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Carcinoembryonic antigen-related cell adhesion molecule 6 (Non-specific crossreacting antigen) (Normal cross-reacting antigen) (CD antigen CD66c)

 CEAM6_HUMAN             Reviewed;         344 AA.
P40199; Q13774; Q14920; Q53XP7;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
20-JUN-2018, entry version 165.
RecName: Full=Carcinoembryonic antigen-related cell adhesion molecule 6;
AltName: Full=Non-specific crossreacting antigen;
AltName: Full=Normal cross-reacting antigen;
AltName: CD_antigen=CD66c;
Flags: Precursor;
Name=CEACAM6; Synonyms=NCA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3220478; DOI=10.1016/0888-7543(88)90160-7;
Barnett T., Goebel S.J., Nothdurft M.A., Elting J.J.;
"Carcinoembryonic antigen family: characterization of cDNAs coding for
NCA and CEA and suggestion of nonrandom sequence variation in their
conserved loop-domains.";
Genomics 3:59-66(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-239.
TISSUE=Lung carcinoma;
PubMed=3337731; DOI=10.1016/0006-291X(88)90490-1;
Tawaragi Y., Oikawa S., Matsuoka Y., Kosaki G., Nakazato H.;
"Primary structure of nonspecific crossreacting antigen (NCA), a
member of carcinoembryonic antigen (CEA) gene family, deduced from
cDNA sequence.";
Biochem. Biophys. Res. Commun. 150:89-96(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2830274;
Neumaier M., Zimmermann W., Shively L., Hinoda Y., Riggs A.D.,
Shively J.E.;
"Characterization of a cDNA clone for the nonspecific cross-reacting
antigen (NCA) and a comparison of NCA and carcinoembryonic antigen.";
J. Biol. Chem. 263:3202-3207(1988).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-239.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-239.
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
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.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-239.
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 35-49.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=2803308;
Oikawa S., Inuzuka C., Kuroki M., Matsuoka Y., Kosaki G., Nakazato H.;
"Cell adhesion activity of non-specific cross-reacting antigen (NCA)
and carcinoembryonic antigen (CEA) expressed on CHO cell surface:
homophilic and heterophilic adhesion.";
Biochem. Biophys. Res. Commun. 164:39-45(1989).
[11]
SUBCELLULAR LOCATION, AND GPI-ANCHOR.
PubMed=2317824;
Hefta L.J., Schrewe H., Thompson J.A., Oikawa S., Nakazato H.,
Shively J.E.;
"Expression of complementary DNA and genomic clones for
carcinoembryonic antigen and nonspecific cross-reacting antigen in
Chinese hamster ovary and mouse fibroblast cells and characterization
of the membrane-expressed products.";
Cancer Res. 50:2397-2403(1990).
[12]
FUNCTION, AND DOMAIN.
PubMed=2022629;
Oikawa S., Inuzuka C., Kuroki M., Arakawa F., Matsuoka Y., Kosaki G.,
Nakazato H.;
"A specific heterotypic cell adhesion activity between members of
carcinoembryonic antigen family, W272 and NCA, is mediated by N-
domains.";
J. Biol. Chem. 266:7995-8001(1991).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=1378450;
Kuijpers T.W., Hoogerwerf M., van der Laan L.J., Nagel G.,
van der Schoot C.E., Grunert F., Roos D.;
"CD66 nonspecific cross-reacting antigens are involved in neutrophil
adherence to cytokine-activated endothelial cells.";
J. Cell Biol. 118:457-466(1992).
[14]
FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=8776764; DOI=10.1006/prep.1996.0065;
Yamanaka T., Kuroki M., Kinugasa T., Matsuo Y., Matsuoka Y.;
"Preparation and characterization of two human carcinoembryonic
antigen family proteins of neutrophils, CD66b and c, in silkworm
larvae.";
Protein Expr. Purif. 7:438-446(1996).
[15]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10436421; DOI=10.1159/000030075;
Fraengsmyr L., Baranov V., Hammarstroem S.;
"Four carcinoembryonic antigen subfamily members, CEA, NCA, BGP and
CGM2, selectively expressed in the normal human colonic epithelium,
are integral components of the fuzzy coat.";
Tumor Biol. 20:277-292(1999).
[16]
FUNCTION.
PubMed=10910050;
Ordonez C., Screaton R.A., Ilantzis C., Stanners C.P.;
"Human carcinoembryonic antigen functions as a general inhibitor of
anoikis.";
Cancer Res. 60:3419-3424(2000).
[17]
FUNCTION, DOMAIN, AND MUTAGENESIS OF ALA-55; ASN-61; ARG-62; ILE-63;
SER-66 AND LEU-78.
PubMed=11590190;
Kuroki M., Abe H., Imakiirei T., Liao S., Uchida H., Yamauchi Y.,
Oikawa S., Kuroki M.;
"Identification and comparison of residues critical for cell-adhesion
activities of two neutrophil CD66 antigens, CEACAM6 and CEACAM8.";
J. Leukoc. Biol. 70:543-550(2001).
[18]
FUNCTION, AND INDUCTION.
PubMed=14724575; DOI=10.1038/sj.onc.1207036;
Duxbury M.S., Ito H., Zinner M.J., Ashley S.W., Whang E.E.;
"CEACAM6 gene silencing impairs anoikis resistance and in vivo
metastatic ability of pancreatic adenocarcinoma cells.";
Oncogene 23:465-473(2004).
[19]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16204051; DOI=10.1158/0008-5472.CAN-05-0420;
Blumenthal R.D., Hansen H.J., Goldenberg D.M.;
"Inhibition of adhesion, invasion, and metastasis by antibodies
targeting CEACAM6 (NCA-90) and CEACAM5 (Carcinoembryonic Antigen).";
Cancer Res. 65:8809-8817(2005).
[20]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-197.
TISSUE=Saliva;
PubMed=16740002; DOI=10.1021/pr050492k;
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,
Loo J.A.;
"Identification of N-linked glycoproteins in human saliva by
glycoprotein capture and mass spectrometry.";
J. Proteome Res. 5:1493-1503(2006).
[21]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-224.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[22] {ECO:0000244|PDB:4WHC}
X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 34-141 OF HOMODIMER.
Prive G.G., Kirouac K.N.;
"Human CEACAM6 N-domain.";
Submitted (SEP-2014) to the PDB data bank.
[23] {ECO:0000244|PDB:4WTZ}
X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 34-141 IN COMPLEX WITH
CEACAM8.
Kirouac K.N., Prive G.G.;
"Human CEACAM6-CEACAM8 N-domain heterodimer complex.";
Submitted (OCT-2014) to the PDB data bank.
[24] {ECO:0000244|PDB:4Y8A, ECO:0000244|PDB:4YIQ}
X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 34-141 OF HOMODIMER AND IN
COMPLEX WITH CEACAM8, SUBUNIT, GLYCOSYLATION, AND MUTAGENESIS OF
ILE-38; LEU-53; GLN-123 AND LEU-129.
PubMed=26483485; DOI=10.1073/pnas.1509511112;
Bonsor D.A., Gunther S., Beadenkopf R., Beckett D., Sundberg E.J.;
"Diverse oligomeric states of CEACAM IgV domains.";
Proc. Natl. Acad. Sci. U.S.A. 112:13561-13566(2015).
[25]
VARIANT [LARGE SCALE ANALYSIS] VAL-239, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
-!- FUNCTION: Cell surface glycoprotein that plays a role in cell
adhesion and tumor progression (PubMed:2803308, PubMed:2022629,
PubMed:1378450, PubMed:8776764, PubMed:11590190, PubMed:10910050,
PubMed:14724575, PubMed:16204051). Intercellular adhesion occurs
in a calcium- and fibronectin-independent manner (PubMed:2022629,
PubMed:16204051). Mediates homophilic and heterophilic cell
adhesion with other carcinoembryonic antigen-related cell adhesion
molecules, such as CEACAM5 and CEACAM8 (PubMed:2803308,
PubMed:2022629, PubMed:8776764, PubMed:11590190, PubMed:16204051).
Heterophilic interaction with CEACAM8 occurs in activated
neutrophils (PubMed:8776764). Plays a role in neutrophil adhesion
to cytokine-activated endothelial cells (PubMed:1378450). Plays a
role as an oncogene by promoting tumor progression; positively
regulates cell migration, cell adhesion to endothelial cells and
cell invasion (PubMed:16204051). Also involved in the metastatic
cascade process by inducing gain resistance to anoikis of
pancreatic adenocarcinoma and colorectal carcinoma cells
(PubMed:10910050, PubMed:14724575). {ECO:0000269|PubMed:10910050,
ECO:0000269|PubMed:11590190, ECO:0000269|PubMed:1378450,
ECO:0000269|PubMed:14724575, ECO:0000269|PubMed:16204051,
ECO:0000269|PubMed:2022629, ECO:0000269|PubMed:2803308,
ECO:0000269|PubMed:8776764}.
-!- SUBUNIT: Homodimer; homodimerizes via its Ig-like V-type domain.
Heterodimer with CEACAM8; heterodimerizes via its Ig-like V-type
domain. {ECO:0000269|PubMed:26483485}.
-!- INTERACTION:
Q16568:CARTPT; NbExp=3; IntAct=EBI-4314501, EBI-4314526;
P13688:CEACAM1; NbExp=2; IntAct=EBI-4314501, EBI-4314481;
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor
{ECO:0000269|PubMed:2317824}. Apical cell membrane
{ECO:0000269|PubMed:10436421}. Cell surface
{ECO:0000269|PubMed:1378450, ECO:0000269|PubMed:16204051,
ECO:0000269|PubMed:2317824, ECO:0000269|PubMed:8776764,
ECO:0000305|PubMed:2803308}. Note=Localized to the apical
glycocalyx surface. {ECO:0000269|PubMed:10436421}.
-!- TISSUE SPECIFICITY: Expressed in neutrophils (PubMed:1378450).
Expressed in columnar epithelial and goblet cells of the colon
(PubMed:10436421). Expressed in numerous tumor cell lines (at
protein level) (PubMed:16204051). {ECO:0000269|PubMed:10436421,
ECO:0000269|PubMed:1378450, ECO:0000269|PubMed:16204051}.
-!- INDUCTION: Up-regulated in anoikis-resistant pancreatic
adenocarcinoma cells (at protein level).
{ECO:0000269|PubMed:14724575}.
-!- DOMAIN: The extracellular N-terminus Ig-like V-type domain is
necessary for homophilic and heterophilic intercellular adhesion.
{ECO:0000269|PubMed:11590190, ECO:0000269|PubMed:2022629,
ECO:0000269|PubMed:8776764}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:26483485}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. CEA family.
{ECO:0000305}.
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EMBL; M29541; AAA59915.1; -; mRNA.
EMBL; M18728; AAA59907.1; -; mRNA.
EMBL; M18216; AAA51739.1; -; mRNA.
EMBL; BT009774; AAP88776.1; -; mRNA.
EMBL; AK312542; BAG35441.1; -; mRNA.
EMBL; AC011513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471126; EAW57061.1; -; Genomic_DNA.
EMBL; BC005008; AAH05008.1; -; mRNA.
CCDS; CCDS12585.1; -.
RefSeq; NP_002474.4; NM_002483.6.
UniGene; Hs.466814; -.
PDB; 4WHC; X-ray; 2.71 A; A/B=34-141.
PDB; 4WTZ; X-ray; 2.52 A; A/B/C/D/E/F=34-141.
PDB; 4Y8A; X-ray; 1.83 A; A/B=34-141.
PDB; 4YIQ; X-ray; 1.85 A; B/D=34-141.
PDBsum; 4WHC; -.
PDBsum; 4WTZ; -.
PDBsum; 4Y8A; -.
PDBsum; 4YIQ; -.
ProteinModelPortal; P40199; -.
SMR; P40199; -.
BioGrid; 110760; 7.
IntAct; P40199; 5.
STRING; 9606.ENSP00000199764; -.
iPTMnet; P40199; -.
PhosphoSitePlus; P40199; -.
BioMuta; CEACAM6; -.
DMDM; 296439410; -.
MaxQB; P40199; -.
PaxDb; P40199; -.
PeptideAtlas; P40199; -.
PRIDE; P40199; -.
ProteomicsDB; 55345; -.
DNASU; 4680; -.
Ensembl; ENST00000199764; ENSP00000199764; ENSG00000086548.
GeneID; 4680; -.
KEGG; hsa:4680; -.
UCSC; uc032hyc.2; human.
CTD; 4680; -.
DisGeNET; 4680; -.
EuPathDB; HostDB:ENSG00000086548.8; -.
GeneCards; CEACAM6; -.
HGNC; HGNC:1818; CEACAM6.
HPA; CAB008370; -.
HPA; HPA011041; -.
MIM; 163980; gene.
neXtProt; NX_P40199; -.
PharmGKB; PA26362; -.
eggNOG; ENOG410IFE1; Eukaryota.
eggNOG; ENOG410YR1P; LUCA.
HOGENOM; HOG000233417; -.
HOVERGEN; HBG007922; -.
InParanoid; P40199; -.
KO; K06499; -.
OrthoDB; EOG091G0AMM; -.
PhylomeDB; P40199; -.
TreeFam; TF336859; -.
Reactome; R-HSA-1566977; Fibronectin matrix formation.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; CEACAM6; human.
GeneWiki; CEACAM6; -.
GenomeRNAi; 4680; -.
PRO; PR:P40199; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000086548; -.
CleanEx; HS_CEACAM6; -.
ExpressionAtlas; P40199; baseline and differential.
Genevisible; P40199; HS.
GO; GO:0031225; C:anchored component of membrane; IDA:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:UniProtKB.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IMP:UniProtKB.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:BHF-UCL.
GO; GO:1904906; P:positive regulation of endothelial cell-matrix adhesion via fibronectin; IMP:UniProtKB.
GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IMP:UniProtKB.
GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013106; Ig_V-set.
Pfam; PF13895; Ig_2; 1.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 3.
SMART; SM00408; IGc2; 2.
SUPFAM; SSF48726; SSF48726; 3.
PROSITE; PS50835; IG_LIKE; 2.
1: Evidence at protein level;
3D-structure; Apoptosis; Cell adhesion; Cell membrane;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; GPI-anchor; Immunoglobulin domain; Lipoprotein;
Membrane; Oncogene; Polymorphism; Reference proteome; Repeat; Signal.
SIGNAL 1 34 {ECO:0000269|PubMed:15340161}.
CHAIN 35 320 Carcinoembryonic antigen-related cell
adhesion molecule 6.
/FTId=PRO_0000014568.
PROPEP 321 344 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000014569.
DOMAIN 35 142 Ig-like V-type.
{ECO:0000250|UniProtKB:P31997}.
DOMAIN 145 232 Ig-like C2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
DOMAIN 240 314 Ig-like C2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
LIPID 320 320 GPI-anchor amidated glycine.
{ECO:0000250|UniProtKB:P31997}.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 111 111 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 115 115 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 152 152 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 173 173 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 197 197 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498,
ECO:0000269|PubMed:16740002}.
CARBOHYD 224 224 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498,
ECO:0000269|PubMed:19159218}.
CARBOHYD 256 256 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 274 274 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 288 288 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 292 292 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 309 309 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 167 215 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 259 299 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VARIANT 239 239 G -> V (in dbSNP:rs11548735).
{ECO:0000244|PubMed:18318008,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:3337731,
ECO:0000269|Ref.4}.
/FTId=VAR_034680.
MUTAGEN 38 38 I->A: Loss of homodimerization and
heterodimerization with CEACAM8.
{ECO:0000269|PubMed:26483485}.
MUTAGEN 53 53 L->A: No effect on homodimerization.
Reduces heterodimerization with CEACAM8.
{ECO:0000269|PubMed:26483485}.
MUTAGEN 55 55 A->V: No effect on homophilic and
heterophilic cell adhesion.
{ECO:0000269|PubMed:11590190}.
MUTAGEN 61 61 N->H: Inhibits homophilic and
heterophilic cell adhesion.
{ECO:0000269|PubMed:11590190}.
MUTAGEN 62 62 R->L: No effect on homophilic cell
adhesion. Reduces heterophilic cell
adhesion. {ECO:0000269|PubMed:11590190}.
MUTAGEN 63 63 I->F: No effect on homophilic cell
adhesion. Inhibits heterophilic cell
adhesion. {ECO:0000269|PubMed:11590190}.
MUTAGEN 66 66 S->N: Inhibits homophilic cell adhesion.
Reduces heterophilic cell adhesion.
{ECO:0000269|PubMed:11590190}.
MUTAGEN 78 78 L->Q: Inhibits homophilic cell adhesion.
No effect on heterophilic cell adhesion.
{ECO:0000269|PubMed:11590190}.
MUTAGEN 123 123 Q->A: No effect on homodimerization.
Reduces heterodimerization with CEACAM8.
{ECO:0000269|PubMed:26483485}.
MUTAGEN 129 129 L->A: Reduces homodimerization. Loss of
heterodimerization with CEACAM8.
{ECO:0000269|PubMed:26483485}.
CONFLICT 138 138 F -> L (in Ref. 1; AAA59915).
{ECO:0000305}.
STRAND 37 45 {ECO:0000244|PDB:4Y8A}.
STRAND 51 57 {ECO:0000244|PDB:4Y8A}.
STRAND 62 72 {ECO:0000244|PDB:4Y8A}.
HELIX 75 77 {ECO:0000244|PDB:4Y8A}.
STRAND 78 83 {ECO:0000244|PDB:4Y8A}.
TURN 84 87 {ECO:0000244|PDB:4Y8A}.
STRAND 88 91 {ECO:0000244|PDB:4Y8A}.
STRAND 99 101 {ECO:0000244|PDB:4Y8A}.
STRAND 107 109 {ECO:0000244|PDB:4Y8A}.
HELIX 114 116 {ECO:0000244|PDB:4Y8A}.
STRAND 118 126 {ECO:0000244|PDB:4Y8A}.
STRAND 132 140 {ECO:0000244|PDB:4Y8A}.
SEQUENCE 344 AA; 37195 MW; 28469487A74C18A4 CRC64;
MGPPSAPPCR LHVPWKEVLL TASLLTFWNP PTTAKLTIES TPFNVAEGKE VLLLAHNLPQ
NRIGYSWYKG ERVDGNSLIV GYVIGTQQAT PGPAYSGRET IYPNASLLIQ NVTQNDTGFY
TLQVIKSDLV NEEATGQFHV YPELPKPSIS SNNSNPVEDK DAVAFTCEPE VQNTTYLWWV
NGQSLPVSPR LQLSNGNMTL TLLSVKRNDA GSYECEIQNP ASANRSDPVT LNVLYGPDGP
TISPSKANYR PGENLNLSCH AASNPPAQYS WFINGTFQQS TQELFIPNIT VNNSGSYMCQ
AHNSATGLNR TTVTMITVSG SAPVLSAVAT VGITIGVLAR VALI


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