Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00495
Entry Name
UniProt Accession
Theoretical PI
7.45
Molecular Weight
28295.11
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
CD151 antigen
Protein Synonyms/Alias
GP27; Membrane glycoprotein SFA-1; Platelet-endothelial tetraspan antigen 3; PETA-3; Tetraspanin-24; Tspan-24; CD151;
Gene Name
CD151
Gene Synonyms/Alias
TSPAN24;
Created Date
01-FEB-1996
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
11
Canonical
FNEKKTTCGTVCLKY
[1][2]
S-Palmitoylation
15
Canonical
KTTCGTVCLKYLLFT
[1][2]
S-Palmitoylation
79
Canonical
MVTGVLGCCATFKER
[3]
S-Palmitoylation
80
Canonical
VTGVLGCCATFKERR
[3]
S-Palmitoylation
242
Canonical
VFGMIFTCCLYRSLK
[1][2]
S-Palmitoylation
243
Canonical
FGMIFTCCLYRSLKL
[1][2]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Yang X, Claas C, Kraeft SK, Chen LB, Wang Z, Kreidberg JA, Hemler ME.Palmitoylation of tetraspanin proteins: modulation of CD151 lateral interactions,subcellular distribution, and integrin-dependent cell morphology. Mol Biol Cell. 2002 Mar;13(3):767-81.[PMID:11907260]
[2] Stipp CS, Kolesnikova TV, Hemler ME. Functional domains in tetraspaninproteins. Trends Biochem Sci. 2003 Feb;28(2):106-12. Review. Erratum in: TrendsBiochem Sci. 2003 Mar;28(3):124.[PMID:12575999]
[3] Predicted from GPS-Lipid
Functional Description
Essential for the proper assembly of the glomerular and tubular basement membranes in kidney.
Sequence Annotation
Topological domain: 1 18 Cytoplasmic.
Transmembrane: 19 39 Helical.
Topological domain: 40 57 Extracellular.
Transmembrane: 58 78 Helical.
Topological domain: 79 91 Cytoplasmic.
Transmembrane: 92 112 Helical.
Topological domain: 113 221 Extracellular.
Transmembrane: 222 242 Helical.
Topological domain: 243 253 Cytoplasmic.
Protein Length
253 AA.
Protein Sequence
(Canonical)
MGEFNEKKTT CGTVCLKYLL FTYNCCFWLA GLAVMAVGIW TLALKSDYIS LLASGTYLAT  60
AYILVVAGTV VMVTGVLGCC ATFKERRNLL RLYFILLLII FLLEIIAGIL AYAYYQQLNT  120
ELKENLKDTM TKRYHQPGHE AVTSAVDQLQ QEFHCCGSNN SQDWRDSEWI RSQEAGGRVV  180
PDSCCKTVVA LCGQRDHASN IYKVEGGCIT KLETFIQEHL RVIGAVGIGI ACVQVFGMIF  240
TCCLYRSLKL EHY                                                     253
FASTA
(Canonical)
>LipidDB-9606-00495|P48509
MGEFNEKKTTCGTVCLKYLLFTYNCCFWLAGLAVMAVGIWTLALKSDYISLLASGTYLAT
AYILVVAGTVVMVTGVLGCCATFKERRNLLRLYFILLLIIFLLEIIAGILAYAYYQQLNT
ELKENLKDTMTKRYHQPGHEAVTSAVDQLQQEFHCCGSNNSQDWRDSEWIRSQEAGGRVV
PDSCCKTVVALCGQRDHASNIYKVEGGCITKLETFIQEHLRVIGAVGIGIACVQVFGMIF
TCCLYRSLKLEHY
Gene Ontology
GO:0005829; C:cytosol; TAS:Reactome
GO:0005925; C:focal adhesion; IDA:UniProtKB
GO:0005887; C:integral component of plasma membrane; TAS:ProtInc
GO:0016020; C:membrane; TAS:ProtInc
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0005178; F:integrin binding; IPI:UniProtKB
GO:0007155; P:cell adhesion; NAS:ProtInc
GO:0034329; P:cell junction assembly; TAS:Reactome
GO:0016477; P:cell migration; IEA:Ensembl
GO:0030198; P:extracellular matrix organization; TAS:Reactome
GO:0031581; P:hemidesmosome assembly; TAS:Reactome
GO:0042098; P:T cell proliferation; IEA:Ensembl
Interpro
InterPro; IPR000301; Tetraspanin
InterPro; IPR018499; Tetraspanin/Peripherin
InterPro; IPR018503; Tetraspanin_CS
InterPro; IPR008952; Tetraspanin_EC2
Pfam
Pfam; PF00335; Tetraspannin;
SMART
PROSITE
PROSITE; PS00421; TM4_1;
PRINTS
PRINTS; PR00259; TMFOUR;