TPD52_MOUSE
ID TPD52_MOUSE Reviewed; 224 AA.
AC Q62393; Q545M5; Q8CCU1; Q8K564; Q99KP8;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Tumor protein D52;
DE Short=mD52;
GN Name=Tpd52;
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 [MRNA] (ISOFORM 2).
RC TISSUE=Mammary gland;
RX PubMed=8812487; DOI=10.1006/geno.1996.0393;
RA Byrne J.A., Mattei M.-G., Basset P.;
RT "Definition of the tumor protein D52 (TPD52) gene family through cloning of
RT D52 homologues in human (hD53) and mouse (mD52).";
RL Genomics 35:523-532(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zhou J.-G., Huang C.-F.;
RT "Cloning and characterization of PC-1 homolog in Mouse (mPC-1).";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Amnion, Bone marrow macrophage, Dendritic cell, Medulla oblongata,
RC Placenta, and Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland;
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 [6]
RP PROTEIN SEQUENCE OF 110-123, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=8632896;
RA Chen S.-L., Maroulakou I.G., Green J.E., Romano-Spica V., Modi W.,
RA Lautenberger J., Bhat N.K.;
RT "Isolation and characterization of a novel gene expressed in multiple
RT cancers.";
RL Oncogene 12:741-751(1996).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35; SER-36; SER-40 AND
RP SER-175, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138 (ISOFORM 3), 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).
CC -!- SUBUNIT: Forms a homodimer or heterodimer with other members of the
CC family. {ECO:0000250}.
CC -!- INTERACTION:
CC Q62393; P55327: TPD52; Xeno; NbExp=2; IntAct=EBI-782591, EBI-782581;
CC Q62393; Q16890: TPD52L1; Xeno; NbExp=3; IntAct=EBI-782591, EBI-717470;
CC Q62393; O43399-2: TPD52L2; Xeno; NbExp=2; IntAct=EBI-782591, EBI-782616;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q62393-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62393-2; Sequence=VSP_037379;
CC Name=3;
CC IsoId=Q62393-3; Sequence=VSP_037379, VSP_037380;
CC -!- TISSUE SPECIFICITY: Isoform 2 is expressed at higher levels in kidney
CC and brain than in liver, lung, testis and heart. Within the brain,
CC isoform 2 is highly expressed in the granular layer of the cerebellum,
CC the cortex and the hippocampus. In embryos, isoform 2 is expressed in
CC the epithelium of the developing intestine, stomach, olfactory
CC epithelium, neuronal layers of the retina, salivary gland, kidney and
CC dorsal root ganglion. {ECO:0000269|PubMed:8632896}.
CC -!- SIMILARITY: Belongs to the TPD52 family. {ECO:0000305}.
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DR EMBL; U44426; AAB40897.1; -; mRNA.
DR EMBL; AY048852; AAL05266.1; -; mRNA.
DR EMBL; AK005456; BAB24048.1; -; mRNA.
DR EMBL; AK032111; BAC27709.1; -; mRNA.
DR EMBL; AK151471; BAE30428.1; -; mRNA.
DR EMBL; AK151744; BAE30655.1; -; mRNA.
DR EMBL; AK152543; BAE31298.1; -; mRNA.
DR EMBL; AK153266; BAE31856.1; -; mRNA.
DR EMBL; AK153292; BAE31875.1; -; mRNA.
DR EMBL; AK161753; BAE36558.1; -; mRNA.
DR EMBL; AK168379; BAE40308.1; -; mRNA.
DR EMBL; AK168817; BAE40644.1; -; mRNA.
DR EMBL; AK169751; BAE41345.1; -; mRNA.
DR EMBL; AK170725; BAE41982.1; -; mRNA.
DR EMBL; AK171050; BAE42212.1; -; mRNA.
DR EMBL; CH466577; EDL05193.1; -; Genomic_DNA.
DR EMBL; BC002036; AAH02036.1; -; mRNA.
DR EMBL; BC004068; AAH04068.1; -; mRNA.
DR EMBL; BC094018; AAH94018.1; -; mRNA.
DR CCDS; CCDS38384.1; -. [Q62393-3]
DR CCDS; CCDS38386.1; -. [Q62393-1]
DR CCDS; CCDS50860.1; -. [Q62393-2]
DR RefSeq; NP_001020433.1; NM_001025262.1. [Q62393-1]
DR RefSeq; NP_001020434.1; NM_001025263.1. [Q62393-3]
DR RefSeq; NP_033438.1; NM_009412.2. [Q62393-2]
DR AlphaFoldDB; Q62393; -.
DR SMR; Q62393; -.
DR BioGRID; 204287; 9.
DR IntAct; Q62393; 4.
DR STRING; 10090.ENSMUSP00000091943; -.
DR iPTMnet; Q62393; -.
DR PhosphoSitePlus; Q62393; -.
DR EPD; Q62393; -.
DR jPOST; Q62393; -.
DR MaxQB; Q62393; -.
DR PeptideAtlas; Q62393; -.
DR PRIDE; Q62393; -.
DR ProteomicsDB; 297501; -. [Q62393-1]
DR ProteomicsDB; 297502; -. [Q62393-2]
DR ProteomicsDB; 297503; -. [Q62393-3]
DR DNASU; 21985; -.
DR Ensembl; ENSMUST00000091354; ENSMUSP00000088913; ENSMUSG00000027506. [Q62393-1]
DR Ensembl; ENSMUST00000091355; ENSMUSP00000088914; ENSMUSG00000027506. [Q62393-3]
DR Ensembl; ENSMUST00000120143; ENSMUSP00000112830; ENSMUSG00000027506. [Q62393-2]
DR GeneID; 21985; -.
DR KEGG; mmu:21985; -.
DR UCSC; uc008oos.1; mouse. [Q62393-1]
DR UCSC; uc008oot.1; mouse. [Q62393-3]
DR UCSC; uc008oov.1; mouse. [Q62393-2]
DR CTD; 7163; -.
DR MGI; MGI:107749; Tpd52.
DR VEuPathDB; HostDB:ENSMUSG00000027506; -.
DR eggNOG; KOG4010; Eukaryota.
DR GeneTree; ENSGT00940000155294; -.
DR InParanoid; Q62393; -.
DR OrthoDB; 1225782at2759; -.
DR PhylomeDB; Q62393; -.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR BioGRID-ORCS; 21985; 6 hits in 72 CRISPR screens.
DR ChiTaRS; Tpd52; mouse.
DR PRO; PR:Q62393; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q62393; protein.
DR Bgee; ENSMUSG00000027506; Expressed in prostate gland ventral lobe and 290 other tissues.
DR ExpressionAtlas; Q62393; baseline and differential.
DR Genevisible; Q62393; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
DR InterPro; IPR007327; TPD52.
DR PANTHER; PTHR19307; PTHR19307; 1.
DR Pfam; PF04201; TPD52; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Direct protein sequencing;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..224
FT /note="Tumor protein D52"
FT /id="PRO_0000185739"
FT REGION 29..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 61..113
FT /evidence="ECO:0000255"
FT COMPBIAS 29..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 35
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55327"
FT VAR_SEQ 1..45
FT /note="MECRDMELADDYQSPFDFDSGVNKNYLYLSPSGNTSPPGSPTQNV -> MDR
FT GEQ (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:8812487"
FT /id="VSP_037379"
FT VAR_SEQ 168
FT /note="K -> NIRSIQHSISMPAMR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_037380"
FT CONFLICT 129
FT /note="V -> L (in Ref. 5; AAH04068)"
FT /evidence="ECO:0000305"
FT MOD_RES Q62393-3:138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 224 AA; 24313 MW; C80D8AB9038B0D73 CRC64;
MECRDMELAD DYQSPFDFDS GVNKNYLYLS PSGNTSPPGS PTQNVGLLKT EPVAEEGEDA
VTMLSAPEAL TEEEQEELRR ELTKVEEEIQ TLSQVLAAKE KHLAELKRKL GISSLQEFKQ
NIAKGWQDVT ATNAYKKTSE TLSQAGQKAS AAFSSVGSVI TKKLEDVKNS PTFKSFEEKV
ENLKSKVGGA KPAGGDFGEV LNSTANATST MTTEPPPEQM TESP
