SART3_MOUSE
ID SART3_MOUSE Reviewed; 962 AA.
AC Q9JLI8; Q6ZQI2; Q8BPK9; Q8C3B7; Q8CFU9;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Squamous cell carcinoma antigen recognized by T-cells 3 {ECO:0000305};
DE Short=SART-3 {ECO:0000303|PubMed:10761712};
DE Short=mSART-3 {ECO:0000303|PubMed:10761712};
DE AltName: Full=Tumor-rejection antigen SART3 {ECO:0000303|PubMed:10761712};
GN Name=Sart3 {ECO:0000312|MGI:MGI:1858230};
GN Synonyms=Kiaa0156 {ECO:0000312|EMBL:BAC97877.2};
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Squamous cell carcinoma;
RX PubMed=10761712; DOI=10.1111/j.1349-7006.2000.tb00937.x;
RA Harada K., Yamada A., Mine T., Kawagoe N., Takasu H., Itoh K.;
RT "Mouse homologue of the human SART3 gene encoding tumor-rejection
RT antigen.";
RL Jpn. J. Cancer Res. 91:239-247(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Eye, and Head;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=NMRI; TISSUE=Mammary gland, and Mammary tumor;
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 [6]
RP REGION.
RX PubMed=10463607;
RA Yang D., Nakao M., Shichijo S., Sasatomi T., Takasu H., Matsumoto H.,
RA Mori K., Hayashi A., Yamana H., Shirouzu K., Itoh K.;
RT "Identification of a gene coding for a protein possessing shared tumor
RT epitopes capable of inducing HLA-A24-restricted cytotoxic T lymphocytes in
RT cancer patients.";
RL Cancer Res. 59:4056-4063(1999).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=12578909; DOI=10.1083/jcb.200210087;
RA Stanek D., Rader S.D., Klingauf M., Neugebauer K.M.;
RT "Targeting of U4/U6 small nuclear RNP assembly factor SART3/p110 to Cajal
RT bodies.";
RL J. Cell Biol. 160:505-516(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [9]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=21447833; DOI=10.1182/blood-2010-12-325332;
RA Liu Y., Timani K., Mantel C., Fan Y., Hangoc G., Cooper S., He J.J.,
RA Broxmeyer H.E.;
RT "TIP110/p110nrb/SART3/p110 regulation of hematopoiesis through CMYC.";
RL Blood 117:5643-5651(2011).
CC -!- FUNCTION: U6 snRNP-binding protein that functions as a recycling factor
CC of the splicing machinery. Promotes the initial reassembly of U4 and U6
CC snRNPs following their ejection from the spliceosome during its
CC maturation. Also binds U6atac snRNPs and may function as a recycling
CC factor for U4atac/U6atac spliceosomal snRNP, an initial step in the
CC assembly of U12-type spliceosomal complex. The U12-type spliceosomal
CC complex plays a role in the splicing of introns with non-canonical
CC splice sites. May also function as a substrate-targeting factor for
CC deubiquitinases like USP4 and USP15. Recruits USP4 to ubiquitinated
CC PRPF3 within the U4/U5/U6 tri-snRNP complex, promoting PRPF3
CC deubiquitination and thereby regulating the spliceosome U4/U5/U6 tri-
CC snRNP spliceosomal complex disassembly. May also recruit the
CC deubiquitinase USP15 to histone H2B and mediate histone
CC deubiquitination, thereby regulating gene expression and/or DNA repair
CC (By similarity). May play a role in hematopoiesis probably through
CC transcription regulation of specific genes including MYC
CC (PubMed:21447833). {ECO:0000250|UniProtKB:Q15020,
CC ECO:0000269|PubMed:21447833}.
CC -!- SUBUNIT: Component of the 7SK snRNP complex at least composed of P-TEFb
CC (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2, BCDIN3, SART3
CC proteins and 7SK and U6 snRNAs. Interacts with AGO1 and AGO2. Interacts
CC with PRPF3 and USP4; the interaction with PRPF3 is direct and recruits
CC USP4 to its substrate PRPF3. Interacts with USP15; the interaction is
CC direct. {ECO:0000250|UniProtKB:Q15020}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:12578909}. Nucleus, Cajal body
CC {ECO:0000269|PubMed:12578909}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q15020}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q15020}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JLI8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JLI8-2; Sequence=VSP_017252, VSP_017253;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with low level of
CC expression in liver, heart and skeletal (PubMed:10761712). Also
CC detected in hematopoietic cells (at protein level) (PubMed:21447833).
