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CD97 antigen; Leukocyte antigen CD97; CD97; contains CD97 antigen subunit alpha & CD97 antigen subunit beta (CD97)
Function:
- receptor potentially involved in both adhesion & signaling processes early after leukocyte activation
- role in leukocyte migration (putative)
- interacts with complement decay-accelerating factor (DAF)
- the largest isoform (isoform 1) interacts with chondroitin sulfate
- proteolytically cleaved into 2 subunits, an extracellular alpha subunit & a seven-transmembrane subunit (putative)
- binds to CD55
Structure:
- forms a heterodimer, consisting of a large extracellular region (alpha subunit) non-covalently linked to a seven- transmembrane moiety (beta subunit).
- the first 2 EGF domains mediate the interaction with DAF
- a 3rd tandemly arranged EGF domain is necessary for the structural integrity of the binding region
- binding to chondroitin sulfate is mediated by the 4th EGF domain
- belongs to the G-protein coupled receptor 2 family LN-TM7 subfamily
- contains 5 EGF-like domains
- contains 1 GPS domain
Compartment:
- cell membrane
- CD97 antigen subunit alpha: secreted
Alternative splicing: named isoforms=3
Expression:
- broadly expressed
- present on the surface of most activated leukocytes
- rapid up-regulation during lymphocyte activation
- found on most hematopoietic cells, including
a) activated lymphocytes, activated T > B cells
b) monocytes, macrophages,
c) dendritic cells
d) granulocytes
e) smooth muscle cells
- increased expression of CD97 in the synovium is accompanied by detectable levels of soluble CD97 in the synovial fluid
- microglia stain negatively with antibody
Pathology:
- CD97 is expressed in some carcinomas
a) thyroid carcinomas
b) GI adenocarcinomas
1] colorectal carcinoma
2] gastric cancer
3] esophageal cancer
4] pancreatic cancer
- expressed in sites of inflammation in skin, lung, brain, joints
- expression is increased under inflammatory conditions in the CNS of multiple sclerosis & in synovial tissue of patients with rheumatoid arthritis
General
cluster-of-differentiation antigen; cluster designation antigen; CD antigen
glycoprotein
G-protein coupled receptor; serpentine receptor
Properties
SIZE: entity length = 835 aa
MW = 92 kD
COMPARTMENT: plasma membrane
MOTIF: exoplasmic domain {21-552}
MOTIF: signal sequence {1-20}
EGF domain {22-63}
cysteine residue {C26}
MODIFICATION: cysteine residue {C36}
cysteine residue {C30}
MODIFICATION: cysteine residue {C42}
N-glycosylation site {N33}
cysteine residue {C36}
MODIFICATION: cysteine residue {C26}
N-glycosylation site {N38}
cysteine residue {C42}
MODIFICATION: cysteine residue {C30}
cysteine residue {C44}
MODIFICATION: cysteine residue {C62}
cysteine residue {C62}
MODIFICATION: cysteine residue {C44}
EGF domain {64-115}
cysteine residue {C68}
MODIFICATION: cysteine residue {C82}
cysteine residue {C76}
MODIFICATION: cysteine residue {C91}
cysteine residue {C82}
MODIFICATION: cysteine residue {C68}
cysteine residue {C91}
MODIFICATION: cysteine residue {C76}
cysteine residue {C93}
MODIFICATION: cysteine residue {C114}
N-glycosylation site {N108}
cysteine residue {C114}
MODIFICATION: cysteine residue {C93}
EGF domain {116-159}
cysteine residue {C120}
MODIFICATION: cysteine residue {C133}
cysteine residue {C127}
MODIFICATION: cysteine residue {C142}
cysteine residue {C133}
MODIFICATION: cysteine residue {C120}
cysteine residue {C142}
MODIFICATION: cysteine residue {C127}
cysteine residue {C144}
MODIFICATION: cysteine residue {C158}
cysteine residue {C158}
MODIFICATION: cysteine residue {C144}
EGF domain {160-208}
cysteine residue {C164}
MODIFICATION: cysteine residue {C177}
cysteine residue {C171}
MODIFICATION: cysteine residue {C186}
cysteine residue {C177}
MODIFICATION: cysteine residue {C164}
cysteine residue {C186}
MODIFICATION: cysteine residue {C171}
cysteine residue {C188}
MODIFICATION: cysteine residue {C207}
N-glycosylation site {N203}
cysteine residue {C207}
MODIFICATION: cysteine residue {C188}
EGF domain {209-257}
cysteine residue {C213}
MODIFICATION: cysteine residue {C226}
cysteine residue {C220}
MODIFICATION: cysteine residue {C235}
cysteine residue {C226}
MODIFICATION: cysteine residue {C213}
cysteine residue {C235}
MODIFICATION: cysteine residue {C220}
cysteine residue {C237}
MODIFICATION: cysteine residue {C256}
cysteine residue {C256}
MODIFICATION: cysteine residue {C237}
N-glycosylation site {N371}
N-glycosylation site {N406}
N-glycosylation site {N413}
N-glycosylation site {N453}
GPS {492-542}
N-glycosylation site {N520}
peptide motif {530-531}
transmembrane domain {553-572}
cytoplasmic loop {573-581}
transmembrane domain {582-601}
exoplasmic loop {602-620}
transmembrane domain {621-642}
cytoplasmic loop {643-653}
transmembrane domain {654-674}
exoplasmic loop {675-691}
transmembrane domain {692-712}
cytoplasmic loop {713-739}
transmembrane domain {740-760}
exoplasmic loop {761-766}
transmembrane domain {767-789}
cytoplasmic domain {790-835}
Database Correlations
OMIM 601211
UniProt P48960
PFAM correlations
Entrez Gene 976
Kegg hsa:976
References
- UniProt :accession P48960
- http://www.pathologyoutlines.com/cdmarkers.html
11 June 2005
- Protein Reviews on the Web
http://mpr.nci.nih.gov/prow/guide/1000600212_g.htm