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   13-FEB-2019, entry version 128.
DE   RecName: Full=Carcinoembryonic antigen-related 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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION, TISSUE SPECIFICITY, AND
RP   VARIANT ASP-29.
RX   PubMed=2050678;
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.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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.,
RA   Kuespert K., Hauck C.R.;
RT   "The granulocyte orphan receptor CEACAM4 is able to trigger
RT   phagocytosis of bacteria.";
RL   J. Leukoc. Biol. 97:521-531(2015).
CC   -!- FUNCTION: Granulocyte orphan receptor that acts as an trigger
CC       efficient phagocytosis of attached particles.
CC       {ECO:0000269|PubMed:25567962}.
CC   -!- SUBUNIT: Interacts through its phosphorylated ITAM domain with the
CC       SH2 domain-containing cytoplasmic proteins involved in signaling
CC       processes during phagocytosis. {ECO:0000269|PubMed:25567962}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       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
CC       phosphorylated by SRC family PTKs upon ligand-mediated receptor
CC       clustering and allows to initiate phagocytosis of bound ligand.
CC       {ECO:0000269|PubMed:25567962}.
CC   -!- MISCELLANEOUS: To study the function of the orphan receptor
CC       CEACAM4 chimeric proteins containing the extracellular bacteria-
CC       binding domain of CEACAM3 and the transmembrane and cytoplasmic
CC       part of CEACAM4 has 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   UniGene; Hs.12; -.
DR   ProteinModelPortal; O75871; -.
DR   STRING; 9606.ENSP00000221954; -.
DR   iPTMnet; O75871; -.
DR   PhosphoSitePlus; O75871; -.
DR   BioMuta; CEACAM4; -.
DR   PaxDb; O75871; -.
DR   PeptideAtlas; O75871; -.
DR   PRIDE; O75871; -.
DR   ProteomicsDB; 50233; -.
DR   Ensembl; ENST00000221954; ENSP00000221954; ENSG00000105352.
DR   Ensembl; ENST00000616476; ENSP00000481247; ENSG00000274131.
DR   GeneID; 1089; -.
DR   KEGG; hsa:1089; -.
DR   UCSC; uc002orh.1; human.
DR   CTD; 1089; -.
DR   DisGeNET; 1089; -.
DR   EuPathDB; HostDB:ENSG00000105352.10; -.
DR   GeneCards; CEACAM4; -.
DR   H-InvDB; HIX0040149; -.
DR   HGNC; HGNC:1816; CEACAM4.
DR   neXtProt; NX_O75871; -.
DR   OpenTargets; ENSG00000105352; -.
DR   PharmGKB; PA26360; -.
DR   eggNOG; ENOG410JEDW; Eukaryota.
DR   eggNOG; ENOG41119IN; LUCA.
DR   GeneTree; ENSGT00940000153056; -.
DR   HOGENOM; HOG000233417; -.
DR   HOVERGEN; HBG007922; -.
DR   InParanoid; O75871; -.
DR   KO; K06499; -.
DR   OrthoDB; 998214at2759; -.
DR   PhylomeDB; O75871; -.
DR   TreeFam; TF336859; -.
DR   GenomeRNAi; 1089; -.
DR   PRO; PR:O75871; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   Bgee; ENSG00000105352; Expressed in 85 organ(s), highest expression level in blood.
DR   ExpressionAtlas; O75871; baseline and differential.
DR   Genevisible; O75871; HS.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0006909; P:phagocytosis; IDA:UniProtKB.
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   Complete proteome; Glycoprotein; Immunoglobulin domain; Membrane;
KW   Polymorphism; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     35       {ECO:0000255}.
FT   CHAIN        36    244       Carcinoembryonic antigen-related cell
FT                                adhesion molecule 4.
FT                                /FTId=PRO_0000316847.
FT   TOPO_DOM     36    155       Extracellular. {ECO:0000255}.
FT   TRANSMEM    156    176       Helical. {ECO:0000255}.
FT   TOPO_DOM    177    244       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       36    139       Ig-like V-type.
FT   MOTIF       222    236       ITAM. {ECO:0000305}.
FT   CARBOHYD     57     57       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    104    104       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    111    111       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    126    126       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VARIANT      29     29       H -> D (in dbSNP:rs1126454).
FT                                {ECO:0000269|PubMed:2050678}.
FT                                /FTId=VAR_038404.
FT   VARIANT      69     69       K -> R (in dbSNP:rs3848568).
FT                                /FTId=VAR_038405.
FT   MUTAGEN     222    222       Y->F: No internalization of bacteria;
FT                                when associated with F-233.
FT                                {ECO:0000269|PubMed:25567962}.
FT   MUTAGEN     233    233       Y->F: No internalization of bacteria;
FT                                when associated with F-222.
FT                                {ECO:0000269|PubMed:25567962}.
FT   CONFLICT    100    100       T -> Q (in Ref. 1; BAA14320).
FT                                {ECO:0000305}.
FT   CONFLICT    223    225       EEL -> VEF (in Ref. 1; BAA14320).
FT                                {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
//