SF3A3_MOUSE
ID SF3A3_MOUSE Reviewed; 501 AA.
AC Q9D554;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Splicing factor 3A subunit 3;
DE AltName: Full=SF3a60;
DE AltName: Full=Spliceosome-associated protein 61;
DE Short=SAP 61;
GN Name=Sf3a3; Synonyms=Sap61;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-169.
RC STRAIN=C57BL/6J; TISSUE=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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Lung, 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).
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:Q12874}.
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:Q12874}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00130}.
CC -!- SIMILARITY: Belongs to the SF3A3 family. {ECO:0000305}.
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DR EMBL; BC009141; AAH09141.1; -; mRNA.
DR EMBL; AK015776; BAB29971.1; -; mRNA.
DR CCDS; CCDS38875.1; -.
DR RefSeq; NP_083433.1; NM_029157.3.
DR AlphaFoldDB; Q9D554; -.
DR BMRB; Q9D554; -.
DR SMR; Q9D554; -.
DR BioGRID; 217189; 89.
DR IntAct; Q9D554; 6.
DR STRING; 10090.ENSMUSP00000030734; -.
DR iPTMnet; Q9D554; -.
DR PhosphoSitePlus; Q9D554; -.
DR SwissPalm; Q9D554; -.
DR EPD; Q9D554; -.
DR jPOST; Q9D554; -.
DR MaxQB; Q9D554; -.
DR PaxDb; Q9D554; -.
DR PRIDE; Q9D554; -.
DR ProteomicsDB; 261175; -.
DR Antibodypedia; 31818; 134 antibodies from 29 providers.
DR DNASU; 75062; -.
DR Ensembl; ENSMUST00000030734; ENSMUSP00000030734; ENSMUSG00000028902.
DR GeneID; 75062; -.
DR KEGG; mmu:75062; -.
DR UCSC; uc008uqx.1; mouse.
DR CTD; 10946; -.
DR MGI; MGI:1922312; Sf3a3.
DR VEuPathDB; HostDB:ENSMUSG00000028902; -.
DR eggNOG; KOG2636; Eukaryota.
DR GeneTree; ENSGT00530000063402; -.
DR HOGENOM; CLU_027160_2_0_1; -.
DR InParanoid; Q9D554; -.
DR OMA; KDAHRRN; -.
DR OrthoDB; 383503at2759; -.
DR PhylomeDB; Q9D554; -.
DR TreeFam; TF315227; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 75062; 25 hits in 72 CRISPR screens.
DR ChiTaRS; Sf3a3; mouse.
DR PRO; PR:Q9D554; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9D554; protein.
DR Bgee; ENSMUSG00000028902; Expressed in otic placode and 267 other tissues.
DR ExpressionAtlas; Q9D554; baseline and differential.
DR Genevisible; Q9D554; 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; ISO: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:0005684; C:U2-type spliceosomal complex; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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:1903241; P:U2-type prespliceosome assembly; ISS:UniProtKB.
DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR InterPro; IPR031776; SF3A3.
DR InterPro; IPR031774; SF3A3_dom.
DR InterPro; IPR024598; SF3a60/Prp9_C.
DR InterPro; IPR021966; SF3a60_bindingd.
DR PANTHER; PTHR12786:SF3; PTHR12786:SF3; 1.
DR Pfam; PF16837; SF3A3; 1.
DR Pfam; PF12108; SF3a60_bindingd; 1.
DR Pfam; PF11931; SF3a60_Prp9_C; 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; Spliceosome; Zinc; Zinc-finger.
FT CHAIN 1..501
FT /note="Splicing factor 3A subunit 3"
FT /id="PRO_0000174319"
FT ZN_FING 406..437
FT /note="Matrin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT REGION 342..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 175..179
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q12874"
FT COMPBIAS 356..373
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q12874"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12874"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12874"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12874"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12874"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12874"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12874"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12874"
FT MOD_RES 475
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12874"
SQ SEQUENCE 501 AA; 58842 MW; 46EE0928FC8271D7 CRC64;
METILEQQRR YHEEKERLMD VMAKEMLTKK STLRDQINSD HRTRAMQDRY MEVSGNLRDL
YDDKDGLRKE ELNAISGPNE FAEFYNRLKQ IKEFHRKHPN EICVPMSVEF EELLKARENP
SEEAQNLVEF TDEEGYGRYL DLHDCYLKYI NLKASEKLDY ITYLSIFDQL FDIPKERKNA
EYKRYLEMLL EYLQDYTDRV KPLQDQNELF GKIQTDFEKK WDNGTFPGWP KETSSALTHA
GAHLDLSAFS SWEELASLGL DRLKSALLAL GLKCGGTLEE RAQRLFSTKG KSLESLDTSL
FAKNPKSKGT KRDTERNKDI AFLEAQIYEY VEILGEQRQL THENVQRKQA RTGEEREEEE
EEQISESESE DEENEIIYNP KNLPLGWDGK PIPYWLYKLH GLNINYNCEI CGNYTYRGPK
AFQRHFAEWR HAHGMRCLGI PNTAHFANVT QIEDAVSLWA KLKLQKASER WQPDTEEEYE
DSSGNVVNKK TYEDLKRQGL L
