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EGF-like module-containing mucin-like hormone receptor-like 2; EGF-like module EMR2; CD312 antigen (CD312, EMR2)
Function:
- receptor probably involved in cell attachment
- forms a heterodimer, consisting of a large extracellular region non-covalently linked to a seven-transmembrane moiety
- interacts with chondroitin sulfate
- proteolytically cleaved into 2 subunits, an extracellular alpha subunit & a seven-transmembrane subunit
Structure:
- GPS domain is necessary, but not sufficient for receptor cleavage, which requires the entire extracellular stalk
- binding to chondroitin sulfate is mediated by the fourth 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
Alternative splicing: named isoforms=1
- a number of isoforms consisting of various number of EGF-like domains seems to exist
- a soluble form due to a frameshift which introduced a stop codon immediately before the first transmembrane domain is also detected
Expression:
- expression is restricted to myeloid cells
- highest expression found in peripheral blood leukocytes, followed by spleen & lymph nodes
- intermediate to low levels in thymus, bone marrow, fetal liver, placenta, & lung,
- no expression in heart, brain, skeletal muscle, kidney, or pancreas
- expression detected in monocyte/macrophage & Jurkat cell lines but not in other cell lines tested
General
cluster-of-differentiation antigen; cluster designation antigen; CD antigen
glycoprotein
G-protein coupled receptor; serpentine receptor
Properties
SIZE: MW = 91 kD
entity length = 823 aa
COMPARTMENT: cellular membrane
MOTIF: signal sequence {1-23}
exoplasmic domain {24-540}
MOTIF: EGF domain {25-66}
cysteine residue {C29}
MODIFICATION: cysteine residue {C39}
cysteine residue {C33}
MODIFICATION: cysteine residue {C45}
cysteine residue {C39}
MODIFICATION: cysteine residue {C29}
N-glycosylation site {N41}
cysteine residue {C45}
MODIFICATION: cysteine residue {C33}
cysteine residue {C47}
MODIFICATION: cysteine residue {C65}
cysteine residue {C65}
MODIFICATION: cysteine residue {C47}
EGF domain {67-118}
cysteine residue {C71}
MODIFICATION: cysteine residue {C85}
cysteine residue {C79}
MODIFICATION: cysteine residue {C94}
cysteine residue {C85}
MODIFICATION: cysteine residue {C71}
cysteine residue {C94}
MODIFICATION: cysteine residue {C79}
cysteine residue {C96}
MODIFICATION: cysteine residue {C117}
N-glycosylation site {N111}
cysteine residue {C117}
MODIFICATION: cysteine residue {C96}
EGF domain {119-162}
cysteine residue {C123}
MODIFICATION: cysteine residue {C136}
cysteine residue {C130}
MODIFICATION: cysteine residue {C145}
cysteine residue {C136}
MODIFICATION: cysteine residue {C123}
cysteine residue {C145}
MODIFICATION: cysteine residue {C130}
cysteine residue {C147}
MODIFICATION: cysteine residue {C161}
cysteine residue {C161}
MODIFICATION: cysteine residue {C147}
EGF domain {163-211}
cysteine residue {C167}
MODIFICATION: cysteine residue {C180}
cysteine residue {C174}
MODIFICATION: cysteine residue {C189}
cysteine residue {C180}
MODIFICATION: cysteine residue {C167}
cysteine residue {C189}
MODIFICATION: cysteine residue {C174}
cysteine residue {C191}
MODIFICATION: cysteine residue {C210}
N-glycosylation site {N206}
cysteine residue {C210}
MODIFICATION: cysteine residue {C191}
EGF domain {212-260}
cysteine residue {C216}
MODIFICATION: cysteine residue {C229}
cysteine residue {C223}
MODIFICATION: cysteine residue {C238}
cysteine residue {C229}
MODIFICATION: cysteine residue {C216}
cysteine residue {C238}
MODIFICATION: cysteine residue {C223}
cysteine residue {C240}
MODIFICATION: cysteine residue {C259}
cysteine residue {C259}
MODIFICATION: cysteine residue {C240}
N-glycosylation site {N298}
N-glycosylation site {N347}
N-glycosylation site {N354}
N-glycosylation site {N456}
N-glycosylation site {N460}
GPS {479-529}
proteolytic site {517-518}
transmembrane domain {541-561}
cytoplasmic loop {562-569}
transmembrane domain {570-590}
exoplasmic loop {591-605}
transmembrane domain {606-626}
cytoplasmic loop {627-644}
transmembrane domain {645-665}
exoplasmic loop {666-683}
transmembrane domain {684-704}
cytoplasmic loop {705-735}
transmembrane domain {736-756}
exoplasmic loop {757-760}
transmembrane domain {761-781}
cytoplasmic domain {782-823}
Database Correlations
OMIM 606100
UniProt Q9UHX3
PFAM correlations
Kegg hsa:3081
References
UniProt :accession Q9UHX3