SF3A1_MOUSE
ID SF3A1_MOUSE Reviewed; 791 AA.
AC Q8K4Z5; Q8C0M7; Q8C128; Q8C175; Q921T3;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Splicing factor 3A subunit 1;
DE AltName: Full=SF3a120;
GN Name=Sf3a1;
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].
RC STRAIN=C57BL/6J; TISSUE=Skin, and Testis;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland, and 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 [4]
RP PROTEIN SEQUENCE OF 238-246; 471-484 AND 755-763, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55, 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 [7]
RP STRUCTURE BY NMR OF 685-786.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of ubiquitin-like domain in Sf3a120.";
RL Submitted (NOV-2004) to the PDB data bank.
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; AK028829; BAC26142.1; -; mRNA.
DR EMBL; AK029095; BAC26294.1; -; mRNA.
DR EMBL; AK030223; BAC26853.1; -; mRNA.
DR EMBL; AL807825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010727; AAH10727.1; -; mRNA.
DR EMBL; BC029753; AAH29753.1; -; mRNA.
DR CCDS; CCDS24380.1; -.
DR RefSeq; NP_080451.4; NM_026175.5.
DR PDB; 1WE7; NMR; -; A=685-786.
DR PDBsum; 1WE7; -.
DR AlphaFoldDB; Q8K4Z5; -.
DR BMRB; Q8K4Z5; -.
DR SMR; Q8K4Z5; -.
DR BioGRID; 212207; 64.
DR IntAct; Q8K4Z5; 38.
DR MINT; Q8K4Z5; -.
DR STRING; 10090.ENSMUSP00000002198; -.
DR iPTMnet; Q8K4Z5; -.
DR PhosphoSitePlus; Q8K4Z5; -.
DR SwissPalm; Q8K4Z5; -.
DR EPD; Q8K4Z5; -.
DR jPOST; Q8K4Z5; -.
DR MaxQB; Q8K4Z5; -.
DR PaxDb; Q8K4Z5; -.
DR PeptideAtlas; Q8K4Z5; -.
DR PRIDE; Q8K4Z5; -.
DR ProteomicsDB; 261504; -.
DR Antibodypedia; 254; 296 antibodies from 27 providers.
DR DNASU; 67465; -.
DR Ensembl; ENSMUST00000002198; ENSMUSP00000002198; ENSMUSG00000002129.
DR GeneID; 67465; -.
DR KEGG; mmu:67465; -.
DR UCSC; uc007hup.2; mouse.
DR CTD; 10291; -.
DR MGI; MGI:1914715; Sf3a1.
DR VEuPathDB; HostDB:ENSMUSG00000002129; -.
DR eggNOG; KOG0007; Eukaryota.
DR GeneTree; ENSGT00730000111077; -.
DR HOGENOM; CLU_013259_1_0_1; -.
DR InParanoid; Q8K4Z5; -.
DR OMA; HFSARMP; -.
DR OrthoDB; 1256232at2759; -.
DR PhylomeDB; Q8K4Z5; -.
DR TreeFam; TF105705; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 67465; 28 hits in 75 CRISPR screens.
DR ChiTaRS; Sf3a1; mouse.
DR EvolutionaryTrace; Q8K4Z5; -.
DR PRO; PR:Q8K4Z5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8K4Z5; protein.
DR Bgee; ENSMUSG00000002129; Expressed in epiblast (generic) and 268 other tissues.
DR Genevisible; Q8K4Z5; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; 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:0006397; P:mRNA processing; ISO:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Isopeptide bond;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Spliceosome; Ubl conjugation.
FT CHAIN 1..791
FT /note="Splicing factor 3A subunit 1"
FT /id="PRO_0000114918"
FT REPEAT 52..94
FT /note="SURP motif 1"
FT REPEAT 166..208
FT /note="SURP motif 2"
FT DOMAIN 705..788
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..700
FT /note="Required and sufficient for nuclear import"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT COMPBIAS 1..18
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..338
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..383
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..582
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:0007744|PubMed:23806337"
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 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT MOD_RES 454
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT MOD_RES 757
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 422
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT CROSSLNK 497
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT CROSSLNK 540
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT CROSSLNK 684
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15459"
FT CONFLICT 257
FT /note="R -> G (in Ref. 1; BAC26142)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="P -> L (in Ref. 1; BAC26294)"
FT /evidence="ECO:0000305"
FT CONFLICT 708
FT /note="Q -> L (in Ref. 1; BAC26853)"
FT /evidence="ECO:0000305"
FT HELIX 685..687
FT /evidence="ECO:0007829|PDB:1WE7"
FT HELIX 692..698
FT /evidence="ECO:0007829|PDB:1WE7"
FT STRAND 703..709
FT /evidence="ECO:0007829|PDB:1WE7"
FT STRAND 713..715
FT /evidence="ECO:0007829|PDB:1WE7"
FT STRAND 721..729
FT /evidence="ECO:0007829|PDB:1WE7"
FT HELIX 736..745
FT /evidence="ECO:0007829|PDB:1WE7"
FT TURN 750..752
FT /evidence="ECO:0007829|PDB:1WE7"
FT STRAND 753..757
FT /evidence="ECO:0007829|PDB:1WE7"
FT STRAND 760..762
FT /evidence="ECO:0007829|PDB:1WE7"
FT HELIX 768..771
FT /evidence="ECO:0007829|PDB:1WE7"
FT STRAND 778..783
FT /evidence="ECO:0007829|PDB:1WE7"
SQ SEQUENCE 791 AA; 88545 MW; D83D0432469C3708 CRC64;
MQAGPVQAVP PPPPVATESK QPIEEEASSK EDPTPSKPVV GIIYPPPEVR NIVDKTASFV
ARNGPEFEAR IRQNEINNPK FNFLNPNDPY HAYYRHKVSE FKEGKAQEPS AAIPKVMQQQ
QQATQQQLPQ KVQAQVIQET IVPKEPPPEF EFIADPPSIS AFDLDVVKLT AQFVARNGRQ
FLTQLMQKEQ RNYQFDFLRP QHSLFNYFTK LVEQYTKILI PPKGLFSKLK KEAENPREVL
DQVCYRVEWA KFQERERKKE EEEKEKERVA YAQIDWHDFV VVETVDFQPN EQGNFPPPTT
PEELGARILI QERYEKFGES EEVEMEVESD EEDQEKAEET PSQLDQDTQV QDMDEGSDDE
EEGQKVPPPP ETPMPPPLPP TPDQVIVRKD YDPKASKPLP PAPAPDEYLV SPITGEKIPA
SKMQEHMRIG LLDPRWLEQR DRSIREKQSD DEVYAPGLDI ESSLKQLAER RTDIFGVEET
AIGKKIGEEE IQKPEEKVTW DGHSGSMART QQAAQANITL QEQIEAIHKA KGLVPEDDTK
EKIGPSKPNE IPQQPPPPSS ATNIPSSAPP ITSVPRPPAM PPPVRTTVVS AVPVMPRPPM
ASVVRLPPGS VIAPMPPIIH APRINVVPMP PAAPPIMAPR PPPMIVPTAF VPAPPVAPVP
APAPMPPVHP PPPMEDEPPS KKLKTEDSLM PEEEFLRRNK GPVSIKVQVP NMQDKTEWKL
NGQGLVFTLP LTDQVSVIKV KIHEATGMPA GKQKLQYEGI FIKDSNSLAY YNMASGAVIH
LALKERGGRK K
