P06731 (CEAM5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	702 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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-anchor › GPI-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

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Immunoglobulin domain Repeat Signal
PTM	GPI-anchor Glycoprotein Lipoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW basolateral plasma membrane Inferred from direct assay. Source: UniProtKB integral to plasma membrane Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 34

34

Chain

35 – 685

651

Carcinoembryonic antigen-related cell adhesion molecule 5

PRO_0000014566

Propeptide

686 – 702

17

Removed in mature form Potential

PRO_0000014567

Regions

Domain

35 – 144

110

Ig-like 1

Domain

146 – 237

92

Ig-like 2

Domain

238 – 322

85

Ig-like 3

Domain

324 – 415

92

Ig-like 4

Domain

416 – 498

83

Ig-like 5

Domain

502 – 593

92

Ig-like 6

Domain

594 – 677

84

Ig-like 7

Amino acid modifications

Lipidation

685

1

GPI-anchor amidated alanine Potential

Glycosylation

104

1

N-linked (GlcNAc...) Potential

Glycosylation

115

1

N-linked (GlcNAc...) Potential

Glycosylation

152

1

N-linked (GlcNAc...) Potential

Glycosylation

182

1

N-linked (GlcNAc...) Potential

Glycosylation

197

1

N-linked (GlcNAc...) Potential

Glycosylation

204

1

N-linked (GlcNAc...) Potential

Glycosylation

208

1

N-linked (GlcNAc...) Potential

Glycosylation

246

1

N-linked (GlcNAc...) Ref.9

Glycosylation

256

1

N-linked (GlcNAc...) Potential

Glycosylation

274

1

N-linked (GlcNAc...) Potential

Glycosylation

288

1

N-linked (GlcNAc...) Potential

Glycosylation

292

1

N-linked (GlcNAc...) Potential

Glycosylation

309

1

N-linked (GlcNAc...) Potential

Glycosylation

330

1

N-linked (GlcNAc...) Potential

Glycosylation

351

1

N-linked (GlcNAc...) Potential

Glycosylation

360

1

N-linked (GlcNAc...) Potential

Glycosylation

375

1

N-linked (GlcNAc...) Potential

Glycosylation

432

1

N-linked (GlcNAc...) Potential

Glycosylation

466

1

N-linked (GlcNAc...) Potential

Glycosylation

480

1

N-linked (GlcNAc...) Potential

Glycosylation

508

1

N-linked (GlcNAc...) Potential

Glycosylation

529

1

N-linked (GlcNAc...) Potential

Glycosylation

553

1

N-linked (GlcNAc...) Potential

Glycosylation

560

1

N-linked (GlcNAc...) Ref.8

Glycosylation

580

1

N-linked (GlcNAc...) Potential

Glycosylation

612

1

N-linked (GlcNAc...) Potential

Glycosylation

650

1

N-linked (GlcNAc...) Potential

Glycosylation

665

1

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

80

1

I → V.
Corresponds to variant rs12971352 [ dbSNP | Ensembl ].

VAR_061310

Natural variant

83

1

V → A.
Corresponds to variant rs28683503 [ dbSNP | Ensembl ].

VAR_061311

Natural variant

137

1

Q → P.
Corresponds to variant rs3815780 [ dbSNP | Ensembl ].

VAR_056028

Natural variant

340

1

A → D.
Corresponds to variant rs10407503 [ dbSNP | Ensembl ].

VAR_031091

Natural variant

398

1

K → E. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6
Corresponds to variant rs7249230 [ dbSNP | Ensembl ].

VAR_024493

Natural variant

664

1

R → S.
Corresponds to variant rs10423171 [ dbSNP | Ensembl ].

VAR_031092

Natural variant

678

1

G → R.
Corresponds to variant rs11545767 [ dbSNP | Ensembl ].

VAR_056029

Experimental info

Mutagenesis

63

1

F → I: No effect on dimerization. Reduced affinity for E.coli Dr adhesins. Ref.11

Mutagenesis

63

1

F → R: Abolishes dimerization. Reduced affinity for E.coli Dr adhesins. Ref.11

Mutagenesis

66

1

S → N: Abolishes dimerization. Ref.7 Ref.11

Mutagenesis

68

1

Y → A: Abolishes dimerization. Ref.7

Mutagenesis

68

1

Y → F: No effect on dimerization. Ref.7

Mutagenesis

69

1

K → A: Abolishes dimerization. Ref.7

Mutagenesis

73

1

V → A: Abolishes dimerization. Ref.11

Mutagenesis

74

1

D → A: No effect on dimerization. Ref.11

Mutagenesis

74

1

D → L or R: Abolishes dimerization. Ref.11

Mutagenesis

78

1

Q → L or R: Abolishes dimerization. Reduced affinity for E.coli Dr adhesins. Ref.7 Ref.11

Mutagenesis

125

1

I → A: Abolishes dimerization. Reduced affinity for E.coli Dr adhesins. Ref.11

Mutagenesis

129

1

L → A or C: No effect on dimerization. Reduced affinity for E.coli Dr adhesins. Ref.11

Mutagenesis

129

1

L → S: Abolishes dimerization. Reduced affinity for E.coli Dr adhesins. Ref.11

Mutagenesis

133

1

E → A: Abolishes dimerization. Ref.11

Sequence conflict

320

1

Missing in CAA34474. Ref.5

Sequence conflict

641

1

F → L in AAA62835. Ref.3

Sequence conflict

646

1

T → Q in AAA62835. Ref.3

Sequence conflict

689

1

V → A in AAA62835. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

702

Helix Strand Turn

Details...

Beta strand

37 – 46

10

Beta strand

51 – 57

7

Beta strand

60 – 72

13

Helix

75 – 77

3

Beta strand

78 – 83

6

Turn

84 – 87

4

Beta strand

88 – 91

4

Beta strand

99 – 101

3

Beta strand

107 – 109

3

Helix

114 – 116

3

Beta strand

118 – 126

9

Beta strand

132 – 141

10

Sequences

	Sequence		Length	Mass (Da)
	P06731 [UniParc]. Last modified January 11, 2011. Version 3. Checksum: 86318E244155DB58	FASTA	702	76,795
	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

References

	« Hide 'large scale' referencesShow '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: 3670312] [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: 3220478] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 2342461] [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. , 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: 15057824] [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: 3814146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-702, 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: 3033671] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 331-702, 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: 10864933] [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: 16740002] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-560, MASS SPECTROMETRY. 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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-246, MASS SPECTROMETRY. 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: 10854848] [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: 18086185] [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

AC008999 Genomic DNA. No translation available.
M59262 , 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.
M17303 Genomic DNA. Translation: AAB59513.1.
M29540 mRNA. Translation: AAA51967.1.
X16455 mRNA. Translation: CAA34474.1.
M15042 mRNA. Translation: AAA51963.1.
M16234 mRNA. Translation: AAA51972.1.

IPI

IPI00027486.

PIR

A36319.

RefSeq

NP_004354.2. NM_004363.2.

UniGene

Hs.709196.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E07	X-ray	-	A	35-676	[»]
2QSQ	X-ray	1.95	A/B	34-144	[»]
2QST	X-ray	2.90	A/B	34-144	[»]
2VER	NMR	-	N	35-144	[»]

ProteinModelPortal

P06731.

SMR

P06731. Positions 34-677.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-57769N.

IntAct

P06731. 3 interactions.

MINT

MINT-1472001.

STRING

P06731.

Polymorphism databases

DMDM

115940.

Proteomic databases

PRIDE

P06731.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000221992; ENSP00000221992; ENSG00000105388.
ENST00000405816; ENSP00000385072; ENSG00000105388.
ENST00000446434; ENSP00000402431; ENSG00000105388.

GeneID

1048.

KEGG

hsa:1048.

UCSC

uc002orj.1. human.

Organism-specific databases

CTD

1048.

GeneCards

GC19P042212.

H-InvDB

HIX0027513.

HGNC

HGNC:1817. CEACAM5.

HPA

CAB000021.
CAB000022.
CAB002146.
HPA011041.
HPA019758.

MIM

114890. gene.

neXtProt

NX_P06731.

PharmGKB

PA26361.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG19710.

HOVERGEN

HBG007922.

InParanoid

P06731.

OMA

NSKPVED.

OrthoDB

EOG41ZFBV.

PhylomeDB

P06731.

Gene expression databases

ArrayExpress

P06731.

Bgee

P06731.

CleanEx

HS_CEACAM5.

Genevestigator

P06731.

Family and domain databases

InterPro

IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR013151. Immunoglobulin.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 7 hits.

KO

K06499.

Pfam

PF07679. I-set. 2 hits.
PF00047. ig. 3 hits.
PF07686. V-set. 1 hit.
[Graphical view]

SMART

SM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 6 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

4393.

SOURCE

Search...

Entry information

Entry name

CEAM5_HUMAN

Accession

Primary (citable) accession number: P06731

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 11, 2011
Last modified:	January 25, 2012
This is version 123 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.