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 01-MAY-2013, entry version 100.
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;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; 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.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA 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.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA 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.,
RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of
RT the 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
RT project: 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 MASS
RP SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=17203969; DOI=10.1021/pr0604155;
RA Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT "Protein phosphorylation and expression profiling by Yin-yang
RT multidimensional liquid chromatography (Yin-yang MDLC) mass
RT spectrometry.";
RL J. Proteome Res. 6:250-262(2007).
RN [6]
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: Subunit of the splicing factor SF3A required for 'A'
CC complex assembly formed by the stable binding of U2 snRNP to the
CC branchpoint sequence (BPS) in pre-mRNA. Sequence independent
CC binding of SF3A/SF3B complex upstream of the branch site is
CC essential, it may anchor U2 snRNP to the pre-mRNA. May also be
CC involved in the assembly of the 'E' complex (By similarity).
CC -!- SUBUNIT: Identified in the spliceosome C complex (By similarity).
CC Component of splicing factor SF3A which is composed of three
CC subunits; SF3A3/SAP61, SF3A2/SAP62, SF3A1/SAP114. SF3A associates
CC with the splicing factor SF3B and a 12S RNA unit to form the U2
CC small nuclear ribonucleoproteins complex (U2 snRNP). Interacts
CC with SF3A3 (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC -!- SIMILARITY: Contains 2 SURP motif repeats.
CC -!- SIMILARITY: Contains 1 ubiquitin-like domain.
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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; CAI25745.1; -; Genomic_DNA.
DR EMBL; BC010727; AAH10727.1; -; mRNA.
DR EMBL; BC029753; AAH29753.1; -; mRNA.
DR IPI; IPI00408796; -.
DR RefSeq; NP_080451.4; NM_026175.5.
DR UniGene; Mm.156914; -.
DR PDB; 1WE7; NMR; -; A=685-786.
DR PDBsum; 1WE7; -.
DR ProteinModelPortal; Q8K4Z5; -.
DR SMR; Q8K4Z5; 48-110, 134-288, 685-788.
DR IntAct; Q8K4Z5; 35.
DR PhosphoSite; Q8K4Z5; -.
DR PaxDb; Q8K4Z5; -.
DR PRIDE; Q8K4Z5; -.
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 eggNOG; NOG300902; -.
DR GeneTree; ENSGT00570000079144; -.
DR HOGENOM; HOG000238941; -.
DR HOVERGEN; HBG059993; -.
DR InParanoid; Q8K4Z5; -.
DR KO; K12825; -.
DR OMA; GMPPAKQ; -.
DR OrthoDB; EOG4N5VWN; -.
DR ChiTaRS; SF3A1; mouse.
DR EvolutionaryTrace; Q8K4Z5; -.
DR NextBio; 324654; -.
DR Bgee; Q8K4Z5; -.
DR CleanEx; MM_SF3A1; -.
DR Genevestigator; Q8K4Z5; -.
DR GermOnline; ENSMUSG00000002129; Mus musculus.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IEA:Compara.
DR GO; GO:0005684; C:U2-type spliceosomal complex; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR InterPro; IPR022030; PRP21-like.
DR InterPro; IPR000061; Surp.
DR InterPro; IPR000626; Ubiquitin.
DR InterPro; IPR019955; Ubiquitin_supergroup.
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 PROSITE; PS50128; SURP; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Spliceosome.
FT CHAIN 1 791 Splicing factor 3A subunit 1.
FT /FTId=PRO_0000114918.
FT REPEAT 52 94 SURP motif 1.
FT REPEAT 166 208 SURP motif 2.
FT DOMAIN 705 788 Ubiquitin-like.
FT COMPBIAS 10 14 Poly-Pro.
FT COMPBIAS 118 122 Poly-Gln.
FT COMPBIAS 260 267 Poly-Glu.
FT COMPBIAS 367 370 Poly-Pro.
FT COMPBIAS 555 558 Poly-Pro.
FT COMPBIAS 670 673 Poly-Pro.
FT MOD_RES 55 55 N6-acetyllysine (By similarity).
FT MOD_RES 320 320 Phosphoserine (By similarity).
FT MOD_RES 329 329 Phosphoserine.
FT MOD_RES 357 357 Phosphoserine (By similarity).
FT MOD_RES 411 411 Phosphoserine (By similarity).
FT MOD_RES 449 449 Phosphoserine (By similarity).
FT MOD_RES 454 454 Phosphotyrosine (By similarity).
FT MOD_RES 757 757 Phosphotyrosine (By similarity).
FT CONFLICT 257 257 R -> G (in Ref. 1; BAC26142).
FT CONFLICT 368 368 P -> L (in Ref. 1; BAC26294).
FT CONFLICT 708 708 Q -> L (in Ref. 1; BAC26853).
FT HELIX 685 687
FT HELIX 692 698
FT STRAND 703 709
FT STRAND 713 715
FT STRAND 721 729
FT HELIX 736 745
FT TURN 750 752
FT STRAND 753 757
FT STRAND 760 762
FT HELIX 768 771
FT STRAND 778 783
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
//