL Structure 16:149-159(2008).
CC -!- FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple
CC functions during transcription by RNA polymerase II and is implicated
CC in regulation of development and maintenance of embryonic stem cell
CC pluripotency. PAF1C associates with RNA polymerase II through
CC interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-
CC 5'-phosphorylated forms and is involved in transcriptional elongation,
CC acting both independently and synergistically with TCEA1 and in
CC cooperation with the DSIF complex and HTATSF1. PAF1C is required for
CC transcription of Hox and Wnt target genes. PAF1C is involved in
CC hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it
CC promotes leukemogenesis through association with KMT2A/MLL1-rearranged
CC oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL.
CC PAF1C is involved in histone modifications such as ubiquitination of
CC histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C
CC recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2
CC enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of
CC 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B
CC ubiquitination is proposed to be coupled to transcription. PAF1C is
CC involved in mRNA 3' end formation probably through association with
CC cleavage and poly(A) factors. In case of infection by influenza A
CC strain H3N2, PAF1C associates with viral NS1 protein, thereby
CC regulating gene transcription. Binds single-stranded DNA. Required for
CC maximal induction of heat-shock genes. Required for the trimethylation
CC of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell
CC pluripotency; this function is synergistic with CXXC1 indicative for an
CC involvement of a SET1 complex (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:19345177, ECO:0000269|PubMed:20178742}.
CC -!- SUBUNIT: Component of the PAF1 complex, which consists of CDC73, PAF1,
CC LEO1, CTR9, RTF1 and WDR61; the association of RTF1 appears to be less
CC stable than that of other subunits. At least in HeLa cells a N-terminal
CC shorter form of RTF1 is also found in the complex (PubMed:20178742).
CC The PAF1 complex interacts with PHF5A (By similarity).
CC {ECO:0000250|UniProtKB:A2AQ19, ECO:0000269|PubMed:20178742}.
CC -!- INTERACTION:
CC Q92541; Q6P1J9: CDC73; NbExp=12; IntAct=EBI-1055239, EBI-930143;
CC Q92541; Q8N7H5: PAF1; NbExp=17; IntAct=EBI-1055239, EBI-2607770;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}.
CC -!- DOMAIN: The Plus3 domain mediates single-stranded DNA-binding.
CC {ECO:0000269|PubMed:18184592}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-41 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH15052.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA13382.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC087721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D87440; BAA13382.2; ALT_INIT; mRNA.
DR EMBL; BC015052; AAH15052.1; ALT_INIT; mRNA.
DR CCDS; CCDS32200.2; -.
DR RefSeq; NP_055953.3; NM_015138.4.
DR PDB; 2BZE; NMR; -; A=353-484.
DR PDB; 2DB9; NMR; -; A=347-482.
DR PDB; 3U1U; X-ray; 1.80 A; A/B=347-482.
DR PDB; 4L1P; X-ray; 2.12 A; A/B=353-484.
DR PDB; 4L1U; X-ray; 2.42 A; A/B/C/D/E/F=353-484.
DR PDB; 6TED; EM; 3.10 A; R=1-710.
DR PDBsum; 2BZE; -.
DR PDBsum; 2DB9; -.
DR PDBsum; 3U1U; -.
DR PDBsum; 4L1P; -.
DR PDBsum; 4L1U; -.
DR PDBsum; 6TED; -.
DR AlphaFoldDB; Q92541; -.
DR BMRB; Q92541; -.
DR SMR; Q92541; -.
DR BioGRID; 116780; 140.
DR IntAct; Q92541; 26.
DR MINT; Q92541; -.
DR STRING; 9606.ENSP00000374280; -.
DR GlyGen; Q92541; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q92541; -.
DR MetOSite; Q92541; -.
DR PhosphoSitePlus; Q92541; -.
DR BioMuta; RTF1; -.
DR DMDM; 313104316; -.
DR EPD; Q92541; -.
DR jPOST; Q92541; -.
DR MassIVE; Q92541; -.
DR MaxQB; Q92541; -.
DR PaxDb; Q92541; -.
DR PeptideAtlas; Q92541; -.
DR PRIDE; Q92541; -.
DR ProteomicsDB; 75301; -.
DR Antibodypedia; 1858; 235 antibodies from 27 providers.
DR CPTC; Q92541; 2 antibodies.
DR DNASU; 23168; -.
DR Ensembl; ENST00000389629.9; ENSP00000374280.4; ENSG00000137815.15.
DR GeneID; 23168; -.
DR KEGG; hsa:23168; -.
DR MANE-Select; ENST00000389629.9; ENSP00000374280.4; NM_015138.5; NP_055953.3.
DR UCSC; uc001zny.3; human.
DR CTD; 23168; -.
DR DisGeNET; 23168; -.
DR GeneCards; RTF1; -.
DR HGNC; HGNC:28996; RTF1.
DR HPA; ENSG00000137815; Low tissue specificity.
DR MIM; 611633; gene.
DR neXtProt; NX_Q92541; -.
DR OpenTargets; ENSG00000137815; -.
DR PharmGKB; PA134961778; -.
DR VEuPathDB; HostDB:ENSG00000137815; -.
DR eggNOG; KOG2402; Eukaryota.
DR GeneTree; ENSGT00390000012493; -.
DR HOGENOM; CLU_018644_0_1_1; -.
DR InParanoid; Q92541; -.
DR OMA; SGCKSAV; -.
DR OrthoDB; 607093at2759; -.
DR PhylomeDB; Q92541; -.
DR TreeFam; TF321360; -.
DR PathwayCommons; Q92541; -.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR SignaLink; Q92541; -.
