PROF2_MOUSE
ID PROF2_MOUSE Reviewed; 140 AA.
AC Q9JJV2; Q3TPT7; Q3V171; Q9ES48; Q9ES49; Q9ES50;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Profilin-2;
DE AltName: Full=Profilin II;
GN Name=Pfn2;
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 [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=11034907; DOI=10.1242/jcs.113.21.3795;
RA Di Nardo A., Gareus R., Kwiatkowski D., Witke W.;
RT "Alternative splicing of the mouse profilin II gene generates functionally
RT different profilin isoforms.";
RL J. Cell Sci. 113:3795-3803(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11027290; DOI=10.1128/mcb.20.21.8209-8219.2000;
RA Lambrechts A., Braun A., Jonckheere V., Aszodi A., Lanier L.M., Robbens J.,
RA Van Colen I., Vandekerckhove J., Faessler R., Ampe C.;
RT "Profilin II is alternatively spliced, resulting in profilin isoforms that
RT are differentially expressed and have distinct biochemical properties.";
RL Mol. Cell. Biol. 20:8209-8219(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Hippocampus, 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP PROTEIN SEQUENCE OF 55-69; 76-89 AND 92-105, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [6]
RP INTERACTION WITH PFN2.
RX PubMed=19403918; DOI=10.1177/1087057109332594;
RA Veniere S., Ampe C., Vandekerckhove J., Lambrechts A.;
RT "The interaction of proline-rich ligands with profilin probed with an
RT enzyme-linked immunosorbent assay.";
RL J. Biomol. Screen. 14:350-359(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, 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: Binds to actin and affects the structure of the cytoskeleton.
CC At high concentrations, profilin prevents the polymerization of actin,
CC whereas it enhances it at low concentrations. By binding to PIP2, it
CC inhibits the formation of IP3 and DG.
CC -!- SUBUNIT: Occurs in many kinds of cells as a complex with monomeric
CC actin in a 1:1 ratio (By similarity). Interacts with PFN2
CC (PubMed:19403918). {ECO:0000250|UniProtKB:P35080,
CC ECO:0000269|PubMed:19403918}.
CC -!- INTERACTION:
CC Q9JJV2-1; P39053: Dnm1; NbExp=2; IntAct=EBI-990256, EBI-397785;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=IIa;
CC IsoId=Q9JJV2-1; Sequence=Displayed;
CC Name=2; Synonyms=IIb;
CC IsoId=Q9JJV2-2; Sequence=VSP_005218;
CC Name=3;
CC IsoId=Q9JJV2-3; Sequence=VSP_024736;
CC -!- TISSUE SPECIFICITY: Isoform IIa is the main isoform and is abundant in
CC brain. Isoform IIb is a minor isoform.
CC -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR EMBL; AJ272203; CAB87382.1; -; mRNA.
DR EMBL; AF237680; AAG09753.1; -; Genomic_DNA.
DR EMBL; AF237680; AAG09755.1; -; Genomic_DNA.
DR EMBL; AF237680; AAG09756.1; -; Genomic_DNA.
DR EMBL; AK132651; BAE21281.1; -; mRNA.
DR EMBL; AK164145; BAE37648.1; -; mRNA.
DR EMBL; BC024363; AAH24363.1; -; mRNA.
DR CCDS; CCDS17364.1; -. [Q9JJV2-1]
DR RefSeq; NP_062283.1; NM_019410.3. [Q9JJV2-1]
DR PDB; 2V8C; X-ray; 1.98 A; A=1-140.
DR PDB; 2V8F; X-ray; 1.10 A; A/B=1-140.
DR PDBsum; 2V8C; -.
DR PDBsum; 2V8F; -.
DR AlphaFoldDB; Q9JJV2; -.
DR BMRB; Q9JJV2; -.
DR SMR; Q9JJV2; -.
DR BioGRID; 202127; 26.
DR CORUM; Q9JJV2; -.
DR IntAct; Q9JJV2; 5.
DR MINT; Q9JJV2; -.
DR STRING; 10090.ENSMUSP00000068890; -.
DR iPTMnet; Q9JJV2; -.
DR PhosphoSitePlus; Q9JJV2; -.
DR SwissPalm; Q9JJV2; -.
DR REPRODUCTION-2DPAGE; Q9JJV2; -.
DR UCD-2DPAGE; Q9JJV2; -.
DR EPD; Q9JJV2; -.
DR jPOST; Q9JJV2; -.
DR MaxQB; Q9JJV2; -.
DR PaxDb; Q9JJV2; -.
DR PeptideAtlas; Q9JJV2; -.
DR PRIDE; Q9JJV2; -.
DR ProteomicsDB; 291596; -. [Q9JJV2-1]
DR ProteomicsDB; 291597; -. [Q9JJV2-2]
DR ProteomicsDB; 291598; -. [Q9JJV2-3]
DR Antibodypedia; 33583; 265 antibodies from 31 providers.
DR DNASU; 18645; -.
DR Ensembl; ENSMUST00000066882; ENSMUSP00000068890; ENSMUSG00000027805. [Q9JJV2-1]
DR Ensembl; ENSMUST00000119344; ENSMUSP00000112391; ENSMUSG00000027805. [Q9JJV2-3]
DR Ensembl; ENSMUST00000122210; ENSMUSP00000113526; ENSMUSG00000027805. [Q9JJV2-3]
DR GeneID; 18645; -.
DR KEGG; mmu:18645; -.
DR UCSC; uc008phm.1; mouse. [Q9JJV2-1]
DR CTD; 5217; -.
DR MGI; MGI:97550; Pfn2.
DR VEuPathDB; HostDB:ENSMUSG00000027805; -.
DR eggNOG; KOG1755; Eukaryota.
DR GeneTree; ENSGT00940000153664; -.
DR HOGENOM; CLU_123405_1_0_1; -.
DR InParanoid; Q9JJV2; -.
DR OMA; CCLEAAI; -.
DR OrthoDB; 1428600at2759; -.
DR PhylomeDB; Q9JJV2; -.
DR TreeFam; TF331744; -.
DR Reactome; R-MMU-376176; Signaling by ROBO receptors.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR BioGRID-ORCS; 18645; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Pfn2; mouse.
DR EvolutionaryTrace; Q9JJV2; -.
DR PRO; PR:Q9JJV2; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9JJV2; protein.
DR Bgee; ENSMUSG00000027805; Expressed in medial ganglionic eminence and 258 other tissues.
DR ExpressionAtlas; Q9JJV2; baseline and differential.
DR Genevisible; Q9JJV2; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0003785; F:actin monomer binding; ISO:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0098885; P:modification of postsynaptic actin cytoskeleton; IDA:SynGO.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; ISO:MGI.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; IMP:UniProtKB.
DR GO; GO:1900028; P:negative regulation of ruffle assembly; IMP:UniProtKB.
DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; ISO:MGI.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:MGI.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISO:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR CDD; cd00148; PROF; 1.
DR InterPro; IPR005455; PFN.
DR InterPro; IPR029891; PFN2.
DR InterPro; IPR036140; PFN_sf.
DR InterPro; IPR005454; Profilin1/2/3_vertebrate.
DR InterPro; IPR027310; Profilin_CS.
DR PANTHER; PTHR13936:SF15; PTHR13936:SF15; 1.
DR Pfam; PF00235; Profilin; 1.
DR PRINTS; PR00392; PROFILIN.
DR PRINTS; PR01639; PROFILINMAML.
DR SMART; SM00392; PROF; 1.
DR SUPFAM; SSF55770; SSF55770; 1.
DR PROSITE; PS00414; PROFILIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P35080"
FT CHAIN 2..140
FT /note="Profilin-2"
FT /id="PRO_0000199576"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P35080"
FT VAR_SEQ 1..49
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024736"
FT VAR_SEQ 109..140
FT /note="VLVFVMGKEGVHGGGLNKKAYSMAKYLRDSGF -> ALVIVMGKEGVHAGTI
FT NKKTYELALYLKRSVTNLYLAS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11034907"
FT /id="VSP_005218"
FT CONFLICT 36
FT /note="A -> G (in Ref. 2; AAG09753/AAG09756)"
FT /evidence="ECO:0000305"
FT HELIX 5..12
FT /evidence="ECO:0007829|PDB:2V8F"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:2V8F"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:2V8F"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:2V8F"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2V8F"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:2V8F"
FT HELIX 58..62
FT /evidence="ECO:0007829|PDB:2V8F"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:2V8F"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:2V8F"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:2V8F"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:2V8F"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2V8F"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:2V8F"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:2V8F"
FT HELIX 121..137
FT /evidence="ECO:0007829|PDB:2V8F"
SQ SEQUENCE 140 AA; 15032 MW; E780BF62E9EC8476 CRC64;
MAGWQSYVDN LMCDGCCQEA AIVGYCDAKY VWAATAGGVF QSITPVEIDM IVGKDREGFF
TNGLTLGAKK CSVIRDSLYV DGDCTMDIRT KSQGGEPTYN VAVGRAGRVL VFVMGKEGVH
GGGLNKKAYS MAKYLRDSGF
