Q9JKS6 (PCLO_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 100.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Protein piccolo Alternative name(s): Aczonin Multidomain presynaptic cytomatrix protein | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 5085 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | May act as a scaffolding protein involved in the organization of synaptic active zones and in synaptic vesicle trafficking By similarity. UniProtKB Q9QYX7 |
| Subunit structure | Interacts with RABAC1/PRA1, RIMS2 and profilin By similarity. Ref.1 |
| Subcellular location | Cell junction › synapse. Note: Concentrated at presynaptic side of synaptic junctions. |
| 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. Ref.3 |
| Sequence similarities | Contains 1 PDZ (DHR) domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell junction Synapse |
| Coding sequence diversity | Alternative splicing |
| Domain | Repeat Zinc-finger |
| Ligand | Calcium Calcium/phospholipid-binding Metal-binding Zinc |
| PTM | Glycoprotein Phosphoprotein |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | cytoskeleton organization Inferred from sequence or structural similarity. Source: UniProtKB synaptic vesicle targetingNon-traceable author statement Ref.1. Source: UniProtKB |
| Cellular_component | cell junction Inferred from electronic annotation. Source: UniProtKB-KW synapseInferred from direct assay Ref.1. Source: UniProtKB |
| Molecular_function | calcium ion binding Inferred from direct assay Ref.3. Source: UniProtKB calcium-dependent phospholipid bindingInferred from direct assay Ref.3. Source: UniProtKB profilin bindingInferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| Rabac1 | Q9Z0S9 | 3 | EBI-2271602,EBI-476965 | From a different organism. |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q9JKS6-1) 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. | ||||||
| Isoform 2 (identifier: Q9JKS6-2) The sequence of this isoform differs from the canonical sequence as follows: 4876-4880: TKPTN → SKRRK 4881-5085: Missing. | ||||||
| Isoform 3 (identifier: Q9JKS6-3) The sequence of this isoform differs from the canonical sequence as follows: 4687-4695: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 5085 | 5085 | Protein piccolo | PRO_0000058252 | |||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||
| Domain | 4442 – 4536 | 95 | PDZ Ref.3 | ||||||||||||||||||||||||||||||||
| Domain | 4653 – 4752 | 100 | C2 1 Ref.3 | ||||||||||||||||||||||||||||||||
| Domain | 4968 – 5059 | 92 | C2 2 Ref.3 | ||||||||||||||||||||||||||||||||
| Zinc finger | 523 – 547 | 25 | C4-type Potential Ref.1 | ||||||||||||||||||||||||||||||||
| Zinc finger | 1010 – 1033 | 24 | C4-type Potential Ref.1 | ||||||||||||||||||||||||||||||||
| Region | 372 – 491 | 120 | 12 X 10 AA tandem approximate repeats of P-A-K-P-Q-P-Q-Q-P-X | ||||||||||||||||||||||||||||||||
| Compositional bias | 2351 – 2362 | 12 | Poly-Pro Ref.3 | ||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||
| Modified residue | 617 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 756 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 873 | 1 | Phosphothreonine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 1133 | 1 | Phosphothreonine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 1352 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 1353 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 1412 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 1451 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 1456 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 1469 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 1587 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 1597 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 1772 | 1 | Phosphothreonine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 1775 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 1778 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 1784 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 1820 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 1840 | 1 | Phosphotyrosine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 1841 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 3014 | 1 | Phosphothreonine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 3374 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 3392 | 1 | Phosphothreonine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 3529 | 1 | Phosphothreonine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 3561 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 3626 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 3632 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 3779 | 1 | Phosphotyrosine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 3781 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 3912 | 1 | Phosphothreonine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 3913 | 1 | Phosphothreonine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 3954 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 3970 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 4304 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 4308 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 4311 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Modified residue | 4343 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||
| Glycosylation | 2702 | 1 | O-linked (GlcNAc) By similarity | ||||||||||||||||||||||||||||||||
| Glycosylation | 2976 | 1 | O-linked (GlcNAc) By similarity | ||||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||||
| Alternative sequence | 4687 – 4695 | 9 | Missing in isoform 3. | VSP_018194 | |||||||||||||||||||||||||||||||
| Alternative sequence | 4876 – 4880 | 5 | TKPTN → SKRRK in isoform 2. Ref.3 | VSP_003930 | |||||||||||||||||||||||||||||||
| Alternative sequence | 4881 – 5085 | 205 | Missing in isoform 2. Ref.3 | VSP_003931 | |||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||
| Mutagenesis | 4668 | 1 | D → A: Complete loss of calcium-binding and calcium-dependent phospholipid binding activity. Ref.3 | ||||||||||||||||||||||||||||||||
| Mutagenesis | 4674 | 1 | D → A: Complete loss of calcium-binding and calcium-dependent phospholipid binding activity. Ref.3 | ||||||||||||||||||||||||||||||||
| Mutagenesis | 4688 – 4689 | 2 | VM → SS: 10-fold increase in affinity for calcium. Ref.3 | ||||||||||||||||||||||||||||||||
| Mutagenesis | 4688 | 1 | V → S: Small increase in affinity for calcium. Ref.3 | ||||||||||||||||||||||||||||||||
| Mutagenesis | 4689 | 1 | M → S: Increased affinity for calcium. Ref.3 | ||||||||||||||||||||||||||||||||
| Mutagenesis | 4690 – 4691 | 2 | VV → SS: 10-fold increase in affinity for calcium. Ref.3 | ||||||||||||||||||||||||||||||||
| Mutagenesis | 4692 – 4693 | 2 | QN → AA: Moderate increase in affinity for calcium. Ref.3 | ||||||||||||||||||||||||||||||||
| Mutagenesis | 4694 | 1 | A → S: No effect on calcium-binding activity. Ref.3 | ||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||
| Beta strand | 4642 – 4650 | 9 | |||||||||||||||||||||||||||||||||
| Beta strand | 4653 – 4663 | 11 | |||||||||||||||||||||||||||||||||
| Beta strand | 4668 – 4671 | 4 | |||||||||||||||||||||||||||||||||
| Beta strand | 4676 – 4681 | 6 | |||||||||||||||||||||||||||||||||
| Helix | 4696 – 4699 | 4 | |||||||||||||||||||||||||||||||||
| Turn | 4700 – 4705 | 6 | |||||||||||||||||||||||||||||||||
| Helix | 4706 – 4709 | 4 | |||||||||||||||||||||||||||||||||
| Beta strand | 4712 – 4719 | 8 | |||||||||||||||||||||||||||||||||
| Helix | 4724 – 4727 | 4 | |||||||||||||||||||||||||||||||||
| Beta strand | 4731 – 4739 | 9 | |||||||||||||||||||||||||||||||||
| Beta strand | 4741 – 4743 | 3 | |||||||||||||||||||||||||||||||||
| Beta strand | 4745 – 4754 | 10 | |||||||||||||||||||||||||||||||||
| Helix | 4759 – 4761 | 3 | |||||||||||||||||||||||||||||||||
| Beta strand | 4766 – 4769 | 4 | |||||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||||||||||||||
References
| [1] | "Piccolo, a presynaptic zinc finger protein structurally related to bassoon." Fenster S.D., Chung W.J., Zhai R., Cases-Langhoff C., Voss B., Garner A.M., Kaempf U., Kindler S., Gundelfinger E.D., Garner C.C. Neuron 25:203-214(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH RABAC1. |
| [2] | Fenster S.D., Cases-Langhoff C., Gundelfinger E.D., Garner C.C. Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). |
| [3] | "An unusual C(2)-domain in the active-zone protein piccolo: implications for Ca(2+) regulation of neurotransmitter release." Gerber S.H., Garcia J., Rizo J., Suedhof T.C. EMBO J. 20:1605-1619(2001) [PubMed] [Europe PMC] [Abstract] Cited for: CALCIUM-BINDING, MUTAGENESIS OF ASP-4668; ASP-4674; VAL-4688; 4688-VAL-MET-4689; MET-4689; 4690-VAL-VAL-4691; 4692-GLN-ASN-4693 AND ALA-4694. |
| [4] | "A conformational switch in the Piccolo C2A domain regulated by alternative splicing." Garcia J., Gerber S.H., Sugita S., Suedhof T.C., Rizo J. Nat. Struct. Mol. Biol. 11:45-53(2004) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 4635-4776, ALTERNATIVE SPLICING (ISOFORM 3). |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AF138789 mRNA. Translation: AAF07822.2. AF227534 mRNA. Translation: AAF63196.1. | ||||||||||||
| IPI | IPI00203018. IPI00231831. IPI00758462. | ||||||||||||
| RefSeq | NP_001104267.1. NM_001110797.1. NP_064483.1. NM_020098.1. | ||||||||||||
| UniGene | Rn.53925. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q9JKS6. | ||||||||||||
| SMR | Q9JKS6. Positions 4430-4538, 4635-4776. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | Q9JKS6. 4 interactions. | ||||||||||||
| STRING | 10116.ENSRNOP00000008637. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | Q9JKS6. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | Q9JKS6. | ||||||||||||
| PRIDE | Q9JKS6. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 56768. | ||||||||||||
| KEGG | rno:56768. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 27445. | ||||||||||||
| RGD | 69406. Pclo. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG5038. | ||||||||||||
| HOGENOM | HOG000168263. | ||||||||||||
| HOVERGEN | HBG031058. | ||||||||||||
| InParanoid | Q9JKS6. | ||||||||||||
| KO | K16882. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q9JKS6. | ||||||||||||
| Genevestigator | Q9JKS6. | ||||||||||||
| GermOnline | ENSRNOG00000005726. Rattus norvegicus. | ||||||||||||
Family and domain databases | |||||||||||||
| Gene3D | 3.30.40.10. 2 hits. | ||||||||||||
| InterPro | IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018029. C2_membr_targeting. IPR001478. PDZ. IPR011011. Znf_FYVE_PHD. IPR008899. Znf_piccolo. IPR013083. Znf_RING/FYVE/PHD. [Graphical view] | ||||||||||||
| Pfam | PF00168. C2. 2 hits. PF00595. PDZ. 1 hit. PF05715. zf-piccolo. 2 hits. [Graphical view] | ||||||||||||
| SMART | SM00239. C2. 2 hits. SM00228. PDZ. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF49562. C2_CaLB. 2 hits. SSF57903. FYVE_PHD_ZnF. 2 hits. SSF50156. PDZ. 1 hit. | ||||||||||||
| PROSITE | PS50004. C2. 2 hits. PS50106. PDZ. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | Q9JKS6. | ||||||||||||
| NextBio | 611161. | ||||||||||||
Entry information
| Entry name | PCLO_RAT | ||||||||
| Accession | Primary (citable) accession number: Q9JKS6 Secondary accession number(s): Q9JLT1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
