ID CEA20_MOUSE Reviewed; 577 AA.
AC Q9D2Z1; Q80Y42;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 159.
DE RecName: Full=Carcinoembryonic antigen-related cell adhesion molecule 20 {ECO:0000303|PubMed:16139472};
DE Flags: Precursor;
GN Name=Ceacam20 {ECO:0000303|PubMed:16139472};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|EMBL:BAB31307.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum {ECO:0000312|EMBL:BAB31307.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000312|EMBL:AAH49361.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH49361.1};
RC TISSUE=Colon {ECO:0000312|EMBL:AAH49361.1};
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 [4] {ECO:0000305}
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=16139472; DOI=10.1016/j.ygeno.2005.07.008;
RA Zebhauser R., Kammerer R., Eisenried A., McLellan A., Moore T.,
RA Zimmermann W.;
RT "Identification of a novel group of evolutionarily conserved members within
RT the rapidly diverging murine Cea family.";
RL Genomics 86:566-580(2005).
RN [5] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=25908210; DOI=10.1111/gtc.12247;
RA Kitamura Y., Murata Y., Park J.H., Kotani T., Imada S., Saito Y.,
RA Okazawa H., Azuma T., Matozaki T.;
RT "Regulation by gut commensal bacteria of carcinoembryonic antigen-related
RT cell adhesion molecule expression in the intestinal epithelium.";
RL Genes Cells 20:578-589(2015).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PTPRH AND SYK, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, PHOSPHORYLATION AT TYR-559 AND TYR-570, MUTAGENESIS OF TYR-559
RP AND TYR-570, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=26195794; DOI=10.1073/pnas.1510167112;
RA Murata Y., Kotani T., Supriatna Y., Kitamura Y., Imada S., Kawahara K.,
RA Nishio M., Daniwijaya E.W., Sadakata H., Kusakari S., Mori M., Kanazawa Y.,
RA Saito Y., Okawa K., Takeda-Morishita M., Okazawa H., Ohnishi H., Azuma T.,
RA Suzuki A., Matozaki T.;
RT "Protein tyrosine phosphatase SAP-1 protects against colitis through
RT regulation of CEACAM20 in the intestinal epithelium.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E4264-E4271(2015).
CC -!- FUNCTION: Together with the tyrosine-protein kinase SYK, enhances
CC production of the cytokine CXCL8/IL-8 via the NFKB pathway and may thus
CC have a role in the intestinal immune response.
CC {ECO:0000269|PubMed:26195794}.
CC -!- SUBUNIT: Interacts (via extracellular domain) with PTPRH (via
CC extracellular domain); the interaction dephosphorylates CEACAM20.
CC Interacts (phosphorylated form) with SYK (via SH2 domains); the
CC interaction further enhances CEACAM20 phosphorylation.
CC {ECO:0000269|PubMed:26195794}.
CC -!- SUBCELLULAR LOCATION: Cell projection, microvillus membrane
CC {ECO:0000269|PubMed:25908210, ECO:0000269|PubMed:26195794}; Single-pass
CC type I membrane protein {ECO:0000305}. Apical cell membrane
CC {ECO:0000269|PubMed:25908210, ECO:0000269|PubMed:26195794}; Single-pass
CC type I membrane protein {ECO:0000305}. Note=Colocalizes with PTPRH and
CC CEACAM1 at the apical brush border of intestinal cells.
CC {ECO:0000269|PubMed:25908210, ECO:0000269|PubMed:26195794}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in the small intestine and colon
CC (at protein level) (PubMed:25908210, PubMed:26195794). Minimal
CC expression in other tissues (at protein level) (PubMed:26195794).
CC Highly expressed in cecum, colon, ileum, jejunum, and testis, and also
CC detected at lower levels in salivary gland and thymus
CC (PubMed:16139472). {ECO:0000269|PubMed:16139472,
CC ECO:0000269|PubMed:25908210, ECO:0000269|PubMed:26195794}.
CC -!- INDUCTION: In intestinal epithelium, up-regulated in the presence of
CC Gram-positive commensal gut bacteria. May also be up-regulated by
CC interferon gamma (IFNG) and butyrate (a product of bacterial
CC fermentation). {ECO:0000269|PubMed:25908210}.
CC -!- PTM: Phosphorylated on tyrosine residues by SYK, SRC and FYN in vitro.
CC {ECO:0000269|PubMed:26195794}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. CEA family.
CC {ECO:0000305}.
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DR EMBL; AK018613; BAB31307.1; -; mRNA.
DR EMBL; AC130530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC049361; AAH49361.1; -; mRNA.
DR CCDS; CCDS20919.1; -.
DR RefSeq; NP_082115.2; NM_027839.2.
DR AlphaFoldDB; Q9D2Z1; -.
DR SMR; Q9D2Z1; -.
DR STRING; 10090.ENSMUSP00000092344; -.
DR GlyCosmos; Q9D2Z1; 3 sites, No reported glycans.
DR GlyGen; Q9D2Z1; 4 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9D2Z1; -.
DR PhosphoSitePlus; Q9D2Z1; -.
DR PaxDb; 10090-ENSMUSP00000092344; -.
DR ProteomicsDB; 281167; -.
DR Antibodypedia; 72273; 25 antibodies from 12 providers.
DR DNASU; 71601; -.
DR Ensembl; ENSMUST00000094753.6; ENSMUSP00000092344.5; ENSMUSG00000070777.6.
DR GeneID; 71601; -.
DR KEGG; mmu:71601; -.
DR UCSC; uc012fbl.1; mouse.
DR AGR; MGI:1918851; -.
DR CTD; 125931; -.
DR MGI; MGI:1918851; Ceacam20.
DR VEuPathDB; HostDB:ENSMUSG00000070777; -.
DR eggNOG; ENOG502RXPD; Eukaryota.
DR GeneTree; ENSGT01100000263479; -.
DR HOGENOM; CLU_032483_0_0_1; -.
DR InParanoid; Q9D2Z1; -.
DR OMA; IYCTAAN; -.
DR OrthoDB; 3033616at2759; -.
DR PhylomeDB; Q9D2Z1; -.
DR TreeFam; TF331199; -.
DR BioGRID-ORCS; 71601; 2 hits in 78 CRISPR screens.
DR ChiTaRS; Ceacam20; mouse.
DR PRO; PR:Q9D2Z1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9D2Z1; Protein.
DR Bgee; ENSMUSG00000070777; Expressed in animal zygote and 25 other cell types or tissues.
DR ExpressionAtlas; Q9D2Z1; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0031528; C:microvillus membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IBA:GO_Central.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0001819; P:positive regulation of cytokine production; IDA:UniProtKB.
DR GO; GO:0002682; P:regulation of immune system process; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00096; Ig; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR PANTHER; PTHR44427; CARCINOEMBRYONIC ANTIGEN-RELATED CELL ADHESION MOLECULE 19; 1.
DR PANTHER; PTHR44427:SF7; CARCINOEMBRYONIC ANTIGEN-RELATED CELL ADHESION MOLECULE 20; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13927; Ig_3; 3.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; Immunoglobulin; 4.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..577
FT /note="Carcinoembryonic antigen-related cell adhesion
FT molecule 20"
FT /id="PRO_5007716426"
FT TOPO_DOM 31..430
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 452..577
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 48..137
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 142..223
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 239..324
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 329..415
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 461..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..549
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 559
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:26195794"
FT MOD_RES 570
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:26195794"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 72..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 259..307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 358..399
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 559
FT /note="Y->F: Abolishes tyrosine phosphorylation and
FT interaction with SYK; when associated with F-570."
FT /evidence="ECO:0000269|PubMed:26195794"
FT MUTAGEN 570
FT /note="Y->F: Abolishes tyrosine phosphorylation and
FT interaction with SYK; when associated with F-559."
FT /evidence="ECO:0000269|PubMed:26195794"
FT CONFLICT 8
FT /note="C -> G (in Ref. 3; AAH49361)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="T -> I (in Ref. 3; AAH49361)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="P -> L (in Ref. 3; AAH49361)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 577 AA; 63444 MW; C3470C7B60F8BB2B CRC64;
MELAGFHCCS WTVILLSALL PTTWRPPAAA HFIHRADLLS NTQMERAPLA KLTLTVNQST
VTEQREMAVF YCNTNADNIT IHWVSNNSLL VLNERMKLSA DNKTLTILIV QREDSGSYLC
EVQHGFEVQR SNTASLTVNY GPDPVSIKLD SGVAAGDVVE VMEGNTVNFR VEAQSSPVPA
YAWYLPSDFI QPPTTGTFTI DAVSREHEGM YRCLVSNPVT NLSRLGVVKV QVLEKVTAPN
IEFPTLALVE NATSVTLTCK TSHQRVGVHW FLKGQPLRPS DRLTLSSQNR TLTIHGLQRD
DIGPYECEVW NWGSQARSVP LKLTINYGPD QVEITQGPAS GVVSTIEAML NSSLTLYCRA
DSIPGARYQW THEHSSKVLD GEQLSIEALR QEHQGIYSCT SSNDVTGLAR SASVLVMVVG
LQSSSMSPGA IAGIVIGILV AIALAIGLGY FLYSTKDRWT RRRSASDTTS SNTIPPTSVM
QSTPESRHNK PMTVYDNTPK PEGEARGKKM WSLPRDSPEQ FYEKKPPSAA PEGPRKPLPQ
IPKQPLMPPG PGRNEESNYE KLLNSNHSLY CKITPSA
//
