PUBLICATION
Characterization of mouse epithelial protein lost in neoplasm (EPLIN) and comparison of mammalian and zebrafish EPLIN
- Authors
- Maul, R.S., Sachi Gerbin, C., and Chang, D.D.
- ID
- ZDB-PUB-010219-4
- Date
- 2001
- Source
- Gene 262(1-2): 155-160 (Journal)
- Registered Authors
- Keywords
- LIM domain; cytoskeleton-associated protein; tissue expression
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Cloning, Molecular
- Conserved Sequence
- Cytoskeletal Proteins/genetics*
- Cytoskeletal Proteins/metabolism
- Exons
- Expressed Sequence Tags
- Gene Expression Regulation
- Humans
- Introns
- Mammals/genetics*
- Mice
- Molecular Sequence Data
- Sequence Homology, Amino Acid
- Zebrafish/genetics*
- PubMed
- 11179679 Full text @ Gene
Citation
Maul, R.S., Sachi Gerbin, C., and Chang, D.D. (2001) Characterization of mouse epithelial protein lost in neoplasm (EPLIN) and comparison of mammalian and zebrafish EPLIN. Gene. 262(1-2):155-160.
Abstract
EPLIN is a cytoskeleton-associated protein that was initially identified as the product of a gene that is transcriptionally down-regulated in cancer cells. In human, there are two known isoforms, EPLIN-alpha and -beta, generated by alternative promoter usage from a single gene. With the exception of a single LIM (lin-11, isl-1, and mec-3) domain, the sequence of EPLIN is unique and does not provide any clues to its function. To identify conserved regions of EPLIN that may be important for its function, we have characterized mouse (m) and zebrafish (zf) EPLIN. As in human, two isoforms, the 593 aa mEPLIN-alpha (77% identity; 83% similarity) and 753 aa mEPLIN-beta (75% identity; 83% similarity), were present in mouse. mEPLIN-alpha is highly expressed in embryonic tissue and adult lung and spleen, whereas mEPLIN-beta is preferentially expressed in kidney, testis, lung and liver. The analysis of mEPLIN gene revealed that the overall organization of the exons in mouse and human are conserved. In zebrafish, there was only one form, the 629 aa zfEPLIN, corresponding to the mammalian EPLIN-beta. Like its mammalian counterparts, ectopically expressed zfEPLIN is co-localized to the actin cytoskeleton. While the overall homology between mammalian and zebrafish EPLIN was not striking (37% identity; 50% similarity), there were seven highly conserved regions, which should be useful in structure-function studies of this novel protein.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping