ID REXO4_HUMAN Reviewed; 422 AA. AC Q9GZR2; B2RAT2; Q5T8S4; Q5T8S5; Q5T8S6; Q9GZW3; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 2. DT 27-MAR-2024, entry version 180. DE RecName: Full=RNA exonuclease 4; DE EC=3.1.-.-; DE AltName: Full=Exonuclease XPMC2; DE AltName: Full=Prevents mitotic catastrophe 2 protein homolog; DE Short=hPMC2; GN Name=REXO4; Synonyms=PMC2, XPMC2H; 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 [MRNA] (ISOFORM 1), AND VARIANT ALA-283. RX PubMed=9325058; DOI=10.1006/geno.1997.4874; RA Kwiatkowska J., Slomski R., Jozwiak S., Short M.P., Kwiatkowski D.J.; RT "Human XPMC2H: cDNA cloning, mapping to 9q34, genomic structure, and RT evaluation as TSC1."; RL Genomics 44:350-354(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND RP INTERACTION WITH ESR1 AND ESR2. RX PubMed=10908561; DOI=10.1074/jbc.m003880200; RA Montano M.M., Wittmann B.M., Bianco N.R.; RT "Identification and characterization of a novel factor that regulates RT quinone reductase gene transcriptional activity."; RL J. Biol. Chem. 275:34306-34313(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 2). RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [8] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271; RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., RA Greco A., Hochstrasser D.F., Diaz J.-J.; RT "Functional proteomic analysis of human nucleolus."; RL Mol. Biol. Cell 13:4100-4109(2002). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, 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 [10] 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 [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-96 AND SER-111, AND RP 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [14] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-115, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). CC -!- SUBUNIT: Can bind ESR1 and ESR2. This interaction is abrogated by CC estrogen and augmented by tamoxifen treatment. CC -!- INTERACTION: CC Q9GZR2; P50570-2: DNM2; NbExp=3; IntAct=EBI-2856313, EBI-10968534; CC Q9GZR2; O75031: HSF2BP; NbExp=3; IntAct=EBI-2856313, EBI-7116203; CC Q9GZR2; P42858: HTT; NbExp=3; IntAct=EBI-2856313, EBI-466029; CC Q9GZR2; P29474: NOS3; NbExp=3; IntAct=EBI-2856313, EBI-1391623; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10908561, CC ECO:0000269|PubMed:12429849}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9GZR2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9GZR2-2; Sequence=VSP_014796, VSP_014797; CC -!- SIMILARITY: Belongs to the REXO4 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAI12845.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAI12847.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAI12848.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF295774; AAG02123.1; -; mRNA. DR EMBL; AF273304; AAF98162.1; -; mRNA. DR EMBL; AL136894; CAB66828.1; -; mRNA. DR EMBL; AK025493; BAB15152.1; -; mRNA. DR EMBL; AK314333; BAG36979.1; -; mRNA. DR EMBL; AL158826; CAI12845.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL158826; CAI12847.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL158826; CAI12848.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL158826; CAI12849.1; -; Genomic_DNA. DR EMBL; CH471090; EAW88082.1; -; Genomic_DNA. DR EMBL; BC009274; AAH09274.1; -; mRNA. DR CCDS; CCDS65179.1; -. [Q9GZR2-2] DR CCDS; CCDS6969.1; -. [Q9GZR2-1] DR RefSeq; NP_001266278.1; NM_001279349.1. [Q9GZR2-2] DR RefSeq; NP_001266279.1; NM_001279350.1. DR RefSeq; NP_001266280.1; NM_001279351.1. DR RefSeq; NP_065118.2; NM_020385.3. [Q9GZR2-1] DR AlphaFoldDB; Q9GZR2; -. DR SMR; Q9GZR2; -. DR BioGRID; 121375; 261. DR IntAct; Q9GZR2; 55. DR MINT; Q9GZR2; -. DR STRING; 9606.ENSP00000361010; -. DR GlyGen; Q9GZR2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9GZR2; -. DR PhosphoSitePlus; Q9GZR2; -. DR SwissPalm; Q9GZR2; -. DR BioMuta; REXO4; -. DR DMDM; 71153418; -. DR EPD; Q9GZR2; -. DR jPOST; Q9GZR2; -. DR MassIVE; Q9GZR2; -. DR MaxQB; Q9GZR2; -. DR PaxDb; 9606-ENSP00000361010; -. DR PeptideAtlas; Q9GZR2; -. DR ProteomicsDB; 80118; -. [Q9GZR2-1] DR ProteomicsDB; 80119; -. [Q9GZR2-2] DR Pumba; Q9GZR2; -. DR Antibodypedia; 18377; 144 antibodies from 25 providers. DR DNASU; 57109; -. DR Ensembl; ENST00000371935.6; ENSP00000361003.2; ENSG00000148300.12. [Q9GZR2-2] DR Ensembl; ENST00000371942.8; ENSP00000361010.3; ENSG00000148300.12. [Q9GZR2-1] DR