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Q9Y6V0 · PCLO_HUMAN

  • Protein
    Protein piccolo
  • Gene
    PCLO
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Scaffold protein of the presynaptic cytomatrix at the active zone (CAZ) which is the place in the synapse where neurotransmitter is released (By similarity).
After synthesis, participates in the formation of Golgi-derived membranous organelles termed Piccolo-Bassoon transport vesicles (PTVs) that are transported along axons to sites of nascent synaptic contacts (By similarity).
At the presynaptic active zone, regulates the spatial organization of synaptic vesicle cluster, the protein complexes that execute membrane fusion and compensatory endocytosis (By similarity).
Organizes as well the readily releasable pool of synaptic vesicles and safeguards a fraction of them to be not immediately available for action potential-induced release (By similarity).
Functions also in processes other than assembly such as the regulation of specific presynaptic protein ubiquitination by interacting with SIAH1 or the regulation of presynaptic autophagy (By similarity).
Mediates also synapse to nucleus communication leading to reconfiguration of gene expression by associating with the transcriptional corepressor CTBP1 and by subsequently reducing the size of its pool available for nuclear import (By similarity).

Cofactor

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Binds 3 Ca2+ ions per C2 domain.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site4723Ca2+ 1 (UniProtKB | ChEBI)
Binding site4723Ca2+ 2 (UniProtKB | ChEBI)
Binding site4729Ca2+ 1 (UniProtKB | ChEBI)
Binding site4793Ca2+ 1 (UniProtKB | ChEBI)
Binding site4793Ca2+ 2 (UniProtKB | ChEBI)
Binding site4795Ca2+ 1 (UniProtKB | ChEBI)
Binding site4795Ca2+ 2 (UniProtKB | ChEBI)
Binding site4795Ca2+ 3 (UniProtKB | ChEBI)
Binding site4798Ca2+ 3 (UniProtKB | ChEBI)
Binding site4801Ca2+ 2 (UniProtKB | ChEBI)
Binding site4801Ca2+ 3 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentaxon
Cellular Componentcytoskeleton
Cellular Componentcytoskeleton of presynaptic active zone
Cellular Componentextracellular exosome
Cellular ComponentGABA-ergic synapse
Cellular Componentglutamatergic synapse
Cellular Componentpostsynaptic density
Cellular Componentsynapse
Molecular Functioncalcium ion binding
Molecular Functioncalcium-dependent phospholipid binding
Molecular Functionprofilin binding
Molecular Functionstructural constituent of presynaptic active zone
Biological Processcytoskeleton organization
Biological Processinsulin secretion
Biological Processpresynaptic actin cytoskeleton organization
Biological Processpresynaptic active zone assembly
Biological Processprotein localization to synapse
Biological Processregulation of exocytosis
Biological Processsynaptic vesicle clustering
Biological Processsynaptic vesicle exocytosis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein piccolo
  • Alternative names
    • Aczonin

Gene names

    • Name
      PCLO
    • Synonyms
      ACZ
      , KIAA0559

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9Y6V0
  • Secondary accessions
    • A4D1A7
    • A6NNX9
    • O43373
    • O60305
    • Q08E72

Proteomes

Organism-specific databases

Subcellular Location

Disease & Variants

Involvement in disease

Pontocerebellar hypoplasia 3 (PCH3)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A form of pontocerebellar hypoplasia, a disorder characterized by structural defects of the pons and cerebellum. Brain MRI shows an abnormally small cerebellum and brainstem, decreased cerebral white matter, and a thin corpus callosum. PCH3 features include seizures, short stature, optic atrophy, progressive microcephaly, severe developmental delay.
  • See also
    MIM:608027

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_0569592671in dbSNP:rs10261848
Natural variantVAR_0569602804in dbSNP:rs976714

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 6,934 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue (large scale data), modified residue.

Type
IDPosition(s)Source
Description
ChainPRO_00000582501-5142UniProtProtein piccolo
Modified residue (large scale data)429PRIDEPhosphoserine
Modified residue (large scale data)656PRIDEPhosphoserine
Modified residue906UniProtPhosphoserine
Modified residue918UniProtPhosphoserine
Modified residue922UniProtPhosphothreonine
Modified residue1356UniProtPhosphoserine
Modified residue1366UniProtPhosphoserine
Modified residue1367UniProtPhosphoserine
Modified residue1396UniProtPhosphoserine
Modified residue1398UniProtPhosphoserine
Modified residue1401UniProtPhosphoserine
Modified residue1402UniProtPhosphoserine
Modified residue1405UniProtPhosphoserine
Modified residue (large scale data)1405PRIDEPhosphoserine
Modified residue (large scale data)1442PRIDEPhosphoserine
Modified residue1516UniProtPhosphoserine
Modified residue (large scale data)1516PRIDEPhosphoserine
Modified residue1517UniProtPhosphoserine
Modified residue (large scale data)1517PRIDEPhosphoserine
Modified residue1519UniProtPhosphoserine
Modified residue1522UniProtPhosphoserine
Modified residue (large scale data)1522PRIDEPhosphoserine
Modified residue1546UniProtPhosphoserine
Modified residue1549UniProtPhosphoserine
Modified residue (large scale data)1549PRIDEPhosphoserine
Modified residue1570UniProtPhosphoserine
Modified residue1572UniProtPhosphoserine
Modified residue1617UniProtPhosphothreonine
Modified residue1618UniProtPhosphoserine
Modified residue1628UniProtPhosphoserine
Modified residue (large scale data)1628PRIDEPhosphoserine
Modified residue1640UniProtPhosphoserine
Modified residue (large scale data)1640PRIDEPhosphoserine
Modified residue1703UniProtPhosphoserine
Modified residue1705UniProtPhosphothreonine
Modified residue1707UniProtPhosphoserine
Modified residue1712UniProtPhosphoserine
Modified residue1773UniProtPhosphoserine
Modified residue1774UniProtPhosphoserine
Modified residue1825UniProtPhosphothreonine
Modified residue (large scale data)1825PRIDEPhosphothreonine
Modified residue1831UniProtPhosphoserine
Modified residue (large scale data)1831PRIDEPhosphoserine
Modified residue (large scale data)1837PRIDEPhosphoserine
Modified residue1860UniProtPhosphoserine
Modified residue1865UniProtPhosphoserine
Modified residue1873UniProtPhosphoserine
Modified residue1894UniProtPhosphoserine
Modified residue (large scale data)1894PRIDEPhosphoserine
Modified residue2562UniProtPhosphoserine
Modified residue3069UniProtPhosphothreonine
Modified residue3443UniProtPhosphoserine
Modified residue3447UniProtPhosphothreonine
Modified residue (large scale data)3447PRIDEPhosphothreonine
Modified residue3474UniProtPhosphothreonine
Modified residue3577UniProtPhosphoserine
Modified residue3585UniProtPhosphoserine
Modified residue3615UniProtPhosphoserine
Modified residue (large scale data)3615PRIDEPhosphoserine
Modified residue3619UniProtPhosphoserine
Modified residue (large scale data)3619PRIDEPhosphoserine
Modified residue3625UniProtPhosphoserine
Modified residue (large scale data)3625PRIDEPhosphoserine
Modified residue3628UniProtPhosphoserine
Modified residue (large scale data)3628PRIDEPhosphoserine
Modified residue3631UniProtPhosphoserine
Modified residue (large scale data)3631PRIDEPhosphoserine
Modified residue3652UniProtPhosphoserine
Modified residue (large scale data)3652PRIDEPhosphoserine
Modified residue3678UniProtPhosphoserine
Modified residue3680UniProtPhosphoserine
Modified residue (large scale data)3680PRIDEPhosphoserine
Modified residue3686UniProtPhosphoserine
Modified residue (large scale data)3686PRIDEPhosphoserine
Modified residue3835UniProtPhosphoserine
Modified residue4088UniProtPhosphoserine
Modified residue4204UniProtPhosphoserine
Modified residue4358UniProtPhosphoserine
Modified residue4362UniProtPhosphoserine
Modified residue4365UniProtPhosphoserine
Modified residue4394UniProtPhosphoserine
Modified residue (large scale data)4397PRIDEPhosphoserine
Modified residue4430UniProtPhosphoserine
Modified residue4664UniProtPhosphoserine
Modified residue (large scale data)4664PRIDEPhosphoserine
Modified residue (large scale data)4670PRIDEPhosphoserine
Modified residue4778UniProtPhosphoserine
Modified residue (large scale data)4846PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Moderately expressed in the developing cerebral cortex.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with BSN, ERC2/CAST1, RIMS1 and UNC13A (By similarity).
Interacts (via C-terminus) with TRIO (via N-terminus) (By similarity).
Interacts with CTBP1 (By similarity).
Interacts with SIAH1; this interaction negatively regulates SIAH1 E3 ligase activity (By similarity).
Directly interacts with GIT1 and GIT2 (By similarity).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, compositional bias, zinc finger, domain.

