CLASR_RAT
ID CLASR_RAT Reviewed; 668 AA.
AC Q5HZB6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=CLK4-associating serine/arginine rich protein;
DE AltName: Full=Splicing factor, arginine/serine-rich 16;
GN Name=Clasrp; Synonyms=Sfrs16;
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 GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [LARGE SCALE ANALYSIS] AT SER-294 AND SER-541, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Probably functions as an alternative splicing regulator. May
CC regulate the mRNA splicing of genes such as CLK1. May act by regulating
CC members of the CLK kinase family (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Probably interacts with CLK4. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Phosphorylated in vitro by CLK4. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-16 is the initiator.
CC {ECO:0000305}.
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DR EMBL; CH473979; EDM08179.1; -; Genomic_DNA.
DR EMBL; BC089090; AAH89090.2; -; mRNA.
DR RefSeq; NP_001019465.2; NM_001024294.1.
DR AlphaFoldDB; Q5HZB6; -.
DR STRING; 10116.ENSRNOP00000066334; -.
DR iPTMnet; Q5HZB6; -.
DR PhosphoSitePlus; Q5HZB6; -.
DR PaxDb; Q5HZB6; -.
DR PRIDE; Q5HZB6; -.
DR Ensembl; ENSRNOT00000075144; ENSRNOP00000066334; ENSRNOG00000046000.
DR GeneID; 499390; -.
DR KEGG; rno:499390; -.
DR CTD; 11129; -.
DR RGD; 1563538; Clasrp.
DR eggNOG; KOG2548; Eukaryota.
DR GeneTree; ENSGT00940000153892; -.
DR InParanoid; Q5HZB6; -.
DR OMA; YSECAPV; -.
DR OrthoDB; 1620115at2759; -.
DR PhylomeDB; Q5HZB6; -.
DR PRO; PR:Q5HZB6; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000046000; Expressed in cerebellum and 20 other tissues.
DR Genevisible; Q5HZB6; RN.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR040397; SWAP.
DR InterPro; IPR019147; SWAP_N_domain.
DR PANTHER; PTHR13161; PTHR13161; 2.
DR Pfam; PF09750; DRY_EERY; 1.
DR SMART; SM01141; DRY_EERY; 1.
PE 1: Evidence at protein level;
KW Coiled coil; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..668
FT /note="CLK4-associating serine/arginine rich protein"
FT /id="PRO_0000370323"
FT REGION 173..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 579..641
FT /evidence="ECO:0000255"
FT COMPBIAS 185..214
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..432
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..485
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N2M8"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N2M8"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 327
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N2M8"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N2M8"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N2M8"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 567
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N2M8"
SQ SEQUENCE 668 AA; 76807 MW; 1673410C203FF581 CRC64;
MWHEARKHER KLRGMMVDYK KRAERRREYY EKIKKDPAQF LQVHGRACKV HLDSAVALAA
ESPVNMMPWQ GDTNNMIDRF DVRAHLDHIP DYTPPLLTTI SPEQESDERK CNYERYRGLV
QNDFAGISEE QCLYQIYIDE LYGGLQRPSE DEKKKLAEKK ASIGYTYEDS TVAEVEKVAE
KPEEEESPAE EESNSDEDEV IPDIDVEVDV DELNQEQVAD LNKQATTYGM ADGDFVRMLR
KDKEEAEAIK HAKALEEEKA MYSGRRSRRQ RREFREKRLR GRKISPPSYA RRDSPTYDPY
KRSPSESSSE SRSRSRSPSP GREEKITFIT SFGGSDEEAA AAAAAAAASG AAPGKPPAPP
QPGGPAPGRN ASARRRSSSS SASRTSSSRS SSRSSSRSRR GYYRSGRHAR SRSRSWSRSR
SRSRRYSRSR SRGRRHSDGG SRDGHRYSRS PARRSGYAPR RRSRSRSRSG DRYKRGARGP
RHHSSSHSRS SWSLSPSRSR SLTRSGSRSQ SRSRSRSQSH SQSQSHSPSP PREKLTRPAA
SPAVGEKLKK TEPAAGKETG AAKPKLTPQE RLKLRMQKAL NRQFKADKKA AQEKMIQQEH
ERQEREDELR AMARKIRMKE RERREKEREE WERQYSRQSR SPSPRYSREY SSSRRRSRSR
SRSPHYRH