DR BioGRID-ORCS; 23168; 595 hits in 1088 CRISPR screens.
DR ChiTaRS; RTF1; human.
DR EvolutionaryTrace; Q92541; -.
DR GeneWiki; RTF1; -.
DR GenomeRNAi; 23168; -.
DR Pharos; Q92541; Tbio.
DR PRO; PR:Q92541; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q92541; protein.
DR Bgee; ENSG00000137815; Expressed in cortical plate and 213 other tissues.
DR ExpressionAtlas; Q92541; baseline and differential.
DR Genevisible; Q92541; HS.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:1990269; F:RNA polymerase II C-terminal domain phosphoserine binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0001832; P:blastocyst growth; IEA:Ensembl.
DR GO; GO:0001711; P:endodermal cell fate commitment; ISS:UniProtKB.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IEA:Ensembl.
DR GO; GO:0019827; P:stem cell population maintenance; IDA:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 3.90.70.200; -; 1.
DR InterPro; IPR004343; Plus-3_dom.
DR InterPro; IPR036128; Plus3-like_sf.
DR Pfam; PF03126; Plus-3; 1.
DR SMART; SM00719; Plus3; 1.
DR SUPFAM; SSF159042; SSF159042; 1.
DR PROSITE; PS51360; PLUS3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Coiled coil; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Wnt signaling pathway.
FT CHAIN 1..710
FT /note="RNA polymerase-associated protein RTF1 homolog"
FT /id="PRO_0000255936"
FT DOMAIN 353..484
FT /note="Plus3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00693"
FT REGION 20..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 526..560
FT /evidence="ECO:0000255"
FT COMPBIAS 67..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..125
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..185
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 55
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MUTAGEN 401
FT /note="R->E: Loss of binding to single-stranded DNA."
FT /evidence="ECO:0000269|PubMed:18184592"
FT MUTAGEN 410
FT /note="E->K: Reduced binding to single-stranded DNA."
FT /evidence="ECO:0000269|PubMed:18184592"
FT MUTAGEN 429
FT /note="R->E: Loss of binding to single-stranded DNA."
FT /evidence="ECO:0000269|PubMed:18184592"
FT MUTAGEN 434
FT /note="Q->A: Reduced binding to single-stranded DNA."
FT /evidence="ECO:0000269|PubMed:18184592"
FT MUTAGEN 435
FT /note="R->E: Loss of binding to single-stranded DNA."
FT /evidence="ECO:0000269|PubMed:18184592"
FT HELIX 356..360
FT /evidence="ECO:0007829|PDB:3U1U"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:6TED"
FT HELIX 366..372
FT /evidence="ECO:0007829|PDB:3U1U"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:2BZE"
FT HELIX 378..382
FT /evidence="ECO:0007829|PDB:3U1U"
FT STRAND 386..392
FT /evidence="ECO:0007829|PDB:3U1U"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:2BZE"
FT STRAND 399..417
FT /evidence="ECO:0007829|PDB:3U1U"
FT STRAND 420..430
FT /evidence="ECO:0007829|PDB:3U1U"
FT STRAND 433..438
FT /evidence="ECO:0007829|PDB:3U1U"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:3U1U"
FT HELIX 449..462
FT /evidence="ECO:0007829|PDB:3U1U"
FT HELIX 469..478
FT /evidence="ECO:0007829|PDB:3U1U"
FT HELIX 491..502
FT /evidence="ECO:0007829|PDB:6TED"
FT STRAND 505..508
FT /evidence="ECO:0007829|PDB:6TED"
FT HELIX 511..523
FT /evidence="ECO:0007829|PDB:6TED"
FT HELIX 528..552
FT /evidence="ECO:0007829|PDB:6TED"
FT TURN 553..557
FT /evidence="ECO:0007829|PDB:6TED"
FT HELIX 558..584
FT /evidence="ECO:0007829|PDB:6TED"
SQ SEQUENCE 710 AA; 80313 MW; 54CC014655AA22B8 CRC64;
MRGRLCVGRA AAAAAAVAVP LAGGQEGSPG GGRRGSRGTT MVKKRKGRVV IDSDTEDSGS
DENLDQELLS LAKRKRSDSE EKEPPVSQPA ASSDSETSDS DDEWTFGSNK NKKKGKARKI
EKKGTMKKQA NKTASSGSSD KDSSAESSAP EEGEVSDSDS NSSSSSSDSD SSSEDEEFHD
GYGEDLMGDE EDRARLEQMT EKEREQELFN RIEKREVLKR RFEIKKKLKT AKKKEKKEKK
KKQEEEQEKK KLTQIQESQV TSHNKERRSK RDEKLDKKSQ AMEELKAERE KRKNRTAELL
AKKQPLKTSE VYSDDEEEEE DDKSSEKSDR SSRTSSSDEE EEKEEIPPKS QPVSLPEELN
RVRLSRHKLE RWCHMPFFAK TVTGCFVRIG IGNHNSKPVY RVAEITGVVE TAKVYQLGGT
RTNKGLQLRH GNDQRVFRLE FVSNQEFTES EFMKWKEAMF SAGMQLPTLD EINKKELSIK
EALNYKFNDQ DIEEIVKEKE RFRKAPPNYA MKKTQLLKEK AMAEDLGDQD KAKQIQDQLN
ELEERAEALD RQRTKNISAI SYINQRNREW NIVESEKALV AESHNMKNQQ MDPFTRRQCK
PTIVSNSRDP AVQAAILAQL NAKYGSGVLP DAPKEMSKGQ GKDKDLNSKS ASDLSEDLFK
VHDFDVKIDL QVPSSESKAL AITSKAPPAK DGAPRRSLNL EDYKKRRGLI
