Human interstitial retinoid-binding protein. Gene structure and primary sequence

Gregory I Liou, D. P. Ma, Y. W. Yang, L. Geng, C. Zhu, W. Baehr

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

Interstitial retinoid-binding protein (IRBP) is synthesized and secreted by rod photoreceptor cells into the interphotoreceptor matrix and is known to bind retinoids and fatty acids. We have used cDNA clones encoding human IRBP to isolate a 15-kilobase genomic fragment that encompasses the complete human IRBP gene. The IRBP gene spans more than 11 kilobases and is interrupted by three introns, all of which are positioned near the 3'-end of the coding sequence. The 3741-base pair coding region of IRBP appears to have been generated by quadruplication of an approximately 900 base pair long ancestral gene. The deduced amino acid sequence predicts a mature protein of 1,230 residues (calculated molecular weight 133,000). The protein sequence can be aligned into four homologous segments, each consisting of about 300 residues. Sequence similarity between segments is as high as 60% when conservative substitutions are taken into account. Two putative N-linked glycosylation sites are located in highly conserved domains in the center of the first and second segment of IRBP. A domain consisting of 41 residues at the COOH-terminal end of the third segment has 15 matching residues (38%) with an intradiscal loop of rhodopsin, a retinal-binding protein in rod photoreceptors.

Original languageEnglish (US)
Pages (from-to)8200-8206
Number of pages7
JournalJournal of Biological Chemistry
Volume264
Issue number14
StatePublished - Jan 1 1989

Fingerprint

Retinol-Binding Proteins
Genes
Retinal Rod Photoreceptor Cells
Base Pairing
Glycosylation
Rhodopsin
Retinoids
Introns
Amino Acid Sequence
Carrier Proteins
Proteins
Substitution reactions
Fatty Acids
Complementary DNA
Clone Cells
Molecular Weight
Molecular weight
Amino Acids

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Liou, G. I., Ma, D. P., Yang, Y. W., Geng, L., Zhu, C., & Baehr, W. (1989). Human interstitial retinoid-binding protein. Gene structure and primary sequence. Journal of Biological Chemistry, 264(14), 8200-8206.

Human interstitial retinoid-binding protein. Gene structure and primary sequence. / Liou, Gregory I; Ma, D. P.; Yang, Y. W.; Geng, L.; Zhu, C.; Baehr, W.

In: Journal of Biological Chemistry, Vol. 264, No. 14, 01.01.1989, p. 8200-8206.

Research output: Contribution to journalArticle

Liou, GI, Ma, DP, Yang, YW, Geng, L, Zhu, C & Baehr, W 1989, 'Human interstitial retinoid-binding protein. Gene structure and primary sequence', Journal of Biological Chemistry, vol. 264, no. 14, pp. 8200-8206.
Liou GI, Ma DP, Yang YW, Geng L, Zhu C, Baehr W. Human interstitial retinoid-binding protein. Gene structure and primary sequence. Journal of Biological Chemistry. 1989 Jan 1;264(14):8200-8206.
Liou, Gregory I ; Ma, D. P. ; Yang, Y. W. ; Geng, L. ; Zhu, C. ; Baehr, W. / Human interstitial retinoid-binding protein. Gene structure and primary sequence. In: Journal of Biological Chemistry. 1989 ; Vol. 264, No. 14. pp. 8200-8206.
@article{244af7cd413c465a911652341be8e5f6,
title = "Human interstitial retinoid-binding protein. Gene structure and primary sequence",
abstract = "Interstitial retinoid-binding protein (IRBP) is synthesized and secreted by rod photoreceptor cells into the interphotoreceptor matrix and is known to bind retinoids and fatty acids. We have used cDNA clones encoding human IRBP to isolate a 15-kilobase genomic fragment that encompasses the complete human IRBP gene. The IRBP gene spans more than 11 kilobases and is interrupted by three introns, all of which are positioned near the 3'-end of the coding sequence. The 3741-base pair coding region of IRBP appears to have been generated by quadruplication of an approximately 900 base pair long ancestral gene. The deduced amino acid sequence predicts a mature protein of 1,230 residues (calculated molecular weight 133,000). The protein sequence can be aligned into four homologous segments, each consisting of about 300 residues. Sequence similarity between segments is as high as 60{\%} when conservative substitutions are taken into account. Two putative N-linked glycosylation sites are located in highly conserved domains in the center of the first and second segment of IRBP. A domain consisting of 41 residues at the COOH-terminal end of the third segment has 15 matching residues (38{\%}) with an intradiscal loop of rhodopsin, a retinal-binding protein in rod photoreceptors.",
author = "Liou, {Gregory I} and Ma, {D. P.} and Yang, {Y. W.} and L. Geng and C. Zhu and W. Baehr",
year = "1989",
month = "1",
day = "1",
language = "English (US)",
volume = "264",
pages = "8200--8206",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "14",

}

TY - JOUR

T1 - Human interstitial retinoid-binding protein. Gene structure and primary sequence

AU - Liou, Gregory I

AU - Ma, D. P.

AU - Yang, Y. W.

AU - Geng, L.

AU - Zhu, C.

AU - Baehr, W.

PY - 1989/1/1

Y1 - 1989/1/1

N2 - Interstitial retinoid-binding protein (IRBP) is synthesized and secreted by rod photoreceptor cells into the interphotoreceptor matrix and is known to bind retinoids and fatty acids. We have used cDNA clones encoding human IRBP to isolate a 15-kilobase genomic fragment that encompasses the complete human IRBP gene. The IRBP gene spans more than 11 kilobases and is interrupted by three introns, all of which are positioned near the 3'-end of the coding sequence. The 3741-base pair coding region of IRBP appears to have been generated by quadruplication of an approximately 900 base pair long ancestral gene. The deduced amino acid sequence predicts a mature protein of 1,230 residues (calculated molecular weight 133,000). The protein sequence can be aligned into four homologous segments, each consisting of about 300 residues. Sequence similarity between segments is as high as 60% when conservative substitutions are taken into account. Two putative N-linked glycosylation sites are located in highly conserved domains in the center of the first and second segment of IRBP. A domain consisting of 41 residues at the COOH-terminal end of the third segment has 15 matching residues (38%) with an intradiscal loop of rhodopsin, a retinal-binding protein in rod photoreceptors.

AB - Interstitial retinoid-binding protein (IRBP) is synthesized and secreted by rod photoreceptor cells into the interphotoreceptor matrix and is known to bind retinoids and fatty acids. We have used cDNA clones encoding human IRBP to isolate a 15-kilobase genomic fragment that encompasses the complete human IRBP gene. The IRBP gene spans more than 11 kilobases and is interrupted by three introns, all of which are positioned near the 3'-end of the coding sequence. The 3741-base pair coding region of IRBP appears to have been generated by quadruplication of an approximately 900 base pair long ancestral gene. The deduced amino acid sequence predicts a mature protein of 1,230 residues (calculated molecular weight 133,000). The protein sequence can be aligned into four homologous segments, each consisting of about 300 residues. Sequence similarity between segments is as high as 60% when conservative substitutions are taken into account. Two putative N-linked glycosylation sites are located in highly conserved domains in the center of the first and second segment of IRBP. A domain consisting of 41 residues at the COOH-terminal end of the third segment has 15 matching residues (38%) with an intradiscal loop of rhodopsin, a retinal-binding protein in rod photoreceptors.

UR - http://www.scopus.com/inward/record.url?scp=0024334087&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024334087&partnerID=8YFLogxK

M3 - Article

C2 - 2542268

AN - SCOPUS:0024334087

VL - 264

SP - 8200

EP - 8206

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 14

ER -