Ceacam1
entrez
26365
canonical
uniprot
P31809
canonical
ensembl
ENSMUSG00000074272
resolver
ensp
ENSMUSP00000096263
resolver
ensp
ENSMUSP00000096265
resolver
ensp
ENSMUSP00000096266
resolver
ensp
ENSMUSP00000145590
resolver
ensp
ENSMUSP00000146066
resolver
enst
ENSMUST00000098668
resolver
enst
ENSMUST00000098669
resolver
enst
ENSMUST00000206676
resolver
genesymbol
Ceacam1
resolver
genesymbol_syn
Bgp
resolver
genesymbol_syn
Bgp1
resolver
genesymbol_syn
CEACAM1a-2L
resolver
genesymbol_syn
CEACAM1a-2S
resolver
genesymbol_syn
CEACAM1a-4C1
resolver
uniprot
A0A0U1RNJ5
resolver
uniprot
F6Q0C2
resolver
uniprot
Q3LFS5
resolver
uniprot
Q3LFS8
resolver
uniprot
Q3LFS9
resolver
uniprot
Q61350
resolver
uniprot
Q61353
resolver
uniprot
Q925P3
resolver
uniprot_entry
A0A0U1RNJ5_MOUSE
resolver
uniprot_entry
CEAM1_MOUSE
resolver
uniprot_entry
F6Q0C2_MOUSE
resolver
uniprot_entry
Q3LFS5_MOUSE
resolver
uniprot_entry
Q3LFS8_MOUSE
resolver
uniprot_entry
Q3LFS9_MOUSE
resolver
uniprot_entry
Q925P3_MOUSE
resolver
uniprot_sec
Q61350
resolver
uniprot_sec
Q61353
resolver
amino_acid_sequence
MELASAHLHKGQVPWGGLLLTASLLASWSPATTAEVTIEAVPPQVAEDNNVLLLVHNLPLALGAFAWYKGNTTAIDKEIARFVPNSNMNFTGQAYSGREIIYSNGSLLFQMITMKDMGVYTLDMTDENYRRTQATVRFHVHPILLKPNITSNNSNPVEGDDSVSLTCDSYTDPDNINYLWSRNGESLSEGDRLKLSEGNRTLTLLNVTRNDTGPYVCETRNPVSVNRSDPFSLNIIYGPDTPIISPSDIYLHPGSNLNLSCHAASNPPAQYFWLINEKPHASSQELFIPNITTNNSGTYTCFVNNSVTGLSRTTVKNITVLEPVTQPFLQVTNTTVKELDSVTLTCLSNDIGANIQWLFNSQSLQLTERMTLSQNNSILRIDPIKREDAGEYQCEISNPVSVRRSNSIKLDIIFDPTQGGLSDGAIAGIVIGVVAGVALIAGLAYFLYSRKSGGGSDQRDLTEHKPSTSNHNLAPSDNSPNKVDDVAYTVLNFNSQQPNRPTSAPSSPRATETVYSEVKKK
uniprot
proteins
function
FUNCTION: [Isoform 1]: Cell adhesion protein that mediates homophilic cell adhesion in a calcium-independent manner (By similarity). Plays a role as coinhibitory receptor in immune response, insulin action and also functions as an activator during angiogenesis (PubMed:16680193, PubMed:17081782, PubMed:18544705, PubMed:21029969, PubMed:21081647, PubMed:22496641, PubMed:22962327, PubMed:23696226). Its coinhibitory receptor function is phosphorylation- and PTPN6 -dependent, which in turn, suppress signal transduction of associated receptors by dephosphorylation of their downstream effectors (PubMed:17081782, PubMed:21029969, PubMed:22496641). Plays a role in immune response, of T-cells, natural killer (NK) and neutrophils (PubMed:17081782, PubMed:21029969, PubMed:22496641, PubMed:23696226). Upon TCR/CD3 complex stimulation, inhibits TCR-mediated cytotoxicity by blocking granule exocytosis by mediating homophilic binding to adjacent cells, allowing interaction with and phosphorylation by LCK and interaction with the TCR/CD3 complex which recruits PTPN6 resulting in dephosphorylation of CD247 and ZAP70 (PubMed:22496641). Also inhibits T-cell proliferation and cytokine production through inhibition of JNK cascade and plays a crucial role in regulating autoimmunity and anti-tumor immunity by inhibiting T-cell through its interaction with HAVCR2 (PubMed:17081782). Upon natural killer (NK) cells activation, inhibit KLRK1-mediated cytolysis of CEACAM1-bearing tumor cells by trans-homophilic interactions with CEACAM1 on the target cell and lead to cis-interaction between CEACAM1 and KLRK1, allowing PTPN6 recruitment and then VAV1 dephosphorylation (PubMed:23696226). Upon neutrophils activation negatively regulates IL1B production by recruiting PTPN6 to a SYK-TLR4-CEACAM1 complex, that dephosphorylates SYK, reducing the production of reactive oxygen species (ROS) and lysosome disruption, which in turn, reduces the activity of the inflammasome (PubMed:22496641). Down-regulates neutrophil production by acting as a coinhibitory receptor for CSF3R by down-regulating the CSF3R-STAT3 pathway through recruitment of PTPN6 that dephosphorylates CSF3R (PubMed:21029969). Also regulates insulin action by promoting INS clearance and regulating lipogenesis in liver through regulating insulin signaling (PubMed:18544705). Upon INS stimulation, undergoes phosphorylation by INSR leading to INS clearance by increasing receptor-mediated insulin endocytosis. This inernalization promotes interaction with FASN leading to receptor-mediated insulin degradation and to reduction of FASN activity leading to negative regulation