LOCUS       NP_001029032             519 aa            linear   ROD 09-FEB-2025
DEFINITION  cell