CDV3_MOUSE
ID CDV3_MOUSE Reviewed; 281 AA.
AC Q4VAA2; Q6P6L7; Q920C7; Q920I4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Protein CDV3;
DE AltName: Full=Carnitine deficiency-associated protein 3;
DE AltName: Full=Tyrosine-phosphorylated protein 36;
DE Short=TPP36;
GN Name=Cdv3;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND TISSUE
RP SPECIFICITY.
RC STRAIN=129/SvJ, and C3H/HeJ;
RX PubMed=12359334; DOI=10.1016/s0167-4781(02)00447-5;
RA Fukumaru S., Horiuchi M., Kobayashi K., Jalil M.A., Iijima M., Masuda M.,
RA Begum L., Higashi M., Wakana S., Kanzaki T., Saheki T.;
RT "Novel mRNA molecules are induced in hypertrophied ventricles of carnitine-
RT deficient mice and belong to a family of up-regulated gene in cells
RT overexpressing c-erbB-2.";
RL Biochim. Biophys. Acta 1577:437-444(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORMS 1
RP AND 2), PHOSPHORYLATION AT TYR-120, ACETYLATION AT ALA-2, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12606058; DOI=10.1016/s0014-5793(03)00127-3;
RA Tsuchiya K., Kawano Y., Kojima T., Nagata K., Takao T., Okada M.,
RA Shinohara H., Maki K., Toyama-Sorimachi N., Miyasaka N., Watanabe M.,
RA Karasuyama H.;
RT "Molecular cloning and characterization of TPP36 and its isoform TPP32,
RT novel substrates of Abl tyrosine kinase.";
RL FEBS Lett. 537:203-209(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=NMRI; TISSUE=Limb, Mammary tumor, and Olfactory epithelium;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-213, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-213, AND IDENTIFICATION BY
RP 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 [7]
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).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12606058}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=B;
CC IsoId=Q4VAA2-1; Sequence=Displayed;
CC Name=2; Synonyms=A;
CC IsoId=Q4VAA2-2; Sequence=VSP_027762, VSP_027763;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (at protein level). Up-
CC regulated in ventricles of juvenile visceral steatosis mice.
CC {ECO:0000269|PubMed:12359334, ECO:0000269|PubMed:12606058}.
CC -!- PTM: Isoform 1 and isoform 2 are phosphorylated on tyrosines by ABL1 in
CC B-cells. {ECO:0000269|PubMed:12606058}.
CC -!- SIMILARITY: Belongs to the CDV3 family. {ECO:0000305}.
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DR EMBL; AF215660; AAL27860.1; -; mRNA.
DR EMBL; AF320340; AAL30162.1; -; mRNA.
DR EMBL; AF414107; AAL65134.1; -; Genomic_DNA.
DR EMBL; AF414103; AAL65134.1; JOINED; Genomic_DNA.
DR EMBL; AF414104; AAL65134.1; JOINED; Genomic_DNA.
DR EMBL; AF414105; AAL65134.1; JOINED; Genomic_DNA.
DR EMBL; AF414106; AAL65134.1; JOINED; Genomic_DNA.
DR EMBL; AF414107; AAL65135.1; -; Genomic_DNA.
DR EMBL; AF414103; AAL65135.1; JOINED; Genomic_DNA.
DR EMBL; AF414104; AAL65135.1; JOINED; Genomic_DNA.
DR EMBL; AF414105; AAL65135.1; JOINED; Genomic_DNA.
DR EMBL; AF414106; AAL65135.1; JOINED; Genomic_DNA.
DR EMBL; AB046372; BAB82988.1; -; mRNA.
DR EMBL; BC052770; AAH52770.1; -; mRNA.
DR EMBL; BC062156; AAH62156.1; -; mRNA.
DR EMBL; BC096479; AAH96479.1; -; mRNA.
DR CCDS; CCDS23454.1; -. [Q4VAA2-1]
DR CCDS; CCDS40748.1; -. [Q4VAA2-2]
DR RefSeq; NP_780774.1; NM_175565.3. [Q4VAA2-2]
DR RefSeq; NP_787027.1; NM_175833.2. [Q4VAA2-1]
DR AlphaFoldDB; Q4VAA2; -.
DR SMR; Q4VAA2; -.
DR IntAct; Q4VAA2; 1.
DR STRING; 10090.ENSMUSP00000044420; -.
DR iPTMnet; Q4VAA2; -.
DR PhosphoSitePlus; Q4VAA2; -.
DR CPTAC; non-CPTAC-4022; -.
DR EPD; Q4VAA2; -.
DR jPOST; Q4VAA2; -.
DR MaxQB; Q4VAA2; -.
DR PaxDb; Q4VAA2; -.
DR PeptideAtlas; Q4VAA2; -.
DR PRIDE; Q4VAA2; -.
DR ProteomicsDB; 283872; -. [Q4VAA2-1]
DR ProteomicsDB; 283873; -. [Q4VAA2-2]
DR Antibodypedia; 33371; 89 antibodies from 17 providers.
DR DNASU; 321022; -.
DR Ensembl; ENSMUST00000035484; ENSMUSP00000044420; ENSMUSG00000032803. [Q4VAA2-1]
DR Ensembl; ENSMUST00000072249; ENSMUSP00000072101; ENSMUSG00000032803. [Q4VAA2-2]
DR GeneID; 321022; -.
DR KEGG; mmu:321022; -.
DR UCSC; uc009rgo.1; mouse. [Q4VAA2-1]
DR UCSC; uc009rgq.1; mouse. [Q4VAA2-2]
DR CTD; 55573; -.
DR MGI; MGI:2448759; Cdv3.
DR VEuPathDB; HostDB:ENSMUSG00000032803; -.
DR eggNOG; ENOG502QRFT; Eukaryota.
DR GeneTree; ENSGT00390000000805; -.
DR HOGENOM; CLU_089760_1_0_1; -.
DR InParanoid; Q4VAA2; -.
DR OMA; SSKMYIS; -.
DR OrthoDB; 1568537at2759; -.
DR PhylomeDB; Q4VAA2; -.
DR TreeFam; TF315891; -.
DR BioGRID-ORCS; 321022; 3 hits in 69 CRISPR screens.
DR ChiTaRS; Cdv3; mouse.
DR PRO; PR:Q4VAA2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q4VAA2; protein.
DR Bgee; ENSMUSG00000032803; Expressed in floor plate of midbrain and 251 other tissues.
DR ExpressionAtlas; Q4VAA2; baseline and differential.
DR Genevisible; Q4VAA2; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR InterPro; IPR026806; CDV3.
DR PANTHER; PTHR16284; PTHR16284; 1.
DR Pfam; PF15359; CDV3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12606058"
FT CHAIN 2..281
FT /note="Protein CDV3"
FT /id="PRO_0000299561"
FT REGION 1..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:12606058"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKY7"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKY7"
FT MOD_RES 120
FT /note="Phosphotyrosine; by ABL"
FT /evidence="ECO:0000269|PubMed:12606058"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKY7"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XIM5"
FT MOD_RES 205
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKY7"
FT MOD_RES 213
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660,
FT ECO:0007744|PubMed:19131326"
FT MOD_RES 267
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKY7"
FT VAR_SEQ 232..236
FT /note="KDKEM -> NRYLK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12359334"
FT /id="VSP_027762"
FT VAR_SEQ 237..281
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12359334"
FT /id="VSP_027763"
FT CONFLICT 81..88
FT /note="Missing (in Ref. 3; AAH62156)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="T -> M (in Ref. 3; AAH96479)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="L -> F (in Ref. 3; AAH96479)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 281 AA; 29729 MW; 1A5BAA4B06D264C5 CRC64;
MAETEERSLD NFFAKRDKKK KKERSSRAAN AASGAGGSSA AAGSRPGDGG SLGSGARSGD
GGSLGSGSRS GDGGSSGSGA RSGDGGSSRS GDGGSAGPAG KAITKDENEW KEFEQREVDY
SGLRVQAMQI SEKEDDDNEK REDPGDNWEE GGGGSGAEKS SGPWNKTAPV QAPPAPVTVT
ETPEPAMPSG VYRPPGARLT TTRKTPQGPP EIYSDTQFPS LQSTAKHVES RKDKEMEKSF
EVVRHKNRDR EEVSKNQALK LQLDNQYAVL ENQKYSHTQY S
