SRSF7_MOUSE
ID SRSF7_MOUSE Reviewed; 267 AA.
AC Q8BL97; Q8BMC6; Q8BUR2; Q8R2N4; Q8R3E9; Q91YS1;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Serine/arginine-rich splicing factor 7;
DE AltName: Full=Splicing factor, arginine/serine-rich 7;
GN Name=Srsf7; Synonyms=Sfrs7;
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] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Wolffian duct;
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] (ISOFORMS 2; 3 AND 4).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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-210 AND SER-212, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [5]
RP INTERACTION WITH YTHDC1.
RX PubMed=29799838; DOI=10.1371/journal.pgen.1007412;
RA Kasowitz S.D., Ma J., Anderson S.J., Leu N.A., Xu Y., Gregory B.D.,
RA Schultz R.M., Wang P.J.;
RT "Nuclear m6A reader YTHDC1 regulates alternative polyadenylation and
RT splicing during mouse oocyte development.";
RL PLoS Genet. 14:e1007412-e1007412(2018).
CC -!- FUNCTION: Required for pre-mRNA splicing. Represses the splicing of
CC MAPT/Tau exon 10. May function as export adapter involved in mRNA
CC nuclear export such as of histone H2A. Binds mRNA which is thought to
CC be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1
CC pathway); enhances NXF1-NXT1 RNA-binding activity. RNA-binding is semi-
CC sequence specific (By similarity). {ECO:0000250|UniProtKB:Q16629}.
CC -!- SUBUNIT: Found in large molecular weight complexes containing CCNL1 and
CC the p110 isoforms of either CDC2L1 or CDC2L2 (By similarity). Interacts
CC with CCNL2 and CPSF6. Interacts with NXF1 (By similarity). Interacts
CC with YTHDC1 (PubMed:29799838). {ECO:0000250|UniProtKB:Q16629,
CC ECO:0000269|PubMed:29799838}.
CC -!- INTERACTION:
CC Q8BL97; Q6PFR5: Tra2a; NbExp=4; IntAct=EBI-913123, EBI-913075;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q16629}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q16629}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Isoforms, lacking all or part of the RS domain, may be
CC involved in modulating Srsf7 function.;
CC Name=1;
CC IsoId=Q8BL97-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BL97-2; Sequence=VSP_013654;
CC Name=3;
CC IsoId=Q8BL97-3; Sequence=VSP_013654, VSP_013655, VSP_013656;
CC Name=4;
CC IsoId=Q8BL97-4; Sequence=VSP_013654, VSP_013657;
CC -!- PTM: Extensively phosphorylated on serine residues in the RS domain.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; AK032861; BAC28058.1; -; mRNA.
DR EMBL; AK045884; BAC32521.1; -; mRNA.
DR EMBL; AK082848; BAC38650.1; -; mRNA.
DR EMBL; BC014857; AAH14857.1; -; mRNA.
DR EMBL; BC025529; AAH25529.1; -; mRNA.
DR EMBL; BC027391; AAH27391.1; -; mRNA.
DR CCDS; CCDS28988.1; -. [Q8BL97-2]
DR RefSeq; NP_001182414.1; NM_001195485.1.
DR RefSeq; NP_001182415.1; NM_001195486.1.
DR RefSeq; NP_001182416.1; NM_001195487.1.
DR RefSeq; NP_666195.1; NM_146083.2. [Q8BL97-2]
DR RefSeq; XP_006524253.1; XM_006524190.2.
DR AlphaFoldDB; Q8BL97; -.
DR BMRB; Q8BL97; -.
DR SMR; Q8BL97; -.
DR BioGRID; 230352; 24.
DR DIP; DIP-36580N; -.
DR IntAct; Q8BL97; 6.
DR MINT; Q8BL97; -.
DR STRING; 10090.ENSMUSP00000070983; -.
DR iPTMnet; Q8BL97; -.
DR PhosphoSitePlus; Q8BL97; -.
DR SwissPalm; Q8BL97; -.
DR EPD; Q8BL97; -.
DR jPOST; Q8BL97; -.
DR MaxQB; Q8BL97; -.
DR PaxDb; Q8BL97; -.
DR PeptideAtlas; Q8BL97; -.
DR PRIDE; Q8BL97; -.
DR ProteomicsDB; 258617; -. [Q8BL97-1]
DR ProteomicsDB; 258618; -. [Q8BL97-2]
DR ProteomicsDB; 258619; -. [Q8BL97-3]
DR ProteomicsDB; 258620; -. [Q8BL97-4]
DR Antibodypedia; 29517; 268 antibodies from 32 providers.
DR DNASU; 225027; -.
DR Ensembl; ENSMUST00000063417; ENSMUSP00000070983; ENSMUSG00000024097. [Q8BL97-2]
DR GeneID; 225027; -.
DR KEGG; mmu:225027; -.
DR UCSC; uc008dqp.1; mouse. [Q8BL97-1]
DR UCSC; uc008dqt.2; mouse. [Q8BL97-4]
DR CTD; 6432; -.
DR MGI; MGI:1926232; Srsf7.
DR VEuPathDB; HostDB:ENSMUSG00000024097; -.
DR eggNOG; KOG0107; Eukaryota.
DR GeneTree; ENSGT00910000144115; -.
DR HOGENOM; CLU_012062_20_0_1; -.
DR InParanoid; Q8BL97; -.
DR OMA; VERSHGM; -.
DR TreeFam; TF351858; -.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-MMU-72187; mRNA 3'-end processing.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR BioGRID-ORCS; 225027; 29 hits in 74 CRISPR screens.
DR ChiTaRS; Srsf7; mouse.
DR PRO; PR:Q8BL97; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8BL97; protein.
DR Bgee; ENSMUSG00000024097; Expressed in ureteric bud tip and 249 other tissues.
DR ExpressionAtlas; Q8BL97; baseline and differential.
DR Genevisible; Q8BL97; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; ISO:MGI.
DR CDD; cd12646; RRM_SRSF7; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034651; SRSF7_RRM.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Isopeptide bond;
KW Metal-binding; mRNA processing; mRNA splicing; mRNA transport; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding;
KW Transport; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..267
FT /note="Serine/arginine-rich splicing factor 7"
FT /id="PRO_0000081933"
FT DOMAIN 40..113
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 182..189
FT /note="1"
FT REPEAT 190..197
FT /note="2"
FT REPEAT 198..205
FT /note="3"
FT REPEAT 206..213
FT /note="4"
FT REPEAT 240..247
FT /note="5; approximate"
FT REPEAT 248..255
FT /note="6; approximate"
FT ZN_FING 133..150
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 110..127
FT /note="Sufficient for interaction with NXF1"
FT /evidence="ECO:0000250"
FT REGION 152..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..255
FT /note="6 X 8 AA repeats of R-R-S-R-S-X-S-X"
FT COMPBIAS 152..205
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..246
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16629"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16629"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16629"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16629"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16629"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16629"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16629"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16629"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16629"
FT CROSSLNK 53
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q16629"
FT VAR_SEQ 1..38
FT /note="MRSSARGRPLQAATAFFLSLFFFLRRFERGFWLWGGDS -> MSRYGRYGG
FT (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_013654"
FT VAR_SEQ 159..186
FT /note="SRSRSHSRSRGRRYSRSRSRSRGRRSRS -> YLINEGMVGILVNQSNSFIS
FT KAETSVFL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_013655"
FT VAR_SEQ 187..267
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_013656"
FT VAR_SEQ 238..249
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013657"
FT CONFLICT 155
FT /note="R -> T (in Ref. 1; BAC28058)"
FT /evidence="ECO:0000305"
FT CONFLICT 208..212
FT /note="SRSGS -> FRFGF (in Ref. 2; AAH14857)"
FT /evidence="ECO:0000305"
FT CONFLICT 218..220
FT /note="Missing (in Ref. 1; BAC38650)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="S -> F (in Ref. 2; AAH14857)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="R -> C (in Ref. 2; AAH14857)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="H -> P (in Ref. 2; AAH14857)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 30818 MW; F193FC4C3A7D8C7C CRC64;
MRSSARGRPL QAATAFFLSL FFFLRRFERG FWLWGGDSET KVYVGNLGTG AGKGELERAF
SYYGPLRTVW IARNPPGFAF VEFEDPRDAE DAVRGLDGKV ICGSRVRVEL STGMPRRSRF
DRPPARRPFD PNDRCYECGE KGHYAYDCHR YSRRRRSRSR SRSHSRSRGR RYSRSRSRSR
GRRSRSASPR RSRSVSLRRS RSASLRRSRS GSIIGSRYFQ SRSRSRSRSR SISRPRSSRS
KSRSPSPKRS RSPSGSPHRS ASPERMD
