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 27-MAR-2024, entry version 195. 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 SMR; P40199; -. DR BioGRID; 110760; 37. DR IntAct; P40199; 31. DR STRING; 9606.ENSP00000199764; -. DR GlyCosmos; P40199; 12 sites, No reported glycans. DR GlyGen; P40199; 16 sites, 6 N-linked glycans (3 sites), 1 O-linked glycan (2 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; 9606-ENSP00000199764; -. DR PeptideAtlas; P40199; -. DR ProteomicsDB; 55345; -. DR ABCD; P40199; 5 sequenced antibodies. DR Antibodypedia; 3642; 678 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 AGR; HGNC:1818; -. 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 MalaCards; CEACAM6; -. 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; ENSGT01100000263479; -. DR HOGENOM; CLU_024555_2_0_1; -. DR InParanoid; P40199; -. DR OMA; GDETEWT; -. DR OrthoDB; 3033616at2759; -. 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; 70 hits in 1136 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 152 other cell types or tissues. DR ExpressionAtlas; P40199; baseline and differential. 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:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW. 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 CDD; cd20948; IgC2_CEACAM5-like; 1. DR CDD; cd05740; IgI_hCEACAM_2_4_6_like; 1. DR CDD; cd05774; IgV_CEACAM_D1; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR44427:SF1; CARCINOEMBRYONIC ANTIGEN-RELATED CELL ADHESION MOLECULE 1; 1. DR PANTHER; PTHR44427; CARCINOEMBRYONIC ANTIGEN-RELATED CELL ADHESION MOLECULE 19; 1. DR Pfam; PF13895; Ig_2; 1. DR Pfam; PF13927; Ig_3; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 3. DR SMART; SM00408; IGc2; 2. DR SUPFAM; SSF48726; Immunoglobulin; 3. DR PROSITE; PS50835; IG_LIKE; 2. DR Genevisible; P40199; HS. 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 //