of fatty acid synthesis. INSR-mediated phosphorylation also provokes a down-regulation of cell proliferation through SHC1 interaction resulting in decrease coupling of SHC1 to the MAPK3/ERK1-MAPK1/ERK2 and phosphatidylinositol 3-kinase pathways (By similarity). Functions as activator in angiogenesis by promoting blood vessel remodeling through endothelial cell differentiation and migration and in arteriogenesis by increasing the number of collateral arteries and collateral vessel calibers after ischemia (PubMed:16680193, PubMed:22962327). Also regulates vascular permeability through the VEGFR2 signaling pathway resulting in control of nitric oxide production (PubMed:21081647). Down-regulates cell growth in response to EGF through its interaction with SHC1 that mediates interaction with EGFR resulting in decrease coupling of SHC1 to the MAPK3/ERK1-MAPK1/ERK2 pathway (PubMed:15467833). Negatively regulates platelet aggregation by decreasing platelet adhesion on type I collagen through the GPVI-FcRgamma complex (PubMed:19008452). Inhibits cell migration and cell scattering through interaction with FLNA; interferes with the interaction of FLNA with RALA (By similarity). Mediates bile acid transport activity in a phosphorylation dependent manner (By similarity). Negatively regulates osteoclastogenesis (PubMed:25490771). {ECO:0000250|UniProtKB:P13688, ECO:0000250|UniProtKB:P16573, ECO:0000269|PubMed:15467833, ECO:0000269|PubMed:16680193, ECO:0000269|PubMed:17081782, ECO:0000269|PubMed:18544705, ECO:0000269|PubMed:19008452, ECO:0000269|PubMed:21029969, ECO:0000269|PubMed:21081647, ECO:0000269|PubMed:22496641, ECO:0000269|PubMed:22962327, ECO:0000269|PubMed:23696226, ECO:0000269|PubMed:25490771}.; FUNCTION: [Isoform 2]: Cell adhesion protein that mediates homophilic cell adhesion in a calcium-independent manner (PubMed:1633107). Promotes populations of T-cells regulating IgA production and secretion associated with control of the commensal microbiota and resistance to enteropathogens (PubMed:23123061). {ECO:0000269|PubMed:1633107, ECO:0000269|PubMed:23123061}.; FUNCTION: (Microbial infection) In case of murine coronavirus (MHV) infection, serves as receptor for MHV S1 spike glycoprotein. {ECO:0000269|PubMed:15331748, ECO:0000269|PubMed:1719235}.
uniprot
proteins
mass_dalton
57016
uniprot
proteins
mutagenesis
MUTAGEN 488; /note="Y->F: Phosphorylated on tyrosine. Abrogates interaction with PTPN11. Abrogates interaction with PTPN11 and phosphorylation; when associated with F-515. Reduces endothelial cell migration and differentiation. Suppresses T cell proliferation; when associated with F-515. Increases cytokine production; when associated with F-515. Activates JNK cascade; when associated with F-515. Abrogates CEACAM1-L phosphorylation in endothelial cells and decreases amounts of released nitric oxide upon VEGF stimulation. Impairs interaction with and inactivation of SYK; when associated with F-515."; /evidence="ECO:0000269|PubMed:16680193, ECO:0000269|PubMed:17081782, ECO:0000269|PubMed:21081647, ECO:0000269|PubMed:22496641, ECO:0000269|PubMed:9867848"; MUTAGEN 503; /note="S->A: Reduces endothelial cell migration and differentiation."; /evidence="ECO:0000269|PubMed:16680193"; MUTAGEN 515; /note="Y->F: Phosphorylated on tyrosine. Abrogates interaction with PTPN11. Abrogates interaction with PTPN11 and phosphorylation; when associated with F-488. Suppresses T cell proliferation; when associated with F-488. Increases cytokine production; when associated with F-488. Activates JNK cascade; when associated with F-488. Abrogates CEACAM1-L phosphorylation in endothelial cells upon VEGF stimulation. Impairs interaction with and inactivation of SYK; when associated with F-488."; /evidence="ECO:0000269|PubMed:17081782, ECO:0000269|PubMed:21081647, ECO:0000269|PubMed:22496641, ECO:0000269|PubMed:9867848"; MUTAGEN 518; /note="V->A: Impairs interaction with PTPN11 and PTPN6. Doesn't affect phosphorylation."; /evidence="ECO:0000269|PubMed:9867848"; MUTAGEN 519..521; /note="Missing: Reduces Tyr phosphorylation by at least 50% and almost completely abrogates interaction with PTPN11 and PTPN6."; /evidence="ECO:0000269|PubMed:9867848
uniprot
proteins
post_translational_modification
PTM: [Isoform 1]: Phosphorylated on serine and tyrosine (By similarity). Isoform 1 is phosphorylated on tyrosine by Src family kinases like SRC and LCK and by receptor like CSF3R, EGFR and INSR upon stimulation (PubMed:21029969, PubMed:9867848). Phosphorylated at Ser-503; mediates activity. Phosphorylated at Tyr-488; regulates activity (By similarity). Phosphorylated at Tyr-488 by EGFR and INSR upon stimulation; this phosphorylation is Ser-503-phosphorylation-dependent; mediates cellular internalization; increases interaction with FASN (By similarity). Phosphorylated at Tyr-488 and Tyr-515 by LCK; mediates PTPN6 association and is regulated by homophilic ligation of CEACAM1 in the absence of T-cell activation (By similarity). Phosphorylated at Tyr-515; mediates interaction with PTPN11 (PubMed:9867848). {ECO:0000250|UniProtKB:P13688, ECO:0000250|UniProtKB:P16573, ECO:0000269|PubMed:21029969, ECO:0000269|PubMed:9867848}.; PTM: [Isoform 2]: Phosphorylated on serine and threonine. {ECO:0000250|UniProtKB:P13688, ECO:0000250|UniProtKB:P16573}.
uniprot
proteins
protein_family
CEA family
uniprot
proteins
protein_family
Immunoglobulin superfamily
uniprot
proteins
pubmed
11501563
uniprot
proteins
pubmed
11980704
uniprot
proteins
pubmed
11994468
uniprot
proteins
pubmed
15331748
uniprot
proteins
pubmed
15467833
uniprot
proteins
pubmed
1633107
uniprot
proteins
pubmed
1648219
uniprot
proteins
pubmed
16680193
uniprot
proteins
pubmed
16944957
uniprot
proteins
pubmed
17081782
uniprot
proteins
pubmed
1719235
uniprot
proteins
pubmed
18544705
uniprot
proteins
pubmed
19008452
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
21029969
uniprot
proteins
pubmed
21081647
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22496641
uniprot
proteins
pubmed
22962327
uniprot
proteins
pubmed
23123061
uniprot
proteins
pubmed
23696226
uniprot
proteins
pubmed
25363763
uniprot
proteins
pubmed
25490771
uniprot
proteins
pubmed
25908210
uniprot
proteins
pubmed
8380065
uniprot
proteins
pubmed
8500759
uniprot
proteins
pubmed
9867848
uniprot
proteins
sequence_length
521
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:19008452, ECO:0000269|PubMed:8380065}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16573}. Lateral cell membrane {ECO:0000250|UniProtKB:P16573}. Apical cell membrane {ECO:0000250|UniProtKB:P16573}. Basal cell membrane {ECO:0000250|UniProtKB:P16573}. Cell junction {ECO:0000250|UniProtKB:P16573}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P16573}. Note=Canalicular domain of hepatocyte plasma membranes. Found as a mixture of monomer, dimer and oligomer in the plasma membrane. Occurs predominantly as cis-dimers and/or small cis-oligomers in the cell junction regions. Found as dimer in the solution. Predominantly localized to the lateral cell membranes. {ECO:0000250|UniProtKB:P16573}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:1633107, ECO:0000269|PubMed:8380065}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16573}. Lateral cell membrane {ECO:0000250|UniProtKB:P16573}. Apical cell membrane {ECO:0000250|UniProtKB:P16573}. Basal cell membrane {ECO:0000250|UniProtKB:P16573}. Cell junction {ECO:0000250|UniProtKB:P16573}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P16573}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:P13688}. Note=Predominantly localized to the lateral cell membranes. Found as a mixture of monomer, dimer and oligomer in the plasma membrane. Occurs predominantly as cis-dimers and/or small cis-oligomers in the cell junction regions (By similarity). Co-localizes with ANXA2 in secretory vesicles and with S100A10/p11 at the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P13688, ECO:0000250|UniProtKB:P16573}.; SUBCELLULAR LOCATION: Cell projection, microvillus membrane {ECO:0000269|PubMed:25908210}; Single-pass type I membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:25908210}; Single-pass type I membrane protein {ECO:0000305}. Note=Localized to the apical glycocalyx surface (By similarity). Colocalizes with CEACAM20 at the apical brush border of intestinal cells (PubMed:25908210). {ECO:0000250|UniProtKB:P13688, ECO:0000269|PubMed:25908210}.
uniprot
proteins
transmembrane_region
TRANSMEM 429..447; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins