Ceacam1
entrez
81613
canonical
uniprot
P16573
canonical
ensembl
ENSRNOG00000020578
resolver
ensembl
ENSRNOG00060031079
resolver
ensembl
ENSRNOG00065032913
resolver
ensp
ENSRNOP00000027933
resolver
ensp
ENSRNOP00000031260
resolver
ensp
ENSRNOP00000046654
resolver
ensp
ENSRNOP00000074820
resolver
enst
ENSRNOT00000027933
resolver
enst
ENSRNOT00000029487
resolver
genesymbol
Ceacam1
resolver
genesymbol_syn
ceacam1
resolver
uniprot
F7EUP5
resolver
uniprot
F7EVH5
resolver
uniprot
Q63093
resolver
uniprot
Q9JHL6
resolver
uniprot
Q9JHL7
resolver
uniprot_entry
CEAM1_RAT
resolver
uniprot_entry
F7EUP5_RAT
resolver
uniprot_entry
F7EVH5_RAT
resolver
uniprot_entry
Q9JHL6_RAT
resolver
uniprot_entry
Q9JHL7_RAT
resolver
uniprot_sec
Q63093
resolver
amino_acid_sequence
MELASARLLRGQIPWRGLLLTASLLTYWSPLTTAQVTVDAVPPNVVEEKSVLLLAHNLPQEFQVFYWYKGTTLNPDSEIARYIRSDNMSKTGPAYSGRETIYSNGSLFFQNVNKTDERAYTLSVFDQQFNPIQTSVQFRVYPALQKPNVTGNNSNPMEGEPFVSLMCEPYTNNTSYLWSRNGESLSEGDRVTFSEGNRTLTLLNVRRTDKGYYECEARNPATFNRSDPFNLDVIYGPDAPVISPPDIYLHQGSNLNLSCHADSNPPAQYFWLINEKLQTSSQELFISNITTNNSGTYACFVNNTVTGLSRTTVKNITVFEPVTQPSIQITNTTVKELGSVTLTCFSKDTGVSVRWLFNSQSLQLTDRMTLSQDNSTLRIDPIKREDAGDYQCEISNPVSFRISHPIKLDVIPDPTQGNSGLSEGAIAGIVIGSVAGVALIAALAYFLYSRKTGGGSDHRDLTEHKPSTSSHNLGPSDDSPNKVDDVSYSVLNFNAQQSKRPTSASSSPTETVYSVVKKK
uniprot
proteins
function
FUNCTION: [Isoform 1]: Cell adhesion protein that mediates homophilic cell adhesion in a calcium-independent manner (PubMed:2373740, PubMed:8454589). Plays a role as coinhibitory receptor in immune response, insulin action and also functions as an activator during angiogenesis (PubMed:11850617). Its coinhibitory receptor function is phosphorylation- and PTPN6 -dependent, which in turn, suppress signal transduction of associated receptors by dephosphorylation of their downstream effectors (By similarity). Plays a role in immune response, of T-cells, natural killer (NK) and neutrophils (By similarity). 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 (By similarity). 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 (By similarity). 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 (By similarity). 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 (By similarity). 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 (By similarity). Also regulates insulin action by promoting INS clearance and regulating lipogenesis in liver through regulating insulin signaling (PubMed:11850617). Upon INS stimulation, undergoes phosphorylation by INSR leading to INS clearance by increasing receptor-mediated insulin endocytosis (PubMed:7592607, PubMed:9712832). 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 (PubMed:16054098, PubMed:7592607). 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 (PubMed:11694516). 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 (By similarity). Also regulates vascular permeability through the VEGFR2 signaling pathway resulting in control of nitric oxide production (By similarity). 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 (By similarity). 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 (PubMed:7518458). Negatively regulates osteoclastogenesis (By similarity). {ECO:0000250|UniProtKB:P13688, ECO:0000250|UniProtKB:P31809, ECO:0000269|PubMed:11694516, ECO:0000269|PubMed:11850617, ECO:0000269|PubMed:15467833, ECO:0000269|PubMed:16054098, ECO:0000269|PubMed:2373740, ECO:0000269|PubMed:7518458, ECO:0000269|PubMed:7592607, ECO:0000269|PubMed:8454589, ECO:0000269|PubMed:9712832}.; FUNCTION: [Isoform 2]: Cell adhesion proteins that mediates homophilic cell adhesion in a calcium-independent manner (PubMed:7774714, PubMed:8536699). Promotes populations of T-cells regulating IgA production and secretion associated with control of the commensal microbiota and resistance to enteropathogens (By similarity). {ECO:0000250|UniProtKB:P31809, ECO:0000269|PubMed:7774714, ECO:0000269|PubMed:8536699}.
uniprot
proteins
mass_dalton
57410
uniprot
proteins
mutagenesis
MUTAGEN 488; /note="Y->F: Phosphorylated on serine. Decreases bile acid transport Doesn't phosphorylated by EGFR. Doesn't increase interaction with SHC1. Completely inhibits insulin-stimulated phosphorylation. No effect on INSR internalization and INS degradation. Prevents CEACAM1 phosphorylation and the increase in its binding to FASN in the presence of INSR. No effect on cell-surface expression in response to INS. Abolishes phosphorylation by INSR. Abolishes indirect interaction with INSR."; /evidence="ECO:0000269|PubMed:15467833, ECO:0000269|PubMed:16054098, ECO:0000269|PubMed:7518458, ECO:0000269|PubMed:7592607, ECO:0000269|PubMed:7626603, ECO:0000269|PubMed:9712832"; MUTAGEN 502..503; /note="TS->AA: Phosphorylated on tyrosine. Impairs bile acid transport."; /evidence="ECO:0000269|PubMed:7518458"; MUTAGEN 503; /note="S->A: Abolishes phosphorylation by EGFR. Reduces interaction with SHC1. Completely inhibits insulin-stimulated phosphorylation. No effect on INSR internalization and INS degradation. In L-SACC1; completely inhibits insulin-stimulated phosphorylation; develops hyperinsulinemia resulting from impaired insulin clearance; the hyperinsulinemia causes secondary insulin resistance with impaired glucose tolerance and random, but not fasting, hyperglycemia; insulin doesn't significantly decrease FASN activity in liver. Prevents CEACAM1 phosphorylation and the increase in its binding to FASN in the presence of INSR. No effect on cell-surface expression in response to INS."; /evidence="ECO:0000269|PubMed:11694516, ECO:0000269|PubMed:11850617, ECO:0000269|PubMed:15467833, ECO:0000269|PubMed:16054098, ECO:0000269|PubMed:7592607, ECO:0000269|PubMed:7626603, ECO:0000269|PubMed:9712832"; MUTAGEN 503; /note="S->D: Preserves the ability of INSR to induce CEACAM1 phosphorylation."; /evidence="ECO:0000269|PubMed:16054098"; MUTAGEN 513; /note="Y->F: Increases INSR internalization and INS degradation. Phosphorylated by INSR. Prevents the increase in CEACAM1 binding to FASN by INSR. Decreases cell-surface expression in response to INS. Doesn't affect phosphorylation by INSR."; /evidence="ECO:0000269|PubMed:16054098, ECO:0000269|PubMed:7592607, ECO:0000269|PubMed:9712832
uniprot
proteins
post_translational_modification
PTM: [Isoform 1]: Phosphorylated on serine and tyrosine (PubMed:8420979). 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:15467833, PubMed:16054098, PubMed:7626603, PubMed:9712832). Phosphorylated at Ser-503; mediates activity. Phosphorylated at Tyr-488; regulates activity (PubMed:7518458). Phosphorylated at Tyr-488 by EGFR and INSR upon stimulation; this phosphorylation is Ser-503-phosphorylation-dependent; mediates cellular internalization; increases interaction with FASN (PubMed:15467833, PubMed:16054098, PubMed:7626603, PubMed:9712832). Phosphorylated at Tyr-488 and Tyr-513 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-513; mediates interaction with PTPN11 (By similarity). {ECO:0000250|UniProtKB:P13688, ECO:0000250|UniProtKB:P31809, ECO:0000269|PubMed:15467833, ECO:0000269|PubMed:16054098, ECO:0000269|PubMed:7518458, ECO:0000269|PubMed:7626603, ECO:0000269|PubMed:8420979, ECO:0000269|PubMed:9712832}.; PTM: [Isoform 2]: Phosphorylated on serine and threonine. {ECO:0000269|PubMed:8420979}.
uniprot
proteins
protein_family
CEA family
uniprot
proteins
protein_family
Immunoglobulin superfamily
uniprot
proteins
pubmed
11501563
uniprot
proteins
pubmed
11694516
uniprot
proteins
pubmed
11850617
uniprot
proteins
pubmed
11994468
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
15467833
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16054098
uniprot
proteins
pubmed
16291724
uniprot
proteins
pubmed
1637321
uniprot
proteins
pubmed
1831973
uniprot
proteins
pubmed
19948503
uniprot
proteins
pubmed
2141577
uniprot
proteins
pubmed
2373740
uniprot
proteins
pubmed
2527235
uniprot
proteins
pubmed
7518458
uniprot
proteins
pubmed
7592607
uniprot
proteins
pubmed
7626603
uniprot
proteins
pubmed
7774714
uniprot
proteins
pubmed
8240240
uniprot
proteins
pubmed
8380406
uniprot
proteins
pubmed
8420979
uniprot
proteins
pubmed
8454589
uniprot
proteins
pubmed
8504806
uniprot
proteins
pubmed
8513803
uniprot
proteins
pubmed
8536699
uniprot
proteins
pubmed
8576129
uniprot
proteins
pubmed
8831574
uniprot
proteins
pubmed
9003371
uniprot
proteins
pubmed
9712832
uniprot
proteins
sequence_length
519
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:16054098, ECO:0000269|PubMed:7518458, ECO:0000269|PubMed:7774714, ECO:0000269|PubMed:8536699, ECO:0000269|PubMed:9003371, ECO:0000269|PubMed:9712832}; Single-pass type I membrane protein. Lateral cell membrane {ECO:0000269|PubMed:7774714}. Apical cell membrane {ECO:0000269|PubMed:7774714}. Basal cell membrane {ECO:0000269|PubMed:7774714}. Cell junction {ECO:0000269|PubMed:19948503, ECO:0000269|PubMed:9003371}. Cell junction, adherens junction {ECO:0000269|PubMed:19948503}. Note=Canalicular domain of hepatocyte plasma membranes (PubMed:8513803). 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 (PubMed:19948503). Found as dimer in the solution (PubMed:9003371). Predominantly localized to the lateral cell membranes (PubMed:7774714). {ECO:0000269|PubMed:19948503, ECO:0000269|PubMed:7774714, ECO:0000269|PubMed:8513803, ECO:0000269|PubMed:9003371}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:7774714, ECO:0000269|PubMed:9003371}; Single-pass type I membrane protein. Lateral cell membrane {ECO:0000269|PubMed:7774714}. Apical cell membrane {ECO:0000269|PubMed:7774714}. Basal cell membrane {ECO:0000269|PubMed:7774714}. Cell junction {ECO:0000269|PubMed:19948503}. Cell junction, adherens junction {ECO:0000269|PubMed:19948503}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:P13688}. Note=Predominantly localized to the lateral cell membranes (PubMed:7774714). 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 (PubMed:19948503). Co-localizes with ANXA2 in secretory vesicles and with S100A10/p11 at the plasma membrane (By similarity). {ECO:0000250|UniProtKB:P13688, ECO:0000269|PubMed:19948503, ECO:0000269|PubMed:7774714}.; SUBCELLULAR LOCATION: Cell projection, microvillus membrane {ECO:0000250|UniProtKB:P31809}; Single-pass type I membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000250|UniProtKB:P31809}; 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 (By similarity). {ECO:0000250|UniProtKB:P13688, ECO:0000250|UniProtKB:P31809}.
uniprot
proteins
transmembrane_region
TRANSMEM 426..446; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins