CEAM6_HUMAN
ID CEAM6_HUMAN Reviewed; 344 AA.
AC P40199; Q13774; Q14920; Q53XP7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 4.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Carcinoembryonic antigen-related cell adhesion molecule 6;
DE AltName: Full=Non-specific crossreacting antigen;
DE AltName: Full=Normal cross-reacting antigen;
DE AltName: CD_antigen=CD66c;
DE Flags: Precursor;
GN Name=CEACAM6; Synonyms=NCA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-239.
RX PubMed=3220478; DOI=10.1016/0888-7543(88)90160-7;
RA Barnett T., Goebel S.J., Nothdurft M.A., Elting J.J.;
RT "Carcinoembryonic antigen family: characterization of cDNAs coding for NCA
RT and CEA and suggestion of nonrandom sequence variation in their conserved
RT loop-domains.";
RL Genomics 3:59-66(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung carcinoma;
RX PubMed=3337731; DOI=10.1016/0006-291x(88)90490-1;
RA Tawaragi Y., Oikawa S., Matsuoka Y., Kosaki G., Nakazato H.;
RT "Primary structure of nonspecific crossreacting antigen (NCA), a member of
RT carcinoembryonic antigen (CEA) gene family, deduced from cDNA sequence.";
RL Biochem. Biophys. Res. Commun. 150:89-96(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-239.
RX PubMed=2830274; DOI=10.1016/s0021-9258(18)69055-6;
RA Neumaier M., Zimmermann W., Shively L., Hinoda Y., Riggs A.D.,
RA Shively J.E.;
RT "Characterization of a cDNA clone for the nonspecific cross-reacting
RT antigen (NCA) and a comparison of NCA and carcinoembryonic antigen.";
RL J. Biol. Chem. 263:3202-3207(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 35-49.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2803308; DOI=10.1016/0006-291x(89)91679-3;
RA Oikawa S., Inuzuka C., Kuroki M., Matsuoka Y., Kosaki G., Nakazato H.;
RT "Cell adhesion activity of non-specific cross-reacting antigen (NCA) and
RT carcinoembryonic antigen (CEA) expressed on CHO cell surface: homophilic
RT and heterophilic adhesion.";
RL Biochem. Biophys. Res. Commun. 164:39-45(1989).
RN [11]
RP SUBCELLULAR LOCATION, AND GPI-ANCHOR.
RX PubMed=2317824;
RA Hefta L.J., Schrewe H., Thompson J.A., Oikawa S., Nakazato H.,
RA Shively J.E.;
RT "Expression of complementary DNA and genomic clones for carcinoembryonic
RT antigen and nonspecific cross-reacting antigen in Chinese hamster ovary and
RT mouse fibroblast cells and characterization of the membrane-expressed
RT products.";
RL Cancer Res. 50:2397-2403(1990).
RN [12]
RP FUNCTION, AND DOMAIN.
RX PubMed=2022629; DOI=10.1016/s0021-9258(18)92930-3;
RA Oikawa S., Inuzuka C., Kuroki M., Arakawa F., Matsuoka Y., Kosaki G.,
RA Nakazato H.;
RT "A specific heterotypic cell adhesion activity between members of
RT carcinoembryonic antigen family, W272 and NCA, is mediated by N-domains.";
RL J. Biol. Chem. 266:7995-8001(1991).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=1378450; DOI=10.1083/jcb.118.2.457;
RA Kuijpers T.W., Hoogerwerf M., van der Laan L.J., Nagel G.,
RA van der Schoot C.E., Grunert F., Roos D.;
RT "CD66 nonspecific cross-reacting antigens are involved in neutrophil
RT adherence to cytokine-activated endothelial cells.";
RL J. Cell Biol. 118:457-466(1992).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=8776764; DOI=10.1006/prep.1996.0065;
RA Yamanaka T., Kuroki M., Kinugasa T., Matsuo Y., Matsuoka Y.;
RT "Preparation and characterization of two human carcinoembryonic antigen
RT family proteins of neutrophils, CD66b and c, in silkworm larvae.";
RL Protein Expr. Purif. 7:438-446(1996).
RN [15]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10436421; DOI=10.1159/000030075;
RA Fraengsmyr L., Baranov V., Hammarstroem S.;
RT "Four carcinoembryonic antigen subfamily members, CEA, NCA, BGP and CGM2,
RT selectively expressed in the normal human colonic epithelium, are integral
RT components of the fuzzy coat.";
RL Tumor Biol. 20:277-292(1999).
RN [16]
RP FUNCTION.
RX PubMed=10910050;
RA Ordonez C., Screaton R.A., Ilantzis C., Stanners C.P.;
RT "Human carcinoembryonic antigen functions as a general inhibitor of
RT anoikis.";
RL Cancer Res. 60:3419-3424(2000).
RN [17]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF ALA-55; ASN-61; ARG-62; ILE-63; SER-66
RP AND LEU-78.
RX PubMed=11590190;
RA Kuroki M., Abe H., Imakiirei T., Liao S., Uchida H., Yamauchi Y.,
RA Oikawa S., Kuroki M.;
RT "Identification and comparison of residues critical for cell-adhesion
RT activities of two neutrophil CD66 antigens, CEACAM6 and CEACAM8.";
RL J. Leukoc. Biol. 70:543-550(2001).
RN [18]
RP FUNCTION, AND INDUCTION.
RX PubMed=14724575; DOI=10.1038/sj.onc.1207036;
RA Duxbury M.S., Ito H., Zinner M.J., Ashley S.W., Whang E.E.;
RT "CEACAM6 gene silencing impairs anoikis resistance and in vivo metastatic
RT ability of pancreatic adenocarcinoma cells.";
RL Oncogene 23:465-473(2004).
RN [19]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16204051; DOI=10.1158/0008-5472.can-05-0420;
RA Blumenthal R.D., Hansen H.J., Goldenberg D.M.;
RT "Inhibition of adhesion, invasion, and metastasis by antibodies targeting
RT CEACAM6 (NCA-90) and CEACAM5 (Carcinoembryonic Antigen).";
RL Cancer Res. 65:8809-8817(2005).
RN [20]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-197.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [21]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-224.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [22] {ECO:0007744|PDB:4WHC}
RP X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 34-141 OF HOMODIMER.
RA Prive G.G., Kirouac K.N.;
RT "Human CEACAM6 N-domain.";
RL Submitted (SEP-2014) to the PDB data bank.
RN [23] {ECO:0007744|PDB:4WTZ}
RP X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 34-141 IN COMPLEX WITH CEACAM8.
RA Kirouac K.N., Prive G.G.;
RT "Human CEACAM6-CEACAM8 N-domain heterodimer complex.";
RL Submitted (OCT-2014) to the PDB data bank.
RN [24] {ECO:0007744|PDB:4Y8A, ECO:0007744|PDB:4YIQ}
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 34-141 OF HOMODIMER AND IN
RP COMPLEX WITH CEACAM8, SUBUNIT, GLYCOSYLATION, AND MUTAGENESIS OF ILE-38;
RP LEU-53; GLN-123 AND LEU-129.
RX PubMed=26483485; DOI=10.1073/pnas.1509511112;
RA Bonsor D.A., Gunther S., Beadenkopf R., Beckett D., Sundberg E.J.;
RT "Diverse oligomeric states of CEACAM IgV domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13561-13566(2015).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
CC -!- FUNCTION: Cell surface glycoprotein that plays a role in cell adhesion
CC and tumor progression (PubMed:2803308, PubMed:2022629, PubMed:1378450,
CC PubMed:8776764, PubMed:11590190, PubMed:10910050, PubMed:14724575,
CC PubMed:16204051). Intercellular adhesion occurs in a calcium- and
CC fibronectin-independent manner (PubMed:2022629, PubMed:16204051).
CC Mediates homophilic and heterophilic cell adhesion with other
CC carcinoembryonic antigen-related cell adhesion molecules, such as
CC CEACAM5 and CEACAM8 (PubMed:2803308, PubMed:2022629, PubMed:8776764,
CC PubMed:11590190, PubMed:16204051). Heterophilic interaction with
CC CEACAM8 occurs in activated neutrophils (PubMed:8776764). Plays a role
CC in neutrophil adhesion to cytokine-activated endothelial cells
CC (PubMed:1378450). Plays a role as an oncogene by promoting tumor
CC progression; positively regulates cell migration, cell adhesion to
CC endothelial cells and cell invasion (PubMed:16204051). Also involved in
CC the metastatic cascade process by inducing gain resistance to anoikis
CC of pancreatic adenocarcinoma and colorectal carcinoma cells
CC (PubMed:10910050, PubMed:14724575). {ECO:0000269|PubMed:10910050,
CC ECO:0000269|PubMed:11590190, ECO:0000269|PubMed:1378450,
CC ECO:0000269|PubMed:14724575, ECO:0000269|PubMed:16204051,
CC ECO:0000269|PubMed:2022629, ECO:0000269|PubMed:2803308,
CC ECO:0000269|PubMed:8776764}.
CC -!- SUBUNIT: Homodimer; homodimerizes via its Ig-like V-type domain.
CC Heterodimer with CEACAM8; heterodimerizes via its Ig-like V-type
CC domain. {ECO:0000269|PubMed:26483485}.
CC -!- INTERACTION:
CC P40199; Q86U10: ASPG; NbExp=3; IntAct=EBI-4314501, EBI-19946665;
CC P40199; Q16568: CARTPT; NbExp=3; IntAct=EBI-4314501, EBI-4314526;
CC P40199; P13688: CEACAM1; NbExp=2; IntAct=EBI-4314501, EBI-4314481;
CC P40199; P40199: CEACAM6; NbExp=6; IntAct=EBI-4314501, EBI-4314501;
CC P40199; P31997: CEACAM8; NbExp=5; IntAct=EBI-4314501, EBI-4314540;
CC P40199; Q99828: CIB1; NbExp=3; IntAct=EBI-4314501, EBI-372594;
CC P40199; P33240: CSTF2; NbExp=3; IntAct=EBI-4314501, EBI-711360;
CC P40199; Q86VI1: EXOC3L1; NbExp=3; IntAct=EBI-4314501, EBI-2813180;
CC P40199; O75593: FOXH1; NbExp=3; IntAct=EBI-4314501, EBI-1759806;
CC P40199; O75603: GCM2; NbExp=3; IntAct=EBI-4314501, EBI-10188645;
CC P40199; O95872: GPANK1; NbExp=3; IntAct=EBI-4314501, EBI-751540;
CC P40199; O14964: HGS; NbExp=3; IntAct=EBI-4314501, EBI-740220;
CC P40199; Q9UM19: HPCAL4; NbExp=3; IntAct=EBI-4314501, EBI-744820;
CC P40199; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-4314501, EBI-2556193;
CC P40199; Q4VC12: MSS51; NbExp=5; IntAct=EBI-4314501, EBI-11599933;
CC P40199; Q9NP98: MYOZ1; NbExp=3; IntAct=EBI-4314501, EBI-744402;
CC P40199; P78337: PITX1; NbExp=3; IntAct=EBI-4314501, EBI-748265;
CC P40199; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-4314501, EBI-11956563;
CC P40199; Q2TAL8: QRICH1; NbExp=3; IntAct=EBI-4314501, EBI-2798044;
CC P40199; Q9BQY4: RHOXF2; NbExp=3; IntAct=EBI-4314501, EBI-372094;
CC P40199; Q92529: SHC3; NbExp=3; IntAct=EBI-4314501, EBI-79084;
CC P40199; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-4314501, EBI-358489;
CC P40199; O43711: TLX3; NbExp=3; IntAct=EBI-4314501, EBI-3939165;
CC P40199; P22105-1: TNXB; NbExp=3; IntAct=EBI-4314501, EBI-20753895;
CC P40199; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-4314501, EBI-947187;
CC P40199; O95231: VENTX; NbExp=3; IntAct=EBI-4314501, EBI-10191303;
CC P40199; Q14119: VEZF1; NbExp=3; IntAct=EBI-4314501, EBI-11980193;
CC P40199; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-4314501, EBI-12040603;
CC P40199; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-4314501, EBI-746595;
CC P40199; P36508: ZNF76; NbExp=3; IntAct=EBI-4314501, EBI-7254550;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:2317824}. Apical cell membrane
CC {ECO:0000269|PubMed:10436421}. Cell surface
CC {ECO:0000269|PubMed:1378450, ECO:0000269|PubMed:16204051,
CC ECO:0000269|PubMed:2317824, ECO:0000269|PubMed:8776764,
CC ECO:0000305|PubMed:2803308}. Note=Localized to the apical glycocalyx
CC surface. {ECO:0000269|PubMed:10436421}.
CC -!- TISSUE SPECIFICITY: Expressed in neutrophils (PubMed:1378450).
CC Expressed in columnar epithelial and goblet cells of the colon
CC (PubMed:10436421). Expressed in numerous tumor cell lines (at protein
CC level) (PubMed:16204051). {ECO:0000269|PubMed:10436421,
CC ECO:0000269|PubMed:1378450, ECO:0000269|PubMed:16204051}.
CC -!- INDUCTION: Up-regulated in anoikis-resistant pancreatic adenocarcinoma
CC cells (at protein level). {ECO:0000269|PubMed:14724575}.
CC -!- DOMAIN: The extracellular N-terminus Ig-like V-type domain is necessary
CC for homophilic and heterophilic intercellular adhesion.
CC {ECO:0000269|PubMed:11590190, ECO:0000269|PubMed:2022629,
CC ECO:0000269|PubMed:8776764}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:26483485}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. CEA family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M29541; AAA59915.1; -; mRNA.
DR EMBL; M18728; AAA59907.1; -; mRNA.
DR EMBL; M18216; AAA51739.1; -; mRNA.
DR EMBL; BT009774; AAP88776.1; -; mRNA.
DR EMBL; AK312542; BAG35441.1; -; mRNA.
DR EMBL; AC011513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471126; EAW57061.1; -; Genomic_DNA.
DR EMBL; BC005008; AAH05008.1; -; mRNA.
DR CCDS; CCDS12585.1; -.
DR RefSeq; NP_002474.4; NM_002483.6.
DR PDB; 4WHC; X-ray; 2.71 A; A/B=34-141.
DR PDB; 4WTZ; X-ray; 2.52 A; A/B/C/D/E/F=34-141.
DR PDB; 4Y8A; X-ray; 1.83 A; A/B=34-141.
DR PDB; 4YIQ; X-ray; 1.85 A; B/D=34-141.
DR PDBsum; 4WHC; -.
DR PDBsum; 4WTZ; -.
DR PDBsum; 4Y8A; -.
DR PDBsum; 4YIQ; -.
DR AlphaFoldDB; P40199; -.
DR BioGRID; 110760; 36.
DR IntAct; P40199; 31.
DR STRING; 9606.ENSP00000199764; -.
DR GlyGen; P40199; 14 sites.
DR iPTMnet; P40199; -.
DR PhosphoSitePlus; P40199; -.
DR BioMuta; CEACAM6; -.
DR DMDM; 296439410; -.
DR EPD; P40199; -.
DR jPOST; P40199; -.
DR MassIVE; P40199; -.
DR MaxQB; P40199; -.
DR PaxDb; P40199; -.
DR PeptideAtlas; P40199; -.
DR PRIDE; P40199; -.
DR ProteomicsDB; 55345; -.
DR ABCD; P40199; 5 sequenced antibodies.
DR Antibodypedia; 3642; 553 antibodies from 34 providers.
DR DNASU; 4680; -.
DR Ensembl; ENST00000199764.7; ENSP00000199764.6; ENSG00000086548.9.
DR GeneID; 4680; -.
DR KEGG; hsa:4680; -.
DR MANE-Select; ENST00000199764.7; ENSP00000199764.6; NM_002483.7; NP_002474.4.
DR UCSC; uc032hyc.2; human.
DR CTD; 4680; -.
DR DisGeNET; 4680; -.
DR GeneCards; CEACAM6; -.
DR HGNC; HGNC:1818; CEACAM6.
DR HPA; ENSG00000086548; Tissue enhanced (bone marrow, esophagus, intestine, lung, salivary gland).
DR MIM; 163980; gene.
DR neXtProt; NX_P40199; -.
DR OpenTargets; ENSG00000086548; -.
DR Orphanet; 586; Cystic fibrosis.
DR PharmGKB; PA26362; -.
DR VEuPathDB; HostDB:ENSG00000086548; -.
DR eggNOG; ENOG502RXPD; Eukaryota.
DR GeneTree; ENSGT00960000186634; -.
DR HOGENOM; CLU_024555_2_0_1; -.
DR InParanoid; P40199; -.
DR OrthoDB; 998214at2759; -.
DR PhylomeDB; P40199; -.
DR TreeFam; TF336859; -.
DR PathwayCommons; P40199; -.
DR Reactome; R-HSA-1566977; Fibronectin matrix formation.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P40199; -.
DR BioGRID-ORCS; 4680; 68 hits in 1056 CRISPR screens.
DR ChiTaRS; CEACAM6; human.
DR GeneWiki; CEACAM6; -.
DR GenomeRNAi; 4680; -.
DR Pharos; P40199; Tbio.
DR PRO; PR:P40199; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P40199; protein.
DR Bgee; ENSG00000086548; Expressed in pancreatic ductal cell and 151 other tissues.
DR ExpressionAtlas; P40199; baseline and differential.
DR Genevisible; P40199; HS.
DR GO; GO:0031225; C:anchored component of membrane; IDA:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IMP:UniProtKB.
DR GO; GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:BHF-UCL.
DR GO; GO:1904906; P:positive regulation of endothelial cell-matrix adhesion via fibronectin; IMP:UniProtKB.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Cell adhesion; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Oncogene; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 35..320
FT /note="Carcinoembryonic antigen-related cell adhesion
FT molecule 6"
FT /id="PRO_0000014568"
FT PROPEP 321..344
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000014569"
FT DOMAIN 35..142
FT /note="Ig-like V-type"
FT /evidence="ECO:0000250|UniProtKB:P31997"
FT DOMAIN 145..232
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 240..314
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT LIPID 320
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000250|UniProtKB:P31997"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:16740002"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 167..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 259..299
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 239
FT /note="V -> G (in dbSNP:rs11548735)"
FT /evidence="ECO:0000269|PubMed:2830274,
FT ECO:0000269|PubMed:3220478"
FT /id="VAR_034680"
FT MUTAGEN 38
FT /note="I->A: Loss of homodimerization and
FT heterodimerization with CEACAM8."
FT /evidence="ECO:0000269|PubMed:26483485"
FT MUTAGEN 53
FT /note="L->A: No effect on homodimerization. Reduces
FT heterodimerization with CEACAM8."
FT /evidence="ECO:0000269|PubMed:26483485"
FT MUTAGEN 55
FT /note="A->V: No effect on homophilic and heterophilic cell
FT adhesion."
FT /evidence="ECO:0000269|PubMed:11590190"
FT MUTAGEN 61
FT /note="N->H: Inhibits homophilic and heterophilic cell
FT adhesion."
FT /evidence="ECO:0000269|PubMed:11590190"
FT MUTAGEN 62
FT /note="R->L: No effect on homophilic cell adhesion. Reduces
FT heterophilic cell adhesion."
FT /evidence="ECO:0000269|PubMed:11590190"
FT MUTAGEN 63
FT /note="I->F: No effect on homophilic cell adhesion.
FT Inhibits heterophilic cell adhesion."
FT /evidence="ECO:0000269|PubMed:11590190"
FT MUTAGEN 66
FT /note="S->N: Inhibits homophilic cell adhesion. Reduces
FT heterophilic cell adhesion."
FT /evidence="ECO:0000269|PubMed:11590190"
FT MUTAGEN 78
FT /note="L->Q: Inhibits homophilic cell adhesion. No effect
FT on heterophilic cell adhesion."
FT /evidence="ECO:0000269|PubMed:11590190"
FT MUTAGEN 123
FT /note="Q->A: No effect on homodimerization. Reduces
FT heterodimerization with CEACAM8."
FT /evidence="ECO:0000269|PubMed:26483485"
FT MUTAGEN 129
FT /note="L->A: Reduces homodimerization. Loss of
FT heterodimerization with CEACAM8."
FT /evidence="ECO:0000269|PubMed:26483485"
FT CONFLICT 138
FT /note="F -> L (in Ref. 1; AAA59915)"
FT /evidence="ECO:0000305"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:4Y8A"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:4Y8A"
FT STRAND 62..72
FT /evidence="ECO:0007829|PDB:4Y8A"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:4Y8A"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:4Y8A"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:4Y8A"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:4Y8A"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4Y8A"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:4Y8A"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:4Y8A"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:4Y8A"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:4Y8A"
SQ SEQUENCE 344 AA; 37237 MW; 4322C5D6E25849F5 CRC64;
MGPPSAPPCR LHVPWKEVLL TASLLTFWNP PTTAKLTIES TPFNVAEGKE VLLLAHNLPQ
NRIGYSWYKG ERVDGNSLIV GYVIGTQQAT PGPAYSGRET IYPNASLLIQ NVTQNDTGFY
TLQVIKSDLV NEEATGQFHV YPELPKPSIS SNNSNPVEDK DAVAFTCEPE VQNTTYLWWV
NGQSLPVSPR LQLSNGNMTL TLLSVKRNDA GSYECEIQNP ASANRSDPVT LNVLYGPDVP
TISPSKANYR PGENLNLSCH AASNPPAQYS WFINGTFQQS TQELFIPNIT VNNSGSYMCQ
AHNSATGLNR TTVTMITVSG SAPVLSAVAT VGITIGVLAR VALI
