CAVN1_HUMAN
ID CAVN1_HUMAN Reviewed; 390 AA.
AC Q6NZI2; B2RAW7; O00535; Q6GMY1; Q96H74; Q9BT85; Q9HAP4;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Caveolae-associated protein 1 {ECO:0000312|HGNC:HGNC:9688};
DE AltName: Full=Cavin-1;
DE AltName: Full=Polymerase I and transcript release factor;
GN Name=CAVIN1 {ECO:0000312|HGNC:HGNC:9688}; Synonyms=PTRF; ORFNames=FKSG13;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAG27093.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lung {ECO:0000312|EMBL:AAG27093.1};
RA Wang Y.-G.;
RT "Cloning of FKSG13, a novel gene encoding a leucine-zipper protein.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAG27093.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAH66123.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Muscle {ECO:0000312|EMBL:AAH08849.1},
RC Pancreas {ECO:0000312|EMBL:AAH73759.1}, and
RC Testis {ECO:0000312|EMBL:AAH66123.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAC63404.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 187-390, AND INTERACTION WITH TTF1.
RC TISSUE=Lung {ECO:0000312|EMBL:AAC63404.1};
RX PubMed=9582279; DOI=10.1093/emboj/17.10.2855;
RA Jansa P., Mason S.W., Hoffmann-Rohrer U., Grummt I.;
RT "Cloning and functional characterization of PTRF, a novel protein which
RT induces dissociation of paused ternary transcription complexes.";
RL EMBO J. 17:2855-2864(1998).
RN [6] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-95; 137-147; 153-165; 174-217; 299-310; 318-327;
RP 338-355 AND 363-370 (ISOFORM 1), SUBCELLULAR LOCATION, ACETYLATION AT
RP MET-1, AND PHOSPHORYLATION AT SER-36; SER-40; SER-365 AND SER-366.
RC TISSUE=Adipocyte {ECO:0000269|PubMed:15242332};
RX PubMed=15242332; DOI=10.1042/bj20040647;
RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
RT "Vectorial proteomics reveal targeting, phosphorylation and specific
RT fragmentation of polymerase I and transcript release factor (PTRF) at the
RT surface of caveolae in human adipocytes.";
RL Biochem. J. 383:237-248(2004).
RN [7] {ECO:0000305}
RP INTERACTION WITH LIPE, AND SUBCELLULAR LOCATION.
RX PubMed=17026959; DOI=10.1016/j.bbrc.2006.09.094;
RA Aboulaich N., Oertegren U., Vener A.V., Stralfors P.;
RT "Association and insulin regulated translocation of hormone-sensitive
RT lipase with PTRF.";
RL Biochem. Biophys. Res. Commun. 350:657-661(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP FUNCTION.
RX PubMed=18191225; DOI=10.1016/j.cell.2007.11.042;
RA Hill M.M., Bastiani M., Luetterforst R., Kirkham M., Kirkham A.,
RA Nixon S.J., Walser P., Abankwa D., Oorschot V.M., Martin S., Hancock J.F.,
RA Parton R.G.;
RT "PTRF-Cavin, a conserved cytoplasmic protein required for caveola formation
RT and function.";
RL Cell 132:113-124(2008).
RN [10]
RP FUNCTION, AND 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; SER-202; SER-203;
RP SER-300; THR-302; SER-365 AND SER-366, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP INVOLVEMENT IN CGL4, AND FUNCTION.
RX PubMed=19726876; DOI=10.1172/jci38660;
RA Hayashi Y.K., Matsuda C., Ogawa M., Goto K., Tominaga K., Mitsuhashi S.,
RA Park Y.E., Nonaka I., Hino-Fukuyo N., Haginoya K., Sugano H., Nishino I.;
RT "Human PTRF mutations cause secondary deficiency of caveolins resulting in
RT muscular dystrophy with generalized lipodystrophy.";
RL J. Clin. Invest. 119:2623-2633(2009).
RN [15]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CAVIN2.
RX PubMed=19525939; DOI=10.1038/ncb1887;
RA Hansen C.G., Bright N.A., Howard G., Nichols B.J.;
RT "SDPR induces membrane curvature and functions in the formation of
RT caveolae.";
RL Nat. Cell Biol. 11:807-814(2009).
RN [16]
RP INVOLVEMENT IN CGL4.
RX PubMed=20684003; DOI=10.1002/ajmg.a.33578;
RA Shastry S., Delgado M.R., Dirik E., Turkmen M., Agarwal A.K., Garg A.;
RT "Congenital generalized lipodystrophy, type 4 (CGL4) associated with
RT myopathy due to novel PTRF mutations.";
RL Am. J. Med. Genet. A 152:2245-2253(2010).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; SER-202; SER-203;
RP THR-302; SER-365; SER-366; SER-387 AND SER-389, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-203; SER-365;
RP SER-366; SER-387 AND SER-389, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; SER-300; THR-302 AND
RP TYR-308, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118; SER-169; SER-202;
RP SER-203; SER-365; SER-366; SER-379; SER-387 AND SER-389, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-116 AND LYS-161, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-161, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [24]
RP INTERACTION WITH CAVIN2; CAVIN4 AND CAV3.
RX PubMed=24567387; DOI=10.1073/pnas.1315359111;
RA Ogata T., Naito D., Nakanishi N., Hayashi Y.K., Taniguchi T., Miyagawa K.,
RA Hamaoka T., Maruyama N., Matoba S., Ikeda K., Yamada H., Oh H., Ueyama T.;
RT "MURC/Cavin-4 facilitates recruitment of ERK to caveolae and concentric
RT cardiac hypertrophy induced by alpha1-adrenergic receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:3811-3816(2014).
RN [25]
RP REVIEW.
RX PubMed=26614875; DOI=10.1016/bs.ircmb.2015.07.009;
RA Nassar Z.D., Parat M.O.;
RT "Cavin family: new players in the biology of caveolae.";
RL Int. Rev. Cell Mol. Biol. 320:235-305(2015).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-116; LYS-122; LYS-161; LYS-165;
RP LYS-170 AND LYS-326, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [27]
RP VARIANT [LARGE SCALE ANALYSIS] THR-14.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Plays an important role in caveolae formation and
CC organization. Essential for the formation of caveolae in all tissues
CC (PubMed:18056712, PubMed:18191225, PubMed:19726876). Core component of
CC the CAVIN complex which is essential for recruitment of the complex to
CC the caveolae in presence of calveolin-1 (CAV1). Essential for normal
CC oligomerization of CAV1. Promotes ribosomal transcriptional activity in
CC response to metabolic challenges in the adipocytes and plays an
CC important role in the formation of the ribosomal transcriptional loop.
CC Dissociates transcription complexes paused by DNA-bound TTF1, thereby
CC releasing both RNA polymerase I and pre-RNA from the template (By
CC similarity) (PubMed:18056712, PubMed:18191225, PubMed:19726876). The
CC caveolae biogenesis pathway is required for the secretion of proteins
CC such as GASK1A (By similarity). {ECO:0000250|UniProtKB:O54724,
CC ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:18191225,
CC ECO:0000269|PubMed:19726876}.
CC -!- SUBUNIT: Component of the CAVIN complex composed of CAVIN1, CAVIN2,
CC CAVIN3 and CAVIN4. Homotrimer (By similarity). Interacts with TTF1
CC (PubMed:9582279). Interacts with RNA polymerase I. Binds the 3' end of
CC pre-rRNA. Interacts with transcription factor ZNF148 (By similarity).
CC Interacts with LIPE in the adipocyte cytoplasm (PubMed:17026959).
CC Interacts with CAV1 and CAVIN3 (By similarity). Interacts with CAVIN2
CC (PubMed:19525939, PubMed:24567387). Interacts with CAVIN4 and CAV3
CC (PubMed:24567387). {ECO:0000250|UniProtKB:O54724,
CC ECO:0000269|PubMed:17026959, ECO:0000269|PubMed:19525939,
CC ECO:0000269|PubMed:24567387, ECO:0000269|PubMed:9582279}.
CC -!- INTERACTION:
CC Q6NZI2; Q03135: CAV1; NbExp=10; IntAct=EBI-2559016, EBI-603614;
CC Q6NZI2; P56539: CAV3; NbExp=3; IntAct=EBI-2559016, EBI-3905936;
CC Q6NZI2; Q6NZI2: CAVIN1; NbExp=5; IntAct=EBI-2559016, EBI-2559016;
CC Q6NZI2; O95810: CAVIN2; NbExp=6; IntAct=EBI-2559016, EBI-742141;
CC Q6NZI2; Q969G5: CAVIN3; NbExp=11; IntAct=EBI-2559016, EBI-3893101;
CC Q6NZI2; Q16543: CDC37; NbExp=3; IntAct=EBI-2559016, EBI-295634;
CC Q6NZI2; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-2559016, EBI-5278764;
CC Q6NZI2; Q5QJE6: DNTTIP2; NbExp=3; IntAct=EBI-2559016, EBI-5666736;
CC Q6NZI2; Q9NVF7: FBXO28; NbExp=4; IntAct=EBI-2559016, EBI-740282;
CC Q6NZI2; Q9C086: INO80B; NbExp=3; IntAct=EBI-2559016, EBI-715611;
CC Q6NZI2; Q92993: KAT5; NbExp=3; IntAct=EBI-2559016, EBI-399080;
CC Q6NZI2; Q9BRJ2: MRPL45; NbExp=3; IntAct=EBI-2559016, EBI-2514313;
CC Q6NZI2; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-2559016, EBI-12023934;
CC Q6NZI2; Q5MJ09: SPANXN3; NbExp=3; IntAct=EBI-2559016, EBI-12037215;
CC Q6NZI2; Q8WVP5: TNFAIP8L1; NbExp=3; IntAct=EBI-2559016, EBI-752102;
CC Q6NZI2; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-2559016, EBI-10241197;
CC Q6NZI2; Q8N0Z6: TTC5; NbExp=3; IntAct=EBI-2559016, EBI-9526213;
CC Q6NZI2; Q8IY57-5: YAF2; NbExp=3; IntAct=EBI-2559016, EBI-12111538;
CC Q6NZI2; Q8TBK6: ZCCHC10; NbExp=3; IntAct=EBI-2559016, EBI-597063;
CC Q6NZI2; Q6P2D0: ZFP1; NbExp=3; IntAct=EBI-2559016, EBI-2555749;
CC Q6NZI2; Q9Y5A6: ZSCAN21; NbExp=3; IntAct=EBI-2559016, EBI-10281938;
CC -!- SUBCELLULAR LOCATION: Membrane, caveola {ECO:0000269|PubMed:15242332,
CC ECO:0000269|PubMed:18056712, ECO:0000269|PubMed:19525939}. Cell
CC membrane {ECO:0000269|PubMed:15242332, ECO:0000269|PubMed:17026959,
CC ECO:0000269|PubMed:18056712}. Microsome {ECO:0000269|PubMed:15242332,
CC ECO:0000269|PubMed:17026959}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P85125}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:15242332}. Mitochondrion
CC {ECO:0000269|PubMed:15242332, ECO:0000269|PubMed:17026959}. Nucleus
CC {ECO:0000269|PubMed:15242332, ECO:0000269|PubMed:17026959}.
CC Note=Translocates to the cytoplasm from the caveolae upon insulin
CC stimulation (PubMed:17026959). Colocalizes with CAV1 in lipid rafts in
CC adipocytes. Localizes in the caveolae in a caveolin-dependent manner
CC (By similarity). {ECO:0000250|UniProtKB:O54724,
CC ECO:0000269|PubMed:17026959}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000305};
CC IsoId=Q6NZI2-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q6NZI2-2; Sequence=VSP_051625;
CC Name=3 {ECO:0000305};
CC IsoId=Q6NZI2-3; Sequence=VSP_051624;
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-156
CC is essential for its functionin the regulation of ribosomal
CC transcriptional activity. {ECO:0000250|UniProtKB:O54724}.
CC -!- PTM: Five truncated forms are found in the caveolae. These are thought
CC to be the result of proteolysis and may be phosphorylation-dependent.
CC {ECO:0000269|PubMed:15242332}.
CC -!- PTM: Monoubiquitinated. {ECO:0000250|UniProtKB:O54724}.
CC -!- DISEASE: Congenital generalized lipodystrophy 4 (CGL4) [MIM:613327]: A
CC disorder characterized by the association of congenital generalized
CC lipodystrophy with muscular dystrophy and cardiac anomalies. Congenital
CC generalized lipodystrophy is characterized by a near complete absence
CC of adipose tissue, extreme insulin resistance, hypertriglyceridemia,
CC hepatic steatosis and early onset of diabetes.
CC {ECO:0000269|PubMed:19726876, ECO:0000269|PubMed:20684003}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the CAVIN family. {ECO:0000305}.
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DR EMBL; AF312393; AAG27093.1; -; mRNA.
DR EMBL; AK314389; BAG37014.1; -; mRNA.
DR EMBL; CH471152; EAW60828.1; -; Genomic_DNA.
DR EMBL; BC004295; AAH04295.1; -; mRNA.
DR EMBL; BC008849; AAH08849.1; -; mRNA.
DR EMBL; BC066123; AAH66123.1; -; mRNA.
DR EMBL; BC073759; AAH73759.1; -; mRNA.
DR EMBL; AF000421; AAC63404.1; -; mRNA.
DR CCDS; CCDS11425.1; -. [Q6NZI2-1]
DR RefSeq; NP_036364.2; NM_012232.5. [Q6NZI2-1]
DR AlphaFoldDB; Q6NZI2; -.
DR SMR; Q6NZI2; -.
DR BioGRID; 129767; 231.
DR DIP; DIP-48550N; -.
DR ELM; Q6NZI2; -.
DR IntAct; Q6NZI2; 117.
DR MINT; Q6NZI2; -.
DR STRING; 9606.ENSP00000349541; -.
DR GlyGen; Q6NZI2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6NZI2; -.
DR MetOSite; Q6NZI2; -.
DR PhosphoSitePlus; Q6NZI2; -.
DR SwissPalm; Q6NZI2; -.
DR BioMuta; CAVIN1; -.
DR DMDM; 56749614; -.
DR EPD; Q6NZI2; -.
DR jPOST; Q6NZI2; -.
DR MassIVE; Q6NZI2; -.
DR MaxQB; Q6NZI2; -.
DR PaxDb; Q6NZI2; -.
DR PeptideAtlas; Q6NZI2; -.
DR PRIDE; Q6NZI2; -.
DR ProteomicsDB; 66794; -. [Q6NZI2-1]
DR ProteomicsDB; 66795; -. [Q6NZI2-2]
DR ProteomicsDB; 66796; -. [Q6NZI2-3]
DR Antibodypedia; 29228; 237 antibodies from 34 providers.
DR DNASU; 284119; -.
DR Ensembl; ENST00000357037.6; ENSP00000349541.4; ENSG00000177469.13. [Q6NZI2-1]
DR GeneID; 284119; -.
DR KEGG; hsa:284119; -.
DR MANE-Select; ENST00000357037.6; ENSP00000349541.4; NM_012232.6; NP_036364.2.
DR UCSC; uc002hzo.4; human. [Q6NZI2-1]
DR CTD; 284119; -.
DR DisGeNET; 284119; -.
DR GeneCards; CAVIN1; -.
DR HGNC; HGNC:9688; CAVIN1.
DR HPA; ENSG00000177469; Low tissue specificity.
DR MalaCards; CAVIN1; -.
DR MIM; 603198; gene.
DR MIM; 613327; phenotype.
DR neXtProt; NX_Q6NZI2; -.
DR OpenTargets; ENSG00000177469; -.
DR Orphanet; 528; Congenital generalized lipodystrophy.
DR PharmGKB; PA34031; -.
DR VEuPathDB; HostDB:ENSG00000177469; -.
DR eggNOG; ENOG502QV3D; Eukaryota.
DR GeneTree; ENSGT00950000182910; -.
DR HOGENOM; CLU_039470_0_0_1; -.
DR InParanoid; Q6NZI2; -.
DR OMA; GRCPGAH; -.
DR OrthoDB; 1060453at2759; -.
DR PhylomeDB; Q6NZI2; -.
DR TreeFam; TF331031; -.
DR PathwayCommons; Q6NZI2; -.
DR Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR SignaLink; Q6NZI2; -.
DR BioGRID-ORCS; 284119; 14 hits in 1090 CRISPR screens.
DR ChiTaRS; PTRF; human.
DR GeneWiki; PTRF; -.
DR GenomeRNAi; 284119; -.
DR Pharos; Q6NZI2; Tbio.
DR PRO; PR:Q6NZI2; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q6NZI2; protein.
DR Bgee; ENSG00000177469; Expressed in right coronary artery and 199 other tissues.
DR Genevisible; Q6NZI2; HS.
DR GO; GO:0005901; C:caveola; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0042134; F:rRNA primary transcript binding; IDA:UniProtKB.
DR GO; GO:2000147; P:positive regulation of cell motility; ISS:UniProtKB.
DR GO; GO:0009306; P:protein secretion; IEA:Ensembl.
DR GO; GO:0009303; P:rRNA transcription; ISS:UniProtKB.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IDA:UniProtKB.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; IDA: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; Alternative splicing; Cell membrane; Coiled coil;
KW Congenital generalized lipodystrophy; Cytoplasm; Diabetes mellitus;
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..390
FT /note="Caveolae-associated protein 1"
FT /id="PRO_0000097094"
FT REGION 1..98
FT /note="Required for homotrimerization and for interaction
FT with CAVIN2 and CAVIN3"
FT /evidence="ECO:0000250|UniProtKB:O54724"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..62
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:O54724"
FT REGION 53..75
FT /note="Leucine-zipper 1"
FT /evidence="ECO:0000250|UniProtKB:O54724"
FT REGION 136..152
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:O54724"
FT REGION 166..186
FT /note="Leucine-zipper 2"
FT /evidence="ECO:0000250|UniProtKB:O54724"
FT REGION 172..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..249
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:O54724"
FT REGION 257..297
FT /note="Leucine-zipper 3"
FT /evidence="ECO:0000250|UniProtKB:O54724"
FT REGION 344..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 199..282
FT /evidence="ECO:0000255"
FT COMPBIAS 174..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:15242332"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15242332"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15242332"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P85125"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 156
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O54724"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54724"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P85125"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 302
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 308
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15242332,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15242332,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT CROSSLNK 116
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 161
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 161
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733"
FT CROSSLNK 165
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 170
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 326
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..193
FT /note="MEDPTLYIVERPLPGYPDAEAPEPSSAGAQAAEEPSGAGSEELIKSDQVNGV
FT LVLSLLDKIIGAVDQIQLTQAQLEERQAEMEGAVQSIQGELSKLGKAHATTSNTVSKLL
FT EKVRKVSVNVKTVRGSLERQAGQIKKLEVNEAELLRRRNFKVMIYQDEVKLPAKLSISK
FT SLKESEALPEKEGEELGEGERPE -> M (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051624"
FT VAR_SEQ 96..185
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051625"
FT VARIANT 14
FT /note="P -> T (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035982"
FT VARIANT 193
FT /note="E -> Q (in dbSNP:rs35308568)"
FT /id="VAR_034416"
FT CONFLICT 47
FT /note="D -> V (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="I -> L (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="E -> K (in Ref. 1; AAG27093)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 43476 MW; E37945A9C9E819D4 CRC64;
MEDPTLYIVE RPLPGYPDAE APEPSSAGAQ AAEEPSGAGS EELIKSDQVN GVLVLSLLDK
IIGAVDQIQL TQAQLEERQA EMEGAVQSIQ GELSKLGKAH ATTSNTVSKL LEKVRKVSVN
VKTVRGSLER QAGQIKKLEV NEAELLRRRN FKVMIYQDEV KLPAKLSISK SLKESEALPE
KEGEELGEGE RPEEDAAALE LSSDEAVEVE EVIEESRAER IKRSGLRRVD DFKKAFSKEK
MEKTKVRTRE NLEKTRLKTK ENLEKTRHTL EKRMNKLGTR LVPAERREKL KTSRDKLRKS
FTPDHVVYAR SKTAVYKVPP FTFHVKKIRE GQVEVLKATE MVEVGADDDE GGAERGEAGD
LRRGSSPDVH ALLEITEESD AVLVDKSDSD
