SF3A1_BOVIN
ID SF3A1_BOVIN Reviewed; 793 AA.
AC A2VDN6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Splicing factor 3A subunit 1;
GN Name=SF3A1;
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=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-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 {ECO:0000250|UniProtKB:Q15459}.
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.
CC {ECO:0000250|UniProtKB:Q15459}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15459}. Nucleus
CC speckle {ECO:0000250|UniProtKB:Q15459}.
CC -!- DOMAIN: SURP motif 2 mediates direct binding to SF3A3. {ECO:0000250}.
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DR EMBL; BC133328; AAI33329.1; -; mRNA.
DR RefSeq; NP_001074979.1; NM_001081510.1.
DR RefSeq; XP_015331030.1; XM_015475544.1.
DR AlphaFoldDB; A2VDN6; -.
DR BMRB; A2VDN6; -.
DR SMR; A2VDN6; -.
DR STRING; 9913.ENSBTAP00000004398; -.
DR PaxDb; A2VDN6; -.
DR PeptideAtlas; A2VDN6; -.
DR PRIDE; A2VDN6; -.
DR Ensembl; ENSBTAT00000004398; ENSBTAP00000004398; ENSBTAG00000003390.
DR GeneID; 504381; -.
DR KEGG; bta:504381; -.
DR CTD; 10291; -.
DR VEuPathDB; HostDB:ENSBTAG00000003390; -.
DR VGNC; VGNC:34506; SF3A1.
DR eggNOG; KOG0007; Eukaryota.
DR GeneTree; ENSGT00730000111077; -.
DR HOGENOM; CLU_013259_1_0_1; -.
DR InParanoid; A2VDN6; -.
DR OMA; HFSARMP; -.
DR OrthoDB; 1256232at2759; -.
DR TreeFam; TF105705; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000003390; Expressed in vas deferens and 108 other tissues.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0005684; C:U2-type spliceosomal complex; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; ISS:UniProtKB.
DR CDD; cd01800; Ubl_SF3a120; 1.
DR Gene3D; 1.10.10.790; -; 2.
DR InterPro; IPR045146; SF3A1.
DR InterPro; IPR022030; SF3A1_dom.
DR InterPro; IPR035563; SF3As1_ubi.
DR InterPro; IPR000061; Surp.
DR InterPro; IPR035967; SWAP/Surp_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR15316; PTHR15316; 1.
DR Pfam; PF12230; PRP21_like_P; 1.
DR Pfam; PF01805; Surp; 2.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00648; SWAP; 2.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF109905; SSF109905; 2.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50128; SURP; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Spliceosome; Ubl conjugation.
FT CHAIN 1..793
FT /note="Splicing factor 3A subunit 1"
FT /id="PRO_0000295296"
FT REPEAT 52..94
FT /note="SURP motif 1"
FT REPEAT 166..208
FT /note="SURP motif 2"
FT DOMAIN 707..793
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..702
FT /note="Required and sufficient for nuclear import"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT COMPBIAS 1..19
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..337
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..385
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..584
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 169
FT /note="Critical for binding to SF3A3"
FT /evidence="ECO:0000250"
FT MOD_RES 55
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT MOD_RES 456
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT MOD_RES 759
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT CROSSLNK 131
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT CROSSLNK 424
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT CROSSLNK 499
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT CROSSLNK 542
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT CROSSLNK 686
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
SQ SEQUENCE 793 AA; 88786 MW; 6FA0AD2E622056FD CRC64;
MPAGPVQAVP PPPPAATEPK QPTEEEASSK EDSTPSKPVV GIIYPPPEVR NIVDKTASFV
ARNGPEFEAR IRQNEINNPK FNFLNPNDPY HAYYRHKVSE FKEGKAQEPS AAIPKVMQQQ
QQASQQQLPQ KVQAQVIQET IVPKEPPPEF EFIADPPSIS AFDLDVVKLT AQFVARNGRQ
FLTQLMQKEQ RNYQFDFLRP QHSLFNYFTK LVEQYTKILI PPKGLFTKLK KEAENPREVL
DQVCYRVEWA KFQERERKKE EEEKEKERVA YAQIDWHDFV VVETVDFQPN EQGNFPPPTT
PEELGARILI QERYEKFGES EEVEMEVESD EEDEKQEKAE EPPSQLDQDT QVQDMDEGSD
DEEEGQKVPP PPETPMPPPL PPTPDQVIVR KDYDPKASKP LPPAPAPDEY LVSPITGEKI
PASKMQEHMR IGLLDPRWLE QRDRSIREKQ SDDEVYAPGL DIESSLKQLA ERRTDIFGVE
ETAIGKKIGE EEIQKPEEKV TWDGHSGSMA RTQQAAQANI TLQEQIEAIH KAKGLVPEDD
TKEKIGPSKP NEIPQQPPPP SSATNIPSSA PPITSVPRPP AMPPPVRTTV VSAVPVMPRP
PMASVVRLPP GSVIAPMPPI IHAPRINVVP MPPSAPPIMA PRPPPMIVPT AFVPAPPVAP
VPAPAPMPPV HPPPPMEDEP ASKKLKTEDS LMPEEEFLRR NKGPVSIKVQ VPNMQDKTEW
KLNGQVLVFT LPLTDQVSVI KVKIHEATGM PAGKQKLQYE GIFIKDSNSL AYYNMANGAV
IHLALKERGG RKK