Type
IDPosition(s)Description
Region1-154Disordered
Compositional bias109-137Polar residues
Compositional bias138-152Basic and acidic residues
Region177-583Disordered
Compositional bias184-201Basic and acidic residues
Compositional bias209-223Pro residues
Compositional bias233-270Polar residues
Compositional bias298-316Pro residues
Compositional bias348-369Pro residues
Region397-55510 X 10 AA tandem approximate repeats of P-A-K-P-Q-P-Q-Q-P-X
Compositional bias400-414Pro residues
Compositional bias469-528Pro residues
Compositional bias529-582Polar residues
Zinc finger589-613C4-type
Region650-929Disordered
Compositional bias660-688Polar residues
Compositional bias762-811Polar residues
Compositional bias845-863Basic and acidic residues
Compositional bias869-886Pro residues
Compositional bias887-928Polar residues
Region945-1058Disordered
Compositional bias966-986Pro residues
Compositional bias999-1032Basic and acidic residues
Zinc finger1059-1082C4-type
Region1120-1163Disordered
Compositional bias1137-1151Polar residues
Region1183-1386Disordered
Compositional bias1194-1282Basic and acidic residues
Compositional bias1286-1300Polar residues
Compositional bias1331-1349Basic and acidic residues
Compositional bias1350-1378Polar residues
Region1391-1410Disordered
Compositional bias1395-1410Polar residues
Region1423-1868Disordered
Compositional bias1427-1454Basic and acidic residues
Compositional bias1462-1514Basic and acidic residues
Compositional bias1516-1543Polar residues
Compositional bias1544-1564Basic and acidic residues
Compositional bias1588-1602Basic and acidic residues
Compositional bias1613-1653Basic and acidic residues
Compositional bias1674-1688Polar residues
Compositional bias1717-1740Polar residues
Compositional bias1784-1825Basic and acidic residues
Compositional bias1840-1854Basic and acidic residues
Region2169-2192Disordered
Compositional bias2365-2385Polar residues
Region2365-2438Disordered
Compositional bias2402-2436Pro residues
Region2504-2536Disordered
Compositional bias2517-2536Polar residues
Compositional bias3407-3473Basic and acidic residues
Region3407-3508Disordered
Compositional bias3482-3506Basic and acidic residues
Region3558-3626Disordered
Compositional bias3566-3584Polar residues
Region3652-3746Disordered
Compositional bias3681-3720Polar residues
Compositional bias3729-3746Polar residues
Region3833-3908Disordered
Compositional bias3855-3908Polar residues
Region4278-4301Disordered
Compositional bias4280-4301Polar residues
Region4389-4411Disordered
Domain4496-4590PDZ
Region4597-4618Disordered
Compositional bias4599-4616Basic and acidic residues
Compositional bias4645-4677Polar residues
Region4645-4690Disordered
Domain4694-4823C2 1
Region4830-4907Disordered
Compositional bias4835-4852Polar residues
Compositional bias4870-4907Polar residues
Compositional bias4930-4971Polar residues
Region4930-4986Disordered
Domain5007-5132C2 2

Domain

C2 domain 1 is involved in binding calcium and phospholipids. Calcium binds with low affinity but with high specificity and induces a large conformational change.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing. Additional isoforms seem to exist.

Q9Y6V0-5

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    5,142
  • Mass (Da)
    560,699
  • Last updated
    2018-03-28 v5
  • MD5 Checksum
    9C3258DAE79D5C74F1C6750B2107ADE0

Q9Y6V0-3

Q9Y6V0-6

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
H7C261H7C261_HUMANPCLO46
H7C114H7C114_HUMANPCLO60
E9PE96E9PE96_HUMANPCLO1217

Sequence caution

The sequence AAB97937.1 differs from that shown. Reason: Erroneous gene model prediction
The sequence AAD21789.2 differs from that shown. Reason: Erroneous gene model prediction
The sequence EAL24187.1 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for alternative sequence, compositional bias, sequence conflict.

Type
IDPosition(s)Description
Alternative sequenceVSP_0594611-4570in isoform 3
Compositional bias109-137Polar residues
Compositional bias138-152Basic and acidic residues
Compositional bias184-201Basic and acidic residues
Compositional bias209-223Pro residues
Compositional bias233-270Polar residues
Compositional bias298-316Pro residues
Compositional bias348-369Pro residues
Compositional bias400-414Pro residues
Sequence conflict441in Ref. 4; CAB60727
Sequence conflict443-496in Ref. 4; CAB60727
Compositional bias469-528Pro residues
Sequence conflict497in Ref. 4; CAB60727
Sequence conflict501in Ref. 3; AAI22566
Compositional bias529-582Polar residues
Sequence conflict554in Ref. 4; CAB60727
Sequence conflict563in Ref. 4; CAB60727
Sequence conflict632in Ref. 4; CAB60727
Compositional bias660-688Polar residues
Compositional bias762-811Polar residues
Sequence conflict814in Ref. 4; CAB60727
Compositional bias845-863Basic and acidic residues
Compositional bias869-886Pro residues
Compositional bias887-928Polar residues
Compositional bias966-986Pro residues
Compositional bias999-1032Basic and acidic residues
Compositional bias1137-1151Polar residues
Compositional bias1194-1282Basic and acidic residues
Compositional bias1286-1300Polar residues
Compositional bias1331-1349Basic and acidic residues
Compositional bias1350-1378Polar residues
Compositional bias1395-1410Polar residues
Compositional bias1427-1454Basic and acidic residues
Compositional bias1462-1514Basic and acidic residues
Compositional bias1516-1543Polar residues
Compositional bias1544-1564Basic and acidic residues
Compositional bias1588-1602Basic and acidic residues
Compositional bias1613-1653Basic and acidic residues
Compositional bias1674-1688Polar residues
Compositional bias1717-1740Polar residues
Compositional bias1784-1825Basic and acidic residues
Compositional bias1840-1854Basic and acidic residues
Compositional bias2365-2385Polar residues
Compositional bias2402-2436Pro residues
Compositional bias2517-2536Polar residues
Compositional bias3407-3473Basic and acidic residues
Compositional bias3482-3506Basic and acidic residues
Compositional bias3566-3584Polar residues
Compositional bias3681-3720Polar residues
Compositional bias3729-3746Polar residues
Compositional bias3855-3908Polar residues
Compositional bias4280-4301Polar residues
Alternative sequenceVSP_0594624571-4588in isoform 3
Compositional bias4599-4616Basic and acidic residues
Compositional bias4645-4677Polar residues
Alternative sequenceVSP_0594634742-4750in isoform 3
Sequence conflict4814in Ref. 3; AAH01304
Compositional bias4835-4852Polar residues
Compositional bias4870-4907Polar residues
Compositional bias4930-4971Polar residues
Alternative sequenceVSP_0594644931-4935in isoform 3 and isoform 6
Alternative sequenceVSP_0594654936-5142in isoform 3 and isoform 6

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC004006
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC004082
EMBL· GenBank· DDBJ
AAB97937.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
AC080093
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC004886
EMBL· GenBank· DDBJ
AAD21789.2
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
AC004903
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC093461
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH236949
EMBL· GenBank· DDBJ
EAL24187.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
BC001304
EMBL· GenBank· DDBJ
AAH01304.2
EMBL· GenBank· DDBJ
mRNA
BC122565
EMBL· GenBank· DDBJ
AAI22566.1
EMBL· GenBank· DDBJ
mRNA
BC125271
EMBL· GenBank· DDBJ
AAI25272.1
EMBL· GenBank· DDBJ
mRNA
Y19188
EMBL· GenBank· DDBJ
CAB60727.1
EMBL· GenBank· DDBJ
mRNA
AB011131
EMBL· GenBank· DDBJ
BAA25485.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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