Hostname: page-component-84b7d79bbc-lrf7s Total loading time: 0 Render date: 2024-07-26T17:29:19.149Z Has data issue: false hasContentIssue false
  • English
  • Français

The L6 membrane proteins—A new four-transmembrane superfamily

Published online by Cambridge University Press:  01 August 2000

MARK D. WRIGHT ,
JIAN NI  and
GEORGE B. RUDY
MARK D. WRIGHT
Affiliation:
The Walter and Eliza Hall Institute of Medical Research, Post Office Royal Melbourne Hospital, 3050 Victoria, Australia
JIAN NI
Affiliation:
Human Genome Sciences, 9410 Key West Avenue, Rockville, Maryland 20850
GEORGE B. RUDY
Affiliation:
The Walter and Eliza Hall Institute of Medical Research, Post Office Royal Melbourne Hospital, 3050 Victoria, Australia
Get access

Abstract

L6, IL-TMP, and TM4SF5 are cell surface proteins predicted to have four transmembrane domains. Previous sequence analysis led to their assignment as members of the tetraspanin superfamily. In this paper, we identify a new sequence (L6D) that is strikingly similar to L6, IL-TMP, and TM4SF5. Analyses of these four sequences indicate that they are not significantly related to genuine tetraspanins, but instead constitute their own L6 superfamily.

Keywords

L6superfamilytetraspanin
Type
FOR THE RECORD
Information
Protein Science , Volume 9 , Issue 8 , August 2000 , pp. 1594 - 1600
Copyright
© 2000 The Protein Society

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)