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CEAM3_RAT
ID   CEAM3_RAT               Reviewed;         709 AA.
AC   Q63111; Q63101;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Carcinoembryonic antigen-related cell adhesion molecule 3;
DE   AltName: Full=Carcinoembryonic antigen CGM1;
DE   Flags: Precursor;
GN   Name=Ceacam3 {ECO:0000312|RGD:2333};
GN   Synonyms=Cea1 {ECO:0000312|EMBL:AAA40908.1};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAA66037.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAA66037.1};
RC   TISSUE=Placenta {ECO:0000312|EMBL:AAA66037.1};
RX   PubMed=2335509; DOI=10.1016/s0021-9258(19)39012-x;
RA   Rebstock S., Lucas K., Thompson J.A., Zimmermann W.;
RT   "cDNA and gene analyses imply a novel structure for a rat carcinoembryonic
RT   antigen-related protein.";
RL   J. Biol. Chem. 265:7872-7879(1990).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAA40908.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-141.
RC   TISSUE=Liver {ECO:0000312|EMBL:AAA40908.1};
RX   PubMed=2708349; DOI=10.1016/s0021-9258(18)83517-7;
RA   Kodelja V., Lucas K., Barnert S., von Kleist S., Thompson J.A.,
RA   Zimmermann W.;
RT   "Identification of a carcinoembryonic antigen gene family in the rat:
RT   Analysis of the N-terminal domains reveals immunoglobulin-like,
RT   hypervariable regions.";
RL   J. Biol. Chem. 264:6906-6912(1989).
CC   -!- FUNCTION: Possibly involved in cell adhesion.
CC       {ECO:0000303|PubMed:2335509}.
CC   -!- TISSUE SPECIFICITY: Expression detected only in placenta.
CC       {ECO:0000269|PubMed:2335509}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in both adult and embryo.
CC       {ECO:0000269|PubMed:2335509}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. CEA family.
CC       {ECO:0000255}.
CC   -!- CAUTION: This is not the ortholog of human CEACAM3. {ECO:0000305}.
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DR   EMBL; M32474; AAA66037.1; -; mRNA.
DR   EMBL; M60023; AAA40908.1; -; Genomic_DNA.
DR   PIR; A33876; A33876.
DR   PIR; A35364; A35364.
DR   AlphaFoldDB; Q63111; -.
DR   STRING; 10116.ENSRNOP00000023663; -.
DR   GlyGen; Q63111; 16 sites.
DR   PhosphoSitePlus; Q63111; -.
DR   PaxDb; Q63111; -.
DR   UCSC; RGD:2333; rat.
DR   RGD; 2333; Ceacam3.
DR   eggNOG; ENOG502RXPD; Eukaryota.
DR   InParanoid; Q63111; -.
DR   PhylomeDB; Q63111; -.
DR   Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   PRO; PR:Q63111; -.
DR   Proteomes; UP000002494; Unplaced.
DR   Gene3D; 2.60.40.10; -; 6.
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   InterPro; IPR013151; Immunoglobulin.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF07686; V-set; 5.
DR   SMART; SM00409; IG; 6.
DR   SMART; SM00408; IGc2; 2.
DR   SUPFAM; SSF48726; SSF48726; 6.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Immunoglobulin domain; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..709
FT                   /note="Carcinoembryonic antigen-related cell adhesion
FT                   molecule 3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000014575"
FT   DOMAIN          35..142
FT                   /note="Ig-like V-type 1"
FT                   /evidence="ECO:0000303|PubMed:2335509"
FT   DOMAIN          155..262
FT                   /note="Ig-like V-type 2"
FT                   /evidence="ECO:0000303|PubMed:2335509"
FT   DOMAIN          275..382
FT                   /note="Ig-like V-type 3"
FT                   /evidence="ECO:0000303|PubMed:2335509"
FT   DOMAIN          393..500
FT                   /note="Ig-like V-type 4"
FT                   /evidence="ECO:0000303|PubMed:2335509"
FT   DOMAIN          509..616
FT                   /note="Ig-like V-type 5"
FT                   /evidence="ECO:0000303|PubMed:2335509"
FT   DOMAIN          631..695
FT                   /note="Ig-like C2-type"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        86
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        224
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        327
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        344
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        351
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        381
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        462
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        561
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        578
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        585
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        54
FT                   /note="H -> R (in Ref. 2; AAA40908)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   709 AA;  78311 MW;  C9BC903D982D006A CRC64;
     MELSSVLPCK RCTPWRGLLL TASLLTCWLL PTTAQVSIES LPPQVVEGEN VLLHVDNLPE
     NLIAFVWYKG LTNMSLGVAL YSLTYNVTVT GPVHSGRETL YSNGSLWIQN VTQKDTGFYT
     LRTISNHGEI VSNTSLHLHV YFSTLTCGRA ATSAQLSIES VPTSISKGES ALLLAHNLPE
     NLRAIFWYKG AIVFKDLEVA RYVIGTNSSV PGPAHSGRET MYSNGSLLLQ NVTRNDAGFY
     TLKTLSTDLK TEIAYVQLQV DTCFMSYAGP PTSAQLTVES APTSVAEGAS VLLLVHNLPE
     NLRAIFWYKG VILFKDLEVA RYVIGTNSSV LGPAHSGRET MYSNGSLLLQ NVTRNDAGFY
     TLRTLSTDLK AKVVHVQLQV NTSSCCDPLT PALLTIDPVP RHAAKGESVL LQVRNLPEDL
     RMFIWFKSVY TSQIFKIAEY SRAINYVFRG PAHSGRETVY TNGSLLLQDA TEKDTGLYTL
     QIIYRNFKIE TAHVQVSVHT CVHPSTTGQL VIESVPPNVV EGGDVLLLVH NMPENLQSFS
     WYKGVAIVNR HEISRNIIAS NRSTLGPAHS GRETIYSNGS LLLHNATEED NGLYTLWTVN
     RHSETQGIHV HIHIYKPVAQ PFIRVTESSV RVKSSVVLTC LSADTGTSIQ WLFNNQNLRL
     TQRMSLSQTK CQLSIDPVRR EDAGEYRCEV SNPVSSKTSL PVSLDVIIE
 
 
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