RSRC1_MOUSE
ID RSRC1_MOUSE Reviewed; 334 AA.
AC Q9DBU6; Q3TF06;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Serine/Arginine-related protein 53;
DE Short=SRrp53;
DE AltName: Full=Arginine/serine-rich coiled-coil protein 1;
GN Name=Rsrc1; Synonyms=Srrp53;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Lung;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
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 [3]
RP PHOSPHORYLATION, SUBCELLULAR LOCATION, AND NUCLEOCYTOPLASMIC SHUTTLING.
RX PubMed=15798186; DOI=10.1128/mcb.25.8.2969-2980.2005;
RA Cazalla D., Newton K., Caceres J.F.;
RT "A novel SR-related protein is required for the second step of pre-mRNA
RT splicing.";
RL Mol. Cell. Biol. 25:2969-2980(2005).
CC -!- FUNCTION: Plays a role in pre-mRNA splicing. Involved in both
CC constitutive and alternative pre-mRNA splicing. May have a role in the
CC recognition of the 3' splice site during the second step of splicing
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via Arg/Ser-rich domain) with LUC7L3, RBM39 and
CC RSF1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15798186}. Nucleus
CC speckle {ECO:0000269|PubMed:15798186}. Cytoplasm
CC {ECO:0000269|PubMed:15798186}. Note=Shuttles between the nucleus and
CC cytoplasm.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:15798186}.
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DR EMBL; AK004742; BAB23523.1; -; mRNA.
DR EMBL; AK169340; BAE41092.1; -; mRNA.
DR EMBL; BC083123; AAH83123.1; -; mRNA.
DR CCDS; CCDS17394.1; -.
DR RefSeq; NP_080098.1; NM_025822.3.
DR AlphaFoldDB; Q9DBU6; -.
DR BioGRID; 211784; 6.
DR STRING; 10090.ENSMUSP00000066797; -.
DR iPTMnet; Q9DBU6; -.
DR PhosphoSitePlus; Q9DBU6; -.
DR EPD; Q9DBU6; -.
DR MaxQB; Q9DBU6; -.
DR PaxDb; Q9DBU6; -.
DR PRIDE; Q9DBU6; -.
DR ProteomicsDB; 256790; -.
DR Antibodypedia; 46770; 82 antibodies from 23 providers.
DR DNASU; 66880; -.
DR Ensembl; ENSMUST00000065074; ENSMUSP00000066797; ENSMUSG00000034544.
DR Ensembl; ENSMUST00000161726; ENSMUSP00000124347; ENSMUSG00000034544.
DR Ensembl; ENSMUST00000162036; ENSMUSP00000125468; ENSMUSG00000034544.
DR GeneID; 66880; -.
DR KEGG; mmu:66880; -.
DR UCSC; uc008plh.1; mouse.
DR CTD; 51319; -.
DR MGI; MGI:1914130; Rsrc1.
DR VEuPathDB; HostDB:ENSMUSG00000034544; -.
DR eggNOG; KOG3406; Eukaryota.
DR GeneTree; ENSGT00730000111251; -.
DR InParanoid; Q9DBU6; -.
DR OMA; VIFHPNF; -.
DR OrthoDB; 1367755at2759; -.
DR BioGRID-ORCS; 66880; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Rsrc1; mouse.
DR PRO; PR:Q9DBU6; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9DBU6; protein.
DR Bgee; ENSMUSG00000034544; Expressed in medial geniculate body and 254 other tissues.
DR ExpressionAtlas; Q9DBU6; baseline and differential.
DR Genevisible; Q9DBU6; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IDA:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISO:MGI.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0046677; P:response to antibiotic; IDA:MGI.
DR GO; GO:0008380; P:RNA splicing; ISO:MGI.
DR InterPro; IPR034604; SRRP53.
DR PANTHER; PTHR31968; PTHR31968; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..334
FT /note="Serine/Arginine-related protein 53"
FT /id="PRO_0000097497"
FT REGION 1..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 180..236
FT /evidence="ECO:0000255"
FT COMPBIAS 45..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..135
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 334 AA; 38637 MW; 8660FA2AADE0BEF4 CRC64;
MGRRSSDTEE ESRSKRKKKH RRRSSSSSSS DSRTYSRKKG GRRPRSDSRS WSRDRQLRSH
SYERRRRRRS SSSSSYGSRR KRSRSRSRGR GKPYRVQRSR SKSRTRRSRS RPRPRSHSRS
SERSSHRRTR SRSRDRDRRK VRDKEKREKE KDKGKDKEVH SIKRGDSGNI KAGLEHLPPA
EQAKARLQLV LEAAAKADEA LKAKERSEEE AKRRKEEDQA TLVEQVKRVK EIEAIESDSF
VQQTFRSSKD VKKAVEPSEV QHVTAASGPA SAAAEPPSTG KEIDPDSIPT AIKYQDDNSL
AHPNLFIEKA EAEEKWFKRL IALRQERLMG SPVA
