Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-01169
Entry Name
UniProt Accession
Theoretical PI
8.22
Molecular Weight
65010.88
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Immunoglobulin superfamily member 8
Protein Synonyms/Alias
IgSF8; CD81 partner 3; Glu-Trp-Ile EWI motif-containing protein 2; EWI-2; Keratinocyte-associated transmembrane protein 4; KCT-4; Prostaglandin regulatory-like protein; PGRL; CD316;
Gene Name
Igsf8
Gene Synonyms/Alias
Ewi2; Kct4; Pgrl;
Created Date
07-MAR-2006
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
602
Canonical
SVLATITCCFMKRMR
[1]
S-Palmitoylation
603
Canonical
VLATITCCFMKRMRK
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] He B, Zhang YH, Richardson MM, Zhang JS, Rubinstein E, Zhang XA. Differential functions of phospholipid binding and palmitoylation of tumour suppressorEWI2/PGRL. Biochem J. 2011 Aug 1;437(3):399-411. doi: 10.1042/BJ20101381.[PMID:21609323]
Functional Description
May play a key role in diverse functions ascribed to CD81 and CD9 such as oocytes fertilization or hepatitis C virus function. May regulate proliferation and differentiation of keratinocytes. May be a negative regulator of cell motility: suppresses T-cell mobility coordinately with CD81, associates with CD82 to suppress prostate cancer cell migration, regulates epidermoid cell reaggregation and motility on laminin-5 with CD9 and CD81 as key linkers. May also play a role on integrin- dependent morphology and motility functions. May participate in the regulation of neurite outgrowth and maintenance of the neural network in the adult brain.
Sequence Annotation
Topological domain: 26 577 Extracellular.
Transmembrane: 578 598 Helical.
Topological domain: 599 611 Cytoplasmic.
Domain: 26 143 Ig-like C2-type 1.
Domain: 160 284 Ig-like C2-type 2.
Domain: 301 422 Ig-like C2-type 3.
Domain: 429 554 Ig-like C2-type 4.
Motif: 272 274 EWI motif.
Protein Length
611 AA.
Protein Sequence
(Canonical)
MGVPSPTPLS SLLLLLLILG TRCYARQVHV PRGPLYRVAG TAVSISCNVS DYEGPAQQDF  60
EWFMYRPEAP ATSLGIVSTK DSQFSYAVFG PRVASGDLQV QRLKGDSVVL KIARLQAQDS  120
GFYECYTPST DTQYLGNYSA KVELRVLPDE LQVSAAPPGP RGRQAATSPS RLTVHEGQEL  180
ALGCLAQTKT KKHTHLSVSF GRAIPEAPVG RATLQEVVGL RSDMAVEAGA PYAERLASGE  240
LRLSKEGTDR YRMVVGGAQA GDSGTYHCTA AEWIQDPDGS WVQVAEKRAV LAHVDVQTLS  300
SQLAVTVGPG ERRIGPGEPL ELLCNVSGAL PPPGRHAAYS VGWEMAPAGA PGPGRLVAQL  360
DTEGIGSLGP GYEDRHIAME KVASRTYRLR LEAARPADAG TYRCLAKAYV RGSGTRLREA  420
ASARSRPLPV HVREEGVVLE AVAWLAGGTV YRGETASLLC NISVRGGPPG LRLAASWWVE  480
RPEEGELSSG PAQLVGGVGQ DGVAELGVRP GGGPVSVELV GPRSHRLRLH GLGPEDEGIY  540
HCAPSAWVQH ADYSWYQAGS ARSGPVTVYP YTHAVDTLFV PLLVGTGVAL VTGASVLATI  600
TCCFMKRMRK R                                                       611
FASTA
(Canonical)
>LipidDB-10090-01169|Q8R366
MGVPSPTPLSSLLLLLLILGTRCYARQVHVPRGPLYRVAGTAVSISCNVSDYEGPAQQDF
EWFMYRPEAPATSLGIVSTKDSQFSYAVFGPRVASGDLQVQRLKGDSVVLKIARLQAQDS
GFYECYTPSTDTQYLGNYSAKVELRVLPDELQVSAAPPGPRGRQAATSPSRLTVHEGQEL
ALGCLAQTKTKKHTHLSVSFGRAIPEAPVGRATLQEVVGLRSDMAVEAGAPYAERLASGE
LRLSKEGTDRYRMVVGGAQAGDSGTYHCTAAEWIQDPDGSWVQVAEKRAVLAHVDVQTLS
SQLAVTVGPGERRIGPGEPLELLCNVSGALPPPGRHAAYSVGWEMAPAGAPGPGRLVAQL
DTEGIGSLGPGYEDRHIAMEKVASRTYRLRLEAARPADAGTYRCLAKAYVRGSGTRLREA
ASARSRPLPVHVREEGVVLEAVAWLAGGTVYRGETASLLCNISVRGGPPGLRLAASWWVE
RPEEGELSSGPAQLVGGVGQDGVAELGVRPGGGPVSVELVGPRSHRLRLHGLGPEDEGIY
HCAPSAWVQHADYSWYQAGSARSGPVTVYPYTHAVDTLFVPLLVGTGVALVTGASVLATI
TCCFMKRMRKR
Gene Ontology
GO:0030424; C:axon; IDA:MGI
GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl
GO:0016021; C:integral component of membrane; ISS:UniProtKB
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW
GO:0045202; C:synapse; IDA:MGI
GO:2000145; P:regulation of cell motility; IGI:MGI
Interpro
InterPro; IPR007110; Ig-like_dom
InterPro; IPR013783; Ig-like_fold
InterPro; IPR003599; Ig_sub
InterPro; IPR013106; Ig_V-set
Pfam
Pfam; PF07686; V-set;
SMART
SMART; SM00409; IG;
PROSITE
PROSITE; PS50835; IG_LIKE;
PRINTS