P32942 (ICAM3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Intercellular adhesion molecule 3
Short name=ICAM-3

Alternative name(s):
CDw50
ICAM-R
CD_antigen=CD50

Gene names

Name:

ICAM3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	547 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell-cell adhesion Inferred from electronic annotation. Source: InterPro regulation of immune response Traceable author statement. Source: Reactome
Cellular_component	integral to plasma membrane Traceable author statement Ref.3. Source: ProtInc
Molecular_function	integrin binding Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 29

29

Potential

Chain

30 – 547

518

Intercellular adhesion molecule 3

PRO_0000014794

Regions

Topological domain

30 – 485

456

Extracellular Potential

Transmembrane

486 – 510

25

Helical; Potential

Topological domain

511 – 547

37

Cytoplasmic Potential

Domain

46 – 103

58

Ig-like C2-type 1

Domain

132 – 197

66

Ig-like C2-type 2

Domain

234 – 301

68

Ig-like C2-type 3

Domain

329 – 382

54

Ig-like C2-type 4

Domain

416 – 469

54

Ig-like C2-type 5

Amino acid modifications

Glycosylation

52

1

N-linked (GlcNAc...) Ref.14

Glycosylation

84

1

N-linked (GlcNAc...) Ref.11

Glycosylation

87

1

N-linked (GlcNAc...) Ref.11

Glycosylation

91

1

N-linked (GlcNAc...) Ref.11

Glycosylation

101

1

N-linked (GlcNAc...) Potential

Glycosylation

110

1

N-linked (GlcNAc...) Ref.14

Glycosylation

134

1

N-linked (GlcNAc...) Ref.11

Glycosylation

206

1

N-linked (GlcNAc...) Ref.9 Ref.10 Ref.11

Glycosylation

264

1

N-linked (GlcNAc...) Potential

Glycosylation

295

1

N-linked (GlcNAc...) Ref.11

Glycosylation

308

1

N-linked (GlcNAc...) Potential

Glycosylation

320

1

N-linked (GlcNAc...) Potential

Glycosylation

363

1

N-linked (GlcNAc...) Ref.9 Ref.10 Ref.11

Glycosylation

389

1

N-linked (GlcNAc...) Potential

Glycosylation

453

1

N-linked (GlcNAc...) Potential

Glycosylation

457

1

N-linked (GlcNAc...) Potential

Disulfide bond

53 ↔ 96

Ref.14

Disulfide bond

139 ↔ 190

Potential

Disulfide bond

241 ↔ 294

Potential

Disulfide bond

336 ↔ 375

Potential

Disulfide bond

423 ↔ 462

Potential

Natural variations

Natural variant

63

1

I → V.
Corresponds to variant rs17697947 [ dbSNP | Ensembl ].

VAR_046547

Natural variant

115

1

R → G. Ref.1 Ref.2 Ref.3
Corresponds to variant rs7258015 [ dbSNP | Ensembl ].

VAR_059394

Natural variant

143

1

D → G. Ref.1 Ref.2 Ref.3
Corresponds to variant rs2304237 [ dbSNP | Ensembl ].

VAR_046548

Natural variant

525

1

S → T.
Corresponds to variant rs2230399 [ dbSNP | Ensembl ].

VAR_024498

Experimental info

Sequence conflict

60

1

S → F in AAB24331. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

547

Helix Strand Turn

Details...

Beta strand

34 – 38

5

Beta strand

48 – 55

8

Beta strand

61 – 66

6

Beta strand

68 – 77

10

Beta strand

80 – 86

7

Beta strand

92 – 100

9

Beta strand

103 – 113

11

Sequences

	Sequence		Length	Mass (Da)
	P32942 [UniParc]. Last modified September 23, 2008. Version 2. Checksum: 4B7BDC02F24F3031	FASTA	547	59,541
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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.

Web resources

R&D Systems' cytokine source book: ICAM-3

Functional Glycomics Gateway - Glycan Binding

ICAM-3

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.

IPI

IPI00031620.

PIR

S28904.

RefSeq

NP_002153.2. NM_002162.3.

UniGene

Hs.654563.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1T0P	X-ray	1.66	B	30-114	[»]

ProteinModelPortal

P32942.

ModBase

Search...

Protein-protein interaction databases

IntAct

P32942. 3 interactions.

MINT

MINT-1391707.

STRING

9606.ENSP00000160262.

PTM databases

GlycoSuiteDB

P32942.

PhosphoSite

P32942.

Polymorphism databases

DMDM

206729872.

Proteomic databases

PaxDb

P32942.

PRIDE

P32942.

Protocols and materials databases

DNASU

3385.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000160262; ENSP00000160262; ENSG00000076662.

GeneID

3385.

KEGG

hsa:3385.

UCSC

uc002mob.2. human.

Organism-specific databases

CTD

3385.

GeneCards

GC19M010444.

H-InvDB

HIX0014743.

HGNC

HGNC:5346. ICAM3.

HPA

CAB002498.

MIM

146631. gene.

neXtProt

NX_P32942.

PharmGKB

PA29594.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG146347.

HOGENOM

HOG000059554.

HOVERGEN

HBG052074.

InParanoid

P32942.

KO

K06486.

OMA

YGPKIDR.

OrthoDB

EOG4THVT8.

PhylomeDB

P32942.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_6900. Immune System.

Gene expression databases

Bgee

P32942.

CleanEx

HS_ICAM3.

Genevestigator

P32942.

GermOnline

ENSG00000076662. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 5 hits.

InterPro

IPR003988. ICAM.
IPR013768. ICAM_N.
IPR003987. ICAM_VCAM_N.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]

Pfam

PF03921. ICAM_N. 1 hit.
[Graphical view]

PRINTS

PR01473. ICAM.
PR01472. ICAMVCAM1.

SMART

SM00409. IG. 2 hits.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P32942.

GenomeRNAi

3385.

NextBio

13392.

SOURCE

Search...

Entry information

Entry name

ICAM3_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 141 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.