Protein detail
LEMD1
LEM domain-containing protein 1 (Cancer/testis antigen 50) (CT50) (LEM domain protein 1) (LEMP-1)
Entry name LEMD1 | UniProt ID | EVMP confidence score 0.50 |
Supporting publications (n) 1 | Transmembrane count 1 | Protein classification |
EVMP confidence score
Annotation confidence score; open for threshold definitions.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40Basic Information8
Protein Names
LEM domain-containing protein 1 (Cancer/testis antigen 50) (CT50) (LEM domain protein 1) (LEMP-1)
Protein Function
Predicted intracellular proteins
Transmembrane
152..172; Helical; Signal-anchor for type II membrane protein
Transmembrane Count
1
Ensembl
Entrez Gene Symbol
Supporting publications (n)
1
EVMP confidence score
0.50
Fluorescence & Localization3
Tissue Specificheart muscleCell SpecificCardiomyocytes
Function & Pathway5
Protein Function
Predicted intracellular proteins
Cellular Component
Molecular Function
Biological Process (3)
Mediation Categories
Other mediation
Relations & Evidence13
Ligand-Receptor Signaling (12)
12 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| transmembrane_sosui | transmembrane_predicted | Almen2009 | No | No | No | No | No |
| transmembrane_tmhmm | transmembrane_predicted | Almen2009 | No | No | No | No | No |
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Sequence, Structure & Domains6
Sequences
Length
181
Mass
20,326
Sequence
MVDVKCLSDCKLQNQLEKLGFSPGPILPSTRKLYEKKLVQLLVSPPCAPPVMNGPRELDGAQDSDDSEELNIILQGNIILSTEKSKKLKKWPEASTTKRKAVDTYCLDYKPSKGRRWAARAPSTRITYGTITKERDYCAEDQTIESWREEGFPVGLKLAVLGIFIIVVFVYLTVENKSLFG
Alternative Products
Event=Alternative splicing; Named isoforms=6; Name=1; Synonyms=LEMD1A; IsoId=Q68G75-1; Sequence=Displayed; Name=2; Synonyms=LEMD1B; IsoId=Q68G75-2; Sequence=VSP_024848, VSP_024849; Name=3; Synonyms=LEMD1C; IsoId=Q68G75-3; Sequence=VSP_024846; Name=4; Synonyms=LEMD1D; IsoId=Q68G75-4; Sequence=VSP_024852, VSP_024853; Name=5; Synonyms=LEMD1E; IsoId=Q68G75-5; Sequence=VSP_024851, VSP_024854; Name=6; Synonyms=LEMD1F; IsoId=Q68G75-6; Sequence=VSP_024847, VSP_024850
Alternative Sequence
28..69; PSTRKLYEKKLVQLLVSPPCAPPVMNGPRELDGAQDSDDSEE -> Q (in isoform 3); 28..67; PSTRKLYEKKLVQLLVSPPCAPPVMNGPRELDGAQDSDDS -> RGLQEHQAPESHMGLSPKRETTARKTRLSRAGEKKVSQWA (in isoform 6); 28..29; PS -> LA (in isoform 2); 30..181; Missing (in isoform 2); 68..181; Missing (in isoform 6); 69..108; ELNIILQGNIILSTEKSKKLKKWPEASTTKRKAVDTYCLD -> GGLQEHQAPESHMGLSPKRETTARKTRLSRAGEKKVSQWA (in isoform 5); 69..70; EL -> VA (in isoform 4); 71..181; Missing (in isoform 4); 109..181; Missing (in isoform 5)
Domain & Motif Annotations
Domain (FT)
1..45; LEM
Supporting Publications1
| PMID | Title | Abstract |
|---|---|---|
| 34265469 | Proteomic Landscape of Exosomes Reveals the Functional Contributions of CD151 in Triple-Negative Breast Cancer. | Furthermore, utilizing quantitative proteomics approach to reveal the proteomes of CD151-deleted exosomes and cells, we found that exosomal CD151 facilitated secretion of ribosomal proteins via exosomes while inhibiting exosome secretion of complement proteins. Moreover, we proved that CD151-deleted exosomes significantly decreased the migration and invasion of TNBC cells. Most importantly, we found that the tetraspanin CD151 expression levels in TNBC-derived serum exosomes were significantly higher than those exosomes from healthy subjects, and we validated our findings with samples from 16 additional donors. This is the first comparative study of the proteomes of TNBC patient-derived and CD151-deleted exosomes. |