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Squamous cell carcinoma antigen recognized by T-cells 3 (SART-3) (mSART-3) (Tumor-rejection antigen SART3)

 SART3_MOUSE             Reviewed;         962 AA.
Q9JLI8; Q6ZQI2; Q8BPK9; Q8C3B7; Q8CFU9;
07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
20-JUN-2018, entry version 140.
RecName: Full=Squamous cell carcinoma antigen recognized by T-cells 3 {ECO:0000305};
Short=SART-3 {ECO:0000303|PubMed:10761712};
Short=mSART-3 {ECO:0000303|PubMed:10761712};
AltName: Full=Tumor-rejection antigen SART3 {ECO:0000303|PubMed:10761712};
Name=Sart3 {ECO:0000312|MGI:MGI:1858230};
Synonyms=Kiaa0156 {ECO:0000312|EMBL:BAC97877.2};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
STRAIN=BALB/cJ; TISSUE=Squamous cell carcinoma;
PubMed=10761712; DOI=10.1111/j.1349-7006.2000.tb00937.x;
Harada K., Yamada A., Mine T., Kawagoe N., Takasu H., Itoh K.;
"Mouse homologue of the human SART3 gene encoding tumor-rejection
antigen.";
Jpn. J. Cancer Res. 91:239-247(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Embryonic tail;
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[3]
SEQUENCE REVISION.
Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Eye, and Head;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=NMRI; TISSUE=Mammary gland, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
REGION.
PubMed=10463607;
Yang D., Nakao M., Shichijo S., Sasatomi T., Takasu H., Matsumoto H.,
Mori K., Hayashi A., Yamana H., Shirouzu K., Itoh K.;
"Identification of a gene coding for a protein possessing shared tumor
epitopes capable of inducing HLA-A24-restricted cytotoxic T
lymphocytes in cancer patients.";
Cancer Res. 59:4056-4063(1999).
[7]
SUBCELLULAR LOCATION.
PubMed=12578909; DOI=10.1083/jcb.200210087;
Stanek D., Rader S.D., Klingauf M., Neugebauer K.M.;
"Targeting of U4/U6 small nuclear RNP assembly factor SART3/p110 to
Cajal bodies.";
J. Cell Biol. 160:505-516(2003).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=21447833; DOI=10.1182/blood-2010-12-325332;
Liu Y., Timani K., Mantel C., Fan Y., Hangoc G., Cooper S., He J.J.,
Broxmeyer H.E.;
"TIP110/p110nrb/SART3/p110 regulation of hematopoiesis through CMYC.";
Blood 117:5643-5651(2011).
-!- FUNCTION: U6 snRNP-binding protein that functions as a recycling
factor of the splicing machinery. Promotes the initial reassembly
of U4 and U6 snRNPs following their ejection from the spliceosome
during its maturation. Also binds U6atac snRNPs and may function
as a recycling factor for U4atac/U6atac spliceosomal snRNP, an
initial step in the assembly of U12-type spliceosomal complex. The
U12-type spliceosomal complex plays a role in the splicing of
introns with non-canonical splice sites. May also function as a
substrate-targeting factor for deubiquitinases like USP4 and
USP15. Recruits USP4 to ubiquitinated PRPF3 within the U4/U5/U6
tri-snRNP complex, promoting PRPF3 deubiquitination and thereby
regulating the spliceosome U4/U5/U6 tri-snRNP spliceosomal complex
disassembly. May also recruit the deubiquitinase USP15 to histone
H2B and mediate histone deubiquitination, thereby regulating gene
expression and/or DNA repair (By similarity). May play a role in
hematopoiesis probably through transcription regulation of
specific genes including MYC (PubMed:21447833).
{ECO:0000250|UniProtKB:Q15020, ECO:0000269|PubMed:21447833}.
-!- SUBUNIT: Component of the 7SK snRNP complex at least composed of
P-TEFb (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2,
BCDIN3, SART3 proteins and 7SK and U6 snRNAs. Interacts with AGO1
and AGO2. Interacts with PRPF3 and USP4; the interaction with
PRPF3 is direct and recruits USP4 to its substrate PRPF3.
