PDC10_MOUSE
ID PDC10_MOUSE Reviewed; 212 AA.
AC Q8VE70; Q9DAR3; Q9WV43;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Programmed cell death protein 10;
DE AltName: Full=TF-1 cell apoptosis-related protein 15;
GN Name=Pdcd10; Synonyms=Tfar15;
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].
RA Sun R., Huang J., Han W., Wang Y., Zhang Y., Song Q., Ma D.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Kidney, Pituitary, Testis, Thymus, and Urinary bladder;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and 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 [4]
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 [5]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP KDR.
RX PubMed=20371769; DOI=10.1126/scisignal.2000722;
RA He Y., Zhang H., Yu L., Gunel M., Boggon T.J., Chen H., Min W.;
RT "Stabilization of VEGFR2 signaling by cerebral cavernous malformation 3 is
RT critical for vascular development.";
RL Sci. Signal. 3:RA26-RA26(2010).
CC -!- FUNCTION: Promotes cell proliferation. Modulates apoptotic pathways.
CC Increases mitogen-activated protein kinase activity and STK26 activity.
CC Important for cell migration, and for normal structure and assembly of
CC the Golgi complex (By similarity). Important for KDR/VEGFR2 signaling.
CC Increases the stability of KDR/VEGFR2 and prevents its breakdown.
CC Required for normal cardiovascular development. Required for normal
CC angiogenesis, vasculogenesis and hematopoiesis during embryonic
CC development (By similarity). {ECO:0000250|UniProtKB:Q9BUL8,
CC ECO:0000269|PubMed:20371769}.
CC -!- SUBUNIT: Homodimer. Interacts (via C-terminus) with CCM2. Interacts
CC (via C-terminus) with PXN. Interacts (via N-terminus) with STK25.
CC Interacts (via N-terminus) with STK26. Interacts (via N-terminus) with
CC STK24. Interacts with GOLGA2. Identified in a complex with KRIT1 and
CC CCM2. Interacts with KDR/VEGFR2 (By similarity). Interaction with
CC KDR/VEGFR2 is enhanced by stimulation with VEGFA (PubMed:20371769).
CC Interacts with RIPOR1 (via C-terminus); this interaction is required
CC for the association of RIPOR1 with either STK24 and STK26 kinases and
CC occurs in a Rho-independent manner (By similarity).
CC {ECO:0000250|UniProtKB:Q9BUL8, ECO:0000269|PubMed:20371769}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:20371769};
CC Peripheral membrane protein {ECO:0000269|PubMed:20371769}; Cytoplasmic
CC side {ECO:0000269|PubMed:20371769}. Note=Partially colocalizes with
CC endogenous PXN at the leading edges of migrating cells. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Lethal at an early embryonic stage due to defects
CC in angiogenesis, vasculogenesis and hematopoiesis. Mice exhibit low
CC levels of KDR/VEGFR2. {ECO:0000269|PubMed:20371769}.
CC -!- SIMILARITY: Belongs to the PDCD10 family. {ECO:0000305}.
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DR EMBL; AF159368; AAD44335.1; -; mRNA.
DR EMBL; AK005594; BAB24143.1; -; mRNA.
DR EMBL; AK075926; BAC36058.1; -; mRNA.
DR EMBL; AK077308; BAC36742.1; -; mRNA.
DR EMBL; AK137198; BAE23263.1; -; mRNA.
DR EMBL; AK168857; BAE40678.1; -; mRNA.
DR EMBL; AK169689; BAE41306.1; -; mRNA.
DR EMBL; BC019650; AAH19650.1; -; mRNA.
DR EMBL; BC086778; AAH86778.1; -; mRNA.
DR CCDS; CCDS17414.1; -.
DR RefSeq; NP_062719.2; NM_019745.4.
DR AlphaFoldDB; Q8VE70; -.
DR SMR; Q8VE70; -.
DR BioGRID; 207970; 20.
DR ComplexPortal; CPX-4621; CCM complex.
