Q4V920
SS
Gene name |
pacsin1b (pacsin1) |
Protein name |
Protein kinase C and casein kinase substrate in neurons protein 1 |
Names |
Syndapin-1 |
Species |
Danio rerio (Zebrafish) (Brachydanio rerio) |
KEGG Pathway |
dre:619246 |
EC number |
|
Protein Class |
|
Descriptions
The F-BAR domain-containing protein PACSIN contributes to vesicle formation at the plasma membrane and induces a spectrum of membrane morphologies including tubules and tubular constriction. Full-length PACSIN1 has reduced activity compared to the isolated F-BAR domain. Autoinhibition is mediated by the SH3 domain interacting with the F-BAR domain in PACSIN1. The SH3 domain is able to bind the proline-rich domain (PRD) of proteins in endocytosis. The autoinhibitory, intramolecular interactions can be released upon binding to the proline-rich domain (PRD) of dynamin-1, resulting in potent membrane deformation activity.
Autoinhibitory domains (AIDs)
Target domain |
18-275 (The F-BAR, FES-CIP4 Homology and Bin/Amphiphysin/Rvs, domain of Protein kinase C and Casein kinase Substrate in Neurons 1, PACSIN1) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
References
- Goh SL et al. (2012) "Versatile membrane deformation potential of activated pacsin", PloS one, 7, e51628
- Rao Y et al. (2010) "Molecular basis for SH3 domain regulation of F-BAR-mediated membrane deformation", Proceedings of the National Academy of Sciences of the United States of America, 107, 8213-8
- Senju Y et al. (2011) "Essential role of PACSIN2/syndapin-II in caveolae membrane sculpting", Journal of cell science, 124, 2032-40
- Wang Q et al. (2009) "Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin", Proceedings of the National Academy of Sciences of the United States of America, 106, 12700-5
- Shimada A et al. (2010) "Mapping of the basic amino-acid residues responsible for tubulation and cellular protrusion by the EFC/F-BAR domain of pacsin2/Syndapin II", FEBS letters, 584, 1111-8
- Plomann M et al. (2010) "A hinge in the distal end of the PACSIN 2 F-BAR domain may contribute to membrane-curvature sensing", Journal of molecular biology, 400, 129-36
Autoinhibited structure
Activated structure
1 structures for Q4V920
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q4V920-F1 | Predicted | AlphaFoldDB |
No variants for Q4V920
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q4V920 | |||||
No associated diseases with Q4V920
Functions
8 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytoplasmic vesicle membrane | The lipid bilayer surrounding a cytoplasmic vesicle. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| endosome | A vacuole to which materials ingested by endocytosis are delivered. |
| neuron projection | A prolongation or process extending from a nerve cell, e.g. an axon or dendrite. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| ruffle membrane | The portion of the plasma membrane surrounding a ruffle. |
| synapse | The junction between an axon of one neuron and a dendrite of another neuron, a muscle fiber or a glial cell. As the axon approaches the synapse it enlarges into a specialized structure, the presynaptic terminal bouton, which contains mitochondria and synaptic vesicles. At the tip of the terminal bouton is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic terminal bouton secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| phospholipid binding | Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester. |
9 GO annotations of biological process
| Name | Definition |
|---|---|
| actin filament organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments. Includes processes that control the spatial distribution of actin filaments, such as organizing filaments into meshworks, bundles, or other structures, as by cross-linking. |
| auditory receptor cell stereocilium organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a stereocilium. A stereocilium is an actin-based protrusion from the apical surface of auditory hair cells. |
| cilium assembly | The assembly of a cilium, a specialized eukaryotic organelle that consists of a filiform extrusion of the cell surface. Each cilium is bounded by an extrusion of the cytoplasmic membrane, and contains a regular longitudinal array of microtubules, anchored basally in a centriole. |
| cytoskeleton organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures. |
| endocytosis | A vesicle-mediated transport process in which cells take up external materials or membrane constituents by the invagination of a part of the plasma membrane to form a new membrane-bounded vesicle. |
| neuron projection morphogenesis | The process in which the anatomical structures of a neuron projection are generated and organized. A neuron projection is any process extending from a neural cell, such as axons or dendrites. |
| plasma membrane tubulation | A membrane tubulation process occurring in a plasma membrane. |
| positive regulation of dendrite development | Any process that activates or increases the frequency, rate or extent of dendrite development. |
| regulation of endocytosis | Any process that modulates the frequency, rate or extent of endocytosis. |
13 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P25623 | SYP1 | Suppressor of yeast profilin deletion | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| A7MBI0 | PACSIN1 | Protein kinase C and casein kinase substrate in neurons protein 1 | Bos taurus (Bovine) | SS |
| O13154 | PACSIN2 | Protein kinase C and casein kinase substrate in neurons protein 2 | Gallus gallus (Chicken) | SS |
| Q9UKS6 | PACSIN3 | Protein kinase C and casein kinase substrate in neurons protein 3 | Homo sapiens (Human) | SS |
| Q9UNF0 | PACSIN2 | Protein kinase C and casein kinase substrate in neurons protein 2 | Homo sapiens (Human) | EV |
| Q9BY11 | PACSIN1 | Protein kinase C and casein kinase substrate in neurons protein 1 | Homo sapiens (Human) | EV |
| Q9H939 | PSTPIP2 | Proline-serine-threonine phosphatase-interacting protein 2 | Homo sapiens (Human) | PR |
| Q99JB8 | Pacsin3 | Protein kinase C and casein kinase II substrate protein 3 | Mus musculus (Mouse) | SS |
| Q61644 | Pacsin1 | Protein kinase C and casein kinase substrate in neurons protein 1 | Mus musculus (Mouse) | EV |
| Q9WVE8 | Pacsin2 | Protein kinase C and casein kinase substrate in neurons protein 2 | Mus musculus (Mouse) | EV |
| Q99M15 | Pstpip2 | Proline-serine-threonine phosphatase-interacting protein 2 | Mus musculus (Mouse) | PR |
| Q9QY17 | Pacsin2 | Protein kinase C and casein kinase substrate in neurons 2 protein | Rattus norvegicus (Rat) | SS |
| Q9Z0W5 | Pacsin1 | Protein kinase C and casein kinase substrate in neurons protein 1 | Rattus norvegicus (Rat) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSGAYDESAM | SDETTDSFWE | VGNYKRTVKR | IEDGHRLCND | MMSCIQERAK | IEKAYSQQLT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DWSKRWRQLV | ERGPQYGTLE | RAWLAVMTEA | EKVSELHQEV | KNNLLNEDLE | KVKNWQKDAY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| HKQMMGGFKE | TKEADEGFRK | AQKPWAKKLK | ELETAKKTYH | MACKEEKIAS | AREANSKGEA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SVTTDQQKKL | QEKVDKCKND | VQKAKEKYEK | SLDELNKCTP | QYMENMEVVF | DQCQQFEEKR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LNFLREVLLD | TKRHLNLTES | QSYATVYREL | ERTIVSASAQ | EDLKWFSSVH | GPGMHMNWPQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FEEFNPDLSH | AISKKEKVKR | NHDGVTLTQV | THGAEHGTPQ | TGDRGSVSSY | EKNQQYSAEW |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SDDEQPPTAA | QSASETNGGN | PFEEDSKGVR | VRALYDYEGQ | EQDELTFKAG | DELTKLEDED |
| 430 | 440 | ||||
| EQGWCKGRLD | SGQLGLYPAN | YVEPV |