Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00751
Entry Name
UniProt Accession
Theoretical PI
4.82
Molecular Weight
85617.15
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
CD44 antigen
Protein Synonyms/Alias
Extracellular matrix receptor III; ECMR-III; GP90 lymphocyte homing/adhesion receptor; HUTCH-I; Hermes antigen; Hyaluronate receptor; Lymphocyte antigen 24; Ly-24; Phagocytic glycoprotein 1; PGP-1; Phagocytic glycoprotein I; PGP-I; CD44;
Gene Name
Cd44
Gene Synonyms/Alias
Ly-24;
Created Date
01-APR-1990
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
13
Canonical
WHTAWGLCLLQLSLA
[1]
S-Palmitoylation
703
Canonical
LALILAVCIAVNSRR
[1]
S-Palmitoylation
712
Canonical
AVNSRRRCGQKKKLV
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Predicted from GPS-Lipid
Functional Description
Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis (By similarity).
Sequence Annotation
Topological domain: 23 685 Extracellular.
Transmembrane: 686 706 Helical.
Topological domain: 707 778 Cytoplasmic.
Domain: 34 123 Link.
Region: 227 685 Stem.
Binding site: 43 43 Hyaluronan.
Binding site: 80 80 Hyaluronan.
Binding site: 81 81 Hyaluronan.
Binding site: 107 107 Hyaluronan.
Modified residue: 410 410 Sulfotyrosine.
Modified residue: 708 708 Phosphoserine; by PKC.
Modified residue: 726 726 Phosphothreonine.
Modified residue: 733 733 Phosphoserine.
Modified residue: 742 742 Phosphoserine.
Protein Length
778 AA.
Protein Sequence
(Canonical)
MDKFWWHTAW GLCLLQLSLA HQQIDLNVTC RYAGVFHVEK NGRYSISRTE AADLCQAFNS  60
TLPTMDQMKL ALSKGFETCR YGFIEGNVVI PRIHPNAICA ANHTGVYILV TSNTSHYDTY  120
CFNASAPPEE DCTSVTDLPN SFDGPVTITI VNRDGTRYSK KGEYRTHQED IDASNIIDDD  180
VSSGSTIEKS TPEGYILHTY LPTEQPTGDQ DDSFFIRSTL ATIASTVHSK SHAAAQKQNN  240
WIWSWFGNSQ STTQTQEPTT SATTALMTTP ETPPKRQEAQ NWFSWLFQPS ESKSHLHTTT  300
KMPGTESNTN PTGWEPNEEN EDETDTYPSF SGSGIDDDED FISSTIATTP RVSARTEDNQ  360
DWTQWKPNHS NPEVLLQTTT RMADIDRIST SAHGENWTPE PQPPFNNHEY QDEEETPHAT  420
STTPNSTAEA AATQQETWFQ NGWQGKNPPT PSEDSHVTEG TTASAHNNHP SQRITTQSQE  480
DVSWTDFFDP ISHPMGQGHQ TESKDTDSSH STTLQPTAAP NTHLVEDLNR TGPLSVTTPQ  540
SHSQNFSTLH GEPEEDENYP TTSILPSSTK SSAKDARRGG SLPTDTTTSV EGYTFQYPDT  600
MENGTLFPVT PAKTEVFGET EVTLATDSNV NVDGSLPGDR DSSKDSRGSS RTVTHGSELA  660
GHSSANQDSG VTTTSGPMRR PQIPEWLIIL ASLLALALIL AVCIAVNSRR RCGQKKKLVI  720
NGGNGTVEDR KPSELNGEAS KSQEMVHLVN KEPSETPDQC MTADETRNLQ SVDMKIGV    778
FASTA
(Canonical)
>LipidDB-10090-00751|P15379
MDKFWWHTAWGLCLLQLSLAHQQIDLNVTCRYAGVFHVEKNGRYSISRTEAADLCQAFNS
TLPTMDQMKLALSKGFETCRYGFIEGNVVIPRIHPNAICAANHTGVYILVTSNTSHYDTY
CFNASAPPEEDCTSVTDLPNSFDGPVTITIVNRDGTRYSKKGEYRTHQEDIDASNIIDDD
VSSGSTIEKSTPEGYILHTYLPTEQPTGDQDDSFFIRSTLATIASTVHSKSHAAAQKQNN
WIWSWFGNSQSTTQTQEPTTSATTALMTTPETPPKRQEAQNWFSWLFQPSESKSHLHTTT
KMPGTESNTNPTGWEPNEENEDETDTYPSFSGSGIDDDEDFISSTIATTPRVSARTEDNQ
DWTQWKPNHSNPEVLLQTTTRMADIDRISTSAHGENWTPEPQPPFNNHEYQDEEETPHAT
STTPNSTAEAAATQQETWFQNGWQGKNPPTPSEDSHVTEGTTASAHNNHPSQRITTQSQE
DVSWTDFFDPISHPMGQGHQTESKDTDSSHSTTLQPTAAPNTHLVEDLNRTGPLSVTTPQ
SHSQNFSTLHGEPEEDENYPTTSILPSSTKSSAKDARRGGSLPTDTTTSVEGYTFQYPDT
MENGTLFPVTPAKTEVFGETEVTLATDSNVNVDGSLPGDRDSSKDSRGSSRTVTHGSELA
GHSSANQDSGVTTTSGPMRRPQIPEWLIILASLLALALILAVCIAVNSRRRCGQKKKLVI
NGGNGTVEDRKPSELNGEASKSQEMVHLVNKEPSETPDQCMTADETRNLQSVDMKIGV
Gene Ontology
GO:0016323; C:basolateral plasma membrane; IDA:MGI
GO:0009986; C:cell surface; IDA:MGI
GO:0009897; C:external side of plasma membrane; IDA:MGI
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0005886; C:plasma membrane; IDA:MGI
GO:0005540; F:hyaluronic acid binding; IDA:MGI
GO:0060442; P:branching involved in prostate gland morphogenesis; IMP:MGI
GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI
GO:0007155; P:cell adhesion; IDA:MGI
GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:BHF-UCL
GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:BHF-UCL
GO:0002906; P:negative regulation of mature B cell apoptotic process; IDA:BHF-UCL
GO:0002821; P:positive regulation of adaptive immune response; NAS:BHF-UCL
GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:BHF-UCL
GO:0010628; P:positive regulation of gene expression; IGI:MGI
GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:BHF-UCL
GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL
GO:0016055; P:Wnt signaling pathway; IDA:MGI
GO:0002246; P:wound healing involved in inflammatory response; IMP:MGI
Interpro
InterPro; IPR016186; C-type_lectin-like
InterPro; IPR016187; C-type_lectin_fold
InterPro; IPR001231; CD44_antigen
InterPro; IPR000538; Link
Pfam
Pfam; PF00193; Xlink;
SMART
SMART; SM00445; LINK;
PROSITE
PROSITE; PS01241; LINK_1;
PROSITE; PS50963; LINK_2;
PRINTS
PRINTS; PR00658; CD44;
PRINTS; PR01265; LINKMODULE;