| IED ID | IndEnz0005000419 |
| Enzyme Type ID | lipase000419 |
| Protein Name |
Caveolae-associated protein 1 Cavin-1 Polymerase I and transcript release factor |
| Gene Name | CAVIN1 PTRF FKSG13 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MEDPTLYIVERPLPGYPDAEAPEPSSAGAQAAEEPSGAGSEELIKSDQVNGVLVLSLLDKIIGAVDQIQLTQAQLEERQAEMEGAVQSIQGELSKLGKAHATTSNTVSKLLEKVRKVSVNVKTVRGSLERQAGQIKKLEVNEAELLRRRNFKVMIYQDEVKLPAKLSISKSLKESEALPEKEGEELGEGERPEEDAAALELSSDEAVEVEEVIEESRAERIKRSGLRRVDDFKKAFSKEKMEKTKVRTRENLEKTRLKTKENLEKTRHTLEKRMNKLGTRLVPAERREKLKTSRDKLRKSFTPDHVVYARSKTAVYKVPPFTFHVKKIREGQVEVLKATEMVEVGADDDEGGAERGEAGDLRRGSSPDVHALLEITEESDAVLVDKSDSD |
| Enzyme Length | 390 |
| Uniprot Accession Number | Q6NZI2 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Plays an important role in caveolae formation and organization. Essential for the formation of caveolae in all tissues (PubMed:18056712, PubMed:18191225, PubMed:19726876). Core component of the CAVIN complex which is essential for recruitment of the complex to the caveolae in presence of calveolin-1 (CAV1). Essential for normal oligomerization of CAV1. Promotes ribosomal transcriptional activity in response to metabolic challenges in the adipocytes and plays an important role in the formation of the ribosomal transcriptional loop. Dissociates transcription complexes paused by DNA-bound TTF1, thereby releasing both RNA polymerase I and pre-RNA from the template (By similarity) (PubMed:18056712, PubMed:18191225, PubMed:19726876). The caveolae biogenesis pathway is required for the secretion of proteins such as GASK1A (By similarity). {ECO:0000250|UniProtKB:O54724, ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:18191225, ECO:0000269|PubMed:19726876}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Chain (1); Coiled coil (1); Compositional bias (2); Cross-link (7); Modified residue (20); Natural variant (2); Region (10); Sequence conflict (3) |
| Keywords | Acetylation;Alternative splicing;Cell membrane;Coiled coil;Congenital generalized lipodystrophy;Cytoplasm;Diabetes mellitus;Direct protein sequencing;Endoplasmic reticulum;Isopeptide bond;Membrane;Microsome;Mitochondrion;Nucleus;Phosphoprotein;RNA-binding;Reference proteome;Repeat;Transcription;Transcription regulation;Transcription termination;Ubl conjugation;rRNA-binding |
| Interact With | Q03135; P56539; Itself; O95810; Q969G5; Q16543; Q96GN5; Q5QJE6; Q9NVF7; Q9C086; Q92993; Q9BRJ2; Q5MJ10; Q5MJ09; Q8WVP5; Q3SY00; Q8N0Z6; Q8IY57-5; Q8TBK6; Q6P2D0; Q9Y5A6 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane, caveola {ECO:0000269|PubMed:15242332, ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:19525939}. Cell membrane {ECO:0000269|PubMed:15242332, ECO:0000269|PubMed:17026959, ECO:0000269|PubMed:18056712}. Microsome {ECO:0000269|PubMed:15242332, ECO:0000269|PubMed:17026959}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P85125}. Cytoplasm, cytosol {ECO:0000269|PubMed:15242332}. Mitochondrion {ECO:0000269|PubMed:15242332, ECO:0000269|PubMed:17026959}. Nucleus {ECO:0000269|PubMed:15242332, ECO:0000269|PubMed:17026959}. Note=Translocates to the cytoplasm from the caveolae upon insulin stimulation (PubMed:17026959). Colocalizes with CAV1 in lipid rafts in adipocytes. Localizes in the caveolae in a caveolin-dependent manner (By similarity). {ECO:0000250|UniProtKB:O54724, ECO:0000269|PubMed:17026959}. |
| Modified Residue | MOD_RES 1; /note="N-acetylmethionine"; /evidence="ECO:0000269|PubMed:15242332"; MOD_RES 36; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:15242332"; MOD_RES 40; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:15242332"; MOD_RES 46; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P85125"; MOD_RES 118; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 156; /note="Phosphotyrosine"; /evidence="ECO:0000250|UniProtKB:O54724"; MOD_RES 167; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"; MOD_RES 169; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 171; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:O54724"; MOD_RES 175; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P85125"; MOD_RES 202; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"; MOD_RES 203; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"; MOD_RES 300; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"; MOD_RES 302; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"; MOD_RES 308; /note="Phosphotyrosine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 365; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:15242332, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"; MOD_RES 366; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:15242332, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"; MOD_RES 379; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 387; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"; MOD_RES 389; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" |
| Post Translational Modification | PTM: Phosphorylated. Present in active and inactive forms. Changes in phosphorylation pattern may alter activity. Phosphorylation at Tyr-156 is essential for its functionin the regulation of ribosomal transcriptional activity. {ECO:0000250|UniProtKB:O54724}.; PTM: Five truncated forms are found in the caveolae. These are thought to be the result of proteolysis and may be phosphorylation-dependent. {ECO:0000269|PubMed:15242332}.; PTM: Monoubiquitinated. {ECO:0000250|UniProtKB:O54724}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10037681; 10490598; 10619026; 10873388; 12221077; 15866170; 16630611; 18158243; 18218625; 18829452; 19068216; 20030946; 20101212; 20300641; 20360068; 20427576; 20591975; 20660154; 20732728; 21150319; 21152401; 21343302; 21351730; 21445100; 21576392; 21683594; 21699497; 21705337; 21913217; 22267324; 22461895; 22790947; 22992742; 23214712; 23404184; 23770857; 23902751; 23934189; 23938946; 24128008; 24189400; 24473072; 24747515; 24812087; 25588833; 25721873; 25904680; 25942420; 26086560; 26496610; 26725982; 27167729; 27203393; 27634346; 27834731; 27894957; 28393200; 28698382; 29146911; 29556340; 29869069; 30949900; 31105010; 31267558; 31332168; 31448673; 31706570; 31871319; 32065471; 32493699; 32550897; 33496726; 8543060; 8571126; 8617235; 8662891; 8756646; 8816443; 9013646; 9111050; 9418861; 9535835; 9792683; 9829970; |
| Motif | |
| Gene Encoded By | |
| Mass | 43,476 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |