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P32942 (ICAM3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Intercellular adhesion molecule 3

Short name=ICAM-3
Alternative name(s):
CDw50
ICAM-R
CD_antigen=CD50
Gene names
Name:ICAM3
OrganismHomo sapiens (Human) [Reference 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.14

Sequence similarities

Belongs to the immunoglobulin superfamily. ICAM family.

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

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 – 51025Helical; 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.14
Glycosylation841N-linked (GlcNAc...) Ref.11
Glycosylation871N-linked (GlcNAc...) Ref.11
Glycosylation911N-linked (GlcNAc...); atypical Ref.11
Glycosylation1011N-linked (GlcNAc...) Potential
Glycosylation1101N-linked (GlcNAc...) Ref.14
Glycosylation1341N-linked (GlcNAc...) Ref.11
Glycosylation2061N-linked (GlcNAc...) Ref.9 Ref.10 Ref.11
Glycosylation2641N-linked (GlcNAc...) Potential
Glycosylation2951N-linked (GlcNAc...) Ref.11
Glycosylation3081N-linked (GlcNAc...) Potential
Glycosylation3201N-linked (GlcNAc...) Potential
Glycosylation3631N-linked (GlcNAc...) Ref.9 Ref.10 Ref.11
Glycosylation3891N-linked (GlcNAc...) Potential
Glycosylation4531N-linked (GlcNAc...) Potential
Glycosylation4571N-linked (GlcNAc...) Potential
Disulfide bond53 ↔ 96 Ref.14
Disulfide bond139 ↔ 190 Potential
Disulfide bond241 ↔ 294 Potential
Disulfide bond336 ↔ 375 Potential
Disulfide bond423 ↔ 462 Potential

Natural variations

Natural variant631I → V.
Corresponds to variant rs17697947 [ dbSNP | Ensembl ].
VAR_046547
Natural variant1151R → G. Ref.1 Ref.2 Ref.3
Corresponds to variant rs7258015 [ dbSNP | Ensembl ].
VAR_059394
Natural variant1431D → G. Ref.1 Ref.2 Ref.3
Corresponds to variant rs2304237 [ dbSNP | Ensembl ].
VAR_046548
Natural variant5251S → T.
Corresponds to variant rs2230399 [ dbSNP | Ensembl ].
VAR_024498

Experimental info

Sequence conflict601S → F in AAB24331. Ref.1

Secondary structure

............... 547
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32942 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206 AND ASN-363.
Tissue: Plasma.
[10]"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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206 AND ASN-363.
Tissue: Liver.
[11]"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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-84; ASN-87; ASN-91; ASN-134; ASN-206; ASN-295 AND ASN-363.
Tissue: Leukemic T-cell.
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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] [Europe PMC] [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

EMBL
GenBank
DDBJ
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.
PIRS28904.
RefSeqNP_002153.2. NM_002162.3.
UniGeneHs.654563.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1T0PX-ray1.66B30-114[»]
ProteinModelPortalP32942.
SMRP32942. Positions 30-479.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109612. 5 interactions.
IntActP32942. 3 interactions.
MINTMINT-1391707.
STRING9606.ENSP00000160262.

PTM databases

PhosphoSiteP32942.
UniCarbKBP32942.

Polymorphism databases

DMDM206729872.

Proteomic databases

PaxDbP32942.
PRIDEP32942.

Protocols and materials databases

DNASU3385.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000160262; ENSP00000160262; ENSG00000076662.
GeneID3385.
KEGGhsa:3385.
UCSCuc002mob.2. human.

Organism-specific databases

CTD3385.
GeneCardsGC19M010444.
H-InvDBHIX0014743.
HGNCHGNC:5346. ICAM3.
HPACAB002498.
MIM146631. gene.
neXtProtNX_P32942.
PharmGKBPA29594.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG146347.
HOGENOMHOG000059554.
HOVERGENHBG052074.
InParanoidP32942.
KOK06486.
OMAYGPKIDR.
OrthoDBEOG7QG43X.
PhylomeDBP32942.
TreeFamTF333745.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP32942.
BgeeP32942.
CleanExHS_ICAM3.
GenevestigatorP32942.

Family and domain databases

Gene3D2.60.40.10. 5 hits.
InterProIPR003988. ICAM.
IPR013768. ICAM_N.
IPR003987. ICAM_VCAM_N.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
PfamPF03921. ICAM_N. 1 hit.
[Graphical view]
PRINTSPR01473. ICAM.
PR01472. ICAMVCAM1.
SMARTSM00409. IG. 2 hits.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP32942.
GeneWikiICAM3.
GenomeRNAi3385.
NextBio13392.
PROP32942.
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: March 19, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries