CEAM4_HUMAN
ID CEAM4_HUMAN Reviewed; 244 AA.
AC O75871; Q03715; Q7LDZ7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1999, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Carcinoembryonic antigen-related cell adhesion molecule 4;
DE Short=CEA cell adhesion molecule 4;
DE AltName: Full=Carcinoembryonic antigen CGM7;
DE AltName: Full=Non-specific cross-reacting antigen W236;
DE Flags: Precursor;
GN Name=CEACAM4; Synonyms=CGM7;
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], GLYCOSYLATION, TISSUE SPECIFICITY, AND VARIANT
RP ASP-29.
RX PubMed=2050678; DOI=10.1016/s0021-9258(18)99029-0;
RA Kuroki M., Arakawa F., Matsuo Y., Oikawa S., Misumi Y., Nakazato H.,
RA Matsuoka Y.;
RT "Molecular cloning of nonspecific cross-reacting antigens in human
RT granulocytes.";
RL J. Biol. Chem. 266:11810-11817(1991).
RN [2]
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 [3]
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 [4]
RP FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF TYR-222 AND TYR-233.
RX PubMed=25567962; DOI=10.1189/jlb.2ab0813-449rr;
RA Delgado Tascon J., Adrian J., Kopp K., Scholz P., Tschan M.P., Kuespert K.,
RA Hauck C.R.;
RT "The granulocyte orphan receptor CEACAM4 is able to trigger phagocytosis of
RT bacteria.";
RL J. Leukoc. Biol. 97:521-531(2015).
CC -!- FUNCTION: Granulocyte orphan receptor that acts as an trigger efficient
CC phagocytosis of attached particles. {ECO:0000269|PubMed:25567962}.
CC -!- SUBUNIT: Interacts through its phosphorylated ITAM domain with the SH2
CC domain-containing cytoplasmic proteins involved in signaling processes
CC during phagocytosis. {ECO:0000269|PubMed:25567962}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Granulocytes. {ECO:0000269|PubMed:2050678}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:2050678}.
CC -!- PTM: The cytoplasmic ITAM-like sequence becomes tyrosine phosphorylated
CC by SRC family PTKs upon ligand-mediated receptor clustering and allows
CC to initiate phagocytosis of bound ligand.
CC {ECO:0000269|PubMed:25567962}.
CC -!- MISCELLANEOUS: To study the function of the orphan receptor CEACAM4
CC chimeric proteins containing the extracellular bacteria-binding domain
CC of CEACAM3 and the transmembrane and cytoplasmic part of CEACAM4 has
CC been used. {ECO:0000305|PubMed:25567962}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. CEA family.
CC {ECO:0000305}.
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DR EMBL; D90276; BAA14320.1; -; mRNA.
DR EMBL; AC005794; AAC62829.1; -; Genomic_DNA.
DR EMBL; AC005955; AAC72273.1; -; Genomic_DNA.
DR EMBL; CH471126; EAW57055.1; -; Genomic_DNA.
DR CCDS; CCDS33033.1; -.
DR PIR; A40428; A40428.
DR RefSeq; NP_001808.2; NM_001817.3.
DR AlphaFoldDB; O75871; -.
DR SMR; O75871; -.
DR STRING; 9606.ENSP00000221954; -.
DR GlyGen; O75871; 4 sites.
DR iPTMnet; O75871; -.
DR PhosphoSitePlus; O75871; -.
DR BioMuta; CEACAM4; -.
DR MassIVE; O75871; -.
DR PaxDb; O75871; -.
DR PeptideAtlas; O75871; -.
DR PRIDE; O75871; -.
DR ProteomicsDB; 50233; -.
DR Antibodypedia; 2296; 98 antibodies from 20 providers.
DR DNASU; 1089; -.
DR Ensembl; ENST00000221954.7; ENSP00000221954.2; ENSG00000105352.11.
DR Ensembl; ENST00000616476.1; ENSP00000481247.1; ENSG00000274131.3.
DR GeneID; 1089; -.
DR KEGG; hsa:1089; -.
DR MANE-Select; ENST00000221954.7; ENSP00000221954.2; NM_001817.4; NP_001808.2.
DR UCSC; uc002orh.1; human.
DR CTD; 1089; -.
DR DisGeNET; 1089; -.
DR GeneCards; CEACAM4; -.
DR HGNC; HGNC:1816; CEACAM4.
DR HPA; ENSG00000105352; Group enriched (bone marrow, lymphoid tissue).
DR MIM; 619159; gene.
DR neXtProt; NX_O75871; -.
DR OpenTargets; ENSG00000105352; -.
DR PharmGKB; PA26360; -.
DR VEuPathDB; HostDB:ENSG00000105352; -.
DR eggNOG; ENOG502S42Z; Eukaryota.
DR GeneTree; ENSGT00960000186634; -.
DR HOGENOM; CLU_024555_4_2_1; -.
DR InParanoid; O75871; -.
DR OrthoDB; 998214at2759; -.
DR PhylomeDB; O75871; -.
DR TreeFam; TF336859; -.
DR PathwayCommons; O75871; -.
DR BioGRID-ORCS; 1089; 13 hits in 1060 CRISPR screens.
DR GenomeRNAi; 1089; -.
DR Pharos; O75871; Tbio.
DR PRO; PR:O75871; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O75871; protein.
DR Bgee; ENSG00000105352; Expressed in blood and 91 other tissues.
DR ExpressionAtlas; O75871; baseline and differential.
DR Genevisible; O75871; HS.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
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:0006909; P:phagocytosis; IDA:UniProtKB.
DR GO; GO:0002682; P:regulation of immune system process; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Immunoglobulin domain; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..244
FT /note="Carcinoembryonic antigen-related cell adhesion
FT molecule 4"
FT /id="PRO_0000316847"
FT TOPO_DOM 36..155
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..139
FT /note="Ig-like V-type"
FT REGION 186..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 222..236
FT /note="ITAM"
FT /evidence="ECO:0000305"
FT COMPBIAS 200..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 29
FT /note="H -> D (in dbSNP:rs1126454)"
FT /evidence="ECO:0000269|PubMed:2050678"
FT /id="VAR_038404"
FT VARIANT 69
FT /note="K -> R (in dbSNP:rs3848568)"
FT /id="VAR_038405"
FT MUTAGEN 222
FT /note="Y->F: No internalization of bacteria; when
FT associated with F-233."
FT /evidence="ECO:0000269|PubMed:25567962"
FT MUTAGEN 233
FT /note="Y->F: No internalization of bacteria; when
FT associated with F-222."
FT /evidence="ECO:0000269|PubMed:25567962"
FT CONFLICT 100
FT /note="T -> Q (in Ref. 1; BAA14320)"
FT /evidence="ECO:0000305"
FT CONFLICT 223..225
FT /note="EEL -> VEF (in Ref. 1; BAA14320)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 244 AA; 25909 MW; C7D2CB0D1CFDC2EC CRC64;
MGPPSAAPRG GHRPWQGLLI TASLLTFWHP PTTVQFTIEA LPSSAAEGKD VLLLACNISE
TIQAYYWHKG KTAEGSPLIA GYITDIQANI PGAAYSGRET VYPNGSLLFQ NITLEDAGSY
TLRTINASYD SDQATGQLHV HQNNVPGLPV GAVAGIVTGV LVGVALVAAL VCFLLLSRTG
RASIQRDLRE QPPPASTPGH GPSHRSTFSA PLPSPRTATP IYEELLYSDA NIYCQIDHKA
DVVS
