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Protein

CD44 antigen

Gene

Cd44

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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 sitei44 – 441HyaluronanBy similarity
Binding sitei81 – 811HyaluronanBy similarity
Binding sitei82 – 821HyaluronanBy similarity
Binding sitei108 – 1081HyaluronanBy similarity

GO - Molecular functioni

  • epidermal growth factor receptor binding Source: RGD
  • hyaluronic acid binding Source: RGD
  • phosphoprotein binding Source: RGD
  • protein kinase binding Source: RGD

GO - Biological processi

  • blood vessel maturation Source: RGD
  • cell adhesion Source: RGD
  • cell migration Source: RGD
  • inflammatory response Source: RGD
  • macrophage fusion Source: RGD
  • neuron projection development Source: RGD
  • positive regulation of neutrophil apoptotic process Source: RGD
  • regulation of cell growth Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to vitamin A Source: RGD
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2307. Cd44.

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 domaini22 – 410389ExtracellularSequence analysisAdd
BLAST
Transmembranei411 – 43121HelicalSequence analysisAdd
BLAST
Topological domaini432 – 50372CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • apical plasma membrane Source: RGD
  • basolateral plasma membrane Source: RGD
  • integral component of membrane Source: UniProtKB-KW
  • nucleus Source: RGD
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Add
BLAST
Chaini22 – 503482CD44 antigenPRO_0000026691Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei22 – 221Pyrrolidone carboxylic acidCurated
Glycosylationi28 – 281N-linked (GlcNAc...)Sequence analysis
Disulfide bondi31 ↔ 133PROSITE-ProRule annotation
Disulfide bondi56 ↔ 122PROSITE-ProRule annotation
Glycosylationi60 – 601N-linked (GlcNAc...)Sequence analysis
Disulfide bondi80 ↔ 100PROSITE-ProRule annotation
Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence analysis
Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence analysis
Glycosylationi124 – 1241N-linked (GlcNAc...)Sequence analysis
Glycosylationi266 – 2661N-linked (GlcNAc...)Sequence analysis
Glycosylationi274 – 2741N-linked (GlcNAc...)Sequence analysis
Modified residuei288 – 2881Sulfotyrosine; in isoform 21 Publication
Glycosylationi306 – 3061N-linked (GlcNAc...)Sequence analysis
Modified residuei433 – 4331Phosphoserine; by PKCBy similarity
Modified residuei447 – 4471PhosphoserineCombined sources
Modified residuei451 – 4511PhosphothreonineCombined sources
Modified residuei458 – 4581PhosphoserineBy similarity
Modified residuei467 – 4671PhosphoserineCombined sources

Post-translational modificationi

N-glycosylated.By similarity
O-glycosylated; contains chondroitin sulfate glycans which can be more or less sulfated.By similarity
Phosphorylated; activation of PKC results in the dephosphorylation of Ser-467 (constitutive phosphorylation site), and the phosphorylation of Ser-433.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Proteoglycan, Pyrrolidone carboxylic acid, Sulfation

Proteomic databases

PRIDEiP26051.

PTM databases

iPTMnetiP26051.
PhosphoSiteiP26051.

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

GO - Molecular functioni

  • epidermal growth factor receptor binding Source: RGD
  • phosphoprotein binding Source: RGD
  • protein kinase binding Source: RGD

Protein-protein interaction databases

IntActiP26051. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP26051.
SMRiP26051. Positions 23-172.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 12490LinkPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni228 – 410183StemAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi154 – 1629Arg/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

HOVERGENiHBG003850.
InParanoidiP26051.
PhylomeDBiP26051.

