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Protein

CD44 antigen

Gene

CD44

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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. Receptor for LGALS9; the interaction enhances binding of SMAD3 to the FOXP3 promoter, leading to up-regulation of FOXP3 expression and increased induced regulatory T (iTreg) cell stability and suppressive function.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei34HyaluronanBy similarity1
Binding sitei71HyaluronanBy similarity1
Binding sitei72HyaluronanBy similarity1
Binding sitei98HyaluronanBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionReceptor
Biological processCell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
CD44 antigen
Alternative name(s):
Extracellular matrix receptor-III
Short name:
ECMR-III
GP90 lymphocyte homing/adhesion receptor
HUTCH-I
Hermes antigen
Hyaluronate receptor
Phagocytic glycoprotein 1
Short name:
PGP-1
Phagocytic glycoprotein I
Short name:
PGP-I
CD_antigen: CD44
Gene namesi
Name:CD44
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Unplaced

Subcellular locationi

  • Cell membrane By similarity; Single-pass type I membrane protein By similarity

  • Note: Colocalizes with actin in membrane protrusions at wounding edges.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini14 – 263ExtracellularSequence analysisAdd BLAST250
Transmembranei264 – 284HelicalSequence analysisAdd BLAST21
Topological domaini285 – ›351CytoplasmicSequence analysisAdd BLAST›67

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei‹1 – 13Sequence analysisAdd BLAST›13
ChainiPRO_000002668414 – ›351CD44 antigenAdd BLAST›338

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi18N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi21 ↔ 122PROSITE-ProRule annotation
Disulfide bondi46 ↔ 111PROSITE-ProRule annotation
Glycosylationi50N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi70 ↔ 90PROSITE-ProRule annotation
Glycosylationi93N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi103N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi113N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi250N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei286Phosphoserine; by PKCBy similarity1
Modified residuei311PhosphoserineBy similarity1
Modified residuei320PhosphoserineBy similarity1

Post-translational modificationi

Extensively modified including N- and O-linked glycosylation, addition of the glycosaminoglycan chondroitin sulfate, of sulfate, of phosphate to cytoplasmic domain serine residues.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Proteoglycan

Proteomic databases

PaxDbiQ28284.
PRIDEiQ28284.

Expressioni

Tissue specificityi

Lymph nodes.

Interactioni

Subunit structurei

Interacts with HA, as well as other glycosaminoglycans, collagen, laminin, and fibronectin via its N-terminal segment. Interacts with ANK, the ERM proteins (VIL2, RDX and MSN), and NF2 via its C-terminal segment. Interacts with PKN2. Interacts with TIAM1 and TIAM2. Interacts with UNC119.By similarity

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000010256.

Structurei

3D structure databases

ProteinModelPortaliQ28284.
SMRiQ28284.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 113LinkPROSITE-ProRule annotationAdd BLAST89

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni218 – 263StemAdd BLAST46

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi143 – 151Arg/Lys-rich (basic)9

Domaini

The lectin-like LINK domain is responsible for hyaluronan binding.By similarity

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IZCP. Eukaryota.
ENOG4111S6T. LUCA.
HOVERGENiHBG003850.
InParanoidiQ28284.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiView protein in InterPro
IPR016186. C-type_lectin-like/link.
IPR001231. CD44_antigen.
IPR016187. CTDL_fold.
IPR000538. Link_dom.
PANTHERiPTHR10225:SF8. PTHR10225:SF8. 1 hit.
PfamiView protein in Pfam
PF00193. Xlink. 1 hit.
PRINTSiPR00658. CD44.
PR01265. LINKMODULE.
SMARTiView protein in SMART
SM00445. LINK. 1 hit.
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiView protein in PROSITE
PS01241. LINK_1. 1 hit.
PS50963. LINK_2. 1 hit.

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q28284-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
LAWGLCLLRL SLAQIDLNIT CRYAGVFHVE KNGRYSISRT AAADLCKAFN
60 70 80 90 100
STLPTMAQME RALSVGFETC RYGFIEGHVV IPRIQPNAIC AANHTGVYIL
110 120 130 140 150
ISNTSQYDTY CFNASAPPEE DCTSVTHLPN AFDGPITITI VNRDGTRYSQ
160 170 180 190 200
KGEYRTNPED INPSNPTDDD VSSGSSSERS TSAGYNIFHT HLPTAYPTED
210 220 230 240 250
QDSSRVSSNS DHTPITKDHD SSVHPSERSH TTHGSESAGH SSGSQEGGAN
260 270 280 290 300
TTSGPMRKPQ IPEWLIILAS LLALALILAV CIAVNSRRRC GQKKKLVINN
310 320 330 340 350
GNGAVGDRKP SGINGEASKS QEMVHLVNKE PSETPDQYTT ADETRNLQNV

D
Length:351
Mass (Da):38,066
Last modified:November 1, 1997 - v1
Checksum:iE73387E70E20C0E0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Non-terminal residuei3511

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z27115 mRNA. Translation: CAA81630.1.
PIRiS45305.
UniGeneiCfa.3800.

Similar proteinsi

Entry informationi

Entry nameiCD44_CANLF
AccessioniPrimary (citable) accession number: Q28284
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: August 30, 2017
This is version 102 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome