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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHost cell receptor for virus entry, Receptor
Biological processHost-virus interaction

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-1566977 Fibronectin matrix formation
R-MMU-163125 Post-translational modification: synthesis of GPI-anchored proteins
R-MMU-202733 Cell surface interactions at the vascular wall
R-MMU-6798695 Neutrophil degranulation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Ceacam1Imported
Synonyms:Bgp1 Publication, Bgp1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

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MGIi
MGI:1347245 Ceacam1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini35 – 428ExtracellularSequence analysisAdd BLAST394
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei429 – 447HelicalSequence analysisAdd BLAST19
Topological domaini448 – 521CytoplasmicSequence analysisAdd BLAST74

Keywords - Cellular componenti

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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 341 PublicationAdd BLAST34
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001456335 – 521Carcinoembryonic antigen-related cell adhesion molecule 1Add BLAST487

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi71N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation2 Publications1
Glycosylationi89N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation2 Publications1
Glycosylationi104N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication1
Glycosylationi148N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi152N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationBy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi167 ↔ 217PROSITE-ProRule annotation1 Publication
Glycosylationi199N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi206N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication1
Glycosylationi210N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationBy similarity1
Glycosylationi226N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationBy similarity1
Glycosylationi258N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi261 ↔ 301PROSITE-ProRule annotation1 Publication
Glycosylationi290N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi294N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi304N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi317N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication1
Glycosylationi333N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation2 Publications1
Disulfide bondi346 ↔ 394PROSITE-ProRule annotation1 Publication
Glycosylationi375N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei488Phosphotyrosine; by SRC, LCK, INSR and EGFR2 Publications1
Modified residuei503PhosphoserineBy similarity1
Modified residuei515Phosphotyrosine; by INSR, SRC and LCK2 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

MaxQB - The MaxQuant DataBase

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MaxQBi
P31809

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P31809

PeptideAtlas

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PeptideAtlasi
P31809

PRoteomics IDEntifications database

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PRIDEi
P31809

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P31809

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P31809

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000074272 Expressed in 169 organ(s), highest expression level in colon

CleanEx database of gene expression profiles

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CleanExi
MM_CEACAM1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P31809 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P31809 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

(Microbial infection) Interacts with MHV S1 spike glycoprotein.3 Publications
Monomer. Oligomer. Heterodimer. Homodimer (By similarity). 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

Protein-protein interaction databases

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P31809

Database of interacting proteins

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DIPi
DIP-61461N

Protein interaction database and analysis system

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IntActi
P31809, 3 interactors

Molecular INTeraction database

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MINTi
P31809

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000096266

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1521
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P31809

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P31809

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P31809

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini35 – 142Ig-like V-typeBy similarityAdd BLAST108
Domaini147 – 234Ig-like C2-type 1PROSITE-ProRule annotationAdd BLAST88
Domaini239 – 319Ig-like C2-type 2PROSITE-ProRule annotationAdd BLAST81
Domaini323 – 411Ig-like C2-type 3PROSITE-ProRule annotationAdd BLAST89

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the immunoglobulin superfamily. CEA family.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IFE1 Eukaryota
ENOG410YR1P LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153087

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000233417

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG007922

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P31809

KEGG Orthology (KO)

More...
KOi
K06499

Identification of Orthologs from Complete Genome Data

More...
OMAi
ITINSTG

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P31809

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 4 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR013106 Ig_V-set

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF13895 Ig_2, 1 hit
PF07686 V-set, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00409 IG, 3 hits
SM00408 IGc2, 3 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48726 SSF48726, 4 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50835 IG_LIKE, 3 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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.

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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q3LFS8Q3LFS8_MOUSE
CEA-related cell adhesion molecule ...
Ceacam1 CEACAM1a-2S, mCG_126985
278Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q3LFS9Q3LFS9_MOUSE
CEA-related cell adhesion molecule ...
Ceacam1 CEACAM1a-2L
341Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q925P3Q925P3_MOUSE
CEA-related cell adhesion molecule ...
Ceacam1 mCG_126985
521Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q3LFS5Q3LFS5_MOUSE
Carcinoembryonic antigen-related ce...
Ceacam1 CEACAM1a-4C1
450Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q3LFS6Q3LFS6_MOUSE
Carcinoembryonic antigen-related ce...
Ceacam1 CEACAM1a-2C1
270Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q3LFS7Q3LFS7_MOUSE
Carcinoembryonic antigen-related ce...
Ceacam1 CEACAM1a-2
236Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS20984.1 [P31809-1]
CCDS20985.1 [P31809-3]
CCDS39839.1 [P31809-2]
CCDS85244.1 [P31809-4]

Protein sequence database of the Protein Information Resource

More...
PIRi
JC1505 WMMSR1
JC1508
JC1511

NCBI Reference Sequences

More...
RefSeqi
NP_001034274.1, NM_001039185.1
NP_001034275.1, NM_001039186.1 [P31809-2]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.322502
Mm.439731

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000098666; ENSMUSP00000096263; ENSMUSG00000074272 [P31809-2]
ENSMUST00000206171; ENSMUSP00000145584; ENSMUSG00000074272 [P31809-2]
ENSMUST00000206687; ENSMUSP00000146066; ENSMUSG00000074272 [P31809-4]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
26365

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:26365

UCSC genome browser

More...
UCSCi
uc009fsv.1 mouse [P31809-2]
uc009fta.1 mouse [P31809-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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]
CCDS85244.1 [P31809-4]
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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1L6ZX-ray3.32A35-416[»]
3R4DX-ray3.10A/C35-416[»]
5VSTX-ray3.10A35-416[»]
ProteinModelPortaliP31809
SMRiP31809
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

CORUMiP31809
DIPiDIP-61461N
IntActiP31809, 3 interactors
MINTiP31809
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

Comparative Toxicogenomics Database

More...
CTDi
634
MGIiMGI:1347245 Ceacam1

Phylogenomic databases

eggNOGiENOG410IFE1 Eukaryota
ENOG410YR1P LUCA
GeneTreeiENSGT00940000153087
HOGENOMiHOG000233417
HOVERGENiHBG007922
InParanoidiP31809
KOiK06499
OMAiITINSTG
PhylomeDBiP31809

Enzyme and pathway databases

ReactomeiR-MMU-1566977 Fibronectin matrix formation
R-MMU-163125 Post-translational modification: synthesis of GPI-anchored proteins
R-MMU-202733 Cell surface interactions at the vascular wall
R-MMU-6798695 Neutrophil degranulation

Miscellaneous databases

EvolutionaryTraceiP31809

Protein Ontology

More...
PROi
PR:P31809

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000074272 Expressed in 169 organ(s), highest expression level in colon
CleanExiMM_CEACAM1
ExpressionAtlasiP31809 baseline and differential
GenevisibleiP31809 MM

Family and domain databases

Gene3Di2.60.40.10, 4 hits
InterProiView protein in InterPro
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR013106 Ig_V-set
PfamiView protein in Pfam
PF13895 Ig_2, 1 hit
PF07686 V-set, 1 hit
SMARTiView protein in SMART
SM00409 IG, 3 hits
SM00408 IGc2, 3 hits
SUPFAMiSSF48726 SSF48726, 4 hits
PROSITEiView protein in PROSITE
PS50835 IG_LIKE, 3 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCEAM1_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P31809
Secondary accession number(s): Q61350, Q61353
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: December 5, 2018
This is version 170 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

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