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Protein

Carcinoembryonic antigen-related cell adhesion molecule 1

Gene

Ceacam1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 functions also 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:23696226, PubMed:22496641, PubMed:21029969). 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). Downregulates neutrophil production by acting as a coinhibitory receptor for CSF3R by downregulating 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). Downregulates 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; interfers 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).By similarity11 Publications
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).2 Publications
(Microbial infection) In case of murine coronavirus (MHV) infection, serves as receptor for MHV S1 spike glycoprotein.2 Publications

GO - Molecular functioni

  • actin binding Source: MGI
  • bile acid transmembrane transporter activity Source: UniProtKB
  • filamin binding Source: MGI
  • granulocyte colony-stimulating factor receptor binding Source: UniProtKB
  • kinase binding Source: MGI
  • protein dimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein phosphatase binding Source: MGI
  • protein tyrosine kinase binding Source: UniProtKB
  • Toll-like receptor binding Source: UniProtKB
  • virion binding Source: MGI
  • virus receptor activity Source: MGI

GO - Biological processi

  • bile acid and bile salt transport Source: UniProtKB
  • blood vessel development Source: UniProtKB
  • calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules Source: MGI
  • calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules Source: MGI
  • cell-cell junction organization Source: UniProtKB
  • cellular response to insulin stimulus Source: UniProtKB
  • common myeloid progenitor cell proliferation Source: UniProtKB
  • granulocyte colony-stimulating factor signaling pathway Source: UniProtKB
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: MGI
  • insulin catabolic process Source: UniProtKB
  • insulin receptor internalization Source: UniProtKB
  • negative regulation by host of viral genome replication Source: MGI
  • negative regulation by host of viral process Source: MGI
  • negative regulation of bone resorption Source: MGI
  • negative regulation of cytokine production Source: MGI
  • negative regulation of cytotoxic T cell degranulation Source: UniProtKB
  • negative regulation of fatty acid biosynthetic process Source: UniProtKB
  • negative regulation of granulocyte differentiation Source: UniProtKB
  • negative regulation of hepatocyte proliferation Source: UniProtKB
  • negative regulation of interleukin-1 production Source: UniProtKB
  • negative regulation of interleukin-2 production Source: MGI
  • negative regulation of JNK cascade Source: MGI
  • negative regulation of lipid biosynthetic process Source: UniProtKB
  • negative regulation of natural killer cell mediated cytotoxicity directed against tumor cell target Source: UniProtKB
  • negative regulation of osteoclast differentiation Source: MGI
  • negative regulation of platelet aggregation Source: UniProtKB
  • negative regulation of protein kinase activity Source: UniProtKB
  • negative regulation of T cell mediated cytotoxicity Source: UniProtKB
  • negative regulation of T cell proliferation Source: MGI
  • negative regulation of T cell receptor signaling pathway Source: UniProtKB
  • negative regulation of vascular permeability Source: UniProtKB
  • Peyer's patch development Source: MGI
  • positive regulation by host of viral process Source: MGI
  • positive regulation of activation-induced cell death of T cells Source: MGI
  • positive regulation of CD4-positive, alpha-beta T cell activation Source: MGI
  • positive regulation of CD4-positive, alpha-beta T cell proliferation Source: MGI
  • positive regulation of CD8-positive, alpha-beta T cell activation Source: MGI
  • positive regulation of immunoglobulin secretion Source: MGI
  • positive regulation of JNK cascade Source: MGI
  • positive regulation of MAP kinase activity Source: MGI
  • positive regulation of NFAT protein import into nucleus Source: MGI
  • positive regulation of T cell proliferation Source: MGI
  • positive regulation of vasculogenesis Source: UniProtKB
  • regulation of blood vessel remodeling Source: UniProtKB
  • regulation of cell growth Source: UniProtKB
  • regulation of endothelial cell differentiation Source: UniProtKB
  • regulation of endothelial cell migration Source: UniProtKB
  • regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
  • regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • regulation of homophilic cell adhesion Source: UniProtKB
  • regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  • regulation of sprouting angiogenesis Source: UniProtKB
  • viral entry into host cell Source: MGI
  • wound healing, spreading of cells Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Host cell receptor for virus entry, Receptor

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

ReactomeiR-MMU-1566977. Fibronectin matrix formation.
R-MMU-202733. Cell surface interactions at the vascular wall.
R-MMU-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Carcinoembryonic antigen-related cell adhesion molecule 1By similarity
Alternative name(s):
Biliary glycoprotein 1By similarity
Short name:
BGP-1
Biliary glycoprotein D
MHVR1
Murine hepatitis virus receptor
Short name:
MHV-R
CD_antigen: CD66a
Gene namesi
Name:Ceacam1Imported
Synonyms:Bgp1 Publication, Bgp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1347245. Ceacam1.

