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P15379 (CD44_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Cd44
Synonyms:Ly-24
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length778 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.11 Ref.13 Ref.14

Subcellular location

Cell membrane; Single-pass type I membrane protein. Note: Colocalizes with actin in membrane protrusions at wounding edges. Ref.11

Domain

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

Post-translational modification

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.

Polymorphism

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).

Sequence similarities

Contains 1 Link domain.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Proteoglycan
Sulfation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from direct assay PubMed 19056892. Source: MGI

branching involved in prostate gland morphogenesis

Inferred from mutant phenotype PubMed 9374396. Source: MGI

branching involved in ureteric bud morphogenesis

Inferred from mutant phenotype PubMed 10926769. Source: MGI

cell adhesion

Inferred from direct assay Ref.1. Source: MGI

negative regulation of DNA damage response, signal transduction by p53 class mediator

Inferred from mutant phenotype PubMed 17045821. Source: BHF-UCL

negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from mutant phenotype PubMed 17045821. Source: BHF-UCL

negative regulation of mature B cell apoptotic process

Inferred from direct assay PubMed 18056708. Source: BHF-UCL

positive regulation of ERK1 and ERK2 cascade

Inferred from mutant phenotype PubMed 17045821. Source: BHF-UCL

positive regulation of adaptive immune response

Non-traceable author statement PubMed 18056708. Source: BHF-UCL

positive regulation of gene expression

Inferred from genetic interaction PubMed 9847236. Source: MGI

positive regulation of peptidyl-serine phosphorylation

Inferred from mutant phenotype PubMed 17045821. Source: BHF-UCL

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from mutant phenotype PubMed 17045821. Source: BHF-UCL

signal transduction

Inferred from direct assay. Source: GOC

wound healing involved in inflammatory response

Inferred from mutant phenotype PubMed 11935029. Source: MGI

   Cellular_componentbasolateral plasma membrane

Inferred from direct assay PubMed 10027409. Source: MGI

cell surface

Inferred from direct assay Ref.1PubMed 9324354. Source: MGI

external side of plasma membrane

Inferred from direct assay PubMed 10072077PubMed 10704459PubMed 10848813PubMed 10943842PubMed 14609575PubMed 14764662PubMed 15294943PubMed 15477346PubMed 15728238PubMed 16177108PubMed 16203996PubMed 16301745PubMed 16973387PubMed 17082577PubMed 18958875PubMed 19008373PubMed 19723499PubMed 19934022PubMed 20711497PubMed 21460847PubMed 21508411PubMed 21708977PubMed 22072979PubMed 7538697PubMed 7584142PubMed 8043862PubMed 8769481PubMed 9133426. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay PubMed 18085615PubMed 9374396. Source: MGI

   Molecular_functionhyaluronic acid binding

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 13 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P15379-14)

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.
Isoform 2 (identifier: P15379-7)

The sequence of this isoform differs from the canonical sequence as follows:
     223-264: Missing.
Isoform 3 (identifier: P15379-8)

The sequence of this isoform differs from the canonical sequence as follows:
     223-303: Missing.
Isoform 4 (identifier: P15379-4)

Also known as: M2;

The sequence of this isoform differs from the canonical sequence as follows:
     223-346: Missing.
Isoform 5 (identifier: P15379-9)

The sequence of this isoform differs from the canonical sequence as follows:
     223-383: Missing.
Isoform 6 (identifier: P15379-5)

Also known as: M3;

The sequence of this isoform differs from the canonical sequence as follows:
     223-424: Missing.
Isoform 7 (identifier: P15379-6)

Also known as: M4;

The sequence of this isoform differs from the canonical sequence as follows:
     223-504: Missing.
Isoform 8 (identifier: P15379-10)

The sequence of this isoform differs from the canonical sequence as follows:
     223-303: Missing.
     424-504: Missing.
Isoform 9 (identifier: P15379-11)

The sequence of this isoform differs from the canonical sequence as follows:
     223-383: Missing.
     463-504: Missing.
Isoform 10 (identifier: P15379-12)

The sequence of this isoform differs from the canonical sequence as follows:
     569-580: TKSSAKDARRGG → VCLVVVADFSAL
     581-778: Missing.
Isoform 11 (identifier: P15379-13)

The sequence of this isoform differs from the canonical sequence as follows:
     569-592: TKSSAKDARRGGSLPTDTTTSVEG → VRIIKSNWLLSRNQDVMGVSGGGC
     593-778: Missing.
Isoform 12 (identifier: P15379-3)

Also known as: M1;

The sequence of this isoform differs from the canonical sequence as follows:
     223-539: Missing.
Isoform 13 (identifier: P15379-2)

Also known as: M0;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 By similarity
Chain23 – 778756CD44 antigen
PRO_0000026689

Regions

Topological domain23 – 685663Extracellular Potential
Transmembrane686 – 70621Helical; Potential
Topological domain707 – 77872Cytoplasmic Potential
Domain34 – 12390Link
Region227 – 685459Stem
Compositional bias153 – 1619Arg/Lys-rich (basic)

Sites

Binding site431Hyaluronan
Binding site801Hyaluronan
Binding site811Hyaluronan
Binding site1071Hyaluronan

Amino acid modifications

Modified residue4101Sulfotyrosine By similarity
Modified residue7081Phosphoserine; by PKC By similarity
Modified residue7261Phosphothreonine Ref.12
Modified residue7331Phosphoserine Ref.12
Modified residue7421Phosphoserine Ref.12
Glycosylation271N-linked (GlcNAc...) Potential
Glycosylation591N-linked (GlcNAc...) Potential
Glycosylation1021N-linked (GlcNAc...) Potential
Glycosylation1131N-linked (GlcNAc...) Potential
Glycosylation1231N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential
Glycosylation4251N-linked (GlcNAc...) Potential
Glycosylation5291N-linked (GlcNAc...) Potential
Glycosylation5451N-linked (GlcNAc...) Potential
Glycosylation6031N-linked (GlcNAc...) Potential
Disulfide bond30 ↔ 132 Ref.14
Disulfide bond55 ↔ 121 Ref.14
Disulfide bond79 ↔ 99 Ref.14

Natural variations

Alternative sequence223 – 637415Missing in isoform 13.
VSP_005329
Alternative sequence223 – 539317Missing in isoform 12.
VSP_005328
Alternative sequence223 – 504282Missing in isoform 7.
VSP_005327
Alternative sequence223 – 424202Missing in isoform 6.
VSP_005326
Alternative sequence223 – 383161Missing in isoform 5 and isoform 9.
VSP_007332
Alternative sequence223 – 346124Missing in isoform 4.
VSP_007331
Alternative sequence223 – 30381Missing in isoform 3 and isoform 8.
VSP_007330
Alternative sequence223 – 26442Missing in isoform 2.
VSP_007329
Alternative sequence424 – 50481Missing in isoform 8.
VSP_007334
Alternative sequence463 – 50442Missing in isoform 9.
VSP_007335
Alternative sequence569 – 59224TKSSA…TSVEG → VRIIKSNWLLSRNQDVMGVS GGGC in isoform 11.
VSP_007338
Alternative sequence569 – 58012TKSSA…ARRGG → VCLVVVADFSAL in isoform 10.
VSP_007336
Alternative sequence581 – 778198Missing in isoform 10.
VSP_007337
Alternative sequence593 – 778186Missing in isoform 11.
VSP_007339
Alternative sequence6381G → R in isoform 13.
VSP_007333
Natural variant211H → HPH in Ly-24.2.
Natural variant1941G → S in Ly-24.2.

Experimental info

Sequence conflict3261T → K Ref.4
Sequence conflict3261T → K Ref.9
Sequence conflict3481T → S Ref.9
Sequence conflict5591Y → H Ref.4
Sequence conflict5591Y → H Ref.8
Sequence conflict5591Y → H Ref.9
Sequence conflict5721S → G Ref.4
Sequence conflict5721S → G Ref.8
Sequence conflict5721S → G Ref.9
Sequence conflict6391D → RD Ref.7

Secondary structure

........................... 778
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 30, 2003. Version 3.
Checksum: BD2C073250F6C956

FASTA77885,617
        10         20         30         40         50         60 
MDKFWWHTAW GLCLLQLSLA HQQIDLNVTC RYAGVFHVEK NGRYSISRTE AADLCQAFNS 

        70         80         90        100        110        120 
TLPTMDQMKL ALSKGFETCR YGFIEGNVVI PRIHPNAICA ANHTGVYILV TSNTSHYDTY 

       130        140        150        160        170        180 
CFNASAPPEE DCTSVTDLPN SFDGPVTITI VNRDGTRYSK KGEYRTHQED IDASNIIDDD 

       190        200        210        220        230        240 
VSSGSTIEKS TPEGYILHTY LPTEQPTGDQ DDSFFIRSTL ATIASTVHSK SHAAAQKQNN 

       250        260        270        280        290        300 
WIWSWFGNSQ STTQTQEPTT SATTALMTTP ETPPKRQEAQ NWFSWLFQPS ESKSHLHTTT 

       310        320        330        340        350        360 
KMPGTESNTN PTGWEPNEEN EDETDTYPSF SGSGIDDDED FISSTIATTP RVSARTEDNQ 

       370        380        390        400        410        420 
DWTQWKPNHS NPEVLLQTTT RMADIDRIST SAHGENWTPE PQPPFNNHEY QDEEETPHAT 

       430        440        450        460        470        480 
STTPNSTAEA AATQQETWFQ NGWQGKNPPT PSEDSHVTEG TTASAHNNHP SQRITTQSQE 

       490        500        510        520        530        540 
DVSWTDFFDP ISHPMGQGHQ TESKDTDSSH STTLQPTAAP NTHLVEDLNR TGPLSVTTPQ 

       550        560        570        580        590        600 
SHSQNFSTLH GEPEEDENYP TTSILPSSTK SSAKDARRGG SLPTDTTTSV EGYTFQYPDT 

       610        620        630        640        650        660 
MENGTLFPVT PAKTEVFGET EVTLATDSNV NVDGSLPGDR DSSKDSRGSS RTVTHGSELA 

       670        680        690        700        710        720 
GHSSANQDSG VTTTSGPMRR PQIPEWLIIL ASLLALALIL AVCIAVNSRR RCGQKKKLVI 

       730        740        750        760        770 
NGGNGTVEDR KPSELNGEAS KSQEMVHLVN KEPSETPDQC MTADETRNLQ SVDMKIGV 

« Hide

Isoform 2 [UniParc].

Checksum: A4697E905F8DCDA5
Show »

FASTA73681,015
Isoform 3 [UniParc].

Checksum: 796CC452E28B8BC5
Show »

FASTA69776,463
Isoform 4 (M2) [UniParc].

Checksum: 6211C96F93F72A16
Show »

FASTA65471,780
Isoform 5 [UniParc].

Checksum: 2CA109453C5D8A90
Show »

FASTA61767,517
Isoform 6 (M3) [UniParc].

Checksum: E7052A0A1690F9DB
Show »

FASTA57662,858
Isoform 7 (M4) [UniParc].

Checksum: 8CF72BC7AD2C2490
Show »

FASTA49654,055
Isoform 8 [UniParc].

Checksum: F945E31D9E1AB63D
Show »

FASTA61667,563
Isoform 9 [UniParc].

Checksum: 771039FF04C95470
Show »

FASTA57562,800
Isoform 10 [UniParc].

Checksum: F6CB36489A1C9885
Show »

FASTA58064,443
Isoform 11 [UniParc].

Checksum: 60BAF55CBB1308C0
Show »

FASTA59265,797
Isoform 12 (M1) [UniParc].

Checksum: 031244225F1D8AFE
Show »

FASTA46150,398
Isoform 13 (M0) [UniParc].

Checksum: 80031C90F26F8880
Show »

FASTA36339,999

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA34424.
A37009.
B44355.
D44355.
S30397.
RefSeqNP_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.
UniGeneMm.423621.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JCPX-ray1.30A23-174[»]
2JCQX-ray1.25A23-174[»]
2JCRX-ray2.00A23-174[»]
2ZPYX-ray2.10B708-727[»]
ProteinModelPortalP15379.
SMRP15379. Positions 23-171.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29095N.
IntActP15379. 5 interactions.

PTM databases

PhosphoSiteP15379.

Proteomic databases

PaxDbP15379.
PRIDEP15379.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID12505.
KEGGmmu:12505.

Organism-specific databases

CTD960.
MGIMGI:88338. Cd44.

Phylogenomic databases

eggNOGNOG41023.
HOVERGENHBG003850.
InParanoidP15379.
KOK06256.

Gene expression databases

CleanExMM_CD44.
GenevestigatorP15379.

Family and domain databases

Gene3D3.10.100.10. 1 hit.
InterProIPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR001231. CD44_antigen.
IPR000538. Link.
[Graphical view]
PfamPF00193. Xlink. 1 hit.
[Graphical view]
PRINTSPR00658. CD44.
PR01265. LINKMODULE.
SMARTSM00445. LINK. 1 hit.
[Graphical view]
SUPFAMSSF56436. SSF56436. 1 hit.
PROSITEPS01241. LINK_1. 1 hit.
PS50963. LINK_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15379.
NextBio281466.
PROP15379.
SOURCESearch...

Entry information

Entry nameCD44_MOUSE
AccessionPrimary (citable) accession number: P15379
Secondary accession number(s): Q05732 expand/collapse secondary AC list , Q61395, Q62060, Q62061, Q62062, Q62063, Q62408, Q62409, Q64296, Q99J14, Q9QYX8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 30, 2003
Last modified: April 16, 2014
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot