ID   SF3A2_BOVIN             Reviewed;         477 AA.
AC   A5PJN8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Splicing factor 3A subunit 2;
GN   Name=SF3A2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; BC142185; AAI42186.1; -; mRNA.
DR   RefSeq; NP_001092681.1; NM_001099211.1.
DR   AlphaFoldDB; A5PJN8; -.
DR   SMR; A5PJN8; -.
DR   STRING; 9913.ENSBTAP00000035656; -.
DR   PaxDb; A5PJN8; -.
DR   PeptideAtlas; A5PJN8; -.
DR   PRIDE; A5PJN8; -.
DR   Ensembl; ENSBTAT00000035788; ENSBTAP00000035656; ENSBTAG00000025452.
DR   Ensembl; ENSBTAT00000067195; ENSBTAP00000062091; ENSBTAG00000025452.
DR   GeneID; 789082; -.
DR   KEGG; bta:789082; -.
DR   CTD; 8175; -.
DR   VEuPathDB; HostDB:ENSBTAG00000025452; -.
DR   VGNC; VGNC:34507; SF3A2.
DR   eggNOG; KOG0227; Eukaryota.
DR   GeneTree; ENSGT00720000108823; -.
DR   HOGENOM; CLU_050757_1_1_1; -.
DR   InParanoid; A5PJN8; -.
DR   OMA; PGVHPPN; -.
DR   OrthoDB; 1320891at2759; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000025452; Expressed in vas deferens and 105 other tissues.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
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..477
FT                   /note="Splicing factor 3A subunit 2"
FT                   /id="PRO_0000326551"
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..477
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   477 AA;  50612 MW;  5313DB957D41ADAF CRC64;
     MDFQHRPGGK TGSGGVASSS ESNRDRRERL RQLALETIDI NKDPYFMKNH LGSYECKLCL
     TLHNNEGSYL AHTQGKKHQT NLARRAAKEA KEAPAQPAPE KVKVEVKKFV KIGRPGYKVT
     KQRDTEMGQQ SLLFQIDYPE IAEGIMPRHR FMSAYEQRIE PPDRRWQYLL MAAEPYETIA
     FKVPSREIDK AEGKFWTHWN RETKQFFLQF HFKMEKPPAP PSLPAGPPGV KRPPPPLMNG
     LPPRPPLPES LPPPPPGGLP LPPMPPSGPA PSGPPGPPQL PPPAPGVHPP APVVHPPASG
     VHPPAPGVHP PAPGVHPPAP VVHPPASGVH PPAPGVHPPA PGVHPPAPGV HPPAPGVHPP
     PSAGVHPQAP VVHPPAPAVH PQAPGVHPTP AVHPQAPGVH PPAPGVHPPA PGIHPQPPGV
     HPPPPGVHPP APGVHPQPPG VHPSNPGVHP PTPMPPMLRP PLPSEGPGNI PPPPPTN