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Protein

Intercellular adhesion molecule 3

Gene

ICAM3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2) (PubMed:1448173). ICAM3 is also a ligand for integrin alpha-D/beta-2. In association with integrin alpha-L/beta-2, contributes to apoptotic neutrophil phagocytosis by macrophages (PubMed:23775590).2 Publications

GO - Molecular functioni

  • integrin binding Source: BHF-UCL
  • receptor binding Source: ProtInc

GO - Biological processi

Keywordsi

Biological processCell adhesion, Phagocytosis

Enzyme and pathway databases

ReactomeiR-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-5621575. CD209 (DC-SIGN) signaling.
SIGNORiP32942.

Names & Taxonomyi

Protein namesi
Recommended name:
Intercellular adhesion molecule 3
Short name:
ICAM-3
Alternative name(s):
CDw50
ICAM-R
CD_antigen: CD50
Gene namesi
Name:ICAM3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000076662.9.
HGNCiHGNC:5346. ICAM3.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini30 – 485ExtracellularSequence analysisAdd BLAST456
Transmembranei486 – 510HelicalSequence analysisAdd BLAST25
Topological domaini511 – 547CytoplasmicSequence analysisAdd BLAST37

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi3385.
OpenTargetsiENSG00000076662.
PharmGKBiPA29594.

Chemistry databases

ChEMBLiCHEMBL3712862.

Polymorphism and mutation databases

BioMutaiICAM3.
DMDMi206729872.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Sequence analysisAdd BLAST29
ChainiPRO_000001479430 – 547Intercellular adhesion molecule 3Add BLAST518

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi52N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi53 ↔ 96PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi57 ↔ 100Combined sources1 Publication
Glycosylationi84N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi87N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi91N-linked (GlcNAc...) asparagine; atypical1 Publication1
Glycosylationi101N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi110N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi134N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi139 ↔ 190PROSITE-ProRule annotation
Glycosylationi206N-linked (GlcNAc...) asparagine3 Publications1
Disulfide bondi241 ↔ 294PROSITE-ProRule annotation
Glycosylationi264N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi295N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi308N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi320N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi336 ↔ 375PROSITE-ProRule annotation
Glycosylationi363N-linked (GlcNAc...) asparagine3 Publications1
Glycosylationi389N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi423 ↔ 462PROSITE-ProRule annotation
Glycosylationi453N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi457N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

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.4 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP32942.
MaxQBiP32942.
PaxDbiP32942.
PeptideAtlasiP32942.
PRIDEiP32942.

PTM databases

iPTMnetiP32942.
PhosphoSitePlusiP32942.
UniCarbKBiP32942.

Expressioni

Tissue specificityi

Leukocytes.2 Publications

Gene expression databases

BgeeiENSG00000076662.
CleanExiHS_ICAM3.
ExpressionAtlasiP32942. baseline and differential.
GenevisibleiP32942. HS.

Organism-specific databases

HPAiCAB002498.
HPA049820.

Interactioni

GO - Molecular functioni

  • integrin binding Source: BHF-UCL
  • receptor binding Source: ProtInc

Protein-protein interaction databases

BioGridi109612. 9 interactors.
IntActiP32942. 3 interactors.
MINTiMINT-1391707.
STRINGi9606.ENSP00000160262.

Structurei

Secondary structure

1547
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi34 – 38Combined sources5
Beta strandi48 – 55Combined sources8
Beta strandi61 – 66Combined sources6
Beta strandi68 – 77Combined sources10
Beta strandi80 – 86Combined sources7
Beta strandi92 – 100Combined sources9
Beta strandi103 – 113Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1T0PX-ray1.66B30-114[»]
ProteinModelPortaliP32942.
SMRiP32942.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32942.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini46 – 103Ig-like C2-type 1Add BLAST58
Domaini132 – 197Ig-like C2-type 2Add BLAST66
Domaini234 – 301Ig-like C2-type 3Add BLAST68
Domaini329 – 382Ig-like C2-type 4Add BLAST54
Domaini416 – 469Ig-like C2-type 5Add BLAST54

Sequence similaritiesi

Belongs to the immunoglobulin superfamily. ICAM family.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IPHM. Eukaryota.
ENOG410YQ1Q. LUCA.
GeneTreeiENSGT00530000063246.
HOGENOMiHOG000059554.
HOVERGENiHBG052074.
InParanoidiP32942.
KOiK06486.
OMAiYGPKIDR.
OrthoDBiEOG091G022Y.
PhylomeDBiP32942.
TreeFamiTF333745.

Family and domain databases

Gene3Di2.60.40.10. 6 hits.
InterProiView protein in InterPro
IPR003988. ICAM.
IPR013768. ICAM_N.
IPR003987. ICAM_VCAM_N.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
PfamiView protein in Pfam
PF03921. ICAM_N. 1 hit.
PRINTSiPR01473. ICAM.
PR01472. ICAMVCAM1.
SMARTiView protein in SMART
SM00409. IG. 3 hits.
SUPFAMiSSF48726. SSF48726. 5 hits.
PROSITEiView protein in PROSITE
PS50835. IG_LIKE. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P32942-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATMVPSVLW PRACWTLLVC CLLTPGVQGQ EFLLRVEPQN PVLSAGGSLF
60 70 80 90 100
VNCSTDCPSS EKIALETSLS KELVASGMGW AAFNLSNVTG NSRILCSVYC
110 120 130 140 150
NGSQITGSSN ITVYRLPERV ELAPLPPWQP VGQNFTLRCQ VEDGSPRTSL
160 170 180 190 200
TVVLLRWEEE LSRQPAVEEP AEVTATVLAS RDDHGAPFSC RTELDMQPQG
210 220 230 240 250
LGLFVNTSAP RQLRTFVLPV TPPRLVAPRF LEVETSWPVD CTLDGLFPAS
260 270 280 290 300
EAQVYLALGD QMLNATVMNH GDTLTATATA TARADQEGAR EIVCNVTLGG
310 320 330 340 350
ERREARENLT VFSFLGPIVN LSEPTAHEGS TVTVSCMAGA RVQVTLDGVP
360 370 380 390 400
AAAPGQPAQL QLNATESDDG RSFFCSATLE VDGEFLHRNS SVQLRVLYGP
410 420 430 440 450
KIDRATCPQH LKWKDKTRHV LQCQARGNPY PELRCLKEGS SREVPVGIPF
460 470 480 490 500
FVNVTHNGTY QCQASSSRGK YTLVVVMDIE AGSSHFVPVF VAVLLTLGVV
510 520 530 540
TIVLALMYVF REHQRSGSYH VREESTYLPL TSMQPTEAMG EEPSRAE
Length:547
Mass (Da):59,541
Last modified:September 23, 2008 - v2
Checksum:i4B7BDC02F24F3031
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti60S → F in AAB24331 (PubMed:1448173).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04654763I → V. Corresponds to variant dbSNP:rs17697947Ensembl.1
Natural variantiVAR_059394115R → G2 PublicationsCorresponds to variant dbSNP:rs7258015Ensembl.1
Natural variantiVAR_046548143D → G3 PublicationsCorresponds to variant dbSNP:rs2304237Ensembl.1
Natural variantiVAR_024498525S → T. Corresponds to variant dbSNP:rs2230399Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12235.1.
PIRiS28904.
RefSeqiNP_002153.2. NM_002162.4.
UniGeneiHs.654563.

Genome annotation databases

EnsembliENST00000160262; ENSP00000160262; ENSG00000076662.
GeneIDi3385.
KEGGihsa:3385.
UCSCiuc002mob.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiICAM3_HUMAN
AccessioniPrimary (citable) accession number: P32942
Secondary accession number(s): Q6PD68
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: September 23, 2008
Last modified: September 27, 2017
This is version 179 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families