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Protein

CD44 antigen

Gene

CD44

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 4 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei34 – 341HyaluronanBy similarity
Binding sitei71 – 711HyaluronanBy similarity
Binding sitei72 – 721HyaluronanBy similarity
Binding sitei98 – 981HyaluronanBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Cell 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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini14 – 263250ExtracellularSequence analysisAdd
BLAST
Transmembranei264 – 28421HelicalSequence analysisAdd
BLAST
Topological domaini285 – ›351›67CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei‹1 – 13›13Sequence analysisAdd
BLAST
Chaini14 – ›351›338CD44 antigenPRO_0000026684Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi18 – 181N-linked (GlcNAc...)Sequence analysis
Disulfide bondi21 ↔ 122PROSITE-ProRule annotation
Disulfide bondi46 ↔ 111PROSITE-ProRule annotation
Glycosylationi50 – 501N-linked (GlcNAc...)Sequence analysis
Disulfide bondi70 ↔ 90PROSITE-ProRule annotation
Glycosylationi93 – 931N-linked (GlcNAc...)Sequence analysis
Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence analysis
Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence analysis
Glycosylationi250 – 2501N-linked (GlcNAc...)Sequence analysis
Modified residuei286 – 2861Phosphoserine; by PKCBy similarity
Modified residuei311 – 3111PhosphoserineBy similarity
Modified residuei320 – 3201PhosphoserineBy similarity

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. Positions 13-171.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 11389LinkPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni218 – 26346StemAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi143 – 1519Arg/Lys-rich (basic)

Domaini

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

Sequence similaritiesi

Contains 1 Link domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

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

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR001231. CD44_antigen.
IPR000538. Link_dom.
[Graphical view]
PfamiPF00193. Xlink. 1 hit.
[Graphical view]
PRINTSiPR00658. CD44.
PR01265. LINKMODULE.
SMARTiSM00445. LINK. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS01241. LINK_1. 1 hit.
PS50963. LINK_2. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei351 – 3511

Sequence databases

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

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliQ28284.
SMRiQ28284. Positions 13-171.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000010256.

Proteomic databases

PaxDbiQ28284.
PRIDEiQ28284.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

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

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR001231. CD44_antigen.
IPR000538. Link_dom.
[Graphical view]
PfamiPF00193. Xlink. 1 hit.
[Graphical view]
PRINTSiPR00658. CD44.
PR01265. LINKMODULE.
SMARTiSM00445. LINK. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS01241. LINK_1. 1 hit.
PS50963. LINK_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCD44_CANLF
AccessioniPrimary (citable) accession number: Q28284
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: December 9, 2015
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.