Q9R1C7 (PR40A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pre-mRNA-processing factor 40 homolog A

Alternative name(s):
Formin-binding protein 11
Short name=FBP-11
Formin-binding protein 3

Gene names

Name:	Prpf40a
Synonyms:	Fbp11, Fnbp3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	953 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing. Ref.5
Subunit structure	Interacts with the N-terminus of HTT and with the phosphorylated C-terminal domain of POLR2A By similarity. Interacts with AKAP8L, SF1, SRPK1, CARD8, ATBF1 and MECP2. Interacts through the WW domains with formin proline-rich regions and with WASL/N-WASP. Ref.3 Ref.4 Ref.5 Ref.6
Subcellular location	Nucleus speckle. Nucleus matrix. Note: Colocalizes with AKAP8L in the nuclear matrix. Ref.5 Ref.6
Domain	The WW domains are essential for localization to nuclear speckles.
Sequence similarities	Belongs to the PRPF40 family. Contains 5 FF domains. Contains 2 WW domains.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW cell migration Inferred from sequence or structural similarity. Source: UniProtKB cytoskeleton organization Inferred from sequence or structural similarity. Source: UniProtKB mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell shape Inferred from sequence or structural similarity. Source: UniProtKB regulation of cytokinesis Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	nuclear matrix Inferred from direct assay Ref.6. Source: UniProtKB nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	proline-rich region binding Inferred from direct assay PubMed 17915251. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9R1C7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9R1C7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     14-55: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 953	953	Pre-mRNA-processing factor 40 homolog A		PRO_0000076086
Regions
	Domain	140 – 173	34	WW 1
	Domain	181 – 214	34	WW 2
	Domain	389 – 443	55	FF 1
	Domain	521 – 586	66	FF 2
	Domain	523 – 583	61	FF 3
	Domain	603 – 663	61	FF 4
	Domain	739 – 795	57	FF 5
Amino acid modifications
	Modified residue	36	1	Phosphoserine Ref.8
	Modified residue	151	1	Phosphoserine By similarity
	Modified residue	196	1	N6-acetyllysine By similarity
	Modified residue	369	1	Phosphothreonine By similarity
	Modified residue	824	1	Phosphoserine Ref.9
	Modified residue	826	1	Phosphoserine Ref.9
	Modified residue	828	1	Phosphoserine Ref.9
	Modified residue	830	1	Phosphoserine Ref.9
	Modified residue	879	1	Phosphoserine Ref.9
	Modified residue	881	1	Phosphoserine Ref.9
	Modified residue	884	1	Phosphoserine Ref.9
	Modified residue	928	1	Phosphothreonine Ref.7 Ref.10
	Modified residue	929	1	Phosphoserine Ref.7 Ref.10
	Modified residue	931	1	Phosphoserine Ref.7 Ref.10
	Modified residue	934	1	Phosphoserine Ref.7 Ref.8 Ref.10
Natural variations
	Alternative sequence	14 – 55	42	Missing in isoform 2.		VSP_008049
Experimental info
	Sequence conflict	334	1	E → A in BAC40061. Ref.2
	Sequence conflict	355	1	T → I in BAC40061. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 3C627AB7404D2285	FASTA	953	108,481
	10 20 30 40 50 60 MRPGTGAERG GLMVSEMESQ PPSRGPGDGE RRLSGSNLCS SSWVSADGFL RRRPSMGHPG 70 80 90 100 110 120 MHYAPMGMHP MGQRANMPPV PHGMMPQMMP PMGGPPMGQM PGMMSSVMSG MMMSHMSQAS 130 140 150 160 170 180 MQPALPPGVN SMDVAAGAAS GAKSMWTEHK SPDGRTYYYN TETKQSTWEK PDDLKTPAEQ 190 200 210 220 230 240 LLSKCPWKEY KSDSGKPYYY NSQTKESRWA KPKELEDLEG YQNTIVAGGL ITKSNLHAMI 250 260 270 280 290 300 KAEESSKQEE CTTASTAPVP TTEIPTTMST MAAAEAAAAV VAAAAAAAAA ANANTSTTPT 310 320 330 340 350 360 NTVGSVPVAP EPEVTSIVAT AVDNENTVTV STEEQAQLAN TTAIQDLSGD ISSNTGEEPA 370 380 390 400 410 420 KQETVSDFTP KKEEEESQPA KKTYTWNTKE EAKQAFKELL KEKRVPSNAS WEQAMKMIIN 430 440 450 460 470 480 DPRYSALAKL SEKKQAFNAY KVQTEKEEKE EARSKYKEAK ESFQRFLENH EKMTSTTRYK 490 500 510 520 530 540 KAEQMFGEME VWNAISERDR LEIYEDVLFF LSKKEKEQAK QLRKRNWEAL KNILDNMANV 550 560 570 580 590 600 TYSTTWSEAQ QYLMDNPTFA EDEELQNMDK EDALICFEEH IRALEKEEEE EKQKTLLRER 610 620 630 640 650 660 RRQRKNRESF QIFLDELHEH GQLHSMSSWM ELYPTISSDI RFTNMLGQPG STALDLFKFY 670 680 690 700 710 720 VEDLKARYHD EKKIIKDILK DKGFVVEVNT TFEDFVAIIS STKRSTTLDA GNIKLAFNSL 730 740 750 760 770 780 LEKAEARERE REKEEARKMK RKESAFKSML KQATPPIELD AVWEDIRERF VKEPAFEDIT 790 800 810 820 830 840 LESERKRIFK DFMHVLEHEC QHHHSKNKKH SKKSKKHHRK RSRSRSGSES DDDDSHSKKK 850 860 870 880 890 900 RQRSESHSAS ERSSSAESER SYKKSKKHKK KSKKRRHKSD SPESDTEREK DKKEKDRDSE 910 920 930 940 950 KDRSRQRSES KHKSPKKKTG KDSGNWDTSG SELSEGELEK RRRTLLEQLD DDQ
	Isoform 2 [UniParc]. Checksum: 7BE2E454CC5365CA	FASTA	911	103,963
	10 20 30 40 50 60 MRPGTGAERG GLMMGHPGMH YAPMGMHPMG QRANMPPVPH GMMPQMMPPM GGPPMGQMPG 70 80 90 100 110 120 MMSSVMSGMM MSHMSQASMQ PALPPGVNSM DVAAGAASGA KSMWTEHKSP DGRTYYYNTE 130 140 150 160 170 180 TKQSTWEKPD DLKTPAEQLL SKCPWKEYKS DSGKPYYYNS QTKESRWAKP KELEDLEGYQ 190 200 210 220 230 240 NTIVAGGLIT KSNLHAMIKA EESSKQEECT TASTAPVPTT EIPTTMSTMA AAEAAAAVVA 250 260 270 280 290 300 AAAAAAAAAN ANTSTTPTNT VGSVPVAPEP EVTSIVATAV DNENTVTVST EEQAQLANTT 310 320 330 340 350 360 AIQDLSGDIS SNTGEEPAKQ ETVSDFTPKK EEEESQPAKK TYTWNTKEEA KQAFKELLKE 370 380 390 400 410 420 KRVPSNASWE QAMKMIINDP RYSALAKLSE KKQAFNAYKV QTEKEEKEEA RSKYKEAKES 430 440 450 460 470 480 FQRFLENHEK MTSTTRYKKA EQMFGEMEVW NAISERDRLE IYEDVLFFLS KKEKEQAKQL 490 500 510 520 530 540 RKRNWEALKN ILDNMANVTY STTWSEAQQY LMDNPTFAED EELQNMDKED ALICFEEHIR 550 560 570 580 590 600 ALEKEEEEEK QKTLLRERRR QRKNRESFQI FLDELHEHGQ LHSMSSWMEL YPTISSDIRF 610 620 630 640 650 660 TNMLGQPGST ALDLFKFYVE DLKARYHDEK KIIKDILKDK GFVVEVNTTF EDFVAIISST 670 680 690 700 710 720 KRSTTLDAGN IKLAFNSLLE KAEARERERE KEEARKMKRK ESAFKSMLKQ ATPPIELDAV 730 740 750 760 770 780 WEDIRERFVK EPAFEDITLE SERKRIFKDF MHVLEHECQH HHSKNKKHSK KSKKHHRKRS 790 800 810 820 830 840 RSRSGSESDD DDSHSKKKRQ RSESHSASER SSSAESERSY KKSKKHKKKS KKRRHKSDSP 850 860 870 880 890 900 ESDTEREKDK KEKDRDSEKD RSRQRSESKH KSPKKKTGKD SGNWDTSGSE LSEGELEKRR 910 RTLLEQLDDD Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"FBP11, a mammalian ortholog of the essential yeast splicing factor PRP40." Bedford M.T., Das R., Reed R., Leder P. Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-380 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 647-953. Strain: C57BL/6J and NOD. Tissue: Aorta, Embryonic spinal ganglion, Thymus and Vein.
[3]	"Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains." Chan D.C., Bedford M.T., Leder P. EMBO J. 15:1045-1054(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 146-212, INTERACTION WITH FORMIN. Strain: FVB.
[4]	"FBP WW domains and the Abl SH3 domain bind to a specific class of proline-rich ligands." Bedford M.T., Chan D.C., Leder P. EMBO J. 16:2376-2383(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SF1; SRPK1; CARD8; ATBF1 AND MECP2.
[5]	"FBP11 regulates nuclear localization of N-WASP and inhibits N-WASP-dependent microspike formation." Mizutani K., Suetsugu S., Takenawa T. Biochem. Biophys. Res. Commun. 313:468-474(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH WASL.
[6]	"Interaction of the nuclear matrix protein NAKAP with HypA and huntingtin: implications for nuclear toxicity in Huntington's disease pathogenesis." Sayer J.A., Manczak M., Akileswaran L., Reddy P.H., Coghlan V.M. NeuroMolecular Med. 7:297-310(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AKAP8L, SUBCELLULAR LOCATION.
[7]	"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells." Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D. J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-928; SER-929; SER-931 AND SER-934, MASS SPECTROMETRY. Tissue: Teratocarcinoma.
[8]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-934, MASS SPECTROMETRY. Tissue: Liver.
[9]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-824; SER-826; SER-828; SER-830; SER-879; SER-881 AND SER-884, MASS SPECTROMETRY. Tissue: Melanoma.
[10]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-928; SER-929; SER-931 AND SER-934, MASS SPECTROMETRY. Tissue: Macrophage.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF135439 mRNA. Translation: AAD39463.1. AK041205 mRNA. Translation: BAC30863.1. AK051375 mRNA. Translation: BAC34617.1. AK087963 mRNA. Translation: BAC40061.2. U40747 mRNA. Translation: AAC52475.1.
IPI	IPI00284213. IPI00338887.
PIR	S64713.
RefSeq	NP_061255.1. NM_018785.2.
UniGene	Mm.257474. Mm.392945. Mm.393219.
3D structure databases
ProteinModelPortal	Q9R1C7.
SMR	Q9R1C7. Positions 133-222, 378-446, 739-802.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9R1C7. 2 interactions.
STRING	10090.ENSMUSP00000075655.
PTM databases
PhosphoSite	Q9R1C7.
Proteomic databases
PaxDb	Q9R1C7.
PRIDE	Q9R1C7.
Protocols and materials databases
DNASU	56194.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000076313; ENSMUSP00000075655; ENSMUSG00000061136.
GeneID	56194.
KEGG	mmu:56194.
Organism-specific databases
CTD	55660.
MGI	MGI:1860512. Prpf40a.
Phylogenomic databases
eggNOG	COG5104.
GeneTree	ENSGT00530000062987.
HOGENOM	HOG000231802.
HOVERGEN	HBG059634.
InParanoid	Q9R1C7.
KO	K12821.
OMA	QETVADF.
OrthoDB	EOG418BN6.
Gene expression databases
ArrayExpress	Q9R1C7.
Bgee	Q9R1C7.
Genevestigator	Q9R1C7.
GermOnline	ENSMUSG00000061136. Mus musculus.
Family and domain databases
Gene3D	1.10.10.440. 4 hits.
InterPro	IPR002713. FF_domain. IPR001202. WW_dom. [Graphical view]
Pfam	PF01846. FF. 5 hits. PF00397. WW. 2 hits. [Graphical view]
SMART	SM00441. FF. 5 hits. SM00456. WW. 2 hits. [Graphical view]
SUPFAM	SSF81698. FF. 4 hits. SSF51045. WW_Rsp5_WWP. 2 hits.
PROSITE	PS01159. WW_DOMAIN_1. 2 hits. PS50020. WW_DOMAIN_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	312006.
SOURCE	Search...

Entry information

Entry name

PR40A_MOUSE

Accession

Primary (citable) accession number: Q9R1C7
Secondary accession number(s): Q61049 , Q8BQ76, Q8BRW4, Q8C2U1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 22, 2003
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program