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Reviewed, UniProtKB/Swiss-Prot P32942 (ICAM3_HUMAN)

Last modified November 3, 2009. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Intercellular adhesion molecule 3
      Short name=ICAM-3
Alternative name(s):
    ICAM-R
    CDw50
    CD_antigen=CD50
Gene names
Name: ICAM3
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length547 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). ICAM3 is also a ligand for integrin alpha-D/beta-2.

Subcellular location

Membrane; Single-pass type I membrane protein.

Post-translational modification

Upon stimulation by a physiologic stimuli becomes rapidly and transiently phosphorylated on serine residues.

N-glycosylated; glycans consist of a mixture of tri- and tetra-antennary complex-type chains and high-mannose chains. Ref.8 Ref.9 Ref.11 Ref.12 Ref.13

Sequence similarities

Belongs to the immunoglobulin superfamily. ICAM family.

Contains 5 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processcell-cell adhesion

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to plasma membrane Ref.3

Traceable author statement. Source: ProtInc

   Molecular functionintegrin binding Ref.1 Ref.2

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ITGALP207011EBI-725421,EBI-961214

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 547518Intercellular adhesion molecule 3
PRO_0000014794

Regions

Topological domain30 – 485456Extracellular Potential
Transmembrane486 – 51025 Potential
Topological domain511 – 54737Cytoplasmic Potential
Domain46 – 10358Ig-like C2-type 1
Domain132 – 19766Ig-like C2-type 2
Domain234 – 30168Ig-like C2-type 3
Domain329 – 38254Ig-like C2-type 4
Domain416 – 46954Ig-like C2-type 5

Amino acid modifications

Glycosylation521N-linked (GlcNAc...) Ref.13
Glycosylation841N-linked (GlcNAc...) Ref.12
Glycosylation871N-linked (GlcNAc...) Ref.12
Glycosylation911N-linked (GlcNAc...) Ref.12
Glycosylation1011N-linked (GlcNAc...) Potential
Glycosylation1101N-linked (GlcNAc...) Ref.13
Glycosylation1341N-linked (GlcNAc...) Ref.12
Glycosylation2061N-linked (GlcNAc...) Ref.9 Ref.11 Ref.12
Glycosylation2641N-linked (GlcNAc...) Potential
Glycosylation2951N-linked (GlcNAc...) Ref.12
Glycosylation3081N-linked (GlcNAc...) Potential
Glycosylation3201N-linked (GlcNAc...) Potential
Glycosylation3631N-linked (GlcNAc...) Ref.9 Ref.11 Ref.12
Glycosylation3891N-linked (GlcNAc...) Potential
Glycosylation4531N-linked (GlcNAc...) Potential
Glycosylation4571N-linked (GlcNAc...) Potential
Disulfide bond53 ↔ 96 Ref.13
Disulfide bond139 ↔ 190 Potential
Disulfide bond241 ↔ 294 Potential
Disulfide bond336 ↔ 375 Potential
Disulfide bond423 ↔ 462 Potential

Natural variations

Natural variant631I → V: dbSNP rs17697947.
VAR_046547
Natural variant1151R → G: dbSNP rs7258015. Ref.1 Ref.2 Ref.3
VAR_059394
Natural variant1431D → G: dbSNP rs2304237. Ref.1 Ref.2 Ref.3
VAR_046548
Natural variant5251S → T: dbSNP rs2230399.
VAR_024498

Experimental info

Sequence conflict601S → F in AAB24331. Ref.1

Secondary structure

............... 547
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32942-1 [UniParc].

Last modified September 23, 2008. Version 2.
Checksum: 4B7BDC02F24F3031

FASTA54759,541
        10         20         30         40         50         60 
MATMVPSVLW PRACWTLLVC CLLTPGVQGQ EFLLRVEPQN PVLSAGGSLF VNCSTDCPSS 

        70         80         90        100        110        120 
EKIALETSLS KELVASGMGW AAFNLSNVTG NSRILCSVYC NGSQITGSSN ITVYRLPERV 

       130        140        150        160        170        180 
ELAPLPPWQP VGQNFTLRCQ VEDGSPRTSL TVVLLRWEEE LSRQPAVEEP AEVTATVLAS 

       190        200        210        220        230        240 
RDDHGAPFSC RTELDMQPQG LGLFVNTSAP RQLRTFVLPV TPPRLVAPRF LEVETSWPVD 

       250        260        270        280        290        300 
CTLDGLFPAS EAQVYLALGD QMLNATVMNH GDTLTATATA TARADQEGAR EIVCNVTLGG 

       310        320        330        340        350        360 
ERREARENLT VFSFLGPIVN LSEPTAHEGS TVTVSCMAGA RVQVTLDGVP AAAPGQPAQL 

       370        380        390        400        410        420 
QLNATESDDG RSFFCSATLE VDGEFLHRNS SVQLRVLYGP KIDRATCPQH LKWKDKTRHV 

       430        440        450        460        470        480 
LQCQARGNPY PELRCLKEGS SREVPVGIPF FVNVTHNGTY QCQASSSRGK YTLVVVMDIE 

       490        500        510        520        530        540 
AGSSHFVPVF VAVLLTLGVV TIVLALMYVF REHQRSGSYH VREESTYLPL TSMQPTEAMG 


EEPSRAE 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of ICAM-3, a third ligand for LFA-1, constitutively expressed on resting leukocytes."
Fawcett J., Holness C.L., Needham L.A., Turley H., Gatter K.C., Mason D.Y., Simmons D.L.
Nature 360:481-484(1992) [PubMed: 1448173] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS AND GLY-115 GLY-143.
[2]"Cloning and characterization of a new intercellular adhesion molecule ICAM-R."
Vazeux R., Hoffman P.A., Tomita J.K., Dickinson E.S., Jasman R.L., St John T., Gallatin W.M.
Nature 360:485-488(1992) [PubMed: 1448174] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GLY-115 AND GLY-143.
[3]"Cloning and expression of intercellular adhesion molecule 3 reveals strong homology to other immunoglobulin family counter-receptors for lymphocyte function-associated antigen 1."
de Fougerolles A.R., Kilckstein L.B., Springer T.A.
J. Exp. Med. 177:1187-1192(1993) [PubMed: 8459213] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GLY-115 AND GLY-143.
[4]"Genetic variation in immune response genes."
Tan J., Ong R., Hibberd M.L., Seielstad M.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[7]"CDw50 and ICAM-3: two names for the same molecule."
Juan M., Vilella R., Mila J., Yague J., Miralles A., Campbell K.S., Friedrich R.J., Cambier J., Vives J., de Fougerolles A.R., Springer T.A.
Eur. J. Immunol. 23:1508-1512(1993) [PubMed: 8325327] [Abstract]
Cited for: PROTEIN SEQUENCE OF 197-217; 269-293 AND 338-365.
[8]"Structural study of N-linked oligosaccharides of human intercellular adhesion molecule-3 (CD50)."
Funatsu O., Sato T., Kotovuori P., Gahmberg C.G., Ikekita M., Furukawa K.
Eur. J. Biochem. 268:1020-1029(2001) [PubMed: 11179968] [Abstract]
Cited for: STRUCTURE OF N-LINKED CARBOHYDRATES.
[9]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206 AND ASN-363, MASS SPECTROMETRY.
Tissue: Plasma.
[10]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206 AND ASN-363, MASS SPECTROMETRY.
Tissue: Liver.
[12]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed: 19349973] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-84; ASN-87; ASN-91; ASN-134; ASN-206; ASN-295 AND ASN-363, MASS SPECTROMETRY.
[13]"An atomic resolution view of ICAM recognition in a complex between the binding domains of ICAM-3 and integrin alphaLbeta2."
Song G., Yang Y., Liu J.-H., Casasnovas J.M., Shimaoka M., Springer T.A., Wang J.-H.
Proc. Natl. Acad. Sci. U.S.A. 102:3366-3371(2005) [PubMed: 15728350] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 30-115 IN COMPLEX WITH INTEGRIN ALPHALBETA2, DISULFIDE BOND, GLYCOSYLATION AT ASN-52 AND ASN-110.
+Additional computationally mapped references.

Cross-references

Sequence databases

S50015 mRNA. Translation: AAB24331.2. Sequence problems.
X69711 mRNA. Translation: CAA49369.1.
X69819 mRNA. Translation: CAA49473.1.
DQ217937 Genomic DNA. Translation: ABB01007.1.
CH471106 Genomic DNA. Translation: EAW84092.1.
BC058903 mRNA. Translation: AAH58903.1.
IPIIPI00031620.
PIRS28904.
RefSeqNP_002153.2.
UniGeneHs.654563

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1T0PX-ray1.66B30-114[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP32942. 2 interactions.
STRINGP32942.

PTM databases

GlycoSuiteDBP32942.
PhosphoSiteP32942.

Proteomic databases

PRIDEP32942.

Genome annotation databases

EnsemblENST00000160262; ENSP00000160262; ENSG00000076662; Homo sapiens. [Genome view]
GeneID3385.
KEGGhsa:3385.
UCSCuc002mob.2. human.

Organism-specific databases

CTD3385.
GeneCardsGC19M010305.
H-InvDBHIX0039997.
HGNCHGNC:5346. ICAM3.
HPACAB002498.
MIM146631. gene.
PharmGKBPA29594.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP32942.
HOVERGENP32942.
OMAYGPKIDR.

Enzyme and pathway databases

ReactomeREACT_13552. Integrin cell surface interactions.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpressP32942.
BgeeP32942.
CleanExHS_ICAM3.
GenevestigatorP32942.
GermOnlineENSG00000076662. Homo sapiens.

Family and domain databases

InterProIPR003988. ICAM.
IPR013768. ICAM_N.
IPR003987. ICAM_VCAM_N.
IPR013151. Ig.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 3 hits.
PfamPF03921. ICAM_N. 1 hit.
PF00047. ig. 1 hit.
[Graphical view]
PRINTSPR01473. ICAM.
PR01472. ICAMVCAM1.
SMARTSM00409. IG. 2 hits.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry nameICAM3_HUMAN
AccessionPrimary (citable) accession number: P32942
Secondary accession number(s): Q6PD68
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: September 23, 2008
Last modified: November 3, 2009
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents