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PR01472

Identifier
ICAMVCAM1  [View Relations]  [View Alignment]  
Accession
PR01472
No. of Motifs
4
Creation Date
05-FEB-2001
Title
Intercellular adhesion molecule/vascular cell adhesion molecule-1 signature
Database References
PRINTS; PR01473 ICAM; PR01474 VCAM1
PFAM; PF00047 ig
INTERPRO; IPR003006
PDB; 1IAM; 1VCA
SCOP; 1IAM; 1VCA
CATH; 1IAM; 1VCA
Literature References
1. GAHMBERG, C,G., TOLVANEN, M. AND  KOTOVUORI, P.
Leukocyte adhesion. Structure and function of human leukocyte
beta2-integrins and their cellular ligands.
EUR.J.BIOCHEMISTRY 245 215-232 (1997).
 
2. LEE, Y. W., KUHN, H., HENNIG, B., NEISH, A.S. AND TOBOREK, M.
IL-4 induced oxidative stress upregulates VCAM-1 gene expression in human
endothelial cells.
J.MOL.CELL.CARDIO. 33 83-94 (2001).
 
3. STANLEY, P., MCDOWALL, A. BATES, P.A., BRASHAW, J. AND  HOGG, N.
The second domain of intercellular adhesion molecule-1 (ICAM-1) maintains
the structural integrity of the leukocyte function-associated antigen-1
BIOCHEM.J. 351 79-86 (2000).
 
4. BELLA, J., KOLATKAR, P.R., MARLOR, C.W., GREVE, J.M. AND ROSSMANN, M.G.
The structure of the two amino-terminal domains of human ICAM-1 suggests 
how it functions as a rhinovirus receptor and as an LFA-1 integrin ligand.
PROC.NATL.ACAD.SCI.U.S.A. 95 4140-4145(1998). 
 
5. KOTOVUORI, A., PESSA-MORIKAWA, T., KOTOVUORI, P., NORTAMO, P. AND 
GAHMBERG, C.G.
ICAM-2 and a peptide from its binding domain are efficient activators
of leukocyte adhesion and integrin  affinity.
PROC.NATL.ACAD.SCI.U.S.A. 96 3017-3022 (1999).
 
6. NEELAMEGHAM, S., TAYLOR, A.D., SHANKARAN, H., SMITH, W.C. AND SIMON, S.I.
Shear and time-depeneant changes in Mac-1, LFA, and ICAM-3 binding
regulate neutrophil homotypic adhesion.
J.IMMUNOL. 164 3798-3805 (2000).
 
7. HERMAND, P., HUET, M., CALLEBAUT, I., GANE, P., IHANUS, E.,
GAHMBERG, C.G., CARTRON, J.P. AND BAILLY, P.
Binding sites of leukocyte beta 2-integrins (LFA-1, MAC-1) on the human
ICAM-4/LW blood group protein.
J.BIOL.CHEM. 275 26002-26010 (2000).
 
8. TIAN, L., KILGANNON, P., YOSHIHARA, Y., MORI, K., GALLATIN, W.M., 
CARPEN, O. AND GAHMBERG, C.G.
Binding of T lymphocytes to hippocampal neurons through ICAM-5 
integrin CD11a/CD18.
EUR.J.IMMUNOL. 30 810-818 (2000).
 
9. JONES, E.Y., HARLOS, K., BOTTOMLEY, M.J., ROBINSON, R.C., DRISCOLL, P.C.,
EDWARDS, R.M., CLEMENTS, J.M., DUDGEON, T.J. AND STUART, D.I.
Crystal structure of an integrin-binding fragment of vascular cell adhesion
molecule-1 at 1.8 A resolution.
NATURE 373 539-544 (1995). 

Documentation
Intercellular adhesion molecules (ICAMs) and vascular cell adhesion 
molecule-1 (VCAM-1) are part of the immunoglobulin superfamily. They are
important in inflammation, immune responses and in intracellular signalling
events [1]. 
 
The ICAM family consists of five members, designated ICAM-1 to ICAM-5. They
are known to bind to leucocyte integrins CD11/CD18 during inflammation and
in immune responses. In addition, ICAMs may exist in soluble forms in human
plasma, due to activation and proteolysis mechanisms at cell surfaces [1]. 
 
ICAM-1 (CD54) contains five Ig-like domains. It is expressed on leucocytes, 
endothelial and epithelial cells, and is upregulated in response to 
bacterial invasion. The protein is a receptor for CD11a,b/CD18 (also termed
leukocyte-function associated (LFA) anitgen), fibrinogen, human rhinoviruses
and plasmodium falciparum-infected erythrocytes. ICAM-1binding sites for 
CD11a/CD18 and its other binding partners are located in the first domain
and are overlapping. ICAM-1 domain 2 seems to play an important role in
maintaining the conformation of domain 1 and particularly the structural 
integrity of the LFA-1 ligand-binding site [3]. 
 
The 3-dimensional atomic structure of the tandem N-terminal Ig-like domains 
(D1 and D2) of ICAM-1 has been determined to 2.2A resolution and fitted into
a cryoelectron microscopy reconstruction of a rhinovirus-ICAM-1 complex [4].
Extensive charge interactions between ICAM-1 and human rhinoviruses are
largely conserved in  major and minor receptor groups of rhinoviruses [4].
The interaction of ICAMs with LFA-1 is mediated by a divalent cation bound
to the insertion (I)-domain on the alpha chain of LFA-1 and the carboxyl 
group of a conserved glutamic acid residue on ICAMs [4]. 
 
ICAM-2 (CD102) has two Ig-like domains. It is expressed on endothelial
cells, leucocytes and platelets, and binds to CD11a,b/CD18. The protein is
refractory to proinflammatory cytokines, and plays an important role in the
adhesion of leucocytes to the uninduced endothelium [5].
 
ICAM-3 (CD50) contains five Ig-like domains and binds to leucocyte integrins
CD11a,d/CD18. The protein plays an important role in the immune response and
perhaps in signal transduction [6].
 
ICAM-4 (LW blood group Ag) is red blood cell (RBC) specific and binds to 
CD11a,b/CD18. It is associated with the RBC Rh antigens and could be 
important in retaining immature red cells in the bone marrow, or in the 
uptake of senescent cells into the spleen [7].
 
ICAM-5 (telencephalin) has nine Ig-like domains and is confined to the 
telencephalon of the brain. The role of this CD11a/CD18 binding molecule 
is not yet known [8].
 
VCAM-1 was first described as a cytokine-inducible endothelial adhesion
molecule. It can bind to leucocyte integrin VL-4 (very late antigen-4) to 
recruit leucocytes to sites of inflammation [2]. The predominant form of
VCAM-1 in vivo has an N-terminal extracellular region comprising seven
Ig-like domains [9]. A conserved integrin-binding motif has been identified 
in domains 1 and 4, variants of which are present in the N-terminal domain
of all members of the integrin-binding subgroup of the immunoglobulin 
superfamily [9]. The structure of a VLA-4-binding fragment comprising the
first two domains of VCAM-1 has been determined to 1.8A resolution [9]. The
integrin-binding motif is exposed and forms the N-terminal region of the
loop between beta-strands C and D of domain 1 [9]. VCAM-1 domains 1 and 2
are structurally similar to ICAM-1 and ICAM-2 [2]. 
 
ICAMVCAM1 is 4-element fingerprint that provides a signature for the ICAM/
VCAM-1 family of adhesion molecules. The fingerprint was derived from an
initial alignment of 8 sequences: the motifs were drawn from conserved 
regions towards the N-terminal portion of the alignment: motif 1 lies 
partially within the N-terminal region of domain 1; motif 2 lies between
domains 1 and 2; and motifs 3 and 4 lie in the N-terminal region of domain
2. Four iterations on SPTR39_14f were required to reach convergence, at
which point a true set comprising 22 sequences was identified.
Summary Information
22 codes involving  4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
422222222
30000
20000
1234
True Positives
ICA1_BOVIN    ICA1_HUMAN    ICA1_MOUSE    ICA1_RAT      
ICA2_HUMAN ICA2_MOUSE ICA3_BOVIN ICA3_HUMAN
O97692 Q14600 Q28260 Q28730
Q28939 Q29123 Q60625 Q63669
Q9UMF0 Q9Y6F3 Q9Z133 VCA1_HUMAN
VCA1_MOUSE VCA1_RAT
Sequence Titles
ICA1_BOVIN  INTERCELLULAR ADHESION MOLECULE-1 PRECURSOR (ICAM-1) - Bos taurus (Bovine). 
ICA1_HUMAN INTERCELLULAR ADHESION MOLECULE-1 PRECURSOR (ICAM-1) (MAJOR GROUP RHINOVIRUS RECEPTOR) (CD54) - Homo sapiens (Human).
ICA1_MOUSE INTERCELLULAR ADHESION MOLECULE-1 PRECURSOR (MALA-2) - Mus musculus (Mouse).
ICA1_RAT INTERCELLULAR ADHESION MOLECULE-1 PRECURSOR - Rattus norvegicus (Rat).
ICA2_HUMAN INTERCELLULAR ADHESION MOLECULE-2 PRECURSOR (ICAM-2) (CD102) - Homo sapiens (Human).
ICA2_MOUSE INTERCELLULAR ADHESION MOLECULE-2 PRECURSOR (ICAM-2) (CD102) (LYMPHOCYTE FUNCTION-ASSOCIATED AG-1 COUNTER-RECEPTOR) - Mus musculus (Mouse).
ICA3_BOVIN INTERCELLULAR ADHESION MOLECULE-3 PRECURSOR (ICAM-3) - Bos taurus (Bovine).
ICA3_HUMAN INTERCELLULAR ADHESION MOLECULE-3 PRECURSOR (ICAM-3) (CDW50) (CD50 ANTIGEN) (ICAM-R) - Homo sapiens (Human).
O97692 INTERCELLULAR ADHESION MOLECULE-1 PRECURSOR - Ovis aries (Sheep).
Q14600 INTERCELLULAR ADHESION MOLECULE 2 (ICAM-2) - Homo sapiens (Human).
Q28260 VASCULAR CELL ADHESION MOLECULE-1 - Canis familiaris (Dog).
Q28730 TELECEPHALIN PRECURSOR - Oryctolagus cuniculus (Rabbit).
Q28939 VASCULAR CELL ADHESION MOLECULE PRECURSOR - Sus scrofa (Pig).
Q29123 VASCULAR CELL ADHESION MOLECULE - Sus scrofa (Pig).
Q60625 TELENCEPHALIN PRECURSOR - Mus musculus (Mouse).
Q63669 VASCULAR CELL ADHESION MOLECULE 1 PRECURSOR - Rattus norvegicus (Rat).
Q9UMF0 TELENCEPHALIN PRECURSOR - Homo sapiens (Human).
Q9Y6F3 TELENCEPHALIN - Homo sapiens (Human).
Q9Z133 TESTICULAR CELL ADHESION MOLECULE 1 (TCAM1) - Rattus norvegicus (Rat).
VCA1_HUMAN VASCULAR CELL ADHESION PROTEIN 1 PRECURSOR (V-CAM 1) (CD106 ANTIGEN) (INCAM-100) - Homo sapiens (Human).
VCA1_MOUSE VASCULAR CELL ADHESION PROTEIN 1 PRECURSOR (V-CAM 1) - Mus musculus (Mouse).
VCA1_RAT VASCULAR CELL ADHESION PROTEIN 1 PRECURSOR (V-CAM 1) - Rattus norvegicus (Rat).
Scan History
SPTR39_14f 4  60   NSINGLE    
Initial Motifs
Motif 1  width=17
Element Seqn Id St Int Rpt
KAIIPRGDSLTVNCSNS ICA1_BOVIN 35 35 -
KVILPRGGSVLVTCSTS ICA1_HUMAN 35 35 -
NPVLSAGGSLFVNCSTD ICA3_HUMAN 40 40 -
KTIAQIGDSMALTCSTT VCA1_MOUSE 34 34 -
DPVVPFGEPLVVNCTLD ICA3_BOVIN 42 42 -
KLAVEPKGSLEVNCSTT ICA2_HUMAN 35 35 -
RYLAQIGDSVSLTCSTT VCA1_HUMAN 34 34 -
KQIVEATESWKINCSTN ICA2_MOUSE 33 33 -

Motif 2 width=14
Element Seqn Id St Int Rpt
YWFPEHVELAPLPL ICA1_BOVIN 109 57 -
YWTPERVELAPLPS ICA1_HUMAN 110 58 -
YGLPERVELAPLPP ICA3_HUMAN 114 57 -
YSFPKDPEIQFSGP VCA1_MOUSE 113 62 -
FGFPKRVELAPLPL ICA3_BOVIN 116 57 -
YQPPRQVILTLQPT ICA2_HUMAN 109 57 -
YSFPKDPEIHLSGP VCA1_HUMAN 113 62 -
YQPPAQVTLKLQPP ICA2_MOUSE 109 59 -

Motif 3 width=16
Element Seqn Id St Int Rpt
VGEELNLSCLVSGGAP ICA1_BOVIN 126 3 -
VGKNLTLRCQVEGGAP ICA1_HUMAN 127 3 -
VGQNFTLRCQVEGGSP ICA3_HUMAN 131 3 -
VGKPVTVKCLAPDIYP VCA1_MOUSE 129 2 -
VGEELNLSCLVSGGAP ICA3_BOVIN 133 3 -
VGKSFTIECRVPTVEP ICA2_HUMAN 126 3 -
AGKPITVKCSVADVYP VCA1_HUMAN 129 2 -
VGEDFTIECTVSPVQP ICA2_MOUSE 126 3 -

Motif 4 width=19
Element Seqn Id St Int Rpt
PRAHLSVVLLRGEEELGRQ ICA1_BOVIN 141 -1 -
PRANLTVVLLRGEKELKRE ICA1_HUMAN 142 -1 -
PRTSLTVVLLRWEEELSRQ ICA3_HUMAN 146 -1 -
PFDHLEIELLKGETTLMKK VCA1_MOUSE 432 287 -
PRAHLSVVLLRGEEELGRQ ICA3_BOVIN 148 -1 -
PLDSLTLFLFRGNETLHYE ICA2_HUMAN 141 -1 -
PFDRLEIDLLKGDHLMKSQ VCA1_HUMAN 144 -1 -
PLERLTLSLLRGRETLKNQ ICA2_MOUSE 141 -1 -
Final Motifs
Motif 1  width=17
Element Seqn Id St Int Rpt
VAFVERGGSLWLNCSTN Q9UMF0 42 42 -
VAFVERGGSLWLNCSTN Q9Y6F3 42 42 -
VALVERGGSLWLNCSTN Q28730 41 41 -
VALVEPGGSLWLNCSTN Q60625 42 42 -
KAIIPRGDSLTVNCSNS ICA1_BOVIN 35 35 -
KAIIPRGGSLRVNCSIS O97692 35 35 -
KVILPRGGSVLVTCSTS ICA1_HUMAN 35 35 -
EAFLPRGGSVQVNCSSS ICA1_RAT 35 35 -
NPVLSAGGSLFVNCSTD ICA3_HUMAN 40 40 -
EAFLPQGGSVQVNCSSS ICA1_MOUSE 35 35 -
KTLAQIGDSMLLTCSTT Q63669 34 34 -
KTIAQIGDSMALTCSTT VCA1_MOUSE 34 34 -
KTLAQIGDSMLLTCSTT VCA1_RAT 34 34 -
DPVVPFGEPLVVNCTLD ICA3_BOVIN 42 42 -
KLAVEPKGSLEVNCSTT ICA2_HUMAN 35 35 -
KLAVEPKGSLEVNCSTT Q14600 35 35 -
RVAAQIGDVISLTCSTT Q28260 34 34 -
KMIAQIGDSASLTCSAP Q28939 34 34 -
KMIAQIGDSASLTCSAP Q29123 34 34 -
RYLAQIGDSVSLTCSTT VCA1_HUMAN 34 34 -
QALVEFGHSLTINCSTT Q9Z133 33 33 -
KQIVEATESWKINCSTN ICA2_MOUSE 33 33 -

Motif 2 width=14
Element Seqn Id St Int Rpt
FQRPDRVELMPLPP Q9UMF0 117 58 -
FQRPDRVELMPLPP Q9Y6F3 117 58 -
FQRPDRVELVPLPP Q28730 114 56 -
FQRPDRVELVPLPS Q60625 117 58 -
YWFPEHVELAPLPL ICA1_BOVIN 109 57 -
YWFPERVELAPLPL O97692 109 57 -
YWTPERVELAPLPS ICA1_HUMAN 110 58 -
YSFPERVELDPLPA ICA1_RAT 110 58 -
YGLPERVELAPLPP ICA3_HUMAN 114 57 -
YSFPESVELRPLPA ICA1_MOUSE 109 57 -
YSFPKDPEIHLSGP Q63669 113 62 -
YSFPKDPEIQFSGP VCA1_MOUSE 113 62 -
YSFPKDPEIQFSGP VCA1_RAT 113 62 -
FGFPKRVELAPLPL ICA3_BOVIN 116 57 -
YQPPRQVILTLQPT ICA2_HUMAN 109 57 -
YQPPRQVILTLQPT Q14600 109 57 -
YSFPKDPEIQLSGP Q28260 113 62 -
YSFPKDPEIHWSSL Q28939 114 63 -
YSFPKDPEIHWSSL Q29123 114 63 -
YSFPKDPEIHLSGP VCA1_HUMAN 113 62 -
YQPPEQVILDLQPE Q9Z133 107 57 -
YQPPAQVTLKLQPP ICA2_MOUSE 109 59 -

Motif 3 width=16
Element Seqn Id St Int Rpt
VGENFTLSCRVPGAGP Q9UMF0 134 3 -
VGENFTLSCRVPGAGP Q9Y6F3 134 3 -
VGENFTLSCRVPGAGP Q28730 131 3 -
VGENFTLSCRVPGAGP Q60625 134 3 -
VGEELNLSCLVSGGAP ICA1_BOVIN 126 3 -
VGEELNLSCQVSGGGP O97692 126 3 -
VGKNLTLRCQVEGGAP ICA1_HUMAN 127 3 -
VGKNLILRCLVEGGAP ICA1_RAT 127 3 -
VGQNFTLRCQVEGGSP ICA3_HUMAN 131 3 -
VGKDLTLRCHVDGGAP ICA1_MOUSE 126 3 -
VGKPVMVKCLAPDVYP Q63669 129 2 -
VGKPVTVKCLAPDIYP VCA1_MOUSE 129 2 -
VGKPVMVKCLAPDVYP VCA1_RAT 129 2 -
VGEELNLSCLVSGGAP ICA3_BOVIN 133 3 -
VGKSFTIECRVPTVEP ICA2_HUMAN 126 3 -
VGKSFTIECRVPTVEP Q14600 126 3 -
VGKPVTVTCLVRDVYP Q28260 129 2 -
VGKPVTVRCLVPDVYP Q28939 130 2 -
VGKPVTVRCLVPDVYP Q29123 130 2 -
AGKPITVKCSVADVYP VCA1_HUMAN 129 2 -
IDEAFTVKCHVPSVAP Q9Z133 124 3 -
VGEDFTIECTVSPVQP ICA2_MOUSE 126 3 -

Motif 4 width=19
Element Seqn Id St Int Rpt
PRASLTLTLLRGAQELIRR Q9UMF0 149 -1 -
PRASLTLTLLRGAQELIRR Q9Y6F3 149 -1 -
PRGSLTLTLLRGAQELIRR Q28730 146 -1 -
PRASLTLTLLRGGQELIRR Q60625 149 -1 -
PRAHLSVVLLRGEEELGRQ ICA1_BOVIN 141 -1 -
PRHHLSMVLLRGEEELDRQ O97692 141 -1 -
PRANLTVVLLRGEKELKRE ICA1_HUMAN 142 -1 -
PRTQLSVVLLRGNETLSRQ ICA1_RAT 142 -1 -
PRTSLTVVLLRWEEELSRQ ICA3_HUMAN 146 -1 -
PRTQLSAVLLRGEEILSRQ ICA1_MOUSE 141 -1 -
PFDHLEIELLKGETTLLNK Q63669 432 287 -
PFDHLEIELLKGETTLMKK VCA1_MOUSE 432 287 -
PFDHLEIELLKGETTLLNK VCA1_RAT 432 287 -
PRAHLSVVLLRGEEELGRQ ICA3_BOVIN 148 -1 -
PLDSLTLFLFRGNETLHYE ICA2_HUMAN 141 -1 -
PLDSLTLFLFRGNETLHYE Q14600 141 -1 -
PFDRLEMNLLNGNDLLQSK Q28260 144 -1 -
PVEKLEIELLKDNHSMVSQ Q28939 145 -1 -
PVEKLEIELLKDNHSMVSQ Q29123 145 -1 -
PFDRLEIDLLKGDHLMKSQ VCA1_HUMAN 144 -1 -
PLQSLTLTLLQGDQELHRK Q9Z133 139 -1 -
PLERLTLSLLRGRETLKNQ ICA2_MOUSE 141 -1 -