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Q99JB8 (PACN3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein kinase C and casein kinase II substrate protein 3
Gene names
Name:Pacsin3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in endocytosis and regulates internalization of plasma membrane proteins. Overexpression impairs internalization of SLC2A1/GLUT1 and TRPV4 and increases the levels of SLC2A1/GLUT1 and TRPV4 at the cell membrane. Inhibits the TRPV4 calcium channel activity. Ref.1 Ref.4 Ref.5 Ref.7

Subunit structure

Homodimer. May form heterooligomers with other PACSINs. Interacts (via SH3 domain) with DNM1, SYNJ1 and WASL. Interacts with TRPV4. Ref.1 Ref.4 Ref.7 Ref.9

Subcellular location

Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note: Detected at the inner aspect of the plasma membrane in myotubes. Ref.1

Tissue specificity

Highly expressed in skeletal muscle, heart and lung; also detected in brain, kidney and uterus (at protein level). Ref.1

Domain

The F-BAR domain forms a coiled coil and mediates membrane-binding and membrane tubulation. Ref.9

Post-translational modification

Phosphorylated by casein kinase 2 (CK2) and protein kinase C (PKC) Probable.

Sequence similarities

Belongs to the PACSIN family.

Contains 1 FCH domain.

Contains 1 SH3 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 424424Protein kinase C and casein kinase II substrate protein 3
PRO_0000161801

Regions

Domain10 – 7364FCH
Domain363 – 42462SH3
Region1 – 304304F-BAR domain
Coiled coil23 – 272250 Ref.9

Amino acid modifications

Modified residue2761Phosphoserine By similarity
Modified residue3191Phosphoserine By similarity
Modified residue3241Phosphothreonine By similarity
Modified residue3271Phosphoserine By similarity
Modified residue3541Phosphoserine Ref.6 Ref.8
Modified residue3831Phosphoserine By similarity

Experimental info

Mutagenesis4151P → L: Loss of DNM1-, SYNJ1- and WASL-binding. Loss of effect on transferrin endocytosis. Ref.1
Sequence conflict3601R → G in AAG31022. Ref.1

Secondary structure

...................... 424
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q99JB8 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 00475BC0321485B7

FASTA42448,585
        10         20         30         40         50         60 
MAPEEDAGGE VLGGSFWEAG NYRRTVQRVE DGHRLCGDLV SCFQERARIE KAYAQQLADW 

        70         80         90        100        110        120 
ARKWRGAVEK GPQYGTLEKA WHAFFTAAER LSELHLEVRE KLHGPDSERV RTWQRGAFHR 

       130        140        150        160        170        180 
PVLGGFRESR AAEDGFRKAQ KPWLKRLKEV EASKKSYHTA RKDEKTAQTR ESHAKADSSM 

       190        200        210        220        230        240 
SQEQLRKLQE RVGRCTKEAE KMKTQYEQTL AELNRYTPRY MEDMEQAFES CQAAERQRLL 

       250        260        270        280        290        300 
FFKDVLLTLH QHLDLSSSDK FHELHRDLQQ SIEAASDEED LRWWRSTHGP GMAMNWPQFE 

       310        320        330        340        350        360 
EWSLDTQRAI SRKEKGGRSP DEVTLTSIVP TRDGTAPPPQ SPSSPGSGQD EDWSDEESPR 

       370        380        390        400        410        420 
KVATGVRVRA LYDYAGQEAD ELSFRAGEEL LKMSEEDEQG WCQGQLQSGR IGLYPANYVE 


CVGA 

« Hide

References

« Hide 'large scale' references
[1]"All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis."
Modregger J., Ritter B., Witter B., Paulsson M., Plomann M.
J. Cell Sci. 113:4511-4521(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH DNM1; SYNJ1 AND WASL, HOMOOLIGOMERIZATION, HETEROOLIGOMERIZATION WITH PACSIN1 AND PACSIN2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF PRO-415.
Strain: C57BL/6J.
[2]"PACSIN 3 is a novel SH3 domain cytoplasmic adapter protein of the pacsin-syndapin-FAP52 gene family."
Sumoy L., Pluvinet R., Andreu N., Estivill X., Escarceller M.
Gene 262:199-205(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: Neuron.
[4]"PACSINs bind to the TRPV4 cation channel. PACSIN 3 modulates the subcellular localization of TRPV4."
Cuajungco M.P., Grimm C., Oshima K., D'hoedt D., Nilius B., Mensenkamp A.R., Bindels R.J., Plomann M., Heller S.
J. Biol. Chem. 281:18753-18762(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TRPV4.
[5]"PACSIN3 overexpression increases adipocyte glucose transport through GLUT1."
Roach W., Plomann M.
Biochem. Biophys. Res. Commun. 355:745-750(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"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-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[7]"Stimulus-specific modulation of the cation channel TRPV4 by PACSIN 3."
D'hoedt D., Owsianik G., Prenen J., Cuajungco M.P., Grimm C., Heller S., Voets T., Nilius B.
J. Biol. Chem. 283:6272-6280(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TRPV4.
[8]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[9]"Rigidity of wedge loop in PACSIN 3 protein is a key factor in dictating diameters of tubules."
Bai X., Meng G., Luo M., Zheng X.
J. Biol. Chem. 287:22387-22396(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-320, COILED COIL, SUBUNIT, LIPID-BINDING, DOMAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF149824 mRNA. Translation: AAG31022.1.
AF242531 mRNA. Translation: AAK29208.1.
BC003884 mRNA. Translation: AAH03884.1.
RefSeqNP_083009.1. NM_028733.4.
NP_112019.2. NM_030880.3.
XP_006500486.1. XM_006500423.1.
XP_006500487.1. XM_006500424.1.
XP_006500488.1. XM_006500425.1.
XP_006500489.1. XM_006500426.1.
XP_006500490.1. XM_006500427.1.
XP_006500491.1. XM_006500428.1.
UniGeneMm.236650.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3M3WX-ray2.60A/B1-320[»]
3QE6X-ray2.60A/B1-304[»]
3SYVX-ray3.10A/B/C/D/E/F/G/H1-341[»]
ProteinModelPortalQ99JB8.
SMRQ99JB8. Positions 12-302, 324-420.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ99JB8. 4 interactions.
MINTMINT-1850676.

PTM databases

PhosphoSiteQ99JB8.

Proteomic databases

PaxDbQ99JB8.
PRIDEQ99JB8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028694; ENSMUSP00000028694; ENSMUSG00000027257.
ENSMUST00000059566; ENSMUSP00000054391; ENSMUSG00000027257.
ENSMUST00000111349; ENSMUSP00000106981; ENSMUSG00000027257.
ENSMUST00000168916; ENSMUSP00000129175; ENSMUSG00000027257.
GeneID80708.
KEGGmmu:80708.
UCSCuc008kvn.2. mouse.

Organism-specific databases

CTD29763.
MGIMGI:1891410. Pacsin3.

Phylogenomic databases

eggNOGNOG283356.
GeneTreeENSGT00510000046376.
HOGENOMHOG000007245.
HOVERGENHBG053486.
InParanoidQ99JB8.
OMAEQAFESC.
PhylomeDBQ99JB8.
TreeFamTF313677.

Gene expression databases

ArrayExpressQ99JB8.
BgeeQ99JB8.
GenevestigatorQ99JB8.

Family and domain databases

InterProIPR001060. FCH_dom.
IPR028523. PACSIN3.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR10959:SF1. PTHR10959:SF1. 1 hit.
PfamPF00611. FCH. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio350063.
PROQ99JB8.
SOURCESearch...

Entry information

Entry namePACN3_MOUSE
AccessionPrimary (citable) accession number: Q99JB8
Secondary accession number(s): Q9EQP9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot