CEA20_HUMAN
ID CEA20_HUMAN Reviewed; 596 AA.
AC Q6UY09; A0A087WXE1; A0A087WYH6; A0A087WYM6; A0A087WZX4; A0A087X155; A7LFK7;
AC A7LFK8; A7LFK9; A7LFL0;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Carcinoembryonic antigen-related cell adhesion molecule 20 {ECO:0000312|HGNC:HGNC:24879};
DE Flags: Precursor;
GN Name=CEACAM20 {ECO:0000312|HGNC:HGNC:24879};
GN ORFNames=UNQ9366/PRO34155 {ECO:0000312|HGNC:HGNC:24879};
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] (ISOFORMS 1; 2; 3 AND 4), AND VARIANTS LEU-355
RP AND CYS-512.
RC TISSUE=Small intestine;
RA Paptistella M., Eisenried A., Kammerer R., Zimmermann W.;
RT "Cloning of new carcinoembryonic antigen (CEA) family members.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANT CYS-512.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
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).
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:0000250|UniProtKB:Q9D2Z1}.
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:0000250|UniProtKB:Q9D2Z1}.
CC -!- SUBCELLULAR LOCATION: Cell projection, microvillus membrane
CC {ECO:0000250|UniProtKB:Q9D2Z1}; Single-pass type I membrane protein
CC {ECO:0000305}. Apical cell membrane {ECO:0000250|UniProtKB:Q9D2Z1};
CC Single-pass type I membrane protein {ECO:0000305}. Note=Colocalizes
CC with PTPRH and CEACAM1 at the apical brush border of intestinal cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q6UY09-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6UY09-2; Sequence=VSP_059368;
CC Name=3;
CC IsoId=Q6UY09-3; Sequence=VSP_059367;
CC Name=4;
CC IsoId=Q6UY09-4; Sequence=VSP_059367, VSP_059368;
CC Name=5;
CC IsoId=Q6UY09-5; Sequence=VSP_059369;
CC -!- PTM: Phosphorylated on tyrosine residues by SYK, SRC and FYN in vitro.
CC {ECO:0000250|UniProtKB:Q9D2Z1}.
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; EU008600; ABS57247.1; -; mRNA.
DR EMBL; EU008601; ABS57248.1; -; mRNA.
DR EMBL; EU008602; ABS57249.1; -; mRNA.
DR EMBL; EU008603; ABS57250.1; -; mRNA.
DR EMBL; AY358129; AAQ88496.1; -; mRNA.
DR EMBL; AC245748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS74390.1; -. [Q6UY09-4]
DR CCDS; CCDS74391.1; -. [Q6UY09-3]
DR CCDS; CCDS74392.1; -. [Q6UY09-2]
DR CCDS; CCDS74393.1; -. [Q6UY09-1]
DR RefSeq; NP_001096067.2; NM_001102597.2. [Q6UY09-1]
DR RefSeq; NP_001096068.2; NM_001102598.2. [Q6UY09-4]
DR RefSeq; NP_001096069.2; NM_001102599.2. [Q6UY09-3]
DR RefSeq; NP_001096070.2; NM_001102600.2. [Q6UY09-2]
DR AlphaFoldDB; Q6UY09; -.
DR SMR; Q6UY09; -.
DR STRING; 9606.ENSP00000481937; -.
DR GlyGen; Q6UY09; 7 sites.
DR iPTMnet; Q6UY09; -.
DR PhosphoSitePlus; Q6UY09; -.
DR BioMuta; CEACAM20; -.
DR DMDM; 73619948; -.
DR MassIVE; Q6UY09; -.
DR PeptideAtlas; Q6UY09; -.
DR PRIDE; Q6UY09; -.
DR Antibodypedia; 72273; 21 antibodies from 9 providers.
DR DNASU; 125931; -.
DR Ensembl; ENST00000611497.4; ENSP00000483912.1; ENSG00000273777.6. [Q6UY09-2]
DR Ensembl; ENST00000614577.4; ENSP00000482943.1; ENSG00000273777.6. [Q6UY09-3]
DR Ensembl; ENST00000614924.5; ENSP00000481937.1; ENSG00000273777.6. [Q6UY09-1]
DR Ensembl; ENST00000620096.4; ENSP00000481812.1; ENSG00000273777.6. [Q6UY09-4]
DR Ensembl; ENST00000621342.4; ENSP00000480940.1; ENSG00000273777.6. [Q6UY09-5]
DR GeneID; 125931; -.
DR KEGG; hsa:125931; -.
DR MANE-Select; ENST00000614924.5; ENSP00000481937.1; NM_001102597.3; NP_001096067.2.
DR CTD; 125931; -.
DR DisGeNET; 125931; -.
DR GeneCards; CEACAM20; -.
DR HGNC; HGNC:24879; CEACAM20.
DR HPA; ENSG00000273777; Tissue enriched (intestine).
DR neXtProt; NX_Q6UY09; -.
DR OpenTargets; ENSG00000273777; -.
DR PharmGKB; PA142672134; -.
DR VEuPathDB; HostDB:ENSG00000273777; -.
DR eggNOG; ENOG502RXPD; Eukaryota.
DR GeneTree; ENSGT00960000186634; -.
DR InParanoid; Q6UY09; -.
DR OMA; FKWINGS; -.
DR OrthoDB; 998214at2759; -.
DR PhylomeDB; Q6UY09; -.
DR PathwayCommons; Q6UY09; -.
DR BioGRID-ORCS; 125931; 8 hits in 198 CRISPR screens.
DR ChiTaRS; CEACAM20; human.
DR GenomeRNAi; 125931; -.
DR Pharos; Q6UY09; Tdark.
DR PRO; PR:Q6UY09; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q6UY09; protein.
DR Bgee; ENSG00000273777; Expressed in duodenum and 25 other tissues.
DR ExpressionAtlas; Q6UY09; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
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; IEA:Ensembl.
DR GO; GO:0002682; P:regulation of immune system process; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 4.
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 SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Cell projection; Disulfide bond;
KW Glycoprotein; Immunity; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..596
FT /note="Carcinoembryonic antigen-related cell adhesion
FT molecule 20"
FT /id="PRO_0000014577"
FT TOPO_DOM 31..450
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 472..585
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 58..154
FT /note="Ig-like C2-type 1"
FT DOMAIN 160..246
FT /note="Ig-like C2-type 2"
FT DOMAIN 256..341
FT /note="Ig-like C2-type 3"
FT DOMAIN 346..432
FT /note="Ig-like C2-type 4"
FT REGION 477..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 578
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9D2Z1"
FT MOD_RES 589
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9D2Z1"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 90..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 276..324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 375..416
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 344..437
FT /note="YGPDQVHITRESASEMISTIEAELNSSLTLQCWAESKPGAEYRWTLEHSTGE
FT HLGEQLIIRALTWEHDGIYNCTASNSLTGLARSTSVLVKVVG -> C (in isoform
FT 3 and isoform 4)"
FT /id="VSP_059367"
FT VAR_SEQ 526..537
FT /note="Missing (in isoform 2 and isoform 4)"
FT /id="VSP_059368"
FT VAR_SEQ 580..596
FT /note="ELVNPEPNTYIQINPSV -> VLGMQQ (in isoform 5)"
FT /id="VSP_059369"
FT VARIANT 41
FT /note="A -> V (in dbSNP:rs10408247)"
FT /id="VAR_056030"
FT VARIANT 87
FT /note="T -> I (in dbSNP:rs36053277)"
FT /id="VAR_061312"
FT VARIANT 113
FT /note="R -> H (in dbSNP:rs13345196)"
FT /id="VAR_056031"
FT VARIANT 127
FT /note="I -> V (in dbSNP:rs35443082)"
FT /id="VAR_056032"
FT VARIANT 355
FT /note="S -> L (in dbSNP:rs16959164)"
FT /id="VAR_056033"
FT VARIANT 369
FT /note="S -> F (in dbSNP:rs10414398)"
FT /id="VAR_056034"
FT VARIANT 512
FT /note="R -> C (in dbSNP:rs8100718)"
FT /id="VAR_059385"
FT CONFLICT 108
FT /note="I -> V (in Ref. 1; ABS57247/ABS57248/ABS57249/
FT ABS57250)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="S -> P (in Ref. 1; ABS57247)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 596 AA; 65808 MW; 30472CDCEBB2FD28 CRC64;
MGPADSWGHH WMGILLSASL CTVWSPPAAA QLTLNANPLD ATQSEDVVLP VFGTPRTPQI
HGRSRELAKP SIAVSPGTAI EQKDMVTFYC TTKDVNITIH WVSNNLSIVF HERMQLSKDG
KILTILIVQR EDSGTYQCEA RDALLSQRSD PIFLDVKYGP DPVEIKLESG VASGEVVEVM
EGSSMTFLAE TKSHPPCAYT WFLLDSILSH TTRTFTIHAV SREHEGLYRC LVSNSATHLS
SLGTLKVRVL ETLTMPQVVP SSLNLVENAR SVDLTCQTVN QSVNVQWFLS GQPLLPSEHL
QLSADNRTLI IHGLQRNDTG PYACEVWNWG SRARSEPLEL TINYGPDQVH ITRESASEMI
STIEAELNSS LTLQCWAESK PGAEYRWTLE HSTGEHLGEQ LIIRALTWEH DGIYNCTASN
SLTGLARSTS VLVKVVGPQS SSLSSGAIAG IVIGILAVIA VASELGYFLC IRNARRPSRK
TTEDPSHETS QPIPKEEHPT EPSSESLSPE YRNISQLQGR IRVELMQPPD LPEETYETKL
PSASRRGNSF SPWKPPPKPL MPPLRLVSTV PKNMESIYEE LVNPEPNTYI QINPSV
