RSRC1_RAT
ID RSRC1_RAT Reviewed; 334 AA.
AC Q5PPJ2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 74.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
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 speckle {ECO:0000250}. Nucleus
CC {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Shuttles between the
CC nucleus and cytoplasm. {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q9DBU6}.
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DR EMBL; BC087665; AAH87665.1; -; mRNA.
DR RefSeq; NP_001014194.1; NM_001014172.1.
DR AlphaFoldDB; Q5PPJ2; -.
DR STRING; 10116.ENSRNOP00000039808; -.
DR iPTMnet; Q5PPJ2; -.
DR PhosphoSitePlus; Q5PPJ2; -.
DR PaxDb; Q5PPJ2; -.
DR Ensembl; ENSRNOT00000101324; ENSRNOP00000081280; ENSRNOG00000062777.
DR GeneID; 361956; -.
DR KEGG; rno:361956; -.
DR UCSC; RGD:1304968; rat.
DR CTD; 51319; -.
DR RGD; 1304968; Rsrc1.
DR eggNOG; KOG3406; Eukaryota.
DR GeneTree; ENSGT00730000111251; -.
DR InParanoid; Q5PPJ2; -.
DR OrthoDB; 1367755at2759; -.
DR PhylomeDB; Q5PPJ2; -.
DR PRO; PR:Q5PPJ2; -.
DR Proteomes; UP000002494; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; ISO:RGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0006913; P:nucleocytoplasmic transport; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0046677; P:response to antibiotic; ISO:RGD.
DR GO; GO:0008380; P:RNA splicing; ISO:RGD.
DR InterPro; IPR034604; SRRP53.
DR PANTHER; PTHR31968; PTHR31968; 1.
PE 2: Evidence at transcript 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_0000097498"
FT REGION 1..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 180..234
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; 38668 MW; 827B6B33F36F7DB7 CRC64;
MGRRSSDTEE ESRSKRKKKH RRRSSSSSSS DSRTYSRKKG GRRPRSESRS WSRDRQPRSH
SYERRRRRRS SSSSSYGSRR KRSRSRSRGR GKSYRVQRSR SKSRTRRSRS RPRPRSHSRS
SERSSHRRTR SRSRDRDRRK VRDKEKREKE KDKGKDKEAH TIKRGDCGNI KAGLEHLPPA
EQAKARLQLV LEAAAKADEA LKAKERNEEE AKRRKEEDQA TLGEQVKRVK EIEAIESDSF
VQQTFRSSKD VKKSVEPSEV KHVTPASGPA SVAADPPSTG KEIDPDSIPT AIKYQDDNSL
AHPNLFIEKA EAEEKWFKRL IALRQERLMG SPVA