DERM_MOUSE
ID DERM_MOUSE Reviewed; 201 AA.
AC Q9QZZ6; Q9D2B6;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Dermatopontin;
DE AltName: Full=Early quiescence protein 1;
DE Short=EQ-1;
DE AltName: Full=Tyrosine-rich acidic matrix protein;
DE Short=TRAMP;
DE Flags: Precursor;
GN Name=Dpt;
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], FUNCTION, AND INDUCTION.
RC STRAIN=BALB/cJ; TISSUE=Mesenchymal stem cell;
RX PubMed=14980498; DOI=10.1016/j.yexcr.2003.10.026;
RA Tzen C.-Y., Huang Y.-W.;
RT "Cloning of murine early quiescence-1 gene: the murine counterpart of
RT dermatopontin gene can induce and be induced by cell quiescence.";
RL Exp. Cell Res. 294:30-38(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
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=FVB/N; TISSUE=Salivary 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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12230512; DOI=10.1046/j.1523-1747.2002.01863.x;
RA Takeda U., Utani A., Wu J., Adachi E., Koseki H., Taniguchi M.,
RA Matsumoto T., Ohashi T., Sato M., Shinkai H.;
RT "Targeted disruption of dermatopontin causes abnormal collagen
RT fibrillogenesis.";
RL J. Invest. Dermatol. 119:678-683(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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 -!- FUNCTION: Seems to mediate adhesion by cell surface integrin binding.
CC May serve as a communication link between the dermal fibroblast cell
CC surface and its extracellular matrix environment. Enhances TGFB1
CC activity (By similarity). Inhibits cell proliferation. Accelerates
CC collagen fibril formation, and stabilizes collagen fibrils against low-
CC temperature dissociation. {ECO:0000250, ECO:0000269|PubMed:12230512,
CC ECO:0000269|PubMed:14980498}.
CC -!- SUBUNIT: Interacts with TGFB1, DCN and collagen. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- INDUCTION: Induced by cell quiescence. {ECO:0000269|PubMed:14980498}.
CC -!- PTM: Sulfated on tyrosine residue(s). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice have reduced skin elasticity, a decrease in
CC skin-thickness, and lower collagen content in the skin.
CC {ECO:0000269|PubMed:12230512}.
CC -!- SIMILARITY: Belongs to the dermatopontin family. {ECO:0000305}.
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DR EMBL; AF143374; AAD54221.1; -; mRNA.
DR EMBL; AK019890; BAB31905.1; -; mRNA.
DR EMBL; BC046420; AAH46420.1; -; mRNA.
DR CCDS; CCDS15437.1; -.
DR RefSeq; NP_062733.1; NM_019759.2.
DR AlphaFoldDB; Q9QZZ6; -.
DR STRING; 10090.ENSMUSP00000027861; -.
DR PhosphoSitePlus; Q9QZZ6; -.
DR MaxQB; Q9QZZ6; -.
DR PaxDb; Q9QZZ6; -.
DR PRIDE; Q9QZZ6; -.
DR ProteomicsDB; 277980; -.
DR Antibodypedia; 34354; 168 antibodies from 30 providers.
DR DNASU; 56429; -.
DR Ensembl; ENSMUST00000027861; ENSMUSP00000027861; ENSMUSG00000026574.
DR GeneID; 56429; -.
DR KEGG; mmu:56429; -.
DR UCSC; uc007diq.1; mouse.
DR CTD; 1805; -.
DR MGI; MGI:1928392; Dpt.
DR VEuPathDB; HostDB:ENSMUSG00000026574; -.
DR eggNOG; ENOG502RTKC; Eukaryota.
DR GeneTree; ENSGT00390000010760; -.
DR HOGENOM; CLU_122082_1_0_1; -.
DR InParanoid; Q9QZZ6; -.
DR OMA; QGFSFQC; -.
DR OrthoDB; 1271391at2759; -.
DR PhylomeDB; Q9QZZ6; -.
DR TreeFam; TF328602; -.
DR BioGRID-ORCS; 56429; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Dpt; mouse.
DR PRO; PR:Q9QZZ6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9QZZ6; protein.
DR Bgee; ENSMUSG00000026574; Expressed in semi-lunar valve and 163 other tissues.
DR Genevisible; Q9QZZ6; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:MGI.
DR InterPro; IPR026645; Dermatopontin_fam.
DR PANTHER; PTHR15040; PTHR15040; 1.
DR Pfam; PF14704; DERM; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Disulfide bond; Extracellular matrix;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal;
KW Sulfation.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..201
FT /note="Dermatopontin"
FT /id="PRO_0000007369"
FT REPEAT 26..79
FT /note="1-1"
FT REPEAT 70..75
FT /note="2-1"
FT REPEAT 80..135
FT /note="1-2"
FT REPEAT 125..130
FT /note="2-2"
FT REPEAT 181..186
FT /note="2-3"
FT REGION 19..186
FT /note="2 X 53-55 AA tandem repeats"
FT REGION 70..186
FT /note="3 X 6 AA tandem repeats of D-R-[EQ]-W-[NQK]-[FY]"
FT MOD_RES 19
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P19427"
FT MOD_RES 23
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 162
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 164
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 167
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 194
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT DISULFID 50..77
FT /evidence="ECO:0000250"
FT DISULFID 90..132
FT /note="Or C-90 with C-133"
FT /evidence="ECO:0000250"
FT DISULFID 106..133
FT /note="Or C-106 with C-132"
FT /evidence="ECO:0000250"
FT DISULFID 139..196
FT /evidence="ECO:0000250"
FT DISULFID 143..189
FT /evidence="ECO:0000255"
FT CONFLICT 64
FT /note="S -> T (in Ref. 2; BAB31905)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 201 AA; 23995 MW; DA64550025B9C98E CRC64;
MDLTLLWVLL PLVTTAWGQY GGYGYPYQQY QDYGDDGWVN LNRQGFSYQC PHGQVVVAVR
SIFSKKEGSD RQWNYACMPT PQSLGEPTEC WWEEINRAGM EWYQKCSNNG LVAGFQSRYF
ESVLDREWQF YCCRYSKRCP YSCWMTTEYP SHYGEDMDMI SYDYDFYMRG ATTTFSAVER
DRQWKFIMCR MTDYDCEFEN V
