SF3A2_MOUSE
ID SF3A2_MOUSE Reviewed; 475 AA.
AC Q62203;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Splicing factor 3A subunit 2;
DE AltName: Full=SF3a66;
DE AltName: Full=Spliceosome-associated protein 62;
DE Short=SAP 62;
GN Name=Sf3a2; Synonyms=Sap62;
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 [GENOMIC DNA].
RC STRAIN=129;
RX PubMed=8541848; DOI=10.1093/hmg/4.9.1613;
RA Dresser D.W., Hacker A., Lovell-Badge R., Guerrier D.;
RT "The genes for a spliceosome protein (SAP62) and the anti-Mullerian hormone
RT (AMH) are contiguous.";
RL Hum. Mol. Genet. 4:1613-1618(1995).
RN [2]
RP SEQUENCE REVISION TO 101 AND 195-196.
RC STRAIN=129;
RX PubMed=11602354; DOI=10.1016/s0378-1119(01)00690-4;
RA Dresser D.W., Jamin S.P., Atkins C.J., Guerrier D.;
RT "An expressed GNRP-like gene shares a bi-directional promoter with SF3A2
RT (SAP62) immediately upstream of AMH.";
RL Gene 277:163-173(2001).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-10, 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).
CC -!- FUNCTION: Involved in pre-mRNA splicing as a component of the splicing
CC factor SF3A complex that contributes to the assembly of the 17S U2
CC snRNP, and the subsequent assembly of the pre-spliceosome 'E' complex
CC and the pre-catalytic spliceosome 'A' complex. Involved in pre-mRNA
CC splicing as a component of pre-catalytic spliceosome 'B' complexes,
CC including the Bact complex. Interacts directly with the duplex formed
CC by U2 snRNA and the intron. {ECO:0000250|UniProtKB:Q15428}.
CC -!- SUBUNIT: Component of splicing factor SF3A which is composed of three
CC subunits; SF3A3/SAP61, SF3A2/SAP62 and SF3A1/SAP114. SF3A1 functions as
CC scaffold that interacts directly with both SF3A2 and SF3A3. SF3A
CC associates with the splicing factor SF3B and a 12S RNA unit to form the
CC mature 17S U2 small nuclear ribonucleoprotein complex (17S U2 snRNP).
CC Identified in the spliceosome 'E' complex, a precursor of the
CC spliceosome 'A' complex. Identified in the spliceosome 'A' and 'B'
CC complexes. Identified in the spliceosome 'C' complex. Interacts with
CC HTATSF1. {ECO:0000250|UniProtKB:Q15428}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00130}.
CC -!- TISSUE SPECIFICITY: Found in all tissues examined.
CC -!- SIMILARITY: Belongs to the SF3A2 family. {ECO:0000305}.
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DR EMBL; X83733; CAC10449.1; -; Genomic_DNA.
DR AlphaFoldDB; Q62203; -.
DR SMR; Q62203; -.
DR IntAct; Q62203; 2.
DR STRING; 10090.ENSMUSP00000117160; -.
DR iPTMnet; Q62203; -.
DR PhosphoSitePlus; Q62203; -.
DR EPD; Q62203; -.
DR MaxQB; Q62203; -.
DR PaxDb; Q62203; -.
DR PeptideAtlas; Q62203; -.
DR PRIDE; Q62203; -.
DR ProteomicsDB; 256629; -.
DR MGI; MGI:104912; Sf3a2.
DR eggNOG; KOG0227; Eukaryota.
DR InParanoid; Q62203; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR ChiTaRS; Sf3a2; mouse.
DR PRO; PR:Q62203; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q62203; protein.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005681; C:spliceosomal complex; ISO:MGI.
DR GO; GO:0005686; C:U2 snRNP; ISS:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
DR GO; GO:0005684; C:U2-type spliceosomal complex; ISO:MGI.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; ISO:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:MGI.
DR GO; GO:0000245; P:spliceosomal complex assembly; IBA:GO_Central.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; ISS:UniProtKB.
DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR031781; SF3A2_dom.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR Pfam; PF16835; SF3A2; 1.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50171; ZF_MATRIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Spliceosome; Zinc; Zinc-finger.
FT CHAIN 1..475
FT /note="Splicing factor 3A subunit 2"
FT /id="PRO_0000174316"
FT ZN_FING 54..84
FT /note="Matrin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q15428"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15428"
SQ SEQUENCE 475 AA; 49911 MW; E8651DC3B0E29C7C CRC64;
MDFQHRPGGK TGSGGVASSS ESNRDRRERL RQLALETIDI NKDPYFMKNH LGSYECKLCL
TLHNNEGSYL AHTQGKKHQT NLARRAAKEA KEAPAQPAPE QVKVEVKKFV KIGRPGYKVT
KQRDTEMGQQ SLLFQIDYPE IAEGIMPRHR FMSAYEQRIE PPDRRWQYLL MAAEPYETIA
FKVPSREIDK AEGKFFFLQF HFKMEKPPAP PSLPAGPPGV KRPPPPLMNG LPPRPPLPDA
LPPPPPGGLP LPPMPPTGPA PSGPPGPPQM PPPAPGVHPP APVVHPPTSG VHPPAPGVHP
PAPVVHPPTS GVHPPAPGVH PPTPGVHPPA PGVHPPAPGV HPPAPGVHPP TPGVHPPAPG
VHPPAPGVHP PAPGVHPPPS AGVHPQAPGV HPPAPAVHPQ APGVHPPAPG IHPQAPGVHP
QPPPGVHPAA PGVHPQPPGV HPSNPGVHPA PMPPMLRPPL PSDGPGNMPP PPPGN