Interacts with USP15; the interaction is direct.
{ECO:0000250|UniProtKB:Q15020}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
{ECO:0000269|PubMed:12578909}. Nucleus, Cajal body
{ECO:0000269|PubMed:12578909}. Nucleus speckle
{ECO:0000250|UniProtKB:Q15020}. Cytoplasm
{ECO:0000250|UniProtKB:Q15020}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9JLI8-1; Sequence=Displayed;
Name=2;
IsoId=Q9JLI8-2; Sequence=VSP_017252, VSP_017253;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed, with low level of
expression in liver, heart and skeletal (PubMed:10761712). Also
detected in hematopoietic cells (at protein level)
(PubMed:21447833). {ECO:0000269|PubMed:10761712,
ECO:0000269|PubMed:21447833}.
-!- DEVELOPMENTAL STAGE: Expressed from early prenatal stages, as
early as E7 and increased thereafter.
{ECO:0000269|PubMed:10761712}.
-!- INDUCTION: Up-regulated in proliferating hematopoietic cells.
{ECO:0000269|PubMed:21447833}.
-!- DISRUPTION PHENOTYPE: Knockout of Sart3 is embryonic lethal.
{ECO:0000303|PubMed:21447833}.
-!- SEQUENCE CAUTION:
Sequence=AAH36350.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF172722; AAF65228.1; -; mRNA.
EMBL; AK053828; BAC35544.1; -; mRNA.
EMBL; AK129067; BAC97877.2; -; Transcribed_RNA.
EMBL; AK086398; BAC39661.1; -; mRNA.
EMBL; BC036350; AAH36350.1; ALT_INIT; mRNA.
EMBL; BC057156; AAH57156.1; -; mRNA.
CCDS; CCDS19552.1; -. [Q9JLI8-1]
RefSeq; NP_058622.1; NM_016926.1. [Q9JLI8-1]
UniGene; Mm.29594; -.
ProteinModelPortal; Q9JLI8; -.
SMR; Q9JLI8; -.
BioGrid; 207514; 19.
IntAct; Q9JLI8; 21.
STRING; 10090.ENSMUSP00000019118; -.
iPTMnet; Q9JLI8; -.
PhosphoSitePlus; Q9JLI8; -.
SwissPalm; Q9JLI8; -.
EPD; Q9JLI8; -.
PaxDb; Q9JLI8; -.
PeptideAtlas; Q9JLI8; -.
PRIDE; Q9JLI8; -.
Ensembl; ENSMUST00000019118; ENSMUSP00000019118; ENSMUSG00000018974. [Q9JLI8-1]
Ensembl; ENSMUST00000197041; ENSMUSP00000143778; ENSMUSG00000018974. [Q9JLI8-2]
GeneID; 53890; -.
KEGG; mmu:53890; -.
UCSC; uc008yym.1; mouse. [Q9JLI8-1]
CTD; 9733; -.
MGI; MGI:1858230; Sart3.
eggNOG; KOG0128; Eukaryota.
eggNOG; ENOG410XP88; LUCA.
GeneTree; ENSGT00900000141107; -.
HOGENOM; HOG000063708; -.
HOVERGEN; HBG053888; -.
InParanoid; Q9JLI8; -.
KO; K22611; -.
OMA; SQAVMKM; -.
OrthoDB; EOG091G041L; -.
PhylomeDB; Q9JLI8; -.
TreeFam; TF317554; -.
ChiTaRS; Sart3; mouse.
PRO; PR:Q9JLI8; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000018974; -.
Genevisible; Q9JLI8; MM.
GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0071001; C:U4/U6 snRNP; IEA:Ensembl.
GO; GO:0005691; C:U6atac snRNP; IEA:Ensembl.
GO; GO:0042393; F:histone binding; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0030621; F:U4 snRNA binding; IEA:Ensembl.
