SF3A2_RAT
ID SF3A2_RAT Reviewed; 471 AA.
AC Q6AXT8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Splicing factor 3A subunit 2;
GN Name=Sf3a2;
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=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).
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 -!- SIMILARITY: Belongs to the SF3A2 family. {ECO:0000305}.
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DR EMBL; BC079320; AAH79320.1; -; mRNA.
DR RefSeq; NP_001011986.1; NM_001011986.1.
DR RefSeq; XP_006240947.1; XM_006240885.3.
DR RefSeq; XP_006240948.1; XM_006240886.2.
DR RefSeq; XP_017450207.1; XM_017594718.1.
DR AlphaFoldDB; Q6AXT8; -.
DR SMR; Q6AXT8; -.
DR STRING; 10116.ENSRNOP00000026202; -.
DR jPOST; Q6AXT8; -.
DR PaxDb; Q6AXT8; -.
DR PRIDE; Q6AXT8; -.
DR Ensembl; ENSRNOT00000026202; ENSRNOP00000026202; ENSRNOG00000019349.
DR GeneID; 299620; -.
DR KEGG; rno:299620; -.
DR UCSC; RGD:1308627; rat.
DR CTD; 8175; -.
DR RGD; 1308627; Sf3a2.
DR eggNOG; KOG0227; Eukaryota.
DR GeneTree; ENSGT00720000108823; -.
DR HOGENOM; CLU_050757_1_1_1; -.
DR InParanoid; Q6AXT8; -.
DR OMA; PGVHPPN; -.
DR OrthoDB; 1320891at2759; -.
DR TreeFam; TF314370; -.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q6AXT8; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000019349; Expressed in testis and 18 other tissues.
DR Genevisible; Q6AXT8; RN.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD.
DR GO; GO:0016607; C:nuclear speck; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005681; C:spliceosomal complex; ISO:RGD.
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:RGD.
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:RGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:RGD.
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 2: Evidence at transcript level;
KW Acetylation; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Spliceosome; Zinc; Zinc-finger.
FT CHAIN 1..471
FT /note="Splicing factor 3A subunit 2"
FT /id="PRO_0000326552"
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 217..471
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:0000250|UniProtKB:Q62203"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15428"
SQ SEQUENCE 471 AA; 49890 MW; 8E00B0E89721A5C6 CRC64;
MDFQHRPGGK TGSGGVASSS ESNRDRRERL RQLALETIDI NKDPYFMKNH LGSYECKLCL
TLHNNEGSYL AHTQGKKHQT NLARRAAKEA KEAPAQPAPE KVKVEVKKFV KIGRPGYKVT
KQRDTEMGQQ SLLFQIDYPE IAEGVMPRHR FMSAYEQRIE PPDRRWQYLL MAAEPYETIA
FKVPSREIDK AEGKFWTHWN RETKQFFLQF HFKMEKPPAP PSLPAGPPGV KRPPPPLMNG
LPPRPPLPDA LPPPPPGGLP LPPMPPTGPA PSGPPGPPQM PPPAPGVHPP APVVHPPTSG
VHPPAPGVHP PAPVVHPPTS GVHPPAPGVH PPAPGVHPPA PGVHPPAPGV HPPAPGVHPP
APGVHPPAPG VHPPAPGVHP PPSAGVHPQA PGVHPPAPAV HPQAPGVHPP APGIHPQAPG
VHPQPPPGVH PAAPGVHPQP PGVHPTPMPP MLRPPLPSDG PGNMPPPPPG N