Subcellular locationi

Isoform 1 :
  • Cell membrane 2 Publications; Single-pass type I membrane protein By similarity
  • Lateral cell membrane By similarity
  • Apical cell membrane By similarity
  • Basal cell membrane By similarity
  • Cell junction By similarity
  • Cell junctionadherens junction By similarity

  • 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.By similarity
Isoform 2 :
  • Cell membrane 2 Publications; Single-pass type I membrane protein By similarity
  • Lateral cell membrane By similarity
  • Apical cell membrane By similarity
  • Basal cell membrane By similarity
  • Cell junction By similarity
  • Cell junctionadherens junction By similarity
  • Cytoplasmic vesiclesecretory vesicle By similarity

  • 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).By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini35 – 428ExtracellularSequence analysisAdd BLAST394
Transmembranei429 – 447HelicalSequence analysisAdd BLAST19
Topological domaini448 – 521CytoplasmicSequence analysisAdd BLAST74

GO - Cellular componenti

  • adherens junction Source: UniProtKB
  • apical plasma membrane Source: UniProtKB
  • basal plasma membrane Source: UniProtKB
  • brush border membrane Source: MGI
  • cell-cell junction Source: UniProtKB
  • cell junction Source: UniProtKB
  • cell surface Source: UniProtKB
  • ciliary membrane Source: MGI
  • external side of plasma membrane Source: MGI
  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
  • integral component of membrane Source: MGI
  • lateral plasma membrane Source: UniProtKB
  • membrane Source: MGI
  • plasma membrane Source: MGI
  • transport vesicle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Disruption phenotypei

Knockout mice exhibit impairment of insulin clearance and hyperinsulinemia, which cause insulin resistance; develop insulin resistance primarily in liver (PubMed:18544705). Display normal white blood cell, red blood cell, hemoglobin and platelet. On the other hand, mice have a high number of neutrophils. Display also increased thrombus growth, and enhanced susceptibility to type I collagen induced pulmonary thromboembolism (PubMed:19008452). Spontaneously develop systemic neutrophilia. Upon Listeria Monocytogenes (LM) infection mice die dramatically faster within 7 days and dispaly an improved bacterial clearance accompanied by severe tissue damage and necrosis in the liver (PubMed:21029969). Knockout mice present an increased basal permeability (PubMed:21081647). Knockout mice show a reduced bone mass namely a decreased trabecular bone volume accompanied by a reduction in trabecular number and an increase in trabecular separation (PubMed:25490771).5 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi488Y → 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. 5 Publications1
Mutagenesisi503S → A: Reduces endothelial cell migration and differentiation. 1 Publication1
Mutagenesisi515Y → 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. 4 Publications1
Mutagenesisi518V → A: Impairs interaction with PTPN11 and PTPN6. Doesn't affect phosphorylation. 1 Publication1
Mutagenesisi519 – 521Missing : Reduces Tyr phosphorylation by at least 50% and almost completely abrogates interaction with PTPN11 and PTPN6. 1 Publication3

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 341 PublicationAdd BLAST34
ChainiPRO_000001456335 – 521Carcinoembryonic antigen-related cell adhesion molecule 1Add BLAST487

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi71N-linked (GlcNAc...)2 Publications1
Glycosylationi89N-linked (GlcNAc...)2 Publications1
Glycosylationi104N-linked (GlcNAc...)1 Publication1
Glycosylationi148N-linked (GlcNAc...)Sequence analysis1
Glycosylationi152N-linked (GlcNAc...)By similarity1
Disulfide bondi167 ↔ 2171 Publication
Glycosylationi199N-linked (GlcNAc...)Sequence analysis1
Glycosylationi206N-linked (GlcNAc...)1 Publication1
Glycosylationi210N-linked (GlcNAc...)By similarity1
Glycosylationi226N-linked (GlcNAc...)By similarity1
Glycosylationi258N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi261 ↔ 3011 Publication
Glycosylationi290N-linked (GlcNAc...)Sequence analysis1
Glycosylationi294N-linked (GlcNAc...)Sequence analysis1
Glycosylationi304N-linked (GlcNAc...)Sequence analysis1
Glycosylationi317N-linked (GlcNAc...)1 Publication1
Glycosylationi333N-linked (GlcNAc...)2 Publications1
Disulfide bondi346 ↔ 394PROSITE-ProRule annotation1 Publication
Glycosylationi375N-linked (GlcNAc...)1 Publication1
Glycosylationi376N-linked (GlcNAc...); atypical1 Publication1
Modified residuei488Phosphotyrosine; by SRC; LCK; INSR and EGFRBy similarity2 Publications1
Modified residuei503PhosphoserineBy similarity1
Modified residuei515Phosphotyrosine; by INSR; SRC and LCKBy similarity2 Publications1

Post-translational modificationi

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:9867848, PubMed:21029969). 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).By similarity2 Publications
Isoform 2: Phosphorylated on serine and threonine.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP31809.
PaxDbiP31809.
PeptideAtlasiP31809.
PRIDEiP31809.

PTM databases

iPTMnetiP31809.
PhosphoSitePlusiP31809.

Expressioni

Tissue specificityi

Expressed in granulocytes, lymphocytes, granulocytes, B cells, and T-cells (PubMed:11994468). Expressed in bone. Highly expressed in liver and femur (PubMed:25490771). Highly expressed in neutrophils, and to a lesser extent inmonocytes, and macrophages. Slightly higher expressed in peripheral blood neutrophils (PBNs) (PubMed:21029969). Intestinal T-cells predominantly express isoform 2 while extraintestinal T-cells mainly express isoform 1 (PubMed:23123061). Expressed in small intestine and colon (PubMed:25908210).5 Publications

Developmental stagei

Expression increases during the early stages of osteoblast differentiation, and decreases towards terminal osteoblast differentiation. In addition, expression markedly decreases during the course of osteoclastogenesis.1 Publication

Inductioni

In intestinal epithelium, up-regulated in the presence of Gram-positive commensal gut bacteria (PubMed:25908210). May also be up-regulated by interferon gamma (IFNG) and TNF (TNF-alpha) (PubMed:25908210). Isoform 2: Expression is promoted and maintained by the mucosal environment (PubMed:23123061). Induced by IL2 on natural killer cell (PubMed:23696226).3 Publications

Gene expression databases

BgeeiENSMUSG00000074272.
CleanExiMM_CEACAM1.
ExpressionAtlasiP31809. baseline and differential.
GenevisibleiP31809. MM.

Interactioni

Subunit structurei

(Microbial infection) Interacts with MHV S1 spike glycoprotein.3 Publications
Monomer. Oligomer. Heterodimer. Homodimer. Cis-dimer/oligomer (via Ig-like C2-type and/or via cytoplasmic domains); induced by trans-homophilic cell adhesion through an allosteric mechanism transmitted by the Ig-like V-type domain, and is regulated by intracellular calcium and calmodulin. Interacts (via cytoplasmic domain) with calmodulin in a calcium dependent manner; reduces homophilic cell adhesion through dissociation of dimer (By similarity). Isoform 1 interacts (via cytoplasmic domain) with PTPN11 (preferentially) and PTPN6; cis-homodimer form is preferred; this interaction is decreased by formation of isoform 1 / isoform 2 cis-heterodimers and is dependent on the monomer/dimer equilibrium; this interaction is phosphorylation-dependent (PubMed:9867848). Isoform 1 interacts with LYN (PubMed:22496641). Isoform 1 interacts (via cytoplasmic domain) with SRC (via SH2 domain); this interaction is regulated by trans-homophilic cell adhesion (By similarity). Isoform 1 interacts with LCK; mediates phosphorylation at Tyr-488 and Tyr-515 resulting in PTPN6 association. Isoform 1 interacts with PTPN6; this interaction is phosphorylation-dependent and causes a profound decrease in TCR stimulation-induced CD247 and ZAP70 phosphorylation. Isoform 1 interacts with TCR/CD3 complex through TCR beta chain and CD3E; colocalizes at the cell surface and upon stimulation of the TCR/CD3 complex recuits PTPN6 in the TCR/CD3 complex, resulting in dephosphorylation of CD247 and ZAP70 (By similarity). Isoform 1 interacts (via cytoplasmic domain) with SHC1 (via SH2 domain); SHC1 mediates interaction with INSR or EGFR in a Ser-503 phosphorylation-dependent manner (PubMed:15467833). Isoform 1 interacts with EGFR; the interaction is indirect (By similarity). Isoform 1 interacts with CSF3R; down-regulates the CSF3R-STAT3 pathway through recruitment of PTPN6 that dephosphorylates CSF3R (PubMed:21029969). Isoform 1 (phosphorylated form) interacts with TLR4 and SYK; recruits PTPN6 that dephosphorylates SYK, reducing the production of reactive oxygen species (ROS) and lysosome disruption, leading to a reduction of the inflammasome activity (PubMed:22496641). Isoform 1 interacts with FLNA; inhibits cell migration and cell scattering by interfering with the interaction of FLNA with RALA. Isoform 1 interacts (via cytoplasmic domain) with PXN; the interaction is phosphotyrosyl-dependent. Isoform 1 interacts with KLRK1; recruits PTPN6 that dephosphorylates VAV1. Isoform 1 interacts with CEACAM8 (By similarity). Isoform 1 interacts with FASN; this interaction is insulin and phosphorylation-dependent; reduces fatty-acid synthase activity (By similarity). Interacts (via Ig-like V-type) with HAVCR2 (via Ig-like V-type); facilitates the maturation and cell surface expression of HAVCR2 thereby regulating T-cell tolerance induction (By similarity) (PubMed:25363763). Isoform 2 interacts (via the cytoplasmic domain) with ANXA2; this interaction is regulated by phosphorylation and appears in the AIIt complex. Interacts (via Lewis X moieties) with CD209 (via C-type lectin domain); this interaction is regulated by the glycosylation pattern of CEACAM1 on cell types and regulates contact between dendritic cells and neutrophils (By similarity).By similarity5 Publications

GO - Molecular functioni

  • actin binding Source: MGI
  • filamin binding Source: MGI
  • granulocyte colony-stimulating factor receptor binding Source: UniProtKB
  • kinase binding Source: MGI
  • protein dimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein phosphatase binding Source: MGI
  • protein tyrosine kinase binding Source: UniProtKB
  • Toll-like receptor binding Source: UniProtKB

Protein-protein interaction databases

DIPiDIP-61461N.
IntActiP31809. 1 interactor.
MINTiMINT-4590618.
STRINGi10090.ENSMUSP00000096266.

Structurei

Secondary structure

1521
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi37 – 46Combined sources10
Beta strandi51 – 56Combined sources6
Beta strandi63 – 71Combined sources9
Helixi75 – 77Combined sources3
Beta strandi78 – 83Combined sources6
Helixi84 – 86Combined sources3
Beta strandi88 – 91Combined sources4
Beta strandi97 – 101Combined sources5
Beta strandi107 – 109Combined sources3
Helixi114 – 116Combined sources3
Beta strandi118 – 125Combined sources8
Beta strandi130 – 141Combined sources12
Beta strandi328 – 332Combined sources5
Beta strandi334 – 336Combined sources3
Beta strandi342 – 347Combined sources6
Beta strandi354 – 359Combined sources6
Beta strandi368 – 373Combined sources6
Turni374 – 377Combined sources4
Beta strandi378 – 383Combined sources6
Helixi386 – 388Combined sources3
Beta strandi390 – 397Combined sources8
Beta strandi408 – 410Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1L6ZX-ray3.32A35-416[»]
3R4DX-ray3.10A/C35-416[»]
ProteinModelPortaliP31809.
SMRiP31809.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31809.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini35 – 142Ig-like V-typeAdd BLAST108
Domaini147 – 234Ig-like C2-type 1Add BLAST88
Domaini239 – 319Ig-like C2-type 2Add BLAST81
Domaini323 – 411Ig-like C2-type 3Add BLAST89

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni39 – 142Required for homophilic bindingBy similarityAdd BLAST104
Regioni445 – 457Interaction with calmodulinBy similarityAdd BLAST13
Regioni447 – 521Interaction with FLNABy similarityAdd BLAST75
Regioni484 – 521Required for interaction with PTPN11 and PTPN6 and for control of phosphorylation level1 PublicationAdd BLAST38
Regioni515 – 518Essential for interaction with PTPN11 and PTPN61 Publication4

Domaini

Ig-like V-type domain mediates trans-homophilic cell adhesion through homodimerization and this active process is regulated by tyrosine kinase, PTPN11 AND PTPN6. Ig-like C2-type and/or cytoplasmic domains mediate cis-dimer/oligomer.By similarity

Sequence similaritiesi

Belongs to the immunoglobulin superfamily. CEA family.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IFE1. Eukaryota.
ENOG410YR1P. LUCA.
GeneTreeiENSGT00760000119187.
HOGENOMiHOG000233417.
HOVERGENiHBG007922.
InParanoidiP31809.
KOiK06499.
PhylomeDBiP31809.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF13895. Ig_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
PROSITEiPS50835. IG_LIKE. 3 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P31809-1) [UniParc]FASTAAdd to basket
Also known as: Ceacam1-4L1 Publication, Bgpd

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MELASAHLHK GQVPWGGLLL TASLLASWSP ATTAEVTIEA VPPQVAEDNN
60 70 80 90 100
VLLLVHNLPL ALGAFAWYKG NTTAIDKEIA RFVPNSNMNF TGQAYSGREI
110 120 130 140 150
IYSNGSLLFQ MITMKDMGVY TLDMTDENYR RTQATVRFHV HPILLKPNIT
160 170 180 190 200
SNNSNPVEGD DSVSLTCDSY TDPDNINYLW SRNGESLSEG DRLKLSEGNR
210 220 230 240 250
TLTLLNVTRN DTGPYVCETR NPVSVNRSDP FSLNIIYGPD TPIISPSDIY
260 270 280 290 300
LHPGSNLNLS CHAASNPPAQ YFWLINEKPH ASSQELFIPN ITTNNSGTYT
310 320 330 340 350
CFVNNSVTGL SRTTVKNITV LEPVTQPFLQ VTNTTVKELD SVTLTCLSND
360 370 380 390 400
IGANIQWLFN SQSLQLTERM TLSQNNSILR IDPIKREDAG EYQCEISNPV
410 420 430 440 450
SVRRSNSIKL DIIFDPTQGG LSDGAIAGIV IGVVAGVALI AGLAYFLYSR
460 470 480 490 500
KSGGGSDQRD LTEHKPSTSN HNLAPSDNSP NKVDDVAYTV LNFNSQQPNR
510 520
PTSAPSSPRA TETVYSEVKK K
Length:521
Mass (Da):57,016
Last modified:July 1, 1993 - v1
Checksum:i1C8F71FAC47DD54E
GO
Isoform 2 (identifier: P31809-2) [UniParc]FASTAAdd to basket
Also known as: Ceacam1-4S1 Publication, Bgpa, mmCGM1a

The sequence of this isoform differs from the canonical sequence as follows:
     455-458: GSDQ → SGSF
     459-521: Missing.

Show »
Length:458
Mass (Da):50,057
Checksum:i63E0EC6AC58BA660
GO
Isoform 3 (identifier: P31809-3) [UniParc]FASTAAdd to basket
Also known as: Ceacam1-2L1 Publication, Bgpg

The sequence of this isoform differs from the canonical sequence as follows:
     142-142: P → Q
     143-322: Missing.

Note: Glycosylated at Asn-153.
Show »
Length:341
Mass (Da):37,271
Checksum:i0ABE851287A77290
GO
Isoform 4 (identifier: P31809-4) [UniParc]FASTAAdd to basket
Also known as: Ceacam1-2S1 Publication, Bgpc

The sequence of this isoform differs from the canonical sequence as follows:
     142-322: PILLKPNITS...TTVKNITVLE → Q
     455-458: GSDQ → SGSF
     459-521: Missing.

Show »
Length:278
Mass (Da):30,313
Checksum:iE023AE5CAB27A49D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti361 – 362SQ → RE in CAA47699 (PubMed:8500759).Curated2
Sequence conflicti361 – 362SQ → RE in CAA47695 (PubMed:8500759).Curated2

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_058517142 – 322PILLK…ITVLE → Q in isoform 4. 1 PublicationAdd BLAST181
Alternative sequenceiVSP_036040142P → Q in isoform 3. 1 Publication1
Alternative sequenceiVSP_036041143 – 322Missing in isoform 3. 1 PublicationAdd BLAST180
Alternative sequenceiVSP_002484455 – 458GSDQ → SGSF in isoform 2 and isoform 4. 3 Publications4
Alternative sequenceiVSP_002485459 – 521Missing in isoform 2 and isoform 4. 3 PublicationsAdd BLAST63

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77196 mRNA. Translation: AAA37858.1.
X15351 mRNA. Translation: CAA33409.1.
X67278 mRNA. Translation: CAA47695.1.
X67279 mRNA. Translation: CAA47696.1.
X67282 mRNA. Translation: CAA47699.1.
CCDSiCCDS20984.1. [P31809-1]
CCDS20985.1. [P31809-3]
CCDS39839.1. [P31809-2]
PIRiJC1505. WMMSR1.
JC1508.
JC1511.
RefSeqiNP_001034274.1. NM_001039185.1.
NP_001034275.1. NM_001039186.1. [P31809-2]
UniGeneiMm.322502.
Mm.439731.

Genome annotation databases

EnsembliENSMUST00000098666; ENSMUSP00000096263; ENSMUSG00000074272. [P31809-2]
ENSMUST00000206171; ENSMUSP00000145584; ENSMUSG00000074272. [P31809-2]
ENSMUST00000206687; ENSMUSP00000146066; ENSMUSG00000074272. [P31809-4]
GeneIDi26365.
KEGGimmu:26365.
UCSCiuc009fsv.1. mouse. [P31809-2]
uc009fta.1. mouse. [P31809-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77196 mRNA. Translation: AAA37858.1.
X15351 mRNA. Translation: CAA33409.1.
X67278 mRNA. Translation: CAA47695.1.
X67279 mRNA. Translation: CAA47696.1.
X67282 mRNA. Translation: CAA47699.1.
CCDSiCCDS20984.1. [P31809-1]
CCDS20985.1. [P31809-3]
CCDS39839.1. [P31809-2]
PIRiJC1505. WMMSR1.
JC1508.
JC1511.
RefSeqiNP_001034274.1. NM_001039185.1.
NP_001034275.1. NM_001039186.1. [P31809-2]
UniGeneiMm.322502.
Mm.439731.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1L6ZX-ray3.32A35-416[»]
3R4DX-ray3.10A/C35-416[»]
ProteinModelPortaliP31809.
SMRiP31809.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61461N.
IntActiP31809. 1 interactor.
MINTiMINT-4590618.
STRINGi10090.ENSMUSP00000096266.

PTM databases

iPTMnetiP31809.
PhosphoSitePlusiP31809.

Proteomic databases

MaxQBiP31809.
PaxDbiP31809.
PeptideAtlasiP31809.
PRIDEiP31809.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000098666; ENSMUSP00000096263; ENSMUSG00000074272. [P31809-2]
ENSMUST00000206171; ENSMUSP00000145584; ENSMUSG00000074272. [P31809-2]
ENSMUST00000206687; ENSMUSP00000146066; ENSMUSG00000074272. [P31809-4]
GeneIDi26365.
KEGGimmu:26365.
UCSCiuc009fsv.1. mouse. [P31809-2]
uc009fta.1. mouse. [P31809-1]

Organism-specific databases

CTDi634.
MGIiMGI:1347245. Ceacam1.

Phylogenomic databases

eggNOGiENOG410IFE1. Eukaryota.
ENOG410YR1P. LUCA.
GeneTreeiENSGT00760000119187.
HOGENOMiHOG000233417.
HOVERGENiHBG007922.
InParanoidiP31809.
KOiK06499.
PhylomeDBiP31809.

Enzyme and pathway databases

ReactomeiR-MMU-1566977. Fibronectin matrix formation.
R-MMU-202733. Cell surface interactions at the vascular wall.
R-MMU-6798695. Neutrophil degranulation.

Miscellaneous databases

EvolutionaryTraceiP31809.
PROiP31809.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000074272.
CleanExiMM_CEACAM1.
ExpressionAtlasiP31809. baseline and differential.
GenevisibleiP31809. MM.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF13895. Ig_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
PROSITEiPS50835. IG_LIKE. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCEAM1_MOUSE
AccessioniPrimary (citable) accession number: P31809
Secondary accession number(s): Q61350, Q61353
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 30, 2016
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.