DERM_BOVIN
ID DERM_BOVIN Reviewed; 201 AA.
AC P19427; Q29S18;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Dermatopontin;
DE AltName: Full=22 kDa extracellular matrix protein;
DE AltName: Full=Dermatan sulfate proteoglycan-associated protein 22K;
DE AltName: Full=Tyrosine-rich acidic matrix protein;
DE Short=TRAMP;
DE Flags: Precursor;
GN Name=DPT;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 19-201, PYROGLUTAMATE FORMATION AT GLN-19, AND
RP DISULFIDE BONDS.
RC TISSUE=Skin;
RX PubMed=2925615; DOI=10.1016/s0021-9258(18)83569-4;
RA Neame P.J., Choi H.U., Rosenberg L.C.;
RT "The isolation and primary structure of a 22-kDa extracellular matrix
RT protein from bovine skin.";
RL J. Biol. Chem. 264:5474-5479(1989).
RN [3]
RP PROTEIN SEQUENCE OF 44-65; 72-134 AND 138-201, INTERACTION WITH DCN AND
RP COLLAGEN, AND TISSUE SPECIFICITY.
RX PubMed=8907183; DOI=10.1093/oxfordjournals.jbchem.a021194;
RA Okamoto O., Suzuki Y., Kimura S., Shinkai H.;
RT "Extracellular matrix 22-kDa protein interacts with decorin core protein
RT and is expressed in cutaneous fibrosis.";
RL J. Biochem. 119:106-114(1996).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1939376; DOI=10.1242/jcs.99.3.657;
RA Lewandowska K., Choi H.U., Rosenberg L.C., Sasse J., Neame P.J., Culp L.A.;
RT "Extracellular matrix adhesion-promoting activities of a dermatan sulfate
RT proteoglycan-associated protein (22K) from bovine fetal skin.";
RL J. Cell Sci. 99:657-668(1991).
RN [5]
RP FUNCTION, AND INTERACTION WITH TGFB1 AND DCN.
RX PubMed=9895299; DOI=10.1042/bj3370537;
RA Okamoto O., Fujiwara S., Abe M., Sato Y.;
RT "Dermatopontin interacts with transforming growth factor beta and enhances
RT its biological activity.";
RL Biochem. J. 337:537-541(1999).
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. {ECO:0000269|PubMed:1939376, ECO:0000269|PubMed:9895299}.
CC -!- SUBUNIT: Interacts with TGFB1, DCN and collagen.
CC {ECO:0000269|PubMed:8907183, ECO:0000269|PubMed:9895299}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:1939376}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, heart, pancreas, skin
CC and cultured fibroblasts. {ECO:0000269|PubMed:8907183}.
CC -!- PTM: Sulfated on tyrosine residue(s). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dermatopontin family. {ECO:0000305}.
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DR EMBL; BC113221; AAI13222.1; -; mRNA.
DR PIR; A32851; A32851.
DR RefSeq; NP_001039368.1; NM_001045903.1.
DR AlphaFoldDB; P19427; -.
DR STRING; 9913.ENSBTAP00000028263; -.
DR PaxDb; P19427; -.
DR Ensembl; ENSBTAT00000028263; ENSBTAP00000028263; ENSBTAG00000021211.
DR GeneID; 504963; -.
DR KEGG; bta:504963; -.
DR CTD; 1805; -.
DR VEuPathDB; HostDB:ENSBTAG00000021211; -.
DR VGNC; VGNC:28191; DPT.
DR eggNOG; ENOG502RTKC; Eukaryota.
DR GeneTree; ENSGT00390000010760; -.
DR HOGENOM; CLU_122082_1_0_1; -.
DR InParanoid; P19427; -.
DR OMA; QGFSFQC; -.
DR OrthoDB; 1271391at2759; -.
DR TreeFam; TF328602; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000021211; Expressed in ureter and 102 other tissues.
DR ExpressionAtlas; P19427; baseline and differential.
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; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR InterPro; IPR026645; Dermatopontin_fam.
DR PANTHER; PTHR15040; PTHR15040; 1.
DR Pfam; PF14704; DERM; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Pyrrolidone carboxylic acid; Reference proteome;
KW Repeat; Secreted; Signal; Sulfation.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:2925615"
FT CHAIN 19..201
FT /note="Dermatopontin"
FT /id="PRO_0000145478"
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 26..135
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:0000269|PubMed:2925615"
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:0000269|PubMed:2925615"
FT DISULFID 90..132
FT /note="Or C-90 with C-133"
FT /evidence="ECO:0000269|PubMed:2925615"
FT DISULFID 106..133
FT /note="Or C-106 with C-132"
FT /evidence="ECO:0000269|PubMed:2925615"
FT DISULFID 139..196
FT /evidence="ECO:0000269|PubMed:2925615"
FT DISULFID 143..189
FT /evidence="ECO:0000305|PubMed:2925615"
SQ SEQUENCE 201 AA; 24012 MW; 6AE0F65756AABC7F CRC64;
MDLTLLWVLL PLVTVAWGQY GDYGYSYHQY HDYSDDGWVN LNRQGFSYQC PHGQVVVAVR
SIFNKKEGSD RQWNYACMPT PQSLGEPTEC WWEEINRAGM EWYQTCSNNG LVAGFQSRYF
ESVLDREWQF YCCRYSKRCP YSCWLTTEYP GHYGEEMDMI SYNYDYYMRG ATTTFSAVER
DRQWKFIMCR MTDYDCEFAN V
