CLASR_MOUSE
ID CLASR_MOUSE Reviewed; 668 AA.
AC Q8CFC7; Q5RKW4; Q8CFC8; Q9Z2N3;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=CLK4-associating serine/arginine rich protein;
DE AltName: Full=Clk4-associating SR-related protein;
DE AltName: Full=Serine/arginine-rich splicing factor 16;
DE AltName: Full=Splicing factor, arginine/serine-rich 16;
DE AltName: Full=Suppressor of white-apricot homolog 2;
GN Name=Clasrp; Synonyms=Clasp, Sfrs16, Srsf16, Swap2;
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 3).
RA Yoshiura K., Murray J.C.;
RT "A transcriptional map in the region of 19q13 derived using direct
RT sequencing and exon trapping.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; 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).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-668 (ISOFORMS 1 AND 2).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=12169693; DOI=10.1074/jbc.m206504200;
RA Katsu R., Onogi H., Wada K., Kawaguchi Y., Hagiwara M.;
RT "Novel SR-rich-related protein Clasp specifically interacts with
RT inactivated Clk4 and induces the exon EB inclusion of Clk.";
RL J. Biol. Chem. 277:44220-44228(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-541, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, 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).
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.
CC -!- SUBUNIT: Probably interacts with CLK4.
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Located in nuclear dots.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus, nucleoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=L;
CC IsoId=Q8CFC7-1; Sequence=Displayed;
CC Name=2; Synonyms=S;
CC IsoId=Q8CFC7-2; Sequence=VSP_008211, VSP_008212;
CC Name=3;
CC IsoId=Q8CFC7-3; Sequence=VSP_008213, VSP_008214;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain. Expressed at
CC intermediate level in lung and liver. In brain, it is expressed in the
CC hippocampus, cerebellum and olfactory bulb.
CC -!- PTM: Phosphorylated in vitro by CLK4.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC82338.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB26225.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF042799; AAC82338.1; ALT_INIT; mRNA.
DR EMBL; AK009334; BAB26225.1; ALT_INIT; mRNA.
DR EMBL; BC051916; AAH51916.2; -; mRNA.
DR EMBL; AB080582; BAC15600.1; -; mRNA.
DR EMBL; AB080583; BAC15601.1; -; mRNA.
DR CCDS; CCDS52061.1; -. [Q8CFC7-1]
DR RefSeq; NP_057889.3; NM_016680.5. [Q8CFC7-1]
DR AlphaFoldDB; Q8CFC7; -.
DR BioGRID; 207329; 3.
DR STRING; 10090.ENSMUSP00000083205; -.
DR iPTMnet; Q8CFC7; -.
DR PhosphoSitePlus; Q8CFC7; -.
DR EPD; Q8CFC7; -.
DR jPOST; Q8CFC7; -.
DR MaxQB; Q8CFC7; -.
DR PaxDb; Q8CFC7; -.
DR PeptideAtlas; Q8CFC7; -.
DR PRIDE; Q8CFC7; -.
DR ProteomicsDB; 283359; -. [Q8CFC7-1]
DR ProteomicsDB; 283360; -. [Q8CFC7-2]
DR ProteomicsDB; 283361; -. [Q8CFC7-3]
DR Antibodypedia; 54055; 73 antibodies from 19 providers.
DR DNASU; 53609; -.
DR Ensembl; ENSMUST00000086041; ENSMUSP00000083205; ENSMUSG00000061028. [Q8CFC7-1]
DR Ensembl; ENSMUST00000207907; ENSMUSP00000146982; ENSMUSG00000061028. [Q8CFC7-3]
DR Ensembl; ENSMUST00000208068; ENSMUSP00000147103; ENSMUSG00000061028. [Q8CFC7-2]
DR GeneID; 53609; -.
DR KEGG; mmu:53609; -.
DR UCSC; uc009fml.2; mouse. [Q8CFC7-1]
DR CTD; 11129; -.
DR MGI; MGI:1855695; Clasrp.
DR VEuPathDB; HostDB:ENSMUSG00000061028; -.
DR eggNOG; KOG2548; Eukaryota.
DR GeneTree; ENSGT00940000153892; -.
DR HOGENOM; CLU_008114_1_0_1; -.
DR InParanoid; Q8CFC7; -.
DR OMA; YSECAPV; -.
DR OrthoDB; 1620115at2759; -.
DR PhylomeDB; Q8CFC7; -.
DR TreeFam; TF351621; -.
DR BioGRID-ORCS; 53609; 24 hits in 75 CRISPR screens.
DR ChiTaRS; Clasrp; mouse.
DR PRO; PR:Q8CFC7; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8CFC7; protein.
DR Bgee; ENSMUSG00000061028; Expressed in retinal neural layer and 240 other tissues.
DR ExpressionAtlas; Q8CFC7; baseline and differential.
DR Genevisible; Q8CFC7; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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 Alternative splicing; Coiled coil; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..668
FT /note="CLK4-associating serine/arginine rich protein"
FT /id="PRO_0000081946"
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 366..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:0007744|PubMed:19131326"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N2M8"
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:0007744|PubMed:21183079"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 567
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N2M8"
FT VAR_SEQ 564..627
FT /note="PKLTPQERLKLRMQKALNRQFKADKKAAQEKMIQQEHERQEREDELRAMARK
FT IRMKERERREKE -> VSKNLELARLTPVSSSVQSWARWACRGPRGRGEPAQRLGKGYP
FT GKLSPIPASHGTPAGPQVPDS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_008213"
FT VAR_SEQ 564..588
FT /note="PKLTPQERLKLRMQKALNRQFKADK -> VTQADPTGEAEASDAEGSEPPVQ
FT GG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12169693,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_008211"
FT VAR_SEQ 589..668
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12169693,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_008212"
FT VAR_SEQ 628..668
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_008214"
SQ SEQUENCE 668 AA; 76825 MW; 1A0322702F7A9C40 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
QTGGPAPGRN ASTRRRSSSS SASRTSSSRS SSRSSSRSRR GYYRSGRHAR SRSRSWSRSR
SRSRRYSRSR SRGRRHSDGG SRDGHRYSRS PARRGGYVPR RRSRSRSRSG DRYKRGARGP
RHHSSSHSRS SWSLSPSRSR SVTRSGSRSQ SRSRSRSQSH SQSQSHSPSP PREKLTRPAA
SPAVGEKLKK TEPAAGKETG AAKPKLTPQE RLKLRMQKAL NRQFKADKKA AQEKMIQQEH
ERQEREDELR AMARKIRMKE RERREKEREE WERQYSRQSR SPSPRYSREY SSSRRRSRSR
SRSPHYRH