GO; GO:0017070; F:U6 snRNA binding; ISS:UniProtKB.
GO; GO:0030624; F:U6atac snRNA binding; ISS:UniProtKB.
GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:MGI.
GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
GO; GO:0071425; P:hematopoietic stem cell proliferation; IMP:MGI.
GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI.
GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
GO; GO:1903586; P:positive regulation of histone deubiquitination; ISS:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; ISS:UniProtKB.
CDD; cd12391; RRM1_SART3; 1.
CDD; cd12392; RRM2_SART3; 1.
Gene3D; 1.25.40.10; -; 2.
Gene3D; 3.30.70.330; -; 2.
InterPro; IPR003107; HAT.
InterPro; IPR008669; LSM_interact.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
InterPro; IPR034217; SART3_RRM1.
InterPro; IPR034218; SART3_RRM2.
InterPro; IPR011990; TPR-like_helical_dom_sf.
Pfam; PF05391; Lsm_interact; 1.
Pfam; PF00076; RRM_1; 2.
SMART; SM00386; HAT; 7.
SMART; SM00360; RRM; 2.
SUPFAM; SSF48452; SSF48452; 1.
SUPFAM; SSF54928; SSF54928; 2.
PROSITE; PS50102; RRM; 2.
1: Evidence at protein level;
Acetylation; Alternative splicing; Coiled coil; Complete proteome;
Cytoplasm; Methylation; mRNA processing; mRNA splicing; Nucleus;
Phosphoprotein; Reference proteome; Repeat; RNA-binding.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q15020}.
CHAIN 2 962 Squamous cell carcinoma antigen
recognized by T-cells 3.
/FTId=PRO_0000223314.
REPEAT 127 159 HAT 1. {ECO:0000255}.
REPEAT 165 196 HAT 2. {ECO:0000255}.
REPEAT 202 238 HAT 3. {ECO:0000255}.
REPEAT 243 276 HAT 4. {ECO:0000255}.
REPEAT 325 357 HAT 5. {ECO:0000255}.
REPEAT 360 392 HAT 6. {ECO:0000255}.
REPEAT 395 431 HAT 7. {ECO:0000255}.
REPEAT 441 474 HAT 8. {ECO:0000255}.
REPEAT 488 521 HAT 9. {ECO:0000255}.
DOMAIN 704 782 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 801 878 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 2 352 Mediates interaction with PRPF3.
{ECO:0000250|UniProtKB:Q15020}.
REGION 488 521 Required for interaction with USP4.
{ECO:0000250|UniProtKB:Q15020}.
REGION 538 952 Necessary and sufficient for U6 snRNA
binding. {ECO:0000250|UniProtKB:Q15020}.
REGION 601 670 Required for nuclear localization.
{ECO:0000250|UniProtKB:Q15020}.
COILED 559 618 {ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q15020}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:Q15020}.
MOD_RES 216 216 Phosphoserine.
{ECO:0000250|UniProtKB:Q15020}.
MOD_RES 651 651 Phosphoserine.
{ECO:0000250|UniProtKB:Q15020}.
MOD_RES 795 795 Phosphoserine.
{ECO:0000250|UniProtKB:Q15020}.
MOD_RES 852 852 Phosphoserine.
{ECO:0000250|UniProtKB:Q15020}.
MOD_RES 906 906 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q15020}.
VAR_SEQ 356 401 DRQLKVKDLVLSVHSRAVRNCPWTVALWSRYLLAMERHGLD
HQTIS -> PCCAELPMDSCPVESVPSGHGATWTGPSNDFC
DLRERSECRLHPGH (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_017252.
VAR_SEQ 402 962 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_017253.
CONFLICT 160 160 M -> V (in Ref. 4; BAC39661).
{ECO:0000305}.
CONFLICT 792 814 FRYSTTLEKHKLFISGLPFSCTK -> CFLKKGVFRVGCPI
GSAQ (in Ref. 2; BAC97877).
{ECO:0000305}.
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


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