Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P15379

- CD44_MOUSE

UniProt

P15379 - CD44_MOUSE

Protein

CD44 antigen

Gene

Cd44

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 3 (30 Apr 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei43 – 431Hyaluronan1 Publication
    Binding sitei80 – 801Hyaluronan1 Publication
    Binding sitei81 – 811Hyaluronan1 Publication
    Binding sitei107 – 1071Hyaluronan1 Publication

    GO - Molecular functioni

    1. hyaluronic acid binding Source: MGI
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. branching involved in prostate gland morphogenesis Source: MGI
    2. branching involved in ureteric bud morphogenesis Source: MGI
    3. cell adhesion Source: MGI
    4. negative regulation of DNA damage response, signal transduction by p53 class mediator Source: BHF-UCL
    5. negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: BHF-UCL
    6. negative regulation of mature B cell apoptotic process Source: BHF-UCL
    7. positive regulation of adaptive immune response Source: BHF-UCL
    8. positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
    9. positive regulation of gene expression Source: MGI
    10. positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
    11. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    12. Wnt signaling pathway Source: MGI
    13. wound healing involved in inflammatory response Source: MGI

    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
    Lymphocyte antigen 24
    Short name:
    Ly-24
    Phagocytic glycoprotein 1
    Short name:
    PGP-1
    Phagocytic glycoprotein I
    Short name:
    PGP-I
    CD_antigen: CD44
    Gene namesi
    Name:Cd44
    Synonyms:Ly-24
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:88338. Cd44.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication
    Note: Colocalizes with actin in membrane protrusions at wounding edges.

    GO - Cellular componenti

    1. basolateral plasma membrane Source: MGI
    2. cell surface Source: MGI
    3. external side of plasma membrane Source: MGI
    4. integral component of membrane Source: UniProtKB-KW
    5. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222By similarityAdd
    BLAST
    Chaini23 – 778756CD44 antigenPRO_0000026689Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi27 – 271N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi30 ↔ 1321 PublicationPROSITE-ProRule annotation
    Disulfide bondi55 ↔ 1211 PublicationPROSITE-ProRule annotation
    Glycosylationi59 – 591N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi79 ↔ 991 PublicationPROSITE-ProRule annotation
    Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi123 – 1231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis
    Modified residuei410 – 4101SulfotyrosineBy similarity
    Glycosylationi425 – 4251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi529 – 5291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi545 – 5451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi603 – 6031N-linked (GlcNAc...)Sequence Analysis
    Modified residuei708 – 7081Phosphoserine; by PKCBy similarity
    Modified residuei726 – 7261Phosphothreonine1 Publication
    Modified residuei733 – 7331Phosphoserine1 Publication
    Modified residuei742 – 7421Phosphoserine1 Publication

    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-742 (constitutive phosphorylation site), and the phosphorylation of Ser-708.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Proteoglycan, Sulfation

    Proteomic databases

    PaxDbiP15379.
    PRIDEiP15379.

    PTM databases

    PhosphoSiteiP15379.

    Expressioni

    Gene expression databases

    CleanExiMM_CD44.
    GenevestigatoriP15379.

    Interactioni

    Subunit structurei

    Interacts with HA, as well as other glycosaminoglycans, collagen, laminin, and fibronectin via its N-terminal segment By similarity. 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.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Tiam1Q606108EBI-7565891,EBI-1030321
    Tiam2Q6ZPF38EBI-7565891,EBI-7565978

    Protein-protein interaction databases

    DIPiDIP-29095N.
    IntActiP15379. 5 interactions.

    Structurei

    Secondary structure

    1
    778
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi23 – 286
    Beta strandi35 – 406
    Helixi48 – 5710
    Helixi65 – 739
    Beta strandi85 – 9410
    Helixi100 – 1023
    Beta strandi105 – 1084
    Beta strandi117 – 1226
    Beta strandi128 – 1314
    Beta strandi142 – 15211
    Beta strandi157 – 1637
    Helixi168 – 1703
    Beta strandi715 – 7195

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JCPX-ray1.30A23-174[»]
    2JCQX-ray1.25A23-174[»]
    2JCRX-ray2.00A23-174[»]
    2ZPYX-ray2.10B708-727[»]
    4MRDX-ray2.55A23-171[»]
    4MREX-ray1.58A23-171[»]
    4MRFX-ray1.55A23-171[»]
    4MRGX-ray1.69A23-171[»]
    4MRHX-ray1.12A23-171[»]
    4NP2X-ray1.75A23-171[»]
    4NP3X-ray1.61A23-171[»]
    ProteinModelPortaliP15379.
    SMRiP15379. Positions 23-171.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15379.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 685663ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini707 – 77872CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei686 – 70621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini34 – 12390LinkPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni227 – 685459StemAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi153 – 1619Arg/Lys-rich (basic)

    Domaini

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

    Sequence similaritiesi

    Contains 1 Link domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG41023.
    HOVERGENiHBG003850.
    InParanoidiP15379.
    KOiK06256.

    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.
    [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 (13)i

    Sequence statusi: Complete.

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

    This entry describes 13 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P15379-14) [UniParc]FASTAAdd to Basket

    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

    MDKFWWHTAW GLCLLQLSLA HQQIDLNVTC RYAGVFHVEK NGRYSISRTE    50
    AADLCQAFNS TLPTMDQMKL ALSKGFETCR YGFIEGNVVI PRIHPNAICA 100
    ANHTGVYILV TSNTSHYDTY CFNASAPPEE DCTSVTDLPN SFDGPVTITI 150
    VNRDGTRYSK KGEYRTHQED IDASNIIDDD VSSGSTIEKS TPEGYILHTY 200
    LPTEQPTGDQ DDSFFIRSTL ATIASTVHSK SHAAAQKQNN WIWSWFGNSQ 250
    STTQTQEPTT SATTALMTTP ETPPKRQEAQ NWFSWLFQPS ESKSHLHTTT 300
    KMPGTESNTN PTGWEPNEEN EDETDTYPSF SGSGIDDDED FISSTIATTP 350
    RVSARTEDNQ DWTQWKPNHS NPEVLLQTTT RMADIDRIST SAHGENWTPE 400
    PQPPFNNHEY QDEEETPHAT STTPNSTAEA AATQQETWFQ NGWQGKNPPT 450
    PSEDSHVTEG TTASAHNNHP SQRITTQSQE DVSWTDFFDP ISHPMGQGHQ 500
    TESKDTDSSH STTLQPTAAP NTHLVEDLNR TGPLSVTTPQ SHSQNFSTLH 550
    GEPEEDENYP TTSILPSSTK SSAKDARRGG SLPTDTTTSV EGYTFQYPDT 600
    MENGTLFPVT PAKTEVFGET EVTLATDSNV NVDGSLPGDR DSSKDSRGSS 650
    RTVTHGSELA GHSSANQDSG VTTTSGPMRR PQIPEWLIIL ASLLALALIL 700
    AVCIAVNSRR RCGQKKKLVI NGGNGTVEDR KPSELNGEAS KSQEMVHLVN 750
    KEPSETPDQC MTADETRNLQ SVDMKIGV 778
    Length:778
    Mass (Da):85,617
    Last modified:April 30, 2003 - v3
    Checksum:iBD2C073250F6C956
    GO
    Isoform 2 (identifier: P15379-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         223-264: Missing.

    Show »
    Length:736
    Mass (Da):81,015
    Checksum:iA4697E905F8DCDA5
    GO
    Isoform 3 (identifier: P15379-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         223-303: Missing.

    Show »
    Length:697
    Mass (Da):76,463
    Checksum:i796CC452E28B8BC5
    GO
    Isoform 4 (identifier: P15379-4) [UniParc]FASTAAdd to Basket

    Also known as: M2

    The sequence of this isoform differs from the canonical sequence as follows:
         223-346: Missing.

    Show »
    Length:654
    Mass (Da):71,780
    Checksum:i6211C96F93F72A16
    GO
    Isoform 5 (identifier: P15379-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         223-383: Missing.

    Show »
    Length:617
    Mass (Da):67,517
    Checksum:i2CA109453C5D8A90
    GO
    Isoform 6 (identifier: P15379-5) [UniParc]FASTAAdd to Basket

    Also known as: M3

    The sequence of this isoform differs from the canonical sequence as follows:
         223-424: Missing.

    Show »
    Length:576
    Mass (Da):62,858
    Checksum:iE7052A0A1690F9DB
    GO
    Isoform 7 (identifier: P15379-6) [UniParc]FASTAAdd to Basket

    Also known as: M4

    The sequence of this isoform differs from the canonical sequence as follows:
         223-504: Missing.

    Show »
    Length:496
    Mass (Da):54,055
    Checksum:i8CF72BC7AD2C2490
    GO
    Isoform 8 (identifier: P15379-10) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         223-303: Missing.
         424-504: Missing.

    Show »
    Length:616
    Mass (Da):67,563
    Checksum:iF945E31D9E1AB63D
    GO
    Isoform 9 (identifier: P15379-11) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         223-383: Missing.
         463-504: Missing.

    Show »
    Length:575
    Mass (Da):62,800
    Checksum:i771039FF04C95470
    GO
    Isoform 10 (identifier: P15379-12) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         569-580: TKSSAKDARRGG → VCLVVVADFSAL
         581-778: Missing.

    Show »
    Length:580
    Mass (Da):64,443
    Checksum:iF6CB36489A1C9885
    GO
    Isoform 11 (identifier: P15379-13) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         569-592: TKSSAKDARRGGSLPTDTTTSVEG → VRIIKSNWLLSRNQDVMGVSGGGC
         593-778: Missing.

    Show »
    Length:592
    Mass (Da):65,797
    Checksum:i60BAF55CBB1308C0
    GO
    Isoform 12 (identifier: P15379-3) [UniParc]FASTAAdd to Basket

    Also known as: M1

    The sequence of this isoform differs from the canonical sequence as follows:
         223-539: Missing.

    Show »
    Length:461
    Mass (Da):50,398
    Checksum:i031244225F1D8AFE
    GO
    Isoform 13 (identifier: P15379-2) [UniParc]FASTAAdd to Basket

    Also known as: M0

    The sequence of this isoform differs from the canonical sequence as follows:
         223-637: Missing.
         638-638: G → R

    Show »
    Length:363
    Mass (Da):39,999
    Checksum:i80031C90F26F8880
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti326 – 3261T → K(PubMed:10859330)Curated
    Sequence conflicti326 – 3261T → K(PubMed:8509359)Curated
    Sequence conflicti348 – 3481T → S(PubMed:8509359)Curated
    Sequence conflicti559 – 5591Y → H(PubMed:10859330)Curated
    Sequence conflicti559 – 5591Y → H(PubMed:8464707)Curated
    Sequence conflicti559 – 5591Y → H(PubMed:8509359)Curated
    Sequence conflicti572 – 5721S → G(PubMed:10859330)Curated
    Sequence conflicti572 – 5721S → G(PubMed:8464707)Curated
    Sequence conflicti572 – 5721S → G(PubMed:8509359)Curated
    Sequence conflicti639 – 6391D → RD(PubMed:2403559)Curated

    Polymorphismi

    Two allelic forms of this glycoprotein, PGP-1.1 and PGP-1.2, have been reported. The expressed product is PGP-1.1 (Ly-24.1).

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti21 – 211H → HPH in Ly-24.2.
    Natural varianti194 – 1941G → S in Ly-24.2.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei223 – 637415Missing in isoform 13. 5 PublicationsVSP_005329Add
    BLAST
    Alternative sequencei223 – 539317Missing in isoform 12. 1 PublicationVSP_005328Add
    BLAST
    Alternative sequencei223 – 504282Missing in isoform 7. 2 PublicationsVSP_005327Add
    BLAST
    Alternative sequencei223 – 424202Missing in isoform 6. 2 PublicationsVSP_005326Add
    BLAST
    Alternative sequencei223 – 383161Missing in isoform 5 and isoform 9. 2 PublicationsVSP_007332Add
    BLAST
    Alternative sequencei223 – 346124Missing in isoform 4. 2 PublicationsVSP_007331Add
    BLAST
    Alternative sequencei223 – 30381Missing in isoform 3 and isoform 8. 1 PublicationVSP_007330Add
    BLAST
    Alternative sequencei223 – 26442Missing in isoform 2. 1 PublicationVSP_007329Add
    BLAST
    Alternative sequencei424 – 50481Missing in isoform 8. 1 PublicationVSP_007334Add
    BLAST
    Alternative sequencei463 – 50442Missing in isoform 9. 1 PublicationVSP_007335Add
    BLAST
    Alternative sequencei569 – 59224TKSSA…TSVEG → VRIIKSNWLLSRNQDVMGVS GGGC in isoform 11. CuratedVSP_007338Add
    BLAST
    Alternative sequencei569 – 58012TKSSA…ARRGG → VCLVVVADFSAL in isoform 10. CuratedVSP_007336Add
    BLAST
    Alternative sequencei581 – 778198Missing in isoform 10. CuratedVSP_007337Add
    BLAST
    Alternative sequencei593 – 778186Missing in isoform 11. CuratedVSP_007339Add
    BLAST
    Alternative sequencei638 – 6381G → R in isoform 13. 5 PublicationsVSP_007333

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66084 mRNA. Translation: CAA46883.1.
    X66083 mRNA. Translation: CAA46882.1.
    X66082 mRNA. Translation: CAA46881.1.
    X66081 mRNA. Translation: CAA46880.1.
    M30655 mRNA. Translation: AAA39922.1.
    M27129 mRNA. Translation: AAA37406.1.
    M27130 mRNA. Translation: AAA37407.1.
    AJ251594 mRNA. Translation: CAB61888.1.
    BC005676 mRNA. Translation: AAH05676.1.
    AK045226 mRNA. Translation: BAC32269.1.
    J05163 mRNA. Translation: AAA39923.1.
    X69724 mRNA. Translation: CAA49380.1.
    L13611 mRNA. Translation: AAA37145.1.
    U57610 mRNA. Translation: AAC52804.1.
    U57611 mRNA. Translation: AAB08756.1.
    U57612 Genomic DNA. Translation: AAC52805.1.
    U57612 Genomic DNA. Translation: AAC52806.1.
    PIRiA34424.
    A37009.
    B44355.
    D44355.
    S30397.
    RefSeqiNP_001034240.1. NM_001039151.1.
    NP_001171256.1. NM_001177785.1.
    NP_001171257.1. NM_001177786.1.
    NP_001171258.1. NM_001177787.1.
    NP_033981.2. NM_009851.2.
    UniGeneiMm.423621.

    Genome annotation databases

    GeneIDi12505.
    KEGGimmu:12505.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66084 mRNA. Translation: CAA46883.1 .
    X66083 mRNA. Translation: CAA46882.1 .
    X66082 mRNA. Translation: CAA46881.1 .
    X66081 mRNA. Translation: CAA46880.1 .
    M30655 mRNA. Translation: AAA39922.1 .
    M27129 mRNA. Translation: AAA37406.1 .
    M27130 mRNA. Translation: AAA37407.1 .
    AJ251594 mRNA. Translation: CAB61888.1 .
    BC005676 mRNA. Translation: AAH05676.1 .
    AK045226 mRNA. Translation: BAC32269.1 .
    J05163 mRNA. Translation: AAA39923.1 .
    X69724 mRNA. Translation: CAA49380.1 .
    L13611 mRNA. Translation: AAA37145.1 .
    U57610 mRNA. Translation: AAC52804.1 .
    U57611 mRNA. Translation: AAB08756.1 .
    U57612 Genomic DNA. Translation: AAC52805.1 .
    U57612 Genomic DNA. Translation: AAC52806.1 .
    PIRi A34424.
    A37009.
    B44355.
    D44355.
    S30397.
    RefSeqi NP_001034240.1. NM_001039151.1.
    NP_001171256.1. NM_001177785.1.
    NP_001171257.1. NM_001177786.1.
    NP_001171258.1. NM_001177787.1.
    NP_033981.2. NM_009851.2.
    UniGenei Mm.423621.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JCP X-ray 1.30 A 23-174 [» ]
    2JCQ X-ray 1.25 A 23-174 [» ]
    2JCR X-ray 2.00 A 23-174 [» ]
    2ZPY X-ray 2.10 B 708-727 [» ]
    4MRD X-ray 2.55 A 23-171 [» ]
    4MRE X-ray 1.58 A 23-171 [» ]
    4MRF X-ray 1.55 A 23-171 [» ]
    4MRG X-ray 1.69 A 23-171 [» ]
    4MRH X-ray 1.12 A 23-171 [» ]
    4NP2 X-ray 1.75 A 23-171 [» ]
    4NP3 X-ray 1.61 A 23-171 [» ]
    ProteinModelPortali P15379.
    SMRi P15379. Positions 23-171.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-29095N.
    IntActi P15379. 5 interactions.

    PTM databases

    PhosphoSitei P15379.

    Proteomic databases

    PaxDbi P15379.
    PRIDEi P15379.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 12505.
    KEGGi mmu:12505.

    Organism-specific databases

    CTDi 960.
    MGIi MGI:88338. Cd44.

    Phylogenomic databases

    eggNOGi NOG41023.
    HOVERGENi HBG003850.
    InParanoidi P15379.
    KOi K06256.

    Miscellaneous databases

    EvolutionaryTracei P15379.
    NextBioi 281466.
    PROi P15379.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_CD44.
    Genevestigatori P15379.

    Family and domain databases

    Gene3Di 3.10.100.10. 1 hit.
    InterProi IPR016186. C-type_lectin-like.
    IPR016187. C-type_lectin_fold.
    IPR001231. CD44_antigen.
    IPR000538. Link.
    [Graphical view ]
    Pfami PF00193. Xlink. 1 hit.
    [Graphical view ]
    PRINTSi PR00658. CD44.
    PR01265. LINKMODULE.
    SMARTi SM00445. LINK. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56436. SSF56436. 1 hit.
    PROSITEi PS01241. LINK_1. 1 hit.
    PS50963. LINK_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular isoforms of murine CD44 and evidence that the membrane proximal domain is not critical for hyaluronate recognition."
      He Q., Lesley J., Hyman R., Ishihara K., Kincade P.W.
      J. Cell Biol. 119:1711-1719(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 6; 7 AND 12).
      Strain: DBA/2.
      Tissue: Lung.
    2. "Molecular cloning and expression of Pgp-1. The mouse homolog of the human H-CAM (Hermes) lymphocyte homing receptor."
      Zhou D.F.H., Ding J.F., Picker L.J., Bargatze R.F., Butcher E.C., Goeddel D.V.
      J. Immunol. 143:3390-3395(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 13).
    3. "Isolation of mouse CD44 cDNA: structural features are distinct from the primate cDNA."
      Nottenburg C., Rees G., St John T.
      Proc. Natl. Acad. Sci. U.S.A. 86:8521-8525(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 13).
    4. "Abrogation of experimental colitis correlates with increased apoptosis in mice deficient for CD44 variant exon 7 (CD44v7)."
      Wittig B.M., Johansson B., Zoeller M., Schwaerzler C., Guenthert U.
      J. Exp. Med. 191:2053-2064(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 13).
    6. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 13).
      Strain: C57BL/6J.
      Tissue: Embryo.
    7. "The cDNA sequence of mouse Pgp-1 and homology to human CD44 cell surface antigen and proteoglycan core/link proteins."
      Wolffe E.J., Gause W.C., Pelfrey C.M., Holland S.M., Steinberg A.D., August J.T.
      J. Biol. Chem. 265:341-347(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-778 (ISOFORM 13).
    8. "Splicing choice from ten variant exons establishes CD44 variability."
      Toelg C., Hofmann M., Herrlich P., Ponta H.
      Nucleic Acids Res. 21:1225-1229(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 224-637 (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8).
      Strain: GR.
    9. "The identification of a new alternative exon with highly restricted tissue expression in transcripts encoding the mouse Pgp-1 (CD44) homing receptor. Comparison of all 10 variable exons between mouse, human, and rat."
      Screaton G.R., Bell M.V., Bell J.I., Jackson D.G.
      J. Biol. Chem. 268:12235-12238(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 224-637 (ISOFORM 9).
      Strain: BALB/c.
    10. "A new alternatively spliced exon between v9 and v10 provides a molecular basis for synthesis of soluble CD44."
      Yu Q., Toole B.P.
      J. Biol. Chem. 271:20603-20607(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 10 AND 11).
      Strain: Swiss Webster.
    11. "Hyaluronan-CD44 interaction stimulates Rac1 signaling and PKN gamma kinase activation leading to cytoskeleton function and cell migration in astrocytes."
      Bourguignon L.Y., Gilad E., Peyrollier K., Brightman A., Swanson R.A.
      J. Neurochem. 101:1002-1017(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PKN2, SUBCELLULAR LOCATION.
    12. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-726; SER-733 AND SER-742, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "The PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding module."
      Terawaki S., Kitano K., Mori T., Zhai Y., Higuchi Y., Itoh N., Watanabe T., Kaibuchi K., Hakoshima T.
      EMBO J. 29:236-250(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TIAM1 AND TIAM2.
    14. "Structures of the Cd44-hyaluronan complex provide insight into a fundamental carbohydrate-protein interaction."
      Banerji S., Wright A.J., Noble M., Mahoney D.J., Campbell I.D., Day A.J., Jackson D.G.
      Nat. Struct. Mol. Biol. 14:234-239(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 23-174 ALONE AND IN COMPLEX WITH HYALURONAN, SUBUNIT, DISULFIDE BONDS.

    Entry informationi

    Entry nameiCD44_MOUSE
    AccessioniPrimary (citable) accession number: P15379
    Secondary accession number(s): Q05732
    , Q61395, Q62060, Q62061, Q62062, Q62063, Q62408, Q62409, Q64296, Q99J14, Q9QYX8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 30, 2003
    Last modified: October 1, 2014
    This is version 154 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3