ID DERM_HUMAN Reviewed; 201 AA. AC Q07507; A8K981; Q8N4R2; Q9UIX8; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 13-DEC-2002, sequence version 2. DT 27-MAR-2024, entry version 172. DE RecName: Full=Dermatopontin; DE AltName: Full=Tyrosine-rich acidic matrix protein; DE Short=TRAMP; DE Flags: Precursor; GN Name=DPT; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX PubMed=8104875; DOI=10.1006/geno.1993.1348; RA Superti-Furga A., Rocchi M., Schaefer B.W., Gitzelmann R.; RT "Complementary DNA sequence and chromosomal mapping of a human RT proteoglycan-binding cell-adhesion protein (dermatopontin)."; RL Genomics 17:463-467(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Lung; 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 TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=10233760; DOI=10.1046/j.1523-1747.1999.00563.x; RA Kuroda K., Okamoto O., Shinkai H.; RT "Dermatopontin expression is decreased in hypertrophic scar and systemic RT sclerosis skin fibroblasts and is regulated by transforming growth factor- RT beta1, interleukin-4, and matrix collagen."; RL J. Invest. Dermatol. 112:706-710(1999). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). 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. Inhibits cell proliferation. Accelerates collagen fibril CC formation, and stabilizes collagen fibrils against low-temperature CC dissociation (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with TGFB1, DCN and collagen. {ECO:0000250}. CC -!- INTERACTION: CC Q07507; PRO_0000018520 [P28300]: LOX; NbExp=2; IntAct=EBI-719535, EBI-20724846; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in fibroblasts, heart, skeletal muscle, CC brain and pancreas. Expressed at an intermediate level in lung and CC kidney, and at a low level in liver and placenta. Expressed at a lower CC level in fibroblasts from hypertrophic scar lesional skin and in CC fibroblasts from patients with systemic sclerosis than in normal skin CC fibroblasts. {ECO:0000269|PubMed:10233760, ECO:0000269|PubMed:8104875}. CC -!- INDUCTION: Induced by TGFB1, repressed by IL4/interleukin-4. CC {ECO:0000269|PubMed:10233760}. CC -!- PTM: Sulfated on tyrosine residue(s). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the dermatopontin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z22865; CAA80487.1; -; mRNA. DR EMBL; AK292596; BAF85285.1; -; mRNA. DR EMBL; AL049798; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471067; EAW90830.1; -; Genomic_DNA. DR EMBL; BC033736; AAH33736.1; -; mRNA. DR CCDS; CCDS1275.1; -. DR PIR; A47220; A47220. DR RefSeq; NP_001928.2; NM_001937.4. DR AlphaFoldDB; Q07507; -. DR BioGRID; 108139; 2. DR IntAct; Q07507; 4. DR STRING; 9606.ENSP00000356791; -. DR GlyGen; Q07507; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q07507; -. DR PhosphoSitePlus; Q07507; -. DR BioMuta; DPT; -. DR jPOST; Q07507; -. DR MassIVE; Q07507; -. DR PaxDb; 9606-ENSP00000356791; -. DR PeptideAtlas; Q07507; -. DR ProteomicsDB; 58518; -. DR Antibodypedia; 34354; 193 antibodies from 30 providers. DR DNASU; 1805; -. DR Ensembl; ENST00000367817.4; ENSP00000356791.3; ENSG00000143196.5. DR GeneID; 1805; -. DR KEGG; hsa:1805; -. DR MANE-Select; ENST00000367817.4; ENSP00000356791.3; NM_001937.5; NP_001928.2. DR UCSC; uc001gfp.4; human. DR AGR; HGNC:3011; -. DR CTD; 1805; -. DR DisGeNET; 1805; -. DR GeneCards; DPT; -. DR HGNC; HGNC:3011; DPT. DR HPA; ENSG00000143196; Tissue enhanced (intestine). DR MIM; 125597; gene. DR neXtProt; NX_Q07507; -. DR OpenTargets; ENSG00000143196; -. DR PharmGKB; PA27471; -. DR VEuPathDB; HostDB:ENSG00000143196; -. DR eggNOG; ENOG502RTKC; Eukaryota. DR GeneTree; ENSGT00390000010760; -. DR HOGENOM; CLU_122082_1_0_1; -. DR InParanoid; Q07507; -. DR OMA; EIDMISY; -. DR OrthoDB; 3977498at2759; -. DR PhylomeDB; Q07507; -. DR TreeFam; TF328602; -. DR PathwayCommons; Q07507; -. DR SignaLink; Q07507; -. DR BioGRID-ORCS; 1805; 10 hits in 1143 CRISPR screens. DR ChiTaRS; DPT; human. DR GeneWiki; Dermatopontin; -. DR GenomeRNAi; 1805; -. DR Pharos; Q07507; Tbio. DR PRO; PR:Q07507; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q07507; Protein. DR Bgee; ENSG00000143196; Expressed in smooth muscle tissue and 91 other cell types or tissues. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL. DR GO; GO:0005201; F:extracellular matrix structural constituent; ISS:BHF-UCL. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl. DR InterPro; IPR026645; Dermatopontin. DR PANTHER; PTHR15040:SF2; DERMATOPONTIN; 1. DR PANTHER; PTHR15040; DERMATOPONTIN-RELATED; 1. DR Pfam; PF14704; DERM; 1. DR Genevisible; Q07507; HS. 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_0000007368" 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="3-3" FT REGION 26..186 FT /note="2 X 53-55 AA tandem repeats" FT REGION 70..186 FT /note="3 X 6 AA 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 166 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 VARIANT 201 FT /note="V -> I (in dbSNP:rs6698023)" FT /id="VAR_048888" FT CONFLICT 10 FT /note="L -> M (in Ref. 1; CAA80487)" FT /evidence="ECO:0000305" FT CONFLICT 147 FT /note="T -> I (in Ref. 5; AAH33736)" FT /evidence="ECO:0000305" SQ SEQUENCE 201 AA; 24005 MW; C886D2FB624DDB49 CRC64; MDLSLLWVLL PLVTMAWGQY GDYGYPYQQY HDYSDDGWVN LNRQGFSYQC PQGQVIVAVR SIFSKKEGSD RQWNYACMPT PQSLGEPTEC WWEEINRAGM EWYQTCSNNG LVAGFQSRYF ESVLDREWQF YCCRYSKRCP YSCWLTTEYP GHYGEEMDMI SYNYDYYIRG ATTTFSAVER DRQWKFIMCR MTEYDCEFAN V //