P62962 (PROF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Profilin-1

Alternative name(s):
Profilin I

Gene names

Name:

Pfn1

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	140 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR By similarity.
Subunit structure	Interacts with VASP. Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio. Found in a complex with XPO6, Ran, ACTB and PFN1 By similarity. Interacts with HTT By similarity.
Subcellular location	Cytoplasm › cytoskeleton.
Post-translational modification	Phosphorylation at Ser-138 reduces its affinity for G-actin and blocks its interaction with HTT, reducing its ability to inhibit androgen receptor (AR) and HTT aggregation By similarity.
Sequence similarities	Belongs to the profilin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Ligand	Actin-binding
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization Inferred from electronic annotation. Source: InterPro cellular response to growth factor stimulus Inferred from electronic annotation. Source: Compara neural tube closure Inferred from genetic interaction PubMed 10069337. Source: MGI positive regulation of DNA metabolic process Inferred from electronic annotation. Source: Compara positive regulation of stress fiber assembly Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara positive regulation of viral transcription Inferred from electronic annotation. Source: Compara regulation of transcription from RNA polymerase II promoter Inferred from genetic interaction PubMed 15615774. Source: MGI sequestering of actin monomers Traceable author statement PubMed 11274401. Source: MGI
Cellular_component	cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome extracellular region Traceable author statement. Source: Reactome neuron projection Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay PubMed 15615774. Source: MGI synapse Inferred from electronic annotation. Source: Compara
Molecular_function	phosphatidylinositol-4,5-bisphosphate binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 140	139	Profilin-1		PRO_0000199572
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	108	1	N6-acetyllysine By similarity
	Modified residue	129	1	Phosphotyrosine By similarity
	Modified residue	138	1	Phosphoserine; by ROCK1 By similarity
	Cross-link	54		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P62962 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 1DC8B60D545FF70E	FASTA	140	14,957
	10 20 30 40 50 60 MAGWNAYIDS LMADGTCQDA AIVGYKDSPS VWAAVPGKTF VSITPAEVGV LVGKDRSSFF 70 80 90 100 110 120 VNGLTLGGQK CSVIRDSLLQ DGEFTMDLRT KSTGGAPTFN VTVTMTAKTL VLLMGKEGVH 130 140 GGLINKKCYE MASHLRRSQY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Total coding sequence of profilin cDNA from Mus musculus macrophage." Sri Widada J., Ferraz C., Liautard J.P. Nucleic Acids Res. 17:2855-2855(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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]. Strain: C57BL/6J. Tissue: Embryonic liver.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Mammary tumor.
[4]	Lubec G., Klug S. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 39-54; 57-70 AND 76-89, MASS SPECTROMETRY. Tissue: Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X14425 mRNA. Translation: CAA32586.1. AK011066 mRNA. Translation: BAB27373.1. BC002080 mRNA. Translation: AAH02080.1.
IPI	IPI00224740.
PIR	S04067.
RefSeq	NP_035202.1. NM_011072.4.
UniGene	Mm.2647.
3D structure databases
ProteinModelPortal	P62962.
SMR	P62962. Positions 2-140.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-38075N.
IntAct	P62962. 2 interactions.
MINT	MINT-1868701.
PTM databases
PhosphoSite	P62962.
2D gel databases
REPRODUCTION-2DPAGE	IPI00224740. P62962.
Proteomic databases
PaxDb	P62962.
PRIDE	P62962.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000018437; ENSMUSP00000018437; ENSMUSG00000018293.
GeneID	18643.
KEGG	mmu:18643.
UCSC	uc007jvv.2. mouse.
Organism-specific databases
CTD	5216.
MGI	MGI:97549. Pfn1.
Phylogenomic databases
eggNOG	NOG269129.
HOGENOM	HOG000171592.
HOVERGEN	HBG053683.
InParanoid	P62962.
KO	K05759.
OMA	HLRRAQY.
OrthoDB	EOG4SN1Q1.
Enzyme and pathway databases
Reactome	REACT_89750. Hemostasis.
Gene expression databases
ArrayExpress	P62962.
Bgee	P62962.
CleanEx	MM_PFN1.
Genevestigator	P62962.
GermOnline	ENSMUSG00000018293. Mus musculus.
Family and domain databases
InterPro	IPR005454. Profilin_chordates. IPR027310. Profilin_CS. IPR005455. Profilin_eukaryotes/bac. [Graphical view]
Pfam	PF00235. Profilin. 1 hit. [Graphical view]
PRINTS	PR01639. PROFILINMAML.
SMART	SM00392. PROF. 1 hit. [Graphical view]
SUPFAM	SSF55770. Profilin. 1 hit.
PROSITE	PS00414. PROFILIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	294634.
SOURCE	Search...

Entry information

Entry name

PROF1_MOUSE

Accession

Primary (citable) accession number: P62962
Secondary accession number(s): P10924

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program