The zebrafish thrombospondin 3 and 4 Genes (thbs3 and thbs4)

CDNA and protein structure

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

The cDNA sequences of the zebrafish thrombospondin 3 gene (thbs3) and thrombospondin 4 gene (thbs4) have been determined, and the encoded amino acid sequences (Thbs3 and Thbs4) have been analyzed. Thbs3 cDNA specifies a protein of 962 amino acid residues (MW 105,787), while Thbs4 cDNA specifies a protein of 949 residues (MW 103,989). Both proteins are highly acidic with Asp + Glu contents of 15.8% (Thbs3) and 16.9% (Thbs4). The acidic amino acids are clustered in the region of the Type III repeats and part of the C-terminal domain. The presence of signal peptides indicates that Thbs3 and Thbs4 function as secreted, extracellular proteins. The two polypeptides contain homologous sequences with two cysteines that are likely to form interchain disulfide bonds. Potential glycosylation sites were identified, five for Thbs3 and three for Thbs4. The polypeptides share the domain structure characteristic of the thrombospondin 3/thrombospondin 4/COMP subgroup of thrombospondin proteins. This domain structure consists of an amino-terminal thrombospondin N-terminal-like domain (TSPN domain), four Type II (EGF-like) repeats, seven Type III (calcium-binding) repeats, and a carboxyl terminal region. In aligning the Thbs3 and Thbs4 domain sequences with those of other thrombospondins, a gradient of sequence homology is observed that increases from N-terminus to C-terminus.

Original languageEnglish (US)
Pages (from-to)277-285
Number of pages9
JournalMitochondrial DNA
Volume13
Issue number5
DOIs
StatePublished - Dec 1 2002

Fingerprint

Zebrafish
Thrombospondins
Genes
Complementary DNA
Sequence Homology
Proteins
Acidic Amino Acids
Glycosylation
Amino Acids
Peptides
Protein Sorting Signals
Epidermal Growth Factor
Disulfides
Cysteine
Amino Acid Sequence
thrombospondin 4
thrombospondin 3
Calcium

Keywords

  • Amino acid sequence
  • cDNA
  • thbs3
  • thbs4
  • Thrombospondin 3 and 4
  • Zebrafish (Danio rerio )

Cite this

The zebrafish thrombospondin 3 and 4 Genes (thbs3 and thbs4) : CDNA and protein structure. / Adolph, Kenneth W.

In: Mitochondrial DNA, Vol. 13, No. 5, 01.12.2002, p. 277-285.

Research output: Contribution to journalArticle

@article{dc2aeb0b2558478abb798a7c5e9d2587,
title = "The zebrafish thrombospondin 3 and 4 Genes (thbs3 and thbs4): CDNA and protein structure",
abstract = "The cDNA sequences of the zebrafish thrombospondin 3 gene (thbs3) and thrombospondin 4 gene (thbs4) have been determined, and the encoded amino acid sequences (Thbs3 and Thbs4) have been analyzed. Thbs3 cDNA specifies a protein of 962 amino acid residues (MW 105,787), while Thbs4 cDNA specifies a protein of 949 residues (MW 103,989). Both proteins are highly acidic with Asp + Glu contents of 15.8{\%} (Thbs3) and 16.9{\%} (Thbs4). The acidic amino acids are clustered in the region of the Type III repeats and part of the C-terminal domain. The presence of signal peptides indicates that Thbs3 and Thbs4 function as secreted, extracellular proteins. The two polypeptides contain homologous sequences with two cysteines that are likely to form interchain disulfide bonds. Potential glycosylation sites were identified, five for Thbs3 and three for Thbs4. The polypeptides share the domain structure characteristic of the thrombospondin 3/thrombospondin 4/COMP subgroup of thrombospondin proteins. This domain structure consists of an amino-terminal thrombospondin N-terminal-like domain (TSPN domain), four Type II (EGF-like) repeats, seven Type III (calcium-binding) repeats, and a carboxyl terminal region. In aligning the Thbs3 and Thbs4 domain sequences with those of other thrombospondins, a gradient of sequence homology is observed that increases from N-terminus to C-terminus.",
keywords = "Amino acid sequence, cDNA, thbs3, thbs4, Thrombospondin 3 and 4, Zebrafish (Danio rerio )",
author = "Adolph, {Kenneth W}",
year = "2002",
month = "12",
day = "1",
doi = "10.1080/1042517021000019278",
language = "English (US)",
volume = "13",
pages = "277--285",
journal = "DNA Sequence - Journal of DNA Sequencing and Mapping",
issn = "1940-1744",
publisher = "Informa Healthcare",
number = "5",

}

TY - JOUR

T1 - The zebrafish thrombospondin 3 and 4 Genes (thbs3 and thbs4)

T2 - CDNA and protein structure

AU - Adolph, Kenneth W

PY - 2002/12/1

Y1 - 2002/12/1

N2 - The cDNA sequences of the zebrafish thrombospondin 3 gene (thbs3) and thrombospondin 4 gene (thbs4) have been determined, and the encoded amino acid sequences (Thbs3 and Thbs4) have been analyzed. Thbs3 cDNA specifies a protein of 962 amino acid residues (MW 105,787), while Thbs4 cDNA specifies a protein of 949 residues (MW 103,989). Both proteins are highly acidic with Asp + Glu contents of 15.8% (Thbs3) and 16.9% (Thbs4). The acidic amino acids are clustered in the region of the Type III repeats and part of the C-terminal domain. The presence of signal peptides indicates that Thbs3 and Thbs4 function as secreted, extracellular proteins. The two polypeptides contain homologous sequences with two cysteines that are likely to form interchain disulfide bonds. Potential glycosylation sites were identified, five for Thbs3 and three for Thbs4. The polypeptides share the domain structure characteristic of the thrombospondin 3/thrombospondin 4/COMP subgroup of thrombospondin proteins. This domain structure consists of an amino-terminal thrombospondin N-terminal-like domain (TSPN domain), four Type II (EGF-like) repeats, seven Type III (calcium-binding) repeats, and a carboxyl terminal region. In aligning the Thbs3 and Thbs4 domain sequences with those of other thrombospondins, a gradient of sequence homology is observed that increases from N-terminus to C-terminus.

AB - The cDNA sequences of the zebrafish thrombospondin 3 gene (thbs3) and thrombospondin 4 gene (thbs4) have been determined, and the encoded amino acid sequences (Thbs3 and Thbs4) have been analyzed. Thbs3 cDNA specifies a protein of 962 amino acid residues (MW 105,787), while Thbs4 cDNA specifies a protein of 949 residues (MW 103,989). Both proteins are highly acidic with Asp + Glu contents of 15.8% (Thbs3) and 16.9% (Thbs4). The acidic amino acids are clustered in the region of the Type III repeats and part of the C-terminal domain. The presence of signal peptides indicates that Thbs3 and Thbs4 function as secreted, extracellular proteins. The two polypeptides contain homologous sequences with two cysteines that are likely to form interchain disulfide bonds. Potential glycosylation sites were identified, five for Thbs3 and three for Thbs4. The polypeptides share the domain structure characteristic of the thrombospondin 3/thrombospondin 4/COMP subgroup of thrombospondin proteins. This domain structure consists of an amino-terminal thrombospondin N-terminal-like domain (TSPN domain), four Type II (EGF-like) repeats, seven Type III (calcium-binding) repeats, and a carboxyl terminal region. In aligning the Thbs3 and Thbs4 domain sequences with those of other thrombospondins, a gradient of sequence homology is observed that increases from N-terminus to C-terminus.

KW - Amino acid sequence

KW - cDNA

KW - thbs3

KW - thbs4

KW - Thrombospondin 3 and 4

KW - Zebrafish (Danio rerio )

UR - http://www.scopus.com/inward/record.url?scp=0036805510&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036805510&partnerID=8YFLogxK

U2 - 10.1080/1042517021000019278

DO - 10.1080/1042517021000019278

M3 - Article

VL - 13

SP - 277

EP - 285

JO - DNA Sequence - Journal of DNA Sequencing and Mapping

JF - DNA Sequence - Journal of DNA Sequencing and Mapping

SN - 1940-1744

IS - 5

ER -