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   27-MAR-2024, entry version 168.
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,
RC   Pancreas, 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; 10090-ENSMUSP00000019118; -.
DR   PeptideAtlas; Q9JLI8; -.
DR   ProteomicsDB; 256837; -. [Q9JLI8-1]
DR   ProteomicsDB; 256838; -. [Q9JLI8-2]
DR   Pumba; Q9JLI8; -.
DR   Antibodypedia; 18276; 275 antibodies from 36 providers.
DR   DNASU; 53890; -.
DR   Ensembl; ENSMUST00000019118.8; ENSMUSP00000019118.4; ENSMUSG00000018974.8. [Q9JLI8-1]
DR   Ensembl; ENSMUST00000197041.2; ENSMUSP00000143778.2; ENSMUSG00000018974.8. [Q9JLI8-2]
DR   GeneID; 53890; -.
DR   KEGG; mmu:53890; -.
DR   UCSC; uc008yym.1; mouse. [Q9JLI8-1]
DR   AGR; MGI:1858230; -.
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; LWARYIL; -.
DR   OrthoDB; 2879516at2759; -.
DR   PhylomeDB; Q9JLI8; -.
DR   TreeFam; TF317554; -.
DR   BioGRID-ORCS; 53890; 23 hits in 79 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 254 other cell types or tissues.
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; IEA:Ensembl.
DR   GO; GO:0005691; C:U6atac snRNP; IEA:Ensembl.
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: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   GO; GO:0140673; P:transcription elongation-coupled chromatin remodeling; ISS:UniProtKB.
DR   CDD; cd12391; RRM1_SART3; 1.
DR   CDD; cd12392; RRM2_SART3; 1.
DR   Gene3D; 3.30.70.330; -; 2.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 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   PANTHER; PTHR15481; RIBONUCLEIC ACID BINDING PROTEIN S1; 1.
DR   PANTHER; PTHR15481:SF5; SQUAMOUS CELL CARCINOMA ANTIGEN RECOGNIZED BY T-CELLS 3; 1.
DR   Pfam; PF16605; LSM_int_assoc; 1.
DR   Pfam; PF05391; Lsm_interact; 1.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00386; HAT; 7.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50102; RRM; 2.
DR   Genevisible; Q9JLI8; MM.
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
//