CC {ECO:0000269|PubMed:10761712, ECO:0000269|PubMed:21447833}.
CC -!- DEVELOPMENTAL STAGE: Expressed from early prenatal stages, as early as
CC 7 dpc and increased thereafter. {ECO:0000269|PubMed:10761712}.
CC -!- INDUCTION: Up-regulated in proliferating hematopoietic cells.
CC {ECO:0000269|PubMed:21447833}.
CC -!- DISRUPTION PHENOTYPE: Knockout of Sart3 is embryonic lethal.
CC {ECO:0000303|PubMed:21447833}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH36350.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF172722; AAF65228.1; -; mRNA.
DR EMBL; AK053828; BAC35544.1; -; mRNA.
DR EMBL; AK129067; BAC97877.2; -; Transcribed_RNA.
DR EMBL; AK086398; BAC39661.1; -; mRNA.
DR EMBL; BC036350; AAH36350.1; ALT_INIT; mRNA.
DR EMBL; BC057156; AAH57156.1; -; mRNA.
DR CCDS; CCDS19552.1; -. [Q9JLI8-1]
DR RefSeq; NP_058622.1; NM_016926.1. [Q9JLI8-1]
DR AlphaFoldDB; Q9JLI8; -.
DR SMR; Q9JLI8; -.
DR BioGRID; 207514; 29.
DR IntAct; Q9JLI8; 21.
DR STRING; 10090.ENSMUSP00000019118; -.
DR iPTMnet; Q9JLI8; -.
DR PhosphoSitePlus; Q9JLI8; -.
DR SwissPalm; Q9JLI8; -.
DR EPD; Q9JLI8; -.
DR jPOST; Q9JLI8; -.
DR MaxQB; Q9JLI8; -.
DR PaxDb; Q9JLI8; -.
DR PeptideAtlas; Q9JLI8; -.
DR PRIDE; Q9JLI8; -.
DR ProteomicsDB; 256837; -. [Q9JLI8-1]
DR ProteomicsDB; 256838; -. [Q9JLI8-2]
DR Antibodypedia; 18276; 256 antibodies from 36 providers.
DR DNASU; 53890; -.
DR Ensembl; ENSMUST00000019118; ENSMUSP00000019118; ENSMUSG00000018974. [Q9JLI8-1]
DR Ensembl; ENSMUST00000197041; ENSMUSP00000143778; ENSMUSG00000018974. [Q9JLI8-2]
DR GeneID; 53890; -.
DR KEGG; mmu:53890; -.
DR UCSC; uc008yym.1; mouse. [Q9JLI8-1]
DR CTD; 9733; -.
DR MGI; MGI:1858230; Sart3.
DR VEuPathDB; HostDB:ENSMUSG00000018974; -.
DR eggNOG; KOG0128; Eukaryota.
DR GeneTree; ENSGT00900000141107; -.
DR HOGENOM; CLU_007172_0_0_1; -.
DR InParanoid; Q9JLI8; -.
DR OMA; PRQMYGA; -.
DR OrthoDB; 867827at2759; -.
DR PhylomeDB; Q9JLI8; -.
DR TreeFam; TF317554; -.
DR BioGRID-ORCS; 53890; 22 hits in 74 CRISPR screens.
DR ChiTaRS; Sart3; mouse.
DR PRO; PR:Q9JLI8; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9JLI8; protein.
DR Bgee; ENSMUSG00000018974; Expressed in embryonic post-anal tail and 250 other tissues.
DR Genevisible; Q9JLI8; MM.
DR GO; GO:0061574; C:ASAP complex; IBA:GO_Central.
DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0071001; C:U4/U6 snRNP; ISO:MGI.
DR GO; GO:0005691; C:U6atac snRNP; ISO:MGI.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0030621; F:U4 snRNA binding; IEA:Ensembl.
DR GO; GO:0017070; F:U6 snRNA binding; ISS:UniProtKB.
DR GO; GO:0030624; F:U6atac snRNA binding; ISS:UniProtKB.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:MGI.
DR GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IMP:MGI.
DR GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
DR GO; GO:1903586; P:positive regulation of histone deubiquitination; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; ISS:UniProtKB.
DR CDD; cd12391; RRM1_SART3; 1.
DR CDD; cd12392; RRM2_SART3; 1.
DR Gene3D; 1.25.40.10; -; 2.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR008669; LSM_interact.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034217; SART3_RRM1.
DR InterPro; IPR034218; SART3_RRM2.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF05391; Lsm_interact; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00386; HAT; 7.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Methylation;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT CHAIN 2..962
FT /note="Squamous cell carcinoma antigen recognized by T-
FT cells 3"
FT /id="PRO_0000223314"
FT REPEAT 127..159
FT /note="HAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 165..196
FT /note="HAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 202..238
FT /note="HAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 243..276
FT /note="HAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 325..357
FT /note="HAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 360..392
FT /note="HAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 395..431
FT /note="HAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 441..474
FT /note="HAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 488..521
FT /note="HAT 9"
FT /evidence="ECO:0000255"
FT DOMAIN 704..782
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 801..878
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..352
FT /note="Mediates interaction with PRPF3"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT REGION 488..521
FT /note="Required for interaction with USP4"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT REGION 538..952
FT /note="Necessary and sufficient for U6 snRNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT REGION 591..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..670
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT REGION 880..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 559..618
FT /evidence="ECO:0000255"
FT COMPBIAS 591..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT MOD_RES 795
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT MOD_RES 852
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT MOD_RES 906
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15020"
FT VAR_SEQ 356..401
FT /note="DRQLKVKDLVLSVHSRAVRNCPWTVALWSRYLLAMERHGLDHQTIS -> PC
FT CAELPMDSCPVESVPSGHGATWTGPSNDFCDLRERSECRLHPGH (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017252"
FT VAR_SEQ 402..962
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017253"
FT CONFLICT 160
FT /note="M -> V (in Ref. 4; BAC39661)"
FT /evidence="ECO:0000305"
FT CONFLICT 792..814
FT /note="FRYSTTLEKHKLFISGLPFSCTK -> CFLKKGVFRVGCPIGSAQ (in
FT Ref. 2; BAC97877)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 962 AA; 109619 MW; 23BC235125E7A09C CRC64;
MATTAASSAS EPEVEPQAGP EAEGEEDEAK PAGVQRKVLS GAVAAEAAEA KGPGWDLQRE
GASGSDGDEE DAMASSAESS AGEDEWEYDE EEEKNQLEIE RLEEQLSING YDYNCHVELI
RLLRLEGELS RVRAARQKMS ELFPLTEELW LEWLHDEISM AMDGLDREHV YELFERAVKD
YICPNIWLEY GQYSVGGIGQ KGGLEKVRSV FERALSSVGL HMTKGLAIWE AYREFESAIV
EAARLEKVHS LFRRQLAIPL YEMEATFAEY EEWSEEPMPE SVLQSYQKAL GQLEKYKPYE
EALLQAEAPR LAEYQAYIDF EMKIGDPARI QLIFERALVE NCLVPDLWIR YSQYLDRQLK
VKDLVLSVHS RAVRNCPWTV ALWSRYLLAM ERHGLDHQTI SATFENALSA GFIQATDYVE
IWQVYLDYLR RRVDFRQDSS KELEELRSMF TRALEYLQQE VEERFSESGD PSCLIMQSWA
RVEARLCNNM QKARELWDSI MTRGNAKYAN MWLEYYNLER AHGDTQHCRK ALHRAVQCTS
DYPEHVCEVL LTMERTEGTL EDWDLAIQKT ETRLARVNEQ RMKAAEKEAA LVQQEEEKAE
QRKKVRAEKK ALKKKKKTRG ADKRREDEDE ENEWGEEEEE QPSKRRRTEN SLASGEASAM
KEETELSGKC LTIDVGPPSK QKEKAASLKR DMPKVAHDSS KDSVTVFVSN LPYSIEEPEV
KLRPLFEVCG EVVQIRPIFS NRGDFRGYCY VEFGEEKSAQ QALELDRKIV EGRPMFVSPC
VDKSKNPDFK VFRYSTTLEK HKLFISGLPF SCTKEELEDI CKAHGTVKDL RLVTNRAGKP
KGLAYVEYEN ESQASQAVMK MDGMTIRENV IKVAISNPPQ RKVPEKPEVR TAPGAPMLPR
QMYGARGKGR TQLSLLPRAL QRQGAAPQAE NGPAPGPAVA PSVATEAPKM SNADFAKLLL
RK
