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Q99JB8

- PACN3_MOUSE

UniProt

Q99JB8 - PACN3_MOUSE

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Protein
Protein kinase C and casein kinase II substrate protein 3
Gene
Pacsin3
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  1. calcium channel inhibitor activity Source: UniProtKB
  2. cytoskeletal protein binding Source: MGI
  3. lipid binding Source: UniProtKB
  4. protein binding Source: UniProtKB

GO - Biological processi

  1. endocytosis Source: UniProtKB-KW
  2. membrane tubulation Source: UniProtKB
  3. negative regulation of calcium ion transport Source: UniProtKB
  4. negative regulation of endocytosis Source: UniProtKB
  5. positive regulation of membrane protein ectodomain proteolysis Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase C and casein kinase II substrate protein 3
Gene namesi
Name:Pacsin3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1891410. Pacsin3.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi415 – 4151P → L: Loss of DNM1-, SYNJ1- and WASL-binding. Loss of effect on transferrin endocytosis. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 424424Protein kinase C and casein kinase II substrate protein 3
PRO_0000161801Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei276 – 2761Phosphoserine By similarity
Modified residuei319 – 3191Phosphoserine By similarity
Modified residuei324 – 3241Phosphothreonine By similarity
Modified residuei327 – 3271Phosphoserine By similarity
Modified residuei354 – 3541Phosphoserine2 Publications
Modified residuei383 – 3831Phosphoserine By similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ99JB8.
PaxDbiQ99JB8.
PRIDEiQ99JB8.

PTM databases

PhosphoSiteiQ99JB8.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiQ99JB8.
BgeeiQ99JB8.
GenevestigatoriQ99JB8.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ99JB8. 4 interactions.
MINTiMINT-1850676.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni19 – 224
Helixi23 – 7048
Helixi75 – 10329
Helixi105 – 11713
Beta strandi122 – 1265
Helixi127 – 17044
Beta strandi186 – 1905
Turni191 – 1933
Helixi194 – 25360
Helixi255 – 2573
Helixi259 – 27416
Helixi277 – 28812
Beta strandi289 – 2924

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3M3WX-ray2.60A/B1-320[»]
3QE6X-ray2.60A/B1-304[»]
3SYVX-ray3.10A/B/C/D/E/F/G/H1-341[»]
ProteinModelPortaliQ99JB8.
SMRiQ99JB8. Positions 12-302, 324-420.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 7364FCH
Add
BLAST
Domaini363 – 42462SH3
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 304304F-BAR domain
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili23 – 2722501 Publication
Add
BLAST

Domaini

The F-BAR domain forms a coiled coil and mediates membrane-binding and membrane tubulation.1 Publication

Sequence similaritiesi

Belongs to the PACSIN family.
Contains 1 FCH domain.
Contains 1 SH3 domain.

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiNOG283356.
GeneTreeiENSGT00510000046376.
HOGENOMiHOG000007245.
HOVERGENiHBG053486.
InParanoidiQ99JB8.
OMAiEQAFESC.
PhylomeDBiQ99JB8.
TreeFamiTF313677.

Family and domain databases

InterProiIPR001060. FCH_dom.
IPR028523. PACSIN3.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10959:SF1. PTHR10959:SF1. 1 hit.
PfamiPF00611. FCH. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99JB8-1 [UniParc]FASTAAdd to Basket

« Hide

MAPEEDAGGE VLGGSFWEAG NYRRTVQRVE DGHRLCGDLV SCFQERARIE    50
KAYAQQLADW ARKWRGAVEK GPQYGTLEKA WHAFFTAAER LSELHLEVRE 100
KLHGPDSERV RTWQRGAFHR PVLGGFRESR AAEDGFRKAQ KPWLKRLKEV 150
EASKKSYHTA RKDEKTAQTR ESHAKADSSM SQEQLRKLQE RVGRCTKEAE 200
KMKTQYEQTL AELNRYTPRY MEDMEQAFES CQAAERQRLL FFKDVLLTLH 250
QHLDLSSSDK FHELHRDLQQ SIEAASDEED LRWWRSTHGP GMAMNWPQFE 300
EWSLDTQRAI SRKEKGGRSP DEVTLTSIVP TRDGTAPPPQ SPSSPGSGQD 350
EDWSDEESPR KVATGVRVRA LYDYAGQEAD ELSFRAGEEL LKMSEEDEQG 400
WCQGQLQSGR IGLYPANYVE CVGA 424
Length:424
Mass (Da):48,585
Last modified:June 1, 2001 - v1
Checksum:i00475BC0321485B7
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti360 – 3601R → G in AAG31022. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF149824 mRNA. Translation: AAG31022.1.
AF242531 mRNA. Translation: AAK29208.1.
BC003884 mRNA. Translation: AAH03884.1.
CCDSiCCDS16429.1.
RefSeqiNP_001276606.1. NM_001289677.1.
NP_001276607.1. NM_001289678.1.
NP_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.
UniGeneiMm.236650.

Genome annotation databases

EnsembliENSMUST00000028694; ENSMUSP00000028694; ENSMUSG00000027257.
ENSMUST00000059566; ENSMUSP00000054391; ENSMUSG00000027257.
ENSMUST00000111349; ENSMUSP00000106981; ENSMUSG00000027257.
ENSMUST00000168916; ENSMUSP00000129175; ENSMUSG00000027257.
GeneIDi80708.
KEGGimmu:80708.
UCSCiuc008kvn.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF149824 mRNA. Translation: AAG31022.1 .
AF242531 mRNA. Translation: AAK29208.1 .
BC003884 mRNA. Translation: AAH03884.1 .
CCDSi CCDS16429.1.
RefSeqi NP_001276606.1. NM_001289677.1.
NP_001276607.1. NM_001289678.1.
NP_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.
UniGenei Mm.236650.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3M3W X-ray 2.60 A/B 1-320 [» ]
3QE6 X-ray 2.60 A/B 1-304 [» ]
3SYV X-ray 3.10 A/B/C/D/E/F/G/H 1-341 [» ]
ProteinModelPortali Q99JB8.
SMRi Q99JB8. Positions 12-302, 324-420.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q99JB8. 4 interactions.
MINTi MINT-1850676.

PTM databases

PhosphoSitei Q99JB8.

Proteomic databases

MaxQBi Q99JB8.
PaxDbi Q99JB8.
PRIDEi Q99JB8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028694 ; ENSMUSP00000028694 ; ENSMUSG00000027257 .
ENSMUST00000059566 ; ENSMUSP00000054391 ; ENSMUSG00000027257 .
ENSMUST00000111349 ; ENSMUSP00000106981 ; ENSMUSG00000027257 .
ENSMUST00000168916 ; ENSMUSP00000129175 ; ENSMUSG00000027257 .
GeneIDi 80708.
KEGGi mmu:80708.
UCSCi uc008kvn.2. mouse.

Organism-specific databases

CTDi 29763.
MGIi MGI:1891410. Pacsin3.

Phylogenomic databases

eggNOGi NOG283356.
GeneTreei ENSGT00510000046376.
HOGENOMi HOG000007245.
HOVERGENi HBG053486.
InParanoidi Q99JB8.
OMAi EQAFESC.
PhylomeDBi Q99JB8.
TreeFami TF313677.

Miscellaneous databases

NextBioi 350063.
PROi Q99JB8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q99JB8.
Bgeei Q99JB8.
Genevestigatori Q99JB8.

Family and domain databases

InterProi IPR001060. FCH_dom.
IPR028523. PACSIN3.
IPR001452. SH3_domain.
[Graphical view ]
PANTHERi PTHR10959:SF1. PTHR10959:SF1. 1 hit.
Pfami PF00611. FCH. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view ]
PRINTSi PR00452. SH3DOMAIN.
SMARTi SM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiPACN3_MOUSE
AccessioniPrimary (citable) accession number: Q99JB8
Secondary accession number(s): Q9EQP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 110 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

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi