DERM_PIG
ID DERM_PIG Reviewed; 183 AA.
AC P45846;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 25-MAY-2022, entry version 85.
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;
GN Name=DPT;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE.
RA Cronshaw A.D.;
RT "Amino acid sequence studies of lysyl oxidase and TRAMP (Tyrosine rich
RT acidic matrix protein).";
RL Thesis (1993), University of Edinburgh, United Kingdom.
RN [2]
RP PROTEIN SEQUENCE OF 83-126, MASS SPECTROMETRY, SULFATION, AND POLYMORPHISM.
RC TISSUE=Skin;
RX PubMed=8100985; DOI=10.1016/s0934-8832(11)80009-0;
RA Cronshaw A.D., Macbeath J.R.E., Shackleton D.R., Collins J.F.,
RA Fothergill-Gilmore L.A., Hulmes D.J.S.;
RT "TRAMP (tyrosine rich acidic matrix protein), a protein that co-purifies
RT with lysyl oxidase from porcine skin. Identification of TRAMP as the
RT dermatan sulphate proteoglycan-associated 22K extracellular matrix
RT protein.";
RL Matrix 13:255-266(1993).
RN [3]
RP FUNCTION.
RX PubMed=8103522; DOI=10.1016/s0021-9258(19)36588-3;
RA MacBeath J.R.E., Shackleton D.R., Hulmes D.J.S.;
RT "Tyrosine-rich acidic matrix protein (TRAMP) accelerates collagen fibril
RT formation in vitro.";
RL J. Biol. Chem. 268:19826-19832(1993).
RN [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND SULFATION.
RX PubMed=8082810; DOI=10.1016/0014-5793(94)00907-4;
RA Forbes E.G., Cronshaw A.D., MacBeath J.R.E., Hulmes D.J.S.;
RT "Tyrosine-rich acidic matrix protein (TRAMP) is a tyrosine-sulphated and
RT widely distributed protein of the extracellular matrix.";
RL FEBS Lett. 351:433-436(1994).
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 (By similarity). Accelerates
CC collagen fibril formation, and stabilizes collagen fibrils against low-
CC temperature dissociation. {ECO:0000250, ECO:0000269|PubMed:8103522}.
CC -!- SUBUNIT: Interacts with TGFB1, DCN and collagen. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:8082810}.
CC -!- TISSUE SPECIFICITY: Detected in skin, skeletal muscle, heart, lung,
CC articular cartilage, long bone and calvaria. Smaller amounts detected
CC in kidney. Not detected in brain, liver or spleen.
CC {ECO:0000269|PubMed:8082810}.
CC -!- PTM: Sulfated on tyrosine residue(s). {ECO:0000269|PubMed:8082810,
CC ECO:0000269|PubMed:8100985}.
CC -!- MASS SPECTROMETRY: Mass=22119; Mass_error=22; Method=MALDI; Note=Allele
CC T1.; Evidence={ECO:0000269|PubMed:8100985};
CC -!- MASS SPECTROMETRY: Mass=22183; Mass_error=22; Method=MALDI; Note=Allele
CC T2.; Evidence={ECO:0000269|PubMed:8100985};
CC -!- MASS SPECTROMETRY: Mass=22252; Mass_error=22; Method=MALDI; Note=Allele
CC T3.; Evidence={ECO:0000269|PubMed:8100985};
CC -!- MASS SPECTROMETRY: Mass=22306; Mass_error=22; Method=MALDI; Note=Allele
CC T4.; Evidence={ECO:0000269|PubMed:8100985};
CC -!- MASS SPECTROMETRY: Mass=22352; Mass_error=22; Method=MALDI; Note=Allele
CC T5.; Evidence={ECO:0000269|PubMed:8100985};
CC -!- POLYMORPHISM: Five alleles occur, which differ in mass and pI (T1, T2,
CC T3, T4 and T5). {ECO:0000269|PubMed:8100985}.
CC -!- SIMILARITY: Belongs to the dermatopontin family. {ECO:0000305}.
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DR PIR; S34838; S34838.
DR AlphaFoldDB; P45846; -.
DR STRING; 9823.ENSSSCP00000006714; -.
DR PaxDb; P45846; -.
DR PeptideAtlas; P45846; -.
DR PRIDE; P45846; -.
DR eggNOG; ENOG502RTKC; Eukaryota.
DR HOGENOM; CLU_122082_1_0_1; -.
DR InParanoid; P45846; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P45846; SS.
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 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; Sulfation.
FT CHAIN 1..183
FT /note="Dermatopontin"
FT /id="PRO_0000145479"
FT REPEAT 8..61
FT /note="1-1"
FT REPEAT 52..57
FT /note="2-1"
FT REPEAT 62..117
FT /note="1-2"
FT REPEAT 107..112
FT /note="2-2"
FT REPEAT 163..168
FT /note="2-3"
FT REGION 8..117
FT /note="2 X 53-55 AA tandem repeats"
FT REGION 52..168
FT /note="3 X 6 AA tandem repeats of D-R-[EQ]-W-[NQK]-[FY]"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P19427"
FT MOD_RES 5
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 144
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 146
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 148
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 149
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 176
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT DISULFID 32..59
FT /evidence="ECO:0000250"
FT DISULFID 72..114
FT /note="Or C-90 with C-133"
FT /evidence="ECO:0000250"
FT DISULFID 88..115
FT /note="Or C-106 with C-132"
FT /evidence="ECO:0000250"
FT DISULFID 121..178
FT /evidence="ECO:0000250"
FT DISULFID 125..171
FT /evidence="ECO:0000250"
SQ SEQUENCE 183 AA; 21994 MW; 5FE4FD477242D710 CRC64;
QYGDYGYPYQ QYHDYSDDGW VNLNRQGFSY QCPHGQVVVA VRSIFNKKEG SDRQWNYACM
PTPQSLGEPS ECWWEEINRA GMEWYQTCSN NGLVAGFQSR YFESVLDREW QFYCCRYSKR
CPYSCWMTTE YPGHYGEEMD MISYNYDYYM RGATTTFSAV ERDRQWKFIM CRMTDYDCEF
ANV
