Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Profilin-3

Gene

Pfn3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Binds to actin and affects the structure of the cytoskeleton. Binds to poly-L-proline, phosphatidylinositol 3-phosphate (PtdIns3P), phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol 4-phosphate (PtdIns4P). Slightly reduces actin polymerization. May be involved in spermatogenesis.By similarity

GO - Molecular functioni

  • actin binding Source: MGI
  • ATP:ADP antiporter activity Source: MGI
  • lipid binding Source: UniProtKB-KW

GO - Biological processi

  • actin cytoskeleton organization Source: InterPro
  • ADP transport Source: GOC
  • ATP transport Source: GOC
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Profilin-3
Alternative name(s):
Profilin III
Gene namesi
Name:Pfn3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:2178800. Pfn3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 137137Profilin-3PRO_0000199580Add
BLAST

Proteomic databases

PaxDbiQ9DAD6.
PRIDEiQ9DAD6.

PTM databases

PhosphoSiteiQ9DAD6.

Expressioni

Tissue specificityi

Testis specific.1 Publication

Gene expression databases

BgeeiQ9DAD6.
CleanExiMM_PFN3.
GenevisibleiQ9DAD6. MM.

Interactioni

Subunit structurei

Interacts with ACTRT3.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Actrt3Q8BXF83EBI-6480328,EBI-6480313

Protein-protein interaction databases

IntActiQ9DAD6. 1 interaction.
MINTiMINT-6741638.
STRINGi10090.ENSMUSP00000054053.

Structurei

3D structure databases

ProteinModelPortaliQ9DAD6.
SMRiQ9DAD6. Positions 4-133.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the profilin family.Curated

Phylogenomic databases

eggNOGiNOG147630.
GeneTreeiENSGT00390000010143.
HOGENOMiHOG000171592.
HOVERGENiHBG053683.
InParanoidiQ9DAD6.
KOiK05759.
OMAiRRCCVIR.
OrthoDBiEOG7HXCSV.
PhylomeDBiQ9DAD6.
TreeFamiTF331744.

Family and domain databases

InterProiIPR005455. PFN.
IPR029893. PFN3.
IPR005454. Profilin1/2/3_vertebrate.
[Graphical view]
PANTHERiPTHR13936:SF2. PTHR13936:SF2. 1 hit.
PfamiPF00235. Profilin. 1 hit.
[Graphical view]
PRINTSiPR01639. PROFILINMAML.
SUPFAMiSSF55770. SSF55770. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9DAD6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDWKGYISA VLRDQRIDDV AIVGHSDNRC VWASRPGGLL AAISPQEVGV
60 70 80 90 100
LTGPDRHTFL QTGLSVAGRR CCVIRDYLLA EGDGVLDART KGLDGRAICV
110 120 130
GHTPRALLVL MGRRGVHGGI LNKTVHDLIG GLREQCS
Length:137
Mass (Da):14,697
Last modified:June 1, 2001 - v1
Checksum:i939E617834F71BC8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF422809 Genomic DNA. Translation: AAL65908.1.
AK005930 mRNA. Translation: BAB24322.1.
BC048629 mRNA. Translation: AAH48629.1.
CCDSiCCDS26545.1.
RefSeqiNP_083579.1. NM_029303.2.
UniGeneiMm.432537.
Mm.473625.

Genome annotation databases

EnsembliENSMUST00000054146; ENSMUSP00000054053; ENSMUSG00000044444.
GeneIDi75477.
KEGGimmu:75477.
UCSCiuc007qqu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF422809 Genomic DNA. Translation: AAL65908.1.
AK005930 mRNA. Translation: BAB24322.1.
BC048629 mRNA. Translation: AAH48629.1.
CCDSiCCDS26545.1.
RefSeqiNP_083579.1. NM_029303.2.
UniGeneiMm.432537.
Mm.473625.

3D structure databases

ProteinModelPortaliQ9DAD6.
SMRiQ9DAD6. Positions 4-133.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9DAD6. 1 interaction.
MINTiMINT-6741638.
STRINGi10090.ENSMUSP00000054053.

PTM databases

PhosphoSiteiQ9DAD6.

Proteomic databases

PaxDbiQ9DAD6.
PRIDEiQ9DAD6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000054146; ENSMUSP00000054053; ENSMUSG00000044444.
GeneIDi75477.
KEGGimmu:75477.
UCSCiuc007qqu.1. mouse.

Organism-specific databases

CTDi345456.
MGIiMGI:2178800. Pfn3.

Phylogenomic databases

eggNOGiNOG147630.
GeneTreeiENSGT00390000010143.
HOGENOMiHOG000171592.
HOVERGENiHBG053683.
InParanoidiQ9DAD6.
KOiK05759.
OMAiRRCCVIR.
OrthoDBiEOG7HXCSV.
PhylomeDBiQ9DAD6.
TreeFamiTF331744.

Miscellaneous databases

NextBioi343120.
PROiQ9DAD6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DAD6.
CleanExiMM_PFN3.
GenevisibleiQ9DAD6. MM.

Family and domain databases

InterProiIPR005455. PFN.
IPR029893. PFN3.
IPR005454. Profilin1/2/3_vertebrate.
[Graphical view]
PANTHERiPTHR13936:SF2. PTHR13936:SF2. 1 hit.
PfamiPF00235. Profilin. 1 hit.
[Graphical view]
PRINTSiPR01639. PROFILINMAML.
SUPFAMiSSF55770. SSF55770. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic organization of profilin-III and evidence for a transcript expressed exclusively in testis."
    Braun A., Aszodi A., Hellebrand H., Berna A., Fassler R., Brandau O.
    Gene 283:219-225(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    Strain: 129/Sv.
  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: Testis.
  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: Testis.
  4. "Nuclear localization of profilin III-ArpM1 complex in mouse spermiogenesis."
    Hara Y., Yamagata K., Oguchi K., Baba T.
    FEBS Lett. 582:2998-3004(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ACTRT3.

Entry informationi

Entry nameiPROF3_MOUSE
AccessioniPrimary (citable) accession number: Q9DAD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: June 1, 2001
Last modified: June 24, 2015
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.