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P06731 (CEAM5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carcinoembryonic antigen-related cell adhesion molecule 5
Alternative name(s):
Carcinoembryonic antigen
Short name=CEA
Meconium antigen 100
CD_antigen=CD66e
Gene names
Name:CEACAM5
Synonyms:CEA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length702 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cell surface glycoprotein that plays a role in cell adhesion and in intracellular signaling. Receptor for E.coli Dr adhesins. Ref.7

Subunit structure

Homodimer. Binding of E.coli Dr adhesins leads to dissociation of the homodimer. Ref.11

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor Ref.7 Ref.11.

Tissue specificity

Found in adenocarcinomas of endodermally derived digestive system epithelium and fetal colon.

Post-translational modification

Complex immunoreactive glycoprotein with a MW of 180 kDa comprising 60% carbohydrate.

Sequence similarities

Belongs to the immunoglobulin superfamily. CEA family.

Contains 7 Ig-like (immunoglobulin-like) domains.

Sequence caution

The sequence AAA62835.1 differs from that shown. Reason: Frameshift at positions 359 and 361.

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself6EBI-3914938,EBI-3914938

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P06731-1)

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.
Isoform 2 (identifier: P06731-2)

The sequence of this isoform differs from the canonical sequence as follows:
     320-320: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434
Chain35 – 685651Carcinoembryonic antigen-related cell adhesion molecule 5
PRO_0000014566
Propeptide686 – 70217Removed in mature form Potential
PRO_0000014567

Regions

Domain35 – 144110Ig-like 1
Domain146 – 23792Ig-like 2
Domain238 – 32285Ig-like 3
Domain324 – 41592Ig-like 4
Domain416 – 49883Ig-like 5
Domain502 – 59392Ig-like 6
Domain594 – 67784Ig-like 7

Amino acid modifications

Lipidation6851GPI-anchor amidated alanine Potential
Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation1151N-linked (GlcNAc...) Potential
Glycosylation1521N-linked (GlcNAc...) Potential
Glycosylation1821N-linked (GlcNAc...) Potential
Glycosylation1971N-linked (GlcNAc...) Potential
Glycosylation2041N-linked (GlcNAc...) Potential
Glycosylation2081N-linked (GlcNAc...) Potential
Glycosylation2461N-linked (GlcNAc...) Ref.9
Glycosylation2561N-linked (GlcNAc...) Potential
Glycosylation2741N-linked (GlcNAc...) Potential
Glycosylation2881N-linked (GlcNAc...) Potential
Glycosylation2921N-linked (GlcNAc...) Potential
Glycosylation3091N-linked (GlcNAc...) Potential
Glycosylation3301N-linked (GlcNAc...) Potential
Glycosylation3511N-linked (GlcNAc...) Potential
Glycosylation3601N-linked (GlcNAc...) Potential
Glycosylation3751N-linked (GlcNAc...) Potential
Glycosylation4321N-linked (GlcNAc...) Potential
Glycosylation4661N-linked (GlcNAc...) Potential
Glycosylation4801N-linked (GlcNAc...) Potential
Glycosylation5081N-linked (GlcNAc...) Potential
Glycosylation5291N-linked (GlcNAc...) Potential
Glycosylation5531N-linked (GlcNAc...) Potential
Glycosylation5601N-linked (GlcNAc...) Ref.8
Glycosylation5801N-linked (GlcNAc...) Potential
Glycosylation6121N-linked (GlcNAc...) Potential
Glycosylation6501N-linked (GlcNAc...) Potential
Glycosylation6651N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence3201Missing in isoform 2.
VSP_053414
Natural variant801I → V.
Corresponds to variant rs12971352 [ dbSNP | Ensembl ].
VAR_061310
Natural variant831V → A.
Corresponds to variant rs28683503 [ dbSNP | Ensembl ].
VAR_061311
Natural variant1371Q → P.
Corresponds to variant rs3815780 [ dbSNP | Ensembl ].
VAR_056028
Natural variant3401A → D.
Corresponds to variant rs10407503 [ dbSNP | Ensembl ].
VAR_031091
Natural variant3981K → E. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6
Corresponds to variant rs7249230 [ dbSNP | Ensembl ].
VAR_024493
Natural variant6641R → S.
Corresponds to variant rs10423171 [ dbSNP | Ensembl ].
VAR_031092
Natural variant6781G → R.
Corresponds to variant rs11545767 [ dbSNP | Ensembl ].
VAR_056029

Experimental info

Mutagenesis631F → I: No effect on dimerization. Reduced affinity for E.coli Dr adhesins. Ref.11
Mutagenesis631F → R: Abolishes dimerization. Reduced affinity for E.coli Dr adhesins. Ref.11
Mutagenesis661S → N: Abolishes dimerization. Ref.7 Ref.11
Mutagenesis681Y → A: Abolishes dimerization. Ref.7
Mutagenesis681Y → F: No effect on dimerization. Ref.7
Mutagenesis691K → A: Abolishes dimerization. Ref.7
Mutagenesis731V → A: Abolishes dimerization. Ref.11
Mutagenesis741D → A: No effect on dimerization. Ref.11
Mutagenesis741D → L or R: Abolishes dimerization. Ref.11
Mutagenesis781Q → L or R: Abolishes dimerization. Reduced affinity for E.coli Dr adhesins. Ref.7 Ref.11
Mutagenesis1251I → A: Abolishes dimerization. Reduced affinity for E.coli Dr adhesins. Ref.11
Mutagenesis1291L → A or C: No effect on dimerization. Reduced affinity for E.coli Dr adhesins. Ref.11
Mutagenesis1291L → S: Abolishes dimerization. Reduced affinity for E.coli Dr adhesins. Ref.11
Mutagenesis1331E → A: Abolishes dimerization. Ref.11
Sequence conflict6411F → L in AAA62835. Ref.3
Sequence conflict6461T → Q in AAA62835. Ref.3
Sequence conflict6891V → A in AAA62835. Ref.3

Secondary structure

...................... 702
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: 86318E244155DB58

FASTA70276,795
        10         20         30         40         50         60 
MESPSAPPHR WCIPWQRLLL TASLLTFWNP PTTAKLTIES TPFNVAEGKE VLLLVHNLPQ 

        70         80         90        100        110        120 
HLFGYSWYKG ERVDGNRQII GYVIGTQQAT PGPAYSGREI IYPNASLLIQ NIIQNDTGFY 

       130        140        150        160        170        180 
TLHVIKSDLV NEEATGQFRV YPELPKPSIS SNNSKPVEDK DAVAFTCEPE TQDATYLWWV 

       190        200        210        220        230        240 
NNQSLPVSPR LQLSNGNRTL TLFNVTRNDT ASYKCETQNP VSARRSDSVI LNVLYGPDAP 

       250        260        270        280        290        300 
TISPLNTSYR SGENLNLSCH AASNPPAQYS WFVNGTFQQS TQELFIPNIT VNNSGSYTCQ 

       310        320        330        340        350        360 
AHNSDTGLNR TTVTTITVYA EPPKPFITSN NSNPVEDEDA VALTCEPEIQ NTTYLWWVNN 

       370        380        390        400        410        420 
QSLPVSPRLQ LSNDNRTLTL LSVTRNDVGP YECGIQNKLS VDHSDPVILN VLYGPDDPTI 

       430        440        450        460        470        480 
SPSYTYYRPG VNLSLSCHAA SNPPAQYSWL IDGNIQQHTQ ELFISNITEK NSGLYTCQAN 

       490        500        510        520        530        540 
NSASGHSRTT VKTITVSAEL PKPSISSNNS KPVEDKDAVA FTCEPEAQNT TYLWWVNGQS 

       550        560        570        580        590        600 
LPVSPRLQLS NGNRTLTLFN VTRNDARAYV CGIQNSVSAN RSDPVTLDVL YGPDTPIISP 

       610        620        630        640        650        660 
PDSSYLSGAN LNLSCHSASN PSPQYSWRIN GIPQQHTQVL FIAKITPNNN GTYACFVSNL 

       670        680        690        700 
ATGRNNSIVK SITVSASGTS PGLSAGATVG IMIGVLVGVA LI 

« Hide

Isoform 2 [UniParc].

Checksum: 19149D8E5BDE18E5
Show »

FASTA70176,724

References

« Hide 'large scale' references
[1]"Isolation and characterization of full-length functional cDNA clones for human carcinoembryonic antigen."
Beauchemin N., Benchimol S., Cournoyer D., Fuks A., Stanners C.P.
Mol. Cell. Biol. 7:3221-3230(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-398.
[2]"Carcinoembryonic antigen family: characterization of cDNAs coding for NCA and CEA and suggestion of nonrandom sequence variation in their conserved loop-domains."
Barnett T., Goebel S.J., Nothdurft M.A., Elting J.J.
Genomics 3:59-66(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLU-398.
[3]"Cloning of the complete gene for carcinoembryonic antigen: analysis of its promoter indicates a region conveying cell type-specific expression."
Schrewe H., Thompson J., Bona M., Hefta L.J.F., Maruya A., Hassauer M., Shively J.E., von Kleist S., Zimmermann W.
Mol. Cell. Biol. 10:2738-2748(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-398.
[4]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Primary structure of human carcinoembryonic antigen (CEA) deduced from cDNA sequence."
Oikawa S., Nakazato H., Kosaki G.
Biochem. Biophys. Res. Commun. 142:511-518(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-702 (ISOFORM 2), VARIANT GLU-398.
[6]"Isolation and characterization of cDNA clones encoding the human carcinoembryonic antigen reveal a highly conserved repeating structure."
Zimmermann W., Ortlieb B., Friedrich R., von Kleist S.
Proc. Natl. Acad. Sci. U.S.A. 84:2960-2964(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 331-702 (ISOFORM 1), VARIANT GLU-398.
[7]"Self recognition in the Ig superfamily. Identification of precise subdomains in carcinoembryonic antigen required for intercellular adhesion."
Taheri M., Saragovi U., Fuks A., Makkerh J., Mort J., Stanners C.P.
J. Biol. Chem. 275:26935-26943(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF SER-66; TYR-68; LYS-69 AND GLN-78, SUBCELLULAR LOCATION.
[8]"Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-560.
Tissue: Saliva.
[9]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-246.
Tissue: Liver.
[10]"Structural models for carcinoembryonic antigen and its complex with the single-chain Fv antibody molecule MFE23."
Boehm M.K., Perkins S.J.
FEBS Lett. 475:11-16(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 35-676.
[11]"Binding of Dr adhesins of Escherichia coli to carcinoembryonic antigen triggers receptor dissociation."
Korotkova N., Yang Y., Le Trong I., Cota E., Demeler B., Marchant J., Thomas W.E., Stenkamp R.E., Moseley S.L., Matthews S.
Mol. Microbiol. 67:420-434(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 34-144 IN COMPLEX WITH E.COLI DR ADHESIN, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-63; SER-66; VAL-73; ASP-74; GLN-78; ILE-125; LEU-129 AND GLU-133.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17303 Genomic DNA. Translation: AAB59513.1.
M29540 mRNA. Translation: AAA51967.1.
M59262 expand/collapse EMBL AC list , M59255, M59256, M59257, M59258, M59259, M59260, M59261 Genomic DNA. Translation: AAA62835.1. Frameshift.
M59709 Genomic DNA. No translation available.
M59710 Genomic DNA. No translation available.
AC008999 Genomic DNA. No translation available.
X16455 mRNA. Translation: CAA34474.1.
M15042 mRNA. Translation: AAA51963.1.
M16234 mRNA. Translation: AAA51972.1.
PIRA36319.
RefSeqNP_001278413.1. NM_001291484.1.
NP_004354.3. NM_004363.4. [P06731-1]
UniGeneHs.709196.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E07X-ray-A35-676[»]
2QSQX-ray1.95A/B34-144[»]
2QSTX-ray2.90A/B34-144[»]
2VERNMR-N35-144[»]
ProteinModelPortalP06731.
SMRP06731. Positions 34-676.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107478. 6 interactions.
DIPDIP-57769N.
IntActP06731. 5 interactions.
MINTMINT-1472001.
STRING9606.ENSP00000221992.

PTM databases

PhosphoSiteP06731.

Polymorphism databases

DMDM317373456.

Proteomic databases

MaxQBP06731.
PaxDbP06731.
PRIDEP06731.

Protocols and materials databases

DNASU1048.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000221992; ENSP00000221992; ENSG00000105388. [P06731-1]
ENST00000398599; ENSP00000381600; ENSG00000105388. [P06731-2]
ENST00000405816; ENSP00000385072; ENSG00000105388. [P06731-1]
ENST00000607888; ENSP00000476879; ENSG00000272743.
ENST00000608968; ENSP00000477224; ENSG00000272743.
GeneID1048.
KEGGhsa:1048.
UCSCuc002orl.3. human. [P06731-1]

Organism-specific databases

CTD1048.
GeneCardsGC19P042212.
H-InvDBHIX0027513.
HGNCHGNC:1817. CEACAM5.
HPACAB000021.
CAB000022.
CAB002146.
HPA011041.
HPA019758.
MIM114890. gene.
neXtProtNX_P06731.
PharmGKBPA26361.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG265547.
HOGENOMHOG000233417.
HOVERGENHBG007922.
InParanoidP06731.
KOK06499.
OMAGPDDPTI.
OrthoDBEOG74BJS7.
PhylomeDBP06731.
TreeFamTF336859.

Gene expression databases

ArrayExpressP06731.
BgeeP06731.
CleanExHS_CEACAM5.
GenevestigatorP06731.

Family and domain databases

Gene3D2.60.40.10. 7 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
[Graphical view]
PfamPF07679. I-set. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTSM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
[Graphical view]
PROSITEPS50835. IG_LIKE. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06731.
GeneWikiCEACAM5.
GenomeRNAi1048.
NextBio35531126.
PROP06731.
SOURCESearch...

Entry information

Entry nameCEAM5_HUMAN
AccessionPrimary (citable) accession number: P06731
Secondary accession number(s): H9KVA7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries