MUC3 human intestinal mucin. Analysis of gene structure, the carboxyl terminus, and a novel upstream repetitive region.

MUC3 human intestinal mucin. Analysis of gene structure, the carboxyl terminus, and a novel upstream repetitive region. Research Abstract Details 

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MUC3 human intestinal mucin. Analysis of gene structure, the carboxyl terminus, and a novel upstream repetitive region. Abstract Text:

J R Gum,J J Ho,W S Pratt,J W Hicks,A S Hill,L E Vinall,A M Roberton,D M Swallow,Y S Kim,

MUC3 is a large mucin glycoprotein expressed by the human intestine and gall bladder. In this manuscript, we present details of the deduced protein structure of MUC3. The MUC3 carboxyl-terminal domain is 617 residues in length, including 511 residues of a non-repetitive mucin-like domain (27% Thr, 22% Ser, and 11% Pro) and a 106-residue Cys-rich domain with homology to the epidermal growth factor (EGF) -like structural motifs found in many proteins. The region of MUC3 located upstream of the previously described 51-base pair (bp) tandem repeats, which encode a major Ser and Thr-rich domain, consists of a second type of repetitive structure with an imperfect periodicity of approximately 1125 bp. This domain is also mucin-like and appears to be considerably larger than 2000 residues (6000 bp). The MUC3 gene itself is large and complex. Using pulse field gel electrophoresis and blot analysis, the smallest fragment found that contained all human genomic DNA hybridizing to the 51-bp tandem repeat probe was 200 kilobases with restriction enzyme SwaI. Both PvuII and PstI produced two sets of hybridizing fragments that were hypervariable within the human population with a pattern suggestive of both a variation in the number of tandem repeats (VNTR) and sequence polymorphism. These fragments varied independently of each other, but no genetic recombination was detected in a study of 40 human families. Thus, the MUC3 gene encodes a very large glycoprotein with a structure very different from that of any mucin currently described.

MUC3 human intestinal mucin. Analysis of gene structure, the carboxyl terminus, and a novel upstream repetitive region. Publishing Authors By Initials

JR Gum,JJ Ho,WS Pratt,JW Hicks,AS Hill,LE Vinall,AM Roberton,DM Swallow,YS Kim,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: sequence homology: sequence homology, amino acid research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: sequence homology: sequence homology, amino acid research

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MUC3 human intestinal mucin. Analysis of gene structure, the carboxyl terminus, and a novel upstream repetitive region. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: The Journal of biological chemistry

VOLUME: 272

Page Numbers: 26678-86

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 17

MONTH: Oct

YEAR: 1997

MUC3 human intestinal mucin. Analysis of gene structure, the carboxyl terminus, and a novel upstream repetitive region. Information

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LANGUAGE: eng

NlmUniqueID: 2985121

MUC3 human intestinal mucin. Analysis of gene structure, the carboxyl terminus, and a novel upstream repetitive region. Keywords Mesh Terms:

KEYWORDS: Sequence Homology, Amino Acid

MESH TERMS: genetics

Chemical & Substance for Abstract: MUC3 human intestinal mucin. Analysis of gene structure, the carboxyl terminus, and a novel upstream repetitive region. Information

Substance Name: Mucins

Registry Number: 0

Grant and Affiliation Information for MUC3 human intestinal mucin. Analysis of gene structure, the carboxyl terminus, and a novel upstream repetitive region.

AFFILIATION: Gastrointestinal Research Laboratory (151M2), Department of Veterans Affairs Medical Center, University of California, San Francisco, California 94121, USA.

Country: UNITED STATES

AGENCY: United States NCI

GRANT: CA 24321

ACRONYM: CA

MEDLINETA: J Biol Chem

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