CAVN1_RAT
ID CAVN1_RAT Reviewed; 392 AA.
AC P85125;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Caveolae-associated protein 1 {ECO:0000312|RGD:1307685};
DE AltName: Full=Cavin-1;
DE AltName: Full=Polymerase I and transcript release factor;
DE AltName: Full=cav-p60;
GN Name=Cavin1 {ECO:0000312|RGD:1307685}; Synonyms=Ptrf;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-100 AND 340-357,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16236245; DOI=10.1016/j.bbamem.2005.09.013;
RA Vinten J., Johnsen A.H., Roepstorff P., Harpoth J., Tranum-Jensen J.;
RT "Identification of a major protein on the cytosolic face of caveolae.";
RL Biochim. Biophys. Acta 1717:34-40(2005).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11512676; DOI=10.1007/s004410100389;
RA Vinten J., Voldstedlund M., Clausen H., Christiansen K., Carlsen J.,
RA Tranum-Jensen J.;
RT "A 60-kDa protein abundant in adipocyte caveolae.";
RL Cell Tissue Res. 305:99-106(2001).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11702238; DOI=10.1007/s004410100439;
RA Voldstedlund M., Vinten J., Tranum-Jensen J.;
RT "cav-p60 expression in rat muscle tissues. Distribution of caveolar
RT proteins.";
RL Cell Tissue Res. 306:265-276(2001).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=18056712; DOI=10.1074/jbc.m707890200;
RA Liu L., Pilch P.F.;
RT "A critical role of cavin (polymerase I and transcript release factor) in
RT caveolae formation and organization.";
RL J. Biol. Chem. 283:4314-4322(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-38; THR-40; SER-42;
RP SER-48; SER-120; TYR-158; SER-169; SER-173; SER-177; SER-204; SER-205;
RP THR-304; TYR-310; SER-367; SER-368; SER-381; SER-389 AND SER-391, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plays an important role in caveolae formation and
CC organization. Essential for the formation of caveolae in all tissues.
CC Core component of the CAVIN complex which is essential for recruitment
CC of the complex to the caveolae in presence of calveolin-1 (CAV1).
CC Essential for normal oligomerization of CAV1. Promotes ribosomal
CC transcriptional activity in response to metabolic challenges in the
CC adipocytes and plays an important role in the formation of the
CC ribosomal transcriptional loop. Dissociates transcription complexes
CC paused by DNA-bound TTF1, thereby releasing both RNA polymerase I and
CC pre-RNA from the template. The caveolae biogenesis pathway is required
CC for the secretion of proteins such as GASK1A.
CC {ECO:0000250|UniProtKB:O54724}.
CC -!- SUBUNIT: Component of the CAVIN complex composed of CAVIN1, CAVIN2,
CC CAVIN3 and CAVIN4. Interacts with RNA polymerase I and TTF1. Binds the
CC 3' end of pre-rRNA. Interacts with transcription factor ZNF148.
CC Interacts with LIPE in the adipocyte cytoplasm. Interacts with CAV1,
CC CAV3, CAVIN2, CAVIN3 and CAVIN4. {ECO:0000250|UniProtKB:O54724,
CC ECO:0000250|UniProtKB:Q6NZI2}.
CC -!- SUBCELLULAR LOCATION: Membrane, caveola {ECO:0000269|PubMed:11512676,
CC ECO:0000269|PubMed:11702238, ECO:0000269|PubMed:16236245,
CC ECO:0000269|PubMed:18056712}. Cell membrane
CC {ECO:0000269|PubMed:11512676, ECO:0000269|PubMed:11702238,
CC ECO:0000269|PubMed:16236245, ECO:0000269|PubMed:18056712}. Microsome
CC {ECO:0000269|PubMed:11512676, ECO:0000269|PubMed:16236245}. Endoplasmic
CC reticulum {ECO:0000305}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:11702238}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q6NZI2}. Nucleus {ECO:0000269|PubMed:11702238,
CC ECO:0000269|PubMed:16236245}. Note=Translocates to the cytoplasm from
CC the caveolae upon insulin stimulation (By similarity). Colocalizes with
CC CAV1 in lipid rafts in adipocytes (PubMed:18056712). Localizes in the
CC caveolae in a caveolin-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:O54724, ECO:0000250|UniProtKB:Q6NZI2,
CC ECO:0000269|PubMed:18056712}.
CC -!- TISSUE SPECIFICITY: Expressed in the adipocyte (at protein level).
CC Expressed in all striated and smooth muscles tested including
CC diaphragm, esophageal striated muscle, fibroblast, endocardial
CC endothelium, epicardial mesothelium, intestinal smooth muscle,
CC masseter, soleus muscle, vascular smooth muscle and white gastrocnemius
CC muscle (at protein level). Expressed in the endothelium and perineural
CC sheath (at protein level). Not expressed in hepatocytes.
CC {ECO:0000269|PubMed:11512676, ECO:0000269|PubMed:11702238,
CC ECO:0000269|PubMed:16236245}.
CC -!- DOMAIN: The leucine-zipper domain 1 is essential for its localization
CC in the caveolae. {ECO:0000250|UniProtKB:O54724}.
CC -!- PTM: Phosphorylated. Present in active and inactive forms. Changes in
CC phosphorylation pattern may alter activity. Phosphorylation at Tyr-158
CC is essential for its function in the regulation of ribosomal
CC transcriptional activity. {ECO:0000250|UniProtKB:O54724}.
CC -!- PTM: Monoubiquitinated. {ECO:0000250|UniProtKB:O54724}.
CC -!- SIMILARITY: Belongs to the CAVIN family. {ECO:0000305}.
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DR AlphaFoldDB; P85125; -.
DR SMR; P85125; -.
DR IntAct; P85125; 1.
DR STRING; 10116.ENSRNOP00000026783; -.
DR CarbonylDB; P85125; -.
DR iPTMnet; P85125; -.
DR PhosphoSitePlus; P85125; -.
DR jPOST; P85125; -.
DR PaxDb; P85125; -.
DR PRIDE; P85125; -.
DR UCSC; RGD:1307685; rat.
DR RGD; 1307685; Cavin1.
DR eggNOG; ENOG502QV3D; Eukaryota.
DR InParanoid; P85125; -.
DR PhylomeDB; P85125; -.
DR Reactome; R-RNO-73863; RNA Polymerase I Transcription Termination.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR PRO; PR:P85125; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005901; C:caveola; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0042134; F:rRNA primary transcript binding; ISS:UniProtKB.
DR GO; GO:2000147; P:positive regulation of cell motility; ISS:UniProtKB.
DR GO; GO:0009306; P:protein secretion; ISO:RGD.
DR GO; GO:0009303; P:rRNA transcription; ISS:UniProtKB.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; ISS:UniProtKB.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; ISS:UniProtKB.
DR InterPro; IPR033297; Cavin-1.
DR InterPro; IPR026752; Cavin_fam.
DR PANTHER; PTHR15240; PTHR15240; 1.
DR PANTHER; PTHR15240:SF3; PTHR15240:SF3; 1.
DR Pfam; PF15237; PTRF_SDPR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Endoplasmic reticulum; Isopeptide bond;
KW Membrane; Microsome; Mitochondrion; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; rRNA-binding; Transcription;
KW Transcription regulation; Transcription termination; Ubl conjugation.
FT CHAIN 1..392
FT /note="Caveolae-associated protein 1"
FT /id="PRO_0000284698"
FT REGION 1..100
FT /note="Required for homotrimerization and for interaction
FT with CAVIN2 and CAVIN3"
FT /evidence="ECO:0000250|UniProtKB:O54724"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..64
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:O54724"
FT REGION 55..77
FT /note="Leucine-zipper 1"
FT /evidence="ECO:0000250|UniProtKB:O54724"
FT REGION 138..154
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:O54724"
FT REGION 168..188
FT /note="Leucine-zipper 2"
FT /evidence="ECO:0000250|UniProtKB:O54724"
FT REGION 173..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..251
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:O54724"
FT REGION 259..299
FT /note="Leucine-zipper 3"
FT /evidence="ECO:0000250|UniProtKB:O54724"
FT REGION 347..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 201..284
FT /evidence="ECO:0000255"
FT COMPBIAS 176..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZI2"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 40
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 158
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZI2"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZI2"
FT MOD_RES 304
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 310
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 118
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6NZI2"
FT CROSSLNK 124
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6NZI2"
FT CROSSLNK 163
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q6NZI2"
FT CROSSLNK 163
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q6NZI2"
FT CROSSLNK 167
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6NZI2"
FT CROSSLNK 172
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6NZI2"
FT CROSSLNK 328
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6NZI2"
SQ SEQUENCE 392 AA; 43909 MW; 6C61428D68315DD2 CRC64;
MEDVTLHIVE RPYSGYPDAS SEGPEPTPGE ARATEEPSGT GSDELIKSDQ VNGVLVLSLL
DKIIGAVDQI QLTQAQLEER QAEMEGAVQS IQGELSKLGK AHATTSNTVS KLLEKVRKVS
VNVKTVRGSL ERQAGQIKKL EVNEAELLRR RNFKVMIYQD EVKLPAKLSV SKSLKESEAL
PEKEGDELGE GERPEEDAAA IELSSDEAVE VEEVIEESRA ERIKRSGLRR VDDFKKAFSK
EKMEKTKVRT RENLEKTRLK TKENLEKTRH TLEKRMNKLG TRLVPVERRE KLKTSRDKLR
KSFTPDHVVY ARSKTAVYKV PPFTFHVKKI REGEVEVLKA TEMVEVGPDD DEVGAERGAE
TDLLRGSSPD VHTLLEITEE SDAVLVDKSD SD
