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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-Experimental evidence at protein leveli

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

GO - Molecular functioni

  • bile acid transmembrane transporter activity Source: UniProtKB
  • calmodulin binding Source: UniProtKB
  • protein dimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Protein family/group databases

TCDBi8.A.23.1.4. the basigin (basigin) family.

Names & Taxonomyi

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
Gene namesi
Name:Ceacam1Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi67396. Ceacam1.

Subcellular locationi

Isoform 1 :
Isoform 2 :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini35 – 425ExtracellularCuratedAdd BLAST391
Transmembranei426 – 446HelicalSequence analysisAdd BLAST21
Topological domaini447 – 519CytoplasmicCuratedAdd BLAST73

GO - Cellular componenti

  • adherens junction Source: UniProtKB
  • apical plasma membrane Source: UniProtKB
  • basal plasma membrane Source: UniProtKB
  • cell-cell junction Source: UniProtKB
  • cell junction Source: UniProtKB
  • cell surface Source: UniProtKB
  • integral component of plasma membrane Source: RGD
  • lateral plasma membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • transport vesicle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 34Sequence analysisAdd BLAST34
ChainiPRO_000001456435 – 519Carcinoembryonic antigen-related cell adhesion molecule 1Add BLAST485

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei35Pyrrolidone carboxylic acidBy similarity1
Glycosylationi87N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi104N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi113N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi148N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi152N-linked (GlcNAc...)PROSITE-ProRule annotation1
Disulfide bondi167 ↔ 215PROSITE-ProRule annotation
Glycosylationi172N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi197N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi224N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi256N-linked (GlcNAc...)PROSITE-ProRule annotation1
Disulfide bondi259 ↔ 299PROSITE-ProRule annotation
Glycosylationi288N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi292N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi302N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi315N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi331N-linked (GlcNAc...)PROSITE-ProRule annotation1
Disulfide bondi344 ↔ 392PROSITE-ProRule annotation
Glycosylationi374N-linked (GlcNAc...); atypicalBy similarity1
Modified residuei488Phosphotyrosine; by SRC; LCK; INSR and EGFR5 Publications1
Modified residuei503Phosphoserine2 Publications1
Modified residuei513Phosphotyrosine; by INSR; SRC and LCKBy similarity1 Publication1

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

PaxDbiP16573.
PRIDEiP16573.

PTM databases

iPTMnetiP16573.
PhosphoSitePlusiP16573.

Expressioni

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

BgeeiENSRNOG00000020578.

Interactioni

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

  • calmodulin binding Source: UniProtKB
  • protein dimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: RGD

Protein-protein interaction databases

MINTiMINT-220849.
STRINGi10116.ENSRNOP00000046654.

Structurei

3D structure databases

ProteinModelPortaliP16573.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini42 – 140Ig-like V-typeAdd BLAST99
Domaini147 – 232Ig-like C2-type 1Add BLAST86
Domaini237 – 317Ig-like C2-type 2Add BLAST81
Domaini325 – 403Ig-like C2-type 3Add BLAST79

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

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

Sequence similaritiesi

Belongs to the immunoglobulin superfamily. CEA family.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IFE1. Eukaryota.
ENOG410YR1P. LUCA.
GeneTreeiENSGT00760000119187.
HOGENOMiHOG000233417.
HOVERGENiHBG007922.
InParanoidiP16573.
KOiK06499.
PhylomeDBiP16573.
TreeFamiTF336859.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR013151. Immunoglobulin.
[Graphical view]
PfamiPF00047. ig. 1 hit.
PF13895. Ig_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 4 hits.
SM00408. IGc2. 3 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
PROSITEiPS50835. IG_LIKE. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 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
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
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

Sequence cautioni

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

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
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
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:
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.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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

MINTiMINT-220849.
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

CTDi634.
RGDi67396. Ceacam1.

Phylogenomic databases

eggNOGiENOG410IFE1. Eukaryota.
ENOG410YR1P. LUCA.
GeneTreeiENSGT00760000119187.
HOGENOMiHOG000233417.
HOVERGENiHBG007922.
InParanoidiP16573.
KOiK06499.
PhylomeDBiP16573.
TreeFamiTF336859.

Miscellaneous databases

PROiP16573.

Gene expression databases

BgeeiENSRNOG00000020578.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR013151. Immunoglobulin.
[Graphical view]
PfamiPF00047. ig. 1 hit.
PF13895. Ig_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 4 hits.
SM00408. IGc2. 3 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
PROSITEiPS50835. IG_LIKE. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCEAM1_RAT
AccessioniPrimary (citable) accession number: P16573
Secondary accession number(s): Q63093
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: October 5, 2016
Last modified: November 30, 2016
This is version 149 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

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