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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform 2 (identifier: P26051-1) [UniParc]FASTAAdd to basket

Also known as: Long, Meta-1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDKVWWHTAW GLLCLLQLSL AQQQIDLNIT CRYAGVFHVE KNGRYSISRT
60 70 80 90 100
EAADLCEAFN TTLPTMAQME LALRKGFETC RYGFIEGHVV IPRIHPNAIC
110 120 130 140 150
AANNTGVYIL LASNTSHYDT YCFNASAPLE EDCTSVTDLP NSFDGPVTIT
160 170 180 190 200
IVNRDGTRYS KKGEYRTHQE DIDASNIIDE DVSSGSTIEK STPEGYILHT
210 220 230 240 250
DLPTSQPTGD RDDAFFIGST LATIATTPWV SAHTKQNQER TQWNPIHSNP
260 270 280 290 300
EVLLQTTTRM TDIDRNSTSA HGENWTQEPQ PPFNNHEYQD EEETPHATST
310 320 330 340 350
TWADPNSTTE EAATQKEKWF ENEWQGKNPP TPSEDSHVTE GTTASAHNNH
360 370 380 390 400
PSQRMTTQSQ EDVSWTDFFD PISHPMGQGH QTESKGHSSG NQDSGVTTTS
410 420 430 440 450
GPARRPQIPE WLIILASLLA LALILAVCIA VNSRRRCGQK KKLVINSGNG
460 470 480 490 500
TVEDRKPSEL NGEASKSQEM VHLVNKEPTE TPDQFMTADE TRNLQSVDMK

IGV
Length:503
Mass (Da):55,946
Last modified:November 1, 1997 - v2
Checksum:iFB489D009BD4EE22
GO
Isoform 1 (identifier: P26051-2) [UniParc]FASTAAdd to basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     224-385: IATTPWVSAH...MGQGHQTESK → SDGDSSMDPRGGFDTVTHGSELA

Show »
Length:364
Mass (Da):39,794
Checksum:iC45DE71B059DEA5D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741R → S in AAA97915 (Ref. 2) Curated
Sequence conflicti74 – 741R → S in AAA92920 (Ref. 2) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei224 – 385162IATTP…QTESK → SDGDSSMDPRGGFDTVTHGS ELA in isoform 1. 2 PublicationsVSP_005330Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61875 mRNA. Translation: AAA53532.1.
M61874 mRNA. Translation: AAA53534.1.
U52179 mRNA. Translation: AAA97915.1.
U46957 mRNA. Translation: AAA92920.1.
PIRiB38745.
RefSeqiXP_006234693.1. XM_006234631.2.
UniGeneiRn.1120.

Genome annotation databases

GeneIDi25406.
UCSCiRGD:2307. rat. [P26051-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61875 mRNA. Translation: AAA53532.1.
M61874 mRNA. Translation: AAA53534.1.
U52179 mRNA. Translation: AAA97915.1.
U46957 mRNA. Translation: AAA92920.1.
PIRiB38745.
RefSeqiXP_006234693.1. XM_006234631.2.
UniGeneiRn.1120.

3D structure databases

ProteinModelPortaliP26051.
SMRiP26051. Positions 23-172.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP26051. 1 interaction.

PTM databases

iPTMnetiP26051.
PhosphoSiteiP26051.

Proteomic databases

PRIDEiP26051.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25406.
UCSCiRGD:2307. rat. [P26051-1]

Organism-specific databases

CTDi960.
RGDi2307. Cd44.

Phylogenomic databases

HOVERGENiHBG003850.
InParanoidiP26051.
PhylomeDBiP26051.

Miscellaneous databases

PROiP26051.

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...

Publicationsi

« Hide 'large scale' publications
  1. "A new variant of glycoprotein CD44 confers metastatic potential to rat carcinoma cells."
    Guenthert U., Hofmann M., Rudy W., Reber S., Zoeller M., Haussmann I., Matzku S., Wenzel A., Ponta H., Herrlich P.
    Cell 65:13-24(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Strain: BDIX.
    Tissue: Pancreas.
  2. Stevens J.W., Midura R.J.
    Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "CD44 variant exon v5 encodes a tyrosine that is sulphated."
    Sleeman J.P., Rahmsdorf U., Steffen A., Ponta H., Herrlich P.
    Eur. J. Biochem. 255:74-80(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SULFATION AT TYR-288.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447; THR-451 AND SER-467, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCD44_RAT
AccessioniPrimary (citable) accession number: P26051
Secondary accession number(s): Q99021
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: November 1, 1997
Last modified: June 8, 2016
This is version 127 of the entry and version 2 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.