CAVN2_MOUSE
ID CAVN2_MOUSE Reviewed; 418 AA.
AC Q63918; Q3V1P6; Q78EC3; Q8CBT4;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Caveolae-associated protein 2;
DE AltName: Full=Cavin-2;
DE AltName: Full=Phosphatidylserine-binding protein;
DE AltName: Full=Serum deprivation-response protein;
GN Name=Cavin2;
GN Synonyms=Sdpr {ECO:0000312|MGI:MGI:99513},
GN Sdr {ECO:0000303|PubMed:8241023};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAB28953.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=8241023;
RA Gustincich S., Schneider C.;
RT "Serum deprivation response gene is induced by serum starvation but not by
RT contact inhibition.";
RL Cell Growth Differ. 4:753-760(1993).
RN [2] {ECO:0000312|EMBL:BAC39116.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC39116.1};
RC TISSUE=Embryonic head {ECO:0000312|EMBL:BAE21104.1},
RC Embryonic spinal ganglion {ECO:0000312|EMBL:BAC39116.1}, and
RC Urinary bladder {ECO:0000312|EMBL:BAC29033.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|EMBL:AAH20008.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH27005.1}, and
RC FVB/N {ECO:0000312|EMBL:AAH20008.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH20008.1}, and
RC Retina {ECO:0000312|EMBL:AAH27005.1};
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218 AND SER-293, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=18332105; DOI=10.1128/mcb.02186-07;
RA Ogata T., Ueyama T., Isodono K., Tagawa M., Takehara N., Kawashima T.,
RA Harada K., Takahashi T., Shioi T., Matsubara H., Oh H.;
RT "MURC, a muscle-restricted coiled-coil protein that modulates the Rho/ROCK
RT pathway, induces cardiac dysfunction and conduction disturbance.";
RL Mol. Cell. Biol. 28:3424-3436(2008).
RN [6]
RP IDENTIFICATION IN THE CAVIN COMPLEX, INTERACTION WITH CAVIN1, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=19546242; DOI=10.1083/jcb.200903053;
RA Bastiani M., Liu L., Hill M.M., Jedrychowski M.P., Nixon S.J., Lo H.P.,
RA Abankwa D., Luetterforst R., Fernandez-Rojo M., Breen M.R., Gygi S.P.,
RA Vinten J., Walser P.J., North K.N., Hancock J.F., Pilch P.F., Parton R.G.;
RT "MURC/Cavin-4 and cavin family members form tissue-specific caveolar
RT complexes.";
RL J. Cell Biol. 185:1259-1273(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; SER-293; SER-359 AND
RP SER-363, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-35; SER-37; SER-203;
RP SER-204; SER-218; SER-283; SER-284; SER-287; SER-288; SER-293; SER-296;
RP SER-327; SER-336; SER-359; SER-363; THR-368; TYR-388 AND SER-390, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=23652019; DOI=10.1038/ncomms2808;
RA Hansen C.G., Shvets E., Howard G., Riento K., Nichols B.J.;
RT "Deletion of cavin genes reveals tissue-specific mechanisms for
RT morphogenesis of endothelial caveolae.";
RL Nat. Commun. 4:1831-1831(2013).
RN [10]
RP INTERACTION WITH CAVIN1.
RX PubMed=25588833; DOI=10.1242/jcs.161463;
RA Mohan J., Moren B., Larsson E., Holst M.R., Lundmark R.;
RT "Cavin3 interacts with cavin1 and caveolin1 to increase surface dynamics of
RT caveolae.";
RL J. Cell Sci. 128:979-991(2015).
CC -!- FUNCTION: Plays an important role in caveolar biogenesis and
CC morphology. Regulates caveolae morphology by inducing membrane
CC curvature within caveolae (By similarity). Plays a role in caveola
CC formation in a tissue-specific manner. Required for the formation of
CC caveolae in the lung and fat endothelia but not in the heart
CC endothelia. Negatively regulates the size or stability of CAVIN
CC complexes in the lung endothelial cells (PubMed:23652019). May play a
CC role in targeting PRKCA to caveolae (By similarity).
CC {ECO:0000250|UniProtKB:O95810, ECO:0000250|UniProtKB:Q66H98,
CC ECO:0000269|PubMed:23652019}.
CC -!- SUBUNIT: Component of the CAVIN complex composed of CAVIN1, CAVIN2,
CC CAVIN3 and CAVIN4 (PubMed:19546242). Binds to PRKCA in the presence of
CC phosphatidylserine. Interacts with CAVIN4; this augments the
CC transactivation of NPPA by CAVIN4 (By similarity). Interacts with
CC CAVIN1 (PubMed:25588833, PubMed:19546242). Interacts with CAV3 (By
CC similarity). {ECO:0000250|UniProtKB:O95810,
CC ECO:0000250|UniProtKB:Q66H98, ECO:0000269|PubMed:19546242,
CC ECO:0000269|PubMed:25588833}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18332105,
CC ECO:0000269|PubMed:19546242}. Membrane, caveola
CC {ECO:0000269|PubMed:19546242}. Note=Localizes in the caveolae in a
CC caveolin-dependent manner. {ECO:0000269|PubMed:19546242}.
CC -!- TISSUE SPECIFICITY: Heart, adipose tissue, lung and endothelial cells
CC (at protein level). Highly expressed in kidney and expressed at lower
CC levels in liver, spleen, thymus, stomach, intestine and uterus.
CC {ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:23652019,
CC ECO:0000269|PubMed:8241023}.
CC -!- DEVELOPMENTAL STAGE: Expression gradually increases during embryonic
CC stages and reaches a maximum in neonates.
CC {ECO:0000269|PubMed:18332105}.
CC -!- INDUCTION: Up-regulated in response to cardiac hypertrophy and in
CC serum-starved but not in density-dependent growth-arrested NIH3T3
CC cells. Down-regulated within 6 hours after the addition of serum or
CC epidermal growth factor to serum-starved cells.
CC {ECO:0000269|PubMed:18332105, ECO:0000269|PubMed:8241023}.
CC -!- DOMAIN: The leucine-zipper domain is essential for its localization in
CC the caveolae. {ECO:0000250|UniProtKB:O95810}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice show loss of endothelial caveolae in lung
CC and adipose tissue but no effect on the abundance of endothelial
CC caveolae in the heart. {ECO:0000269|PubMed:23652019}.
CC -!- MISCELLANEOUS: Binds phosphatidylserine (PS) in a calcium-independent
CC manner. PS-binding is inhibited by phosphotidic acid and
CC phosphatidylinositol. Does not bind phosphatidylcholine (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CAVIN family. {ECO:0000305}.
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DR EMBL; S67386; AAB28953.1; -; mRNA.
DR EMBL; AK035324; BAC29033.1; -; mRNA.
DR EMBL; AK084096; BAC39116.1; -; mRNA.
DR EMBL; AK132324; BAE21104.1; -; mRNA.
DR EMBL; BC020008; AAH20008.1; -; mRNA.
DR EMBL; BC027005; AAH27005.1; -; mRNA.
DR CCDS; CCDS14940.1; -.
DR RefSeq; NP_620080.1; NM_138741.1.
DR AlphaFoldDB; Q63918; -.
DR SMR; Q63918; -.
DR BioGRID; 203146; 2.
DR IntAct; Q63918; 3.
DR MINT; Q63918; -.
DR STRING; 10090.ENSMUSP00000055694; -.
DR iPTMnet; Q63918; -.
DR PhosphoSitePlus; Q63918; -.
DR SwissPalm; Q63918; -.
DR CPTAC; non-CPTAC-3772; -.
DR jPOST; Q63918; -.
DR MaxQB; Q63918; -.
DR PaxDb; Q63918; -.
DR PeptideAtlas; Q63918; -.
DR PRIDE; Q63918; -.
DR ProteomicsDB; 265671; -.
DR Antibodypedia; 34051; 129 antibodies from 27 providers.
DR DNASU; 20324; -.
DR Ensembl; ENSMUST00000051572; ENSMUSP00000055694; ENSMUSG00000045954.
DR GeneID; 20324; -.
DR KEGG; mmu:20324; -.
DR UCSC; uc007axk.1; mouse.
DR CTD; 8436; -.
DR MGI; MGI:99513; Cavin2.
DR VEuPathDB; HostDB:ENSMUSG00000045954; -.
DR eggNOG; ENOG502QQCA; Eukaryota.
DR GeneTree; ENSGT00950000182910; -.
DR HOGENOM; CLU_039470_1_0_1; -.
DR InParanoid; Q63918; -.
DR OMA; QMPNDQE; -.
DR OrthoDB; 858587at2759; -.
DR PhylomeDB; Q63918; -.
DR TreeFam; TF331031; -.
DR BioGRID-ORCS; 20324; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Sdpr; mouse.
DR PRO; PR:Q63918; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q63918; protein.
DR Bgee; ENSMUSG00000045954; Expressed in right lung and 232 other tissues.
DR Genevisible; Q63918; MM.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB.
DR GO; GO:0005080; F:protein kinase C binding; IBA:GO_Central.
DR GO; GO:0097320; P:plasma membrane tubulation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR InterPro; IPR033298; Cavin2.
DR InterPro; IPR026752; Cavin_fam.
DR PANTHER; PTHR15240; PTHR15240; 1.
DR PANTHER; PTHR15240:SF1; PTHR15240:SF1; 1.
DR Pfam; PF15237; PTRF_SDPR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Lipid-binding; Membrane;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O95810"
FT CHAIN 2..418
FT /note="Caveolae-associated protein 2"
FT /id="PRO_0000238919"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..168
FT /note="Interaction with CAVIN1"
FT /evidence="ECO:0000269|PubMed:25588833"
FT REGION 62..100
FT /note="Leucine-zipper"
FT /evidence="ECO:0000250|UniProtKB:O95810"
FT REGION 200..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 61..87
FT /evidence="ECO:0000255"
FT COILED 126..268
FT /evidence="ECO:0000255"
FT COMPBIAS 220..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:O95810"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66H98"
FT MOD_RES 196
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95810"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 368
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 388
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66H98"
FT CONFLICT 14
FT /note="P -> L (in Ref. 2; BAE21104)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="Q -> L (in Ref. 2; BAC29033)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="K -> R (in Ref. 2; BAC29033)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 46764 MW; EFD7B4E383785F41 CRC64;
MGEDAAQAEK FQHPNTDMLQ EKPSSPSPMP SSTPSPSLNL GSTEEAIRDN SQVNAVTVHT
LLDKLVNMLD AVRENQHNME QRQINLEGSV KGIQNDLTKL SKYQASTSNT VSKLLEKSRK
VSAHTRAVRE RLERQCVQVK RLENNHAQLL RRNHFKVLIF QEESEIPASV FVKEPVPSAA
EGKEELADEN KSLEETLHNV DLSSDDELPR DEEALEDSAE EKMEESRAEK IKRSSLKKVD
SLKKAFSRQN IEKKMNKLGT KIVSVERREK IKKSLTPNHQ KASSGKSSPF KVSPLSFGRK
KVREGESSVE NETKLEDQMQ EDREEGSFTE GLSEASLPSG LMEGSAEDAE KSARRGNNSA
VGSNADLTIE EDEEEEPVAL QQAQQVRYES GYMLNSEEME EPSEKQVQPA VLHVDQTA
