DAZP2_MOUSE
ID DAZP2_MOUSE Reviewed; 168 AA.
AC Q9DCP9; O88675; Q3UVI4;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=DAZ-associated protein 2;
DE AltName: Full=Deleted in azoospermia-associated protein 2;
DE AltName: Full=Proline-rich protein expressed in brain;
GN Name=Dazap2; Synonyms=Prtb;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=CD-1; TISSUE=Brain;
RX PubMed=10373015;
RX DOI=10.1002/(sici)1097-0177(199906)215:2<108::aid-dvdy3>3.0.co;2-i;
RA Yang W., Mansour S.L.;
RT "Expression and genetic analysis of prtb, a gene that encodes a highly
RT conserved proline-rich protein expressed in the brain.";
RL Dev. Dyn. 215:108-116(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Head, Heart, Kidney, Liver, 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; TISSUE=Brain, and Eye;
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 INDUCTION.
RX PubMed=11787059; DOI=10.1002/jcb.10018;
RA Sommerfeldt D.W., Zhi J., Rubin C.T., Hadjiargyrou M.;
RT "Proline-rich transcript of the brain (prtb) is a serum-responsive gene in
RT osteoblasts and upregulated during adhesion.";
RL J. Cell. Biochem. 84:301-308(2002).
RN [5]
RP TISSUE SPECIFICITY, AND INTERACTION WITH SOX6.
RX PubMed=14530442; DOI=10.1093/nar/gkg807;
RA Cohen-Barak O., Yi Z., Hagiwara N., Monzen K., Komuro I., Brilliant M.H.;
RT "Sox6 regulation of cardiac myocyte development.";
RL Nucleic Acids Res. 31:5941-5948(2003).
CC -!- SUBUNIT: Interacts with DAZ1 and DAZL (By similarity). Interacts with
CC IL17RB (By similarity). May interact with FAM168B (By similarity).
CC Interacts with SOX6 (PubMed:14530442). Interacts with INCA1 (By
CC similarity). {ECO:0000250|UniProtKB:Q15038,
CC ECO:0000269|PubMed:14530442}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Predominantly nuclear in macrophages, stimulation of IL17RB with
CC its ligand IL17E induces accumulation in the cytoplasm. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in brain.
CC {ECO:0000269|PubMed:10373015, ECO:0000269|PubMed:14530442}.
CC -!- DEVELOPMENTAL STAGE: Between 11.5 dpc and 12.5 dpc it is specifically
CC expressed in the developing heart. From 13.5 dpc, expression in the
CC heart disappears, while it become strongly expressed in the brain. Up-
CC regulated during adhesion and differentiation to beating
CC cardiomyocytes. {ECO:0000269|PubMed:10373015}.
CC -!- INDUCTION: By serum stimulation. {ECO:0000269|PubMed:11787059}.
CC -!- PTM: Ubiquitinated by SMURF2, leading to proteasomal degradation.
CC {ECO:0000250}.
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DR EMBL; AF085348; AAC34594.1; -; mRNA.
DR EMBL; AK002595; BAB22216.1; -; mRNA.
DR EMBL; AK050159; BAC34100.1; -; mRNA.
DR EMBL; AK088916; BAC40651.1; -; mRNA.
DR EMBL; AK132139; BAE20995.1; -; mRNA.
DR EMBL; AK137246; BAE23285.1; -; mRNA.
DR EMBL; AK146970; BAE27575.1; -; mRNA.
DR EMBL; BC014808; AAH14808.1; -; mRNA.
DR EMBL; BC083347; AAH83347.1; -; mRNA.
DR CCDS; CCDS27841.1; -.
DR RefSeq; NP_036003.2; NM_011873.2.
DR AlphaFoldDB; Q9DCP9; -.
DR BioGRID; 204844; 3.
DR IntAct; Q9DCP9; 1.
DR STRING; 10090.ENSMUSP00000000356; -.
DR iPTMnet; Q9DCP9; -.
DR PhosphoSitePlus; Q9DCP9; -.
DR PaxDb; Q9DCP9; -.
DR PRIDE; Q9DCP9; -.
DR ProteomicsDB; 277953; -.
DR Antibodypedia; 26360; 113 antibodies from 22 providers.
DR DNASU; 23994; -.
DR Ensembl; ENSMUST00000000356; ENSMUSP00000000356; ENSMUSG00000000346.
DR GeneID; 23994; -.
DR KEGG; mmu:23994; -.
DR UCSC; uc007xrt.1; mouse.
DR CTD; 9802; -.
DR MGI; MGI:1344344; Dazap2.
DR VEuPathDB; HostDB:ENSMUSG00000000346; -.
DR eggNOG; ENOG502QTNQ; Eukaryota.
DR GeneTree; ENSGT00390000000685; -.
DR HOGENOM; CLU_135110_0_0_1; -.
DR InParanoid; Q9DCP9; -.
DR OMA; IYQPRYM; -.
DR OrthoDB; 1429433at2759; -.
DR PhylomeDB; Q9DCP9; -.
DR TreeFam; TF329672; -.
DR BioGRID-ORCS; 23994; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Dazap2; mouse.
DR PRO; PR:Q9DCP9; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9DCP9; protein.
DR Bgee; ENSMUSG00000000346; Expressed in blood and 283 other tissues.
DR Genevisible; Q9DCP9; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IC:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:WormBase.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:WormBase.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:WormBase.
DR GO; GO:0050699; F:WW domain binding; ISO:MGI.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:WormBase.
DR InterPro; IPR022730; DAZ_assoc-2.
DR PANTHER; PTHR31638; PTHR31638; 1.
DR Pfam; PF11029; DAZAP2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Ubl conjugation.
FT CHAIN 1..168
FT /note="DAZ-associated protein 2"
FT /id="PRO_0000079789"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 162
FT /note="D -> N (in Ref. 1; AAC34594)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 168 AA; 17289 MW; 49EDDAA29D8E3AAC CRC64;
MNSKGQYPTQ PTYPVQPPGN PVYPQTLHLP QAPPYTDAPP AYSELYRPSF VHPGAATVPT
MSAAFPGASL YLPMAQSVAV GPLGSTIPMA YYPVGPIYPP GSAVLVEGGY DAGARFGAGA
TAGNIPPPPP GCPPNAAQLA VMQGANVLVT QRKGNFFMGG SDGGYTIW