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Protein

Carcinoembryonic antigen-related cell adhesion molecule 1

Gene

Ceacam1

Organism
Rattus norvegicus (Rat)
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 (PubMed:8454589, PubMed:2373740). Plays a role as coinhibitory receptor in immune response, insulin action and functions also 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). Downregulates neutrophil production by acting as a coinhibitory receptor for CSF3R by downregulating 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:7592607, PubMed:16054098). 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). 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 (By similarity). 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 (PubMed:7518458). Negatively regulates osteoclastogenesis (By similarity).By similarity9 Publications
Isoform 2: Cell adhesion proteins that mediates homophilic cell adhesion in a calcium-independent manner (PubMed:8536699, PubMed:7774714). Promotes populations of T-cells regulating IgA production and secretion associated with control of the commensal microbiota and resistance to enteropathogens (By similarity).By similarity2 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

Biological processCell adhesion

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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

Protein family/group databases

Transport Classification Database

More...
TCDBi
8.A.23.1.4 the basigin (basigin) family

<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):
ATP-dependent taurocolate-carrier protein
Cell-CAM 1051 Publication
Short name:
C-CAM 105
Ecto-ATPase1 Publication
GP1101 Publication
pp120
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
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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 1

Organism-specific databases

Rat genome database

More...
RGDi
67396 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 – 425ExtracellularCuratedAdd BLAST391
<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>Transmembranei426 – 446HelicalSequence analysisAdd BLAST21
Topological domaini447 – 519CytoplasmicCuratedAdd BLAST73

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

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 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. 6 Publications1
Mutagenesisi502 – 503TS → AA: Phosphorylated on tyrosine. Impairs bile acid transport. 1 Publication2
Mutagenesisi503S → 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. 7 Publications1
Mutagenesisi503S → D: Preserves the ability of INSR to induce CEACAM1 phosphorylation. 1 Publication1
Mutagenesisi513Y → 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. 3 Publications1

<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 – 34Sequence analysisAdd 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_000001456435 – 519Carcinoembryonic antigen-related cell adhesion molecule 1Add BLAST485

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei35Pyrrolidone carboxylic acidBy similarity1
<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>Glycosylationi87N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi104N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi113N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi148N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi152N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
<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 ↔ 215PROSITE-ProRule annotation
Glycosylationi173N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi197N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi224N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi256N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi259 ↔ 299PROSITE-ProRule annotation
Glycosylationi288N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi292N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi302N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi315N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi331N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi344 ↔ 392PROSITE-ProRule annotation
Glycosylationi374N-linked (GlcNAc...) asparagine; atypicalPROSITE-ProRule annotationBy similarity1
Modified residuei488Phosphotyrosine; by SRC, LCK, INSR and EGFR5 Publications1
Modified residuei503Phosphoserine2 Publications1
Modified residuei513Phosphotyrosine; by INSR, SRC and LCK1 Publication1

<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 (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:7626603, PubMed:9712832, PubMed:16054098). 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:16054098, PubMed:15467833, 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).By similarity6 Publications
Isoform 2: Phosphorylated on serine and threonine.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Pyrrolidone carboxylic acid

Proteomic databases

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

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PaxDbi
P16573

PRoteomics IDEntifications database

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PRIDEi
P16573

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P16573

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

More...
PhosphoSitePlusi
P16573

<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 epithelia, vessel endothelia, leukocytes and platelets. Isoform 1 and isoform 2 are highly expressed in liver and intestine, moderately in lung, and weakly in muscle, kidney, and spleen (PubMed:8454589). Expressed in granulocytes, lymphocytes, granulocytes, B cells, and T-cells (PubMed:11994468).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000020578 Expressed in 9 organ(s), highest expression level in liver

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P16573 baseline and differential

<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

Monomer (PubMed:9003371, PubMed:19948503). Oligomer. Heterodimer. Homodimer (PubMed:19948503). 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 (PubMed:19948503, PubMed:2373740, PubMed:8831574, PubMed:9003371). Interacts (via cytoplasmic domain) with calmodulin in a calcium dependent manner; reduces homophilic cell adhesion through dissociation of dimer (PubMed:8576129). 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:19948503). Isoform 1 interacts with LYN (By similarity). Isoform 1 interacts (via cytoplasmic domain) with SRC (via SH2 domain); this interaction is regulated by trans-homophilic cell adhesion (PubMed:19948503). Isoform 1 interacts (via cytoplasmic domain) with LCK; mediates phosphorylation at Tyr-488 and Tyr-513 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:11694516). Isoform 1 interacts with EGFR; the interaction is indirect (PubMed:15467833). Isoform 1 interacts with CSF3R; down-regulates the CSF3R-STAT3 pathway through recruitment of PTPN6 that dephosphorylates CSF3R. 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 (By similarity). Isoform 1 interacts with FLNA; inhibits cell migration and cell scattering by interfering with the interaction of FLNA with RALA (PubMed:16291724). 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 (PubMed:16054098). 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. 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 similarity9 Publications

GO - Molecular functioni

Protein-protein interaction databases

Molecular INTeraction database

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MINTi
P16573

STRING: functional protein association networks

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STRINGi
10116.ENSRNOP00000046654

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P16573

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...

<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>Domaini42 – 140Ig-like V-typeBy similarityAdd BLAST99
Domaini147 – 232Ig-like C2-type 1PROSITE-ProRule annotationAdd BLAST86
Domaini237 – 317Ig-like C2-type 2PROSITE-ProRule annotationAdd BLAST81
Domaini325 – 403Ig-like C2-type 3PROSITE-ProRule annotationAdd BLAST79

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 binding1 PublicationAdd BLAST104
Regioni445 – 457Interaction with calmodulin1 PublicationAdd BLAST13
Regioni447 – 519Interaction with FLNA1 PublicationAdd BLAST73
Regioni484 – 519Required for interaction with PTPN11 and PTPN6 and for control of phosphorylation levelBy similarityAdd BLAST36
Regioni513 – 516Essential for interaction with PTPN11 and PTPN6By similarity4

<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.2 Publications

<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

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eggNOGi
ENOG410IFE1 Eukaryota
ENOG410YR1P LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000153087

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000233417

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG007922

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P16573

KEGG Orthology (KO)

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KOi
K06499

Identification of Orthologs from Complete Genome Data

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OMAi
TGISISW

Database of Orthologous Groups

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OrthoDBi
524642at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P16573

TreeFam database of animal gene trees

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TreeFami
TF336859

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.10, 4 hits

Integrated resource of protein families, domains and functional sites

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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
IPR013151 Immunoglobulin

Pfam protein domain database

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Pfami
View protein in Pfam
PF00047 ig, 1 hit
PF13895 Ig_2, 1 hit
PF07686 V-set, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00409 IG, 4 hits
SM00408 IGc2, 3 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48726 SSF48726, 4 hits

PROSITE; a protein domain and family database

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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 (2+)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 2 <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
Note: For each isoform it exists 2 allelic variants, named a and b. The allelic variants differ in 16 amino acids in the Ig-like V-type domain.1 Publication

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P16573-1) [UniParc]FASTAAdd to basket
Also known as: CEACAM1-4L1 Publication, C-CAM1, L-form Cell-CAM105

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
MELASARLLR GQIPWRGLLL TASLLTYWSP LTTAQVTVDA VPPNVVEEKS
60 70 80 90 100
VLLLAHNLPQ EFQVFYWYKG TTLNPDSEIA RYIRSDNMSK TGPAYSGRET
110 120 130 140 150
IYSNGSLFFQ NVNKTDERAY TLSVFDQQFN PIQTSVQFRV YPALQKPNVT
160 170 180 190 200
GNNSNPMEGE PFVSLMCEPY TNNTSYLWSR NGESLSEGDR VTFSEGNRTL
210 220 230 240 250
TLLNVRRTDK GYYECEARNP ATFNRSDPFN LDVIYGPDAP VISPPDIYLH
260 270 280 290 300
QGSNLNLSCH ADSNPPAQYF WLINEKLQTS SQELFISNIT TNNSGTYACF
310 320 330 340 350
VNNTVTGLSR TTVKNITVFE PVTQPSIQIT NTTVKELGSV TLTCFSKDTG
360 370 380 390 400
VSVRWLFNSQ SLQLTDRMTL SQDNSTLRID PIKREDAGDY QCEISNPVSF
410 420 430 440 450
RISHPIKLDV IPDPTQGNSG LSEGAIAGIV IGSVAGVALI AALAYFLYSR
460 470 480 490 500
KTGGGSDHRD LTEHKPSTSS HNLGPSDDSP NKVDDVSYSV LNFNAQQSKR
510
PTSASSSPTE TVYSVVKKK
Note: Allele a.
Length:519
Mass (Da):57,410
Last modified:October 5, 2016 - v4
<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:i9EFE74FD565E7C29
GO
Isoform 2 (identifier: P16573-2) [UniParc]FASTAAdd to basket
Also known as: CEACAM1-4S1 Publication, C-CAM2, S-form Cell-CAM105

The sequence of this isoform differs from the canonical sequence as follows:
     455-458: GSDH → SGSF
     459-519: Missing.

Note: Allele a.
Show »
Length:458
Mass (Da):50,760
Checksum:iA77F43AE372046B1
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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2JSW2A0A0G2JSW2_RAT
Carcinoembryonic antigen-related ce...
Ceacam1 rCG_54207
519Annotation 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>
Q9JHL6Q9JHL6_RAT
Carcinoembryonic antigen-related ce...
Ceacam1 ceacam1, Ceacam1_v4, rCG_54207
459Annotation 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>
Q9JHL7Q9JHL7_RAT
Carcinoembryonic antigen-related ce...
Ceacam1 ceacam1, Ceacam1_v3, rCG_54207
448Annotation 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA16783 differs from that shown. Dubious isoform. Probable cloning artifact lacking polyadenylation evidence.Curated

<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

There are two different allelic variants of CEACAM1, named a and b. The allelic variants differ in 16 amino acids in the Ig-like V-type domain. The sequence shown here, corresponds to allele A.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti49K → S in allele b. 3 Publications1
Natural varianti55A → T in allele b. 3 Publications1
Natural varianti70G → V in allele b. 3 Publications1
Natural varianti73L → T in allele b. 3 Publications1
Natural varianti74N → G in allele b. 3 Publications1
Natural varianti75P → L in allele b. 3 Publications1
Natural varianti76D → N in allele b. 3 Publications1
Natural varianti86D → S in allele b. 3 Publications1
Natural varianti88M → T in allele b. 3 Publications1
Natural varianti90K → Q in allele b. 3 Publications1
Natural varianti92G → E in allele b. 3 Publications1
Natural varianti99E → V in allele b. 3 Publications1
Natural varianti118R → G in allele b. 3 Publications1
Natural varianti119A → P in allele b. 3 Publications1
Natural varianti125F → I in allele b. 3 Publications1
Natural varianti127Q → K in allele b. 3 Publications1

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_002504455 – 458GSDH → SGSF in isoform 2. 3 Publications4
Alternative sequenceiVSP_002505459 – 519Missing in isoform 2. 3 PublicationsAdd BLAST61

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
J04963 mRNA Translation: AAA41104.1
Z12019 mRNA Translation: CAA78054.1
M92848 mRNA Translation: AAA16783.1 Sequence problems.
X71122 mRNA Translation: CAA50435.1
X91137 mRNA Translation: CAA62577.1
AC134759 Genomic DNA No translation available.
CH473979 Genomic DNA Translation: EDM08020.1
BC061740 mRNA Translation: AAH61740.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A44783
S23969
S68177

NCBI Reference Sequences

More...
RefSeqi
NP_001029032.1, NM_001033860.1 [P16573-1]
NP_001029033.1, NM_001033861.1
NP_001029034.1, NM_001033862.1 [P16573-2]
NP_113943.1, NM_031755.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Rn.91235

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000051892; ENSRNOP00000046654; ENSRNOG00000020578 [P16573-1]
ENSRNOT00000090629; ENSRNOP00000074820; ENSRNOG00000020578 [P16573-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
81613

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:81613

UCSC genome browser

More...
UCSCi
RGD:67396 rat [P16573-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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
J04963 mRNA Translation: AAA41104.1
Z12019 mRNA Translation: CAA78054.1
M92848 mRNA Translation: AAA16783.1 Sequence problems.
X71122 mRNA Translation: CAA50435.1
X91137 mRNA Translation: CAA62577.1
AC134759 Genomic DNA No translation available.
CH473979 Genomic DNA Translation: EDM08020.1
BC061740 mRNA Translation: AAH61740.1
PIRiA44783
S23969
S68177
RefSeqiNP_001029032.1, NM_001033860.1 [P16573-1]
NP_001029033.1, NM_001033861.1
NP_001029034.1, NM_001033862.1 [P16573-2]
NP_113943.1, NM_031755.2
UniGeneiRn.91235

3D structure databases

ProteinModelPortaliP16573
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiP16573
STRINGi10116.ENSRNOP00000046654

Protein family/group databases

TCDBi8.A.23.1.4 the basigin (basigin) family

PTM databases

iPTMnetiP16573
PhosphoSitePlusiP16573

Proteomic databases

PaxDbiP16573
PRIDEiP16573

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000051892; ENSRNOP00000046654; ENSRNOG00000020578 [P16573-1]
ENSRNOT00000090629; ENSRNOP00000074820; ENSRNOG00000020578 [P16573-2]
GeneIDi81613
KEGGirno:81613
UCSCiRGD:67396 rat [P16573-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
634
RGDi67396 Ceacam1

Phylogenomic databases

eggNOGiENOG410IFE1 Eukaryota
ENOG410YR1P LUCA
GeneTreeiENSGT00940000153087
HOGENOMiHOG000233417
HOVERGENiHBG007922
InParanoidiP16573
KOiK06499
OMAiTGISISW
OrthoDBi524642at2759
PhylomeDBiP16573
TreeFamiTF336859

Enzyme and pathway databases

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

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P16573

Gene expression databases

BgeeiENSRNOG00000020578 Expressed in 9 organ(s), highest expression level in liver
ExpressionAtlasiP16573 baseline and differential

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
IPR013151 Immunoglobulin
PfamiView protein in Pfam
PF00047 ig, 1 hit
PF13895 Ig_2, 1 hit
PF07686 V-set, 1 hit
SMARTiView protein in SMART
SM00409 IG, 4 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_RAT
<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: P16573
Secondary accession number(s): Q63093
<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: August 1, 1990
Last sequence update: October 5, 2016
Last modified: January 16, 2019
This is version 171 of the entry and version 4 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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