DR CORUM; Q8VE70; -.
DR IntAct; Q8VE70; 1.
DR MINT; Q8VE70; -.
DR STRING; 10090.ENSMUSP00000125752; -.
DR PhosphoSitePlus; Q8VE70; -.
DR EPD; Q8VE70; -.
DR jPOST; Q8VE70; -.
DR MaxQB; Q8VE70; -.
DR PaxDb; Q8VE70; -.
DR PeptideAtlas; Q8VE70; -.
DR PRIDE; Q8VE70; -.
DR ProteomicsDB; 287898; -.
DR Antibodypedia; 18593; 278 antibodies from 31 providers.
DR DNASU; 56426; -.
DR Ensembl; ENSMUST00000161137; ENSMUSP00000125752; ENSMUSG00000027835.
DR GeneID; 56426; -.
DR KEGG; mmu:56426; -.
DR UCSC; uc008pnc.2; mouse.
DR CTD; 11235; -.
DR MGI; MGI:1928396; Pdcd10.
DR VEuPathDB; HostDB:ENSMUSG00000027835; -.
DR eggNOG; KOG4025; Eukaryota.
DR GeneTree; ENSGT00390000017913; -.
DR InParanoid; Q8VE70; -.
DR OMA; HVVLFPI; -.
DR OrthoDB; 1507394at2759; -.
DR PhylomeDB; Q8VE70; -.
DR TreeFam; TF105802; -.
DR BioGRID-ORCS; 56426; 16 hits in 77 CRISPR screens.
DR ChiTaRS; Pdcd10; mouse.
DR PRO; PR:Q8VE70; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8VE70; protein.
DR Bgee; ENSMUSG00000027835; Expressed in spermatocyte and 286 other tissues.
DR ExpressionAtlas; Q8VE70; baseline and differential.
DR Genevisible; Q8VE70; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0090443; C:FAR/SIN/STRIPAK complex; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0003158; P:endothelium development; IC:ComplexPortal.
DR GO; GO:0051683; P:establishment of Golgi localization; ISO:MGI.
DR GO; GO:0090168; P:Golgi reassembly; ISO:MGI.
DR GO; GO:0036481; P:intrinsic apoptotic signaling pathway in response to hydrogen peroxide; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:1903588; P:negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISO:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0045765; P:regulation of angiogenesis; IC:ComplexPortal.
DR GO; GO:1903358; P:regulation of Golgi organization; IBA:GO_Central.
DR GO; GO:0042542; P:response to hydrogen peroxide; ISO:MGI.
DR GO; GO:0044319; P:wound healing, spreading of cells; ISO:MGI.
DR Gene3D; 1.10.12.70; -; 1.
DR InterPro; IPR046409; PDC10_dimerisation_sf.
DR InterPro; IPR009652; PDCD10.
DR PANTHER; PTHR13250; PTHR13250; 1.
PE 1: Evidence at protein level;
KW Acetylation; Angiogenesis; Apoptosis; Cell membrane; Cytoplasm;
KW Golgi apparatus; Isopeptide bond; Membrane; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..212
FT /note="Programmed cell death protein 10"
FT /id="PRO_0000187563"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUL8"
FT CROSSLNK 186
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BUL8"
FT CONFLICT 3
FT /note="M -> V (in Ref. 2; BAB24143)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="A -> E (in Ref. 2; BAB24143)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="A -> Q (in Ref. 2; BAB24143)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 212 AA; 24716 MW; 5AA613F709C63F56 CRC64;
MRMTMEEMKN EAETTSMVSM PLYAVMYPVF NELERVNLSA AQTLRAAFIK AEKENPGLTQ
DIIMKILEKK SVEVNFTESL LRMAADDVEE YMIERPEPEF QDLNEKARAL KQILSKIPDE
INDRVRFLQT IKDIASAIKE LLDTVNNVFK KYQYQNRRAL EHQKKEFVKY SKSFSDTLKT
YFKDGKAINV FISANRLIHQ TNLILQTFKT VA
