QSER1_HUMAN
ID QSER1_HUMAN Reviewed; 1735 AA.
AC Q2KHR3; Q6ZU30; Q6ZUR5;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Glutamine and serine-rich protein 1;
GN Name=QSER1;
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 MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 82-1258 (ISOFORM 1), AND VARIANTS ILE-385 AND
RP SER-1018.
RC TISSUE=Brain, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1696 (ISOFORM 1), AND VARIANTS
RP ILE-385 AND SER-1018.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1239, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-949; SER-1230; SER-1231;
RP THR-1341 AND SER-1348, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1341, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1211; SER-1230; SER-1231;
RP THR-1341 AND SER-1348, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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-586; SER-615; SER-886 AND
RP SER-987, VARIANT [LARGE SCALE ANALYSIS] SER-1018, AND IDENTIFICATION BY
RP 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-1058 AND LYS-1083, AND
RP IDENTIFICATION BY MASS 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).
RN [15]
RP FUNCTION, INTERACTION WITH TET1, AND SUBCELLULAR LOCATION.
RX PubMed=33833093; DOI=10.1126/science.abd0875;
RA Dixon G., Pan H., Yang D., Rosen B.P., Jashari T., Verma N., Pulecio J.,
RA Caspi I., Lee K., Stransky S., Glezer A., Liu C., Rivas M., Kumar R.,
RA Lan Y., Torregroza I., He C., Sidoli S., Evans T., Elemento O., Huangfu D.;
RT "QSER1 protects DNA methylation valleys from de novo methylation.";
RL Science 372:0-0(2021).
CC -!- FUNCTION: Plays an essential role in the protection and maintenance of
CC transcriptional and developmental programs. Protects many bivalent
CC promoters and poised enhancers from hypermethylation, showing a marked
CC preference for these regulatory elements over other types of promoters
CC or enhancers. Mechanistically, cooperates with TET1 and binds to DNA in
CC a common complex to inhibit the binding of DNMT3A/3B and therefore de
CC novo methylation. {ECO:0000269|PubMed:33833093}.
CC -!- SUBUNIT: Interacts with TET1. {ECO:0000269|PubMed:33833093}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:33833093}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2KHR3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2KHR3-2; Sequence=VSP_039815, VSP_039816;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI12936.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAC86397.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK125391; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK126023; BAC86397.1; ALT_SEQ; mRNA.
DR EMBL; AC107939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC112935; AAI12936.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001070254.1; NM_001076786.2.
DR AlphaFoldDB; Q2KHR3; -.
DR BioGRID; 122924; 83.
DR IntAct; Q2KHR3; 48.
DR MINT; Q2KHR3; -.
DR STRING; 9606.ENSP00000382241; -.
DR GlyConnect; 2855; 1 O-Linked glycan (2 sites).
DR GlyGen; Q2KHR3; 10 sites, 1 O-linked glycan (10 sites).
DR iPTMnet; Q2KHR3; -.
DR PhosphoSitePlus; Q2KHR3; -.
DR BioMuta; QSER1; -.
DR DMDM; 308153569; -.
DR EPD; Q2KHR3; -.
DR jPOST; Q2KHR3; -.
DR MassIVE; Q2KHR3; -.
DR MaxQB; Q2KHR3; -.
DR PaxDb; Q2KHR3; -.
DR PeptideAtlas; Q2KHR3; -.
DR PRIDE; Q2KHR3; -.
DR ProteomicsDB; 61307; -. [Q2KHR3-1]
DR ProteomicsDB; 61308; -. [Q2KHR3-2]
DR Antibodypedia; 1555; 74 antibodies from 20 providers.
DR DNASU; 79832; -.
DR Ensembl; ENST00000399302.7; ENSP00000382241.2; ENSG00000060749.16. [Q2KHR3-1]
DR GeneID; 79832; -.
DR KEGG; hsa:79832; -.
DR UCSC; uc001mty.4; human. [Q2KHR3-1]
DR CTD; 79832; -.
DR DisGeNET; 79832; -.
DR GeneCards; QSER1; -.
DR HGNC; HGNC:26154; QSER1.
DR HPA; ENSG00000060749; Low tissue specificity.
DR MIM; 619440; gene.
DR neXtProt; NX_Q2KHR3; -.
DR OpenTargets; ENSG00000060749; -.
DR PharmGKB; PA143485589; -.
DR VEuPathDB; HostDB:ENSG00000060749; -.
DR eggNOG; KOG4805; Eukaryota.
DR GeneTree; ENSGT00440000037417; -.
DR HOGENOM; CLU_000708_2_0_1; -.
DR InParanoid; Q2KHR3; -.
DR OrthoDB; 64109at2759; -.
DR PhylomeDB; Q2KHR3; -.
DR TreeFam; TF333141; -.
DR PathwayCommons; Q2KHR3; -.
DR SignaLink; Q2KHR3; -.
DR BioGRID-ORCS; 79832; 9 hits in 1081 CRISPR screens.
DR ChiTaRS; QSER1; human.
DR GenomeRNAi; 79832; -.
DR Pharos; Q2KHR3; Tdark.
DR PRO; PR:Q2KHR3; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q2KHR3; protein.
DR Bgee; ENSG00000060749; Expressed in caput epididymis and 190 other tissues.
DR ExpressionAtlas; Q2KHR3; baseline and differential.
DR Genevisible; Q2KHR3; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR InterPro; IPR025451; DUF4211.
DR Pfam; PF13926; DUF4211; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromosome; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..1735
FT /note="Glutamine and serine-rich protein 1"
FT /id="PRO_0000288933"
FT REGION 267..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1256..1286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1441..1532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1091
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1446..1483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 886
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 949
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 987
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 1231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 1239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 1341
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT MOD_RES 1348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT CROSSLNK 1058
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1083
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 243..481
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039815"
FT VAR_SEQ 1730..1735
FT /note="VQQKCS -> TGMLGEMQSVSVSSTRRSEQQNILEAGKSKIKVPVSGDC
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039816"
FT VARIANT 385
FT /note="V -> I (in dbSNP:rs1022586)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_056975"
FT VARIANT 644
FT /note="Q -> R (in dbSNP:rs2297781)"
FT /id="VAR_032535"
FT VARIANT 1018
FT /note="N -> S (in dbSNP:rs7940077)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0007744|PubMed:23186163"
FT /id="VAR_032536"
FT VARIANT 1304
FT /note="N -> D (in dbSNP:rs16923676)"
FT /id="VAR_032537"
FT CONFLICT 291
FT /note="S -> P (in Ref. 1; AK125391)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="D -> N (in Ref. 1; AK125391)"
FT /evidence="ECO:0000305"
FT CONFLICT 1075
FT /note="R -> G (in Ref. 1; AK125391)"
FT /evidence="ECO:0000305"
FT CONFLICT 1247
FT /note="S -> P (in Ref. 1; AK125391)"
FT /evidence="ECO:0000305"
FT CONFLICT 1258
FT /note="D -> E (in Ref. 1; AK125391)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1735 AA; 189972 MW; 9FC28818DBB42A92 CRC64;
MNFLSTAESR TAQAAASGTT LLPQFRAPSW QTGMHSSAAT ELFATGPLPS TGTLPPSLSA
YQHPTTFSNR NFATTSPLVL QDSTFNTTSN GILSHHDPLL QIKTSQGTVP TALAFERLGS
SVLSNSIPPQ SSTYRSAQES APHLLQPQFS LLPSALGGSQ QTPQAYSSTL FTSSTASIER
ALLRECSVIK HHQRPSGTQS IQAQLTGSQH SLHSYLSNSS VVNFQETTRQ SSLSCSPIGD
STQVSNGGLQ QKTSQVSVEL AQSYSSAIPS SGYPPSTTKI KSCSTEQPLT STKTPKPQSI
IPPVQTLSYS KPLHNQSSVI SGQAQIYSTA QLPSLLSVSQ SQNYGLVQPH NVPSIVHSQV
YRSSKVEKLP PLYKTLTFSG SSQTVTPENQ TLNYSSNQQE VLSSVTNENY PAQTRDLSSV
SQSQSYSSGH SQGLSPVSQT QVSYSSQSQV LSVVSLSESY ASGESLTLTA PSLSYSSASR
AQNLPDSSPT QNYISMHSSQ NVQTQESSSP QSQKFLPAVQ SSSFASSTHC QTLQNNITSP
DPKSYAERKL DSDVYPSSKQ EDGFPMQELQ VLQPQASLES STQRLSDGEI NAQESTYKVS
KADDRYSQSV IRSNSRLEDQ VIGVALQASK KEESVVGSVT QLNQQIGQVN NAATLDLKNS
TNLIQTPQIR LNTKDLKQQH PLILKVHESK VQEQHDQIIN ASSQIQIPNH ALGHGHQASL
PNTQVLLDSA CDLQILQQSI LQAGLGQVKA SLQAQRVQSP QQIVHPFLQM EGHVIQSNGD
HSQQQLHPQN SEVMKMDLSE SSKPLQQHLT TKGHFSETNQ HDSKNQFVSL GSMCFPEAVL
LSDERNILSN VDDILAATAA ACGVTPTDFS KSTSNETMQA VEDGDSKSHF QQSLDVRHVT
SDFNSMTATV GKPQNINDTS LNGNQVTVNL SPVPALQSKM TLDQQHIETP GQNIPTKVTS
AVVGPSHEVQ EQSSGPFKKQ SATNLESEED SEAPVDSTLN NNRNQEFVSS SRSISGENAT
SESEFTLGGD DSGVSMNPAR SALALLAMAQ SGDAVSVKIE EENQDLMHFN LQKKRAKGKG
QVKEEDNSNQ KQLKRPAQGK RQNPRGTDIY LPYTPPSSES CHDGYQHQEK MRQKIKEVEE
KQPEVKTGFI ASFLDFLKSG PKQQFSTLAV RMPNRTRRPG TQMVRTFCPP PLPKPSSTTP
TPLVSETGGN SPSDKVDNEL KNLEHLSSFS SDEDDPGYSQ DAYKSVSTPL TTLDATSDKK
KKTEALQVAT TSPTANTTGT ATTSSTTVGA VKQEPLHSTS YAVNILENIS SSESSKPIEL
DGLPSDQFAK GQDTVAIEGF TDEEDTESGG EGQYRERDEF VVKIEDIETF KEALKTGKEP
PAIWKVQKAL LQKFVPEIRD GQREFAATNS YLGYFGDAKS KYKRIYVKFI ENANKKEYVR
VCSKKPRNKP SQTIRTVQAK PSSSSKTSDP LASKTTTTKA PSVKPKVKQP KVKAEPPPKK
RKKWKEEFSS SQSDSSPEIH TSSSDDEEFE PPAPFVTRFL NTRAMKETFK SYMELLVSIA
LDPDTMQALE KSNDELLLPH MKKIDGMLND NRKRLLLNLH LDQSFKNALE SFPELTIITR
DSKAKSGGTA ISKIKMNGKA YNKKTLRTSK TTTKSAQEFA VDPEKIQLYS LYHSLHHYKY
HVYLICKDEI SSVQKKNEDL GQEEIVQLCM KNVKWVEDLF EKFGELLNHV QQKCS