Ensembl; ENST00000628678.2; ENSP00000487504.1; ENSG00000280706.3. [Q9GZR2-2] DR Ensembl; ENST00000630460.3; ENSP00000486065.1; ENSG00000280706.3. [Q9GZR2-1] DR GeneID; 57109; -. DR KEGG; hsa:57109; -. DR MANE-Select; ENST00000371942.8; ENSP00000361010.3; NM_020385.4; NP_065118.2. DR UCSC; uc004cdm.5; human. [Q9GZR2-1] DR AGR; HGNC:12820; -. DR CTD; 57109; -. DR DisGeNET; 57109; -. DR GeneCards; REXO4; -. DR HGNC; HGNC:12820; REXO4. DR HPA; ENSG00000148300; Low tissue specificity. DR MIM; 602930; gene. DR neXtProt; NX_Q9GZR2; -. DR OpenTargets; ENSG00000148300; -. DR PharmGKB; PA37414; -. DR VEuPathDB; HostDB:ENSG00000148300; -. DR eggNOG; KOG2249; Eukaryota. DR GeneTree; ENSGT00940000159607; -. DR HOGENOM; CLU_1111086_0_0_1; -. DR InParanoid; Q9GZR2; -. DR OMA; YIKPTEP; -. DR OrthoDB; 5479236at2759; -. DR PhylomeDB; Q9GZR2; -. DR TreeFam; TF313504; -. DR PathwayCommons; Q9GZR2; -. DR SignaLink; Q9GZR2; -. DR BioGRID-ORCS; 57109; 8 hits in 1162 CRISPR screens. DR ChiTaRS; REXO4; human. DR GeneWiki; REXO4; -. DR GenomeRNAi; 57109; -. DR Pharos; Q9GZR2; Tbio. DR PRO; PR:Q9GZR2; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q9GZR2; Protein. DR Bgee; ENSG00000148300; Expressed in sural nerve and 100 other cell types or tissues. DR ExpressionAtlas; Q9GZR2; baseline and differential. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IDA:LIFEdb. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0008408; F:3'-5' exonuclease activity; IDA:ARUK-UCL. DR GO; GO:0003690; F:double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0004519; F:endonuclease activity; IDA:ARUK-UCL. DR GO; GO:0004527; F:exonuclease activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003697; F:single-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0006308; P:DNA catabolic process; IDA:ARUK-UCL. DR GO; GO:0006281; P:DNA repair; IDA:ARUK-UCL. DR GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:UniProtKB. DR GO; GO:0006364; P:rRNA processing; IEA:InterPro. DR CDD; cd06144; REX4_like; 1. DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1. DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3. DR InterPro; IPR037431; REX4_DEDDh_dom. DR InterPro; IPR047021; REXO1/3/4-like. DR InterPro; IPR012337; RNaseH-like_sf. DR InterPro; IPR036397; RNaseH_sf. DR PANTHER; PTHR12801:SF130; RNA EXONUCLEASE 4; 1. DR PANTHER; PTHR12801; RNA EXONUCLEASE REXO1 / RECO3 FAMILY MEMBER-RELATED; 1. DR Pfam; PF00929; RNase_T; 1. DR SMART; SM00479; EXOIII; 1. DR SUPFAM; SSF53098; Ribonuclease H-like; 1. DR SWISS-2DPAGE; Q9GZR2; -. DR Genevisible; Q9GZR2; HS. PE 1: Evidence at protein level; KW Alternative splicing; Exonuclease; Hydrolase; Isopeptide bond; Nuclease; KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation. FT CHAIN 1..422 FT /note="RNA exonuclease 4" FT /id="PRO_0000131703" FT DOMAIN 243..394 FT /note="Exonuclease" FT REGION 1..194 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 25..42 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 141..187 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 15 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 96 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 111 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 115 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 76..132 FT /note="WLLKQKSQAPEKPLVISQMGSKKKPKIIQQNKKETSPQVKGEEMPAGKDQEA FT SRGSV -> VPRWTGGRQYLAPRPVEQSTIRKEPRKGQMVILFQNEGTSSIRSGKLRRQ FT PQPHPPR (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_014796" FT VAR_SEQ 133..304 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_014797" FT VARIANT 141 FT /note="R -> K (in dbSNP:rs6597630)" FT /id="VAR_023067" FT VARIANT 283 FT /note="T -> A (in dbSNP:rs2285487)" FT /evidence="ECO:0000269|PubMed:9325058" FT /id="VAR_023068" FT CONFLICT 202 FT /note="A -> P (in Ref. 1 and 2)" FT /evidence="ECO:0000305" SQ SEQUENCE 422 AA; 46672 MW; 5994D59678B17C21 CRC64; MGKAKVPASK RAPSSPVAKP GPVKTLTRKK NKKKKRFWKS KAREVSKKPA SGPGAVVRPP KAPEDFSQNW KALQEWLLKQ KSQAPEKPLV ISQMGSKKKP KIIQQNKKET SPQVKGEEMP AGKDQEASRG SVPSGSKMDR RAPVPRTKAS GTEHNKKGTK ERTNGDIVPE RGDIEHKKRK AKEAAPAPPT EEDIWFDDVD PADIEAAIGP EAAKIARKQL GQSEGSVSLS LVKEQAFGGL TRALALDCEM VGVGPKGEES MAARVSIVNQ YGKCVYDKYV KPTEPVTDYR TAVSGIRPEN LKQGEELEVV QKEVAEMLKG RILVGHALHN DLKVLFLDHP KKKIRDTQKY KPFKSQVKSG RPSLRLLSEK ILGLQVQQAE HCSIQDAQAA MRLYVMVKKE WESMARDRRP LLTAPDHCSD DA //