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   27-MAR-2024, entry version 153.
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; 10090-ENSMUSP00000027861; -.
DR   ProteomicsDB; 277980; -.
DR   Antibodypedia; 34354; 193 antibodies from 30 providers.
DR   DNASU; 56429; -.
DR   Ensembl; ENSMUST00000027861.6; ENSMUSP00000027861.5; ENSMUSG00000026574.6.
DR   GeneID; 56429; -.
DR   KEGG; mmu:56429; -.
DR   UCSC; uc007diq.1; mouse.
DR   AGR; MGI:1928392; -.
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; EIDMISY; -.
DR   OrthoDB; 3977498at2759; -.
DR   PhylomeDB; Q9QZZ6; -.
DR   TreeFam; TF328602; -.
DR   BioGRID-ORCS; 56429; 0 hits in 78 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 cell types or tissues.
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.
DR   PANTHER; PTHR15040:SF2; DERMATOPONTIN; 1.
DR   PANTHER; PTHR15040; DERMATOPONTIN-RELATED; 1.
DR   Pfam; PF14704; DERM; 1.
DR   Genevisible; Q9QZZ6; MM.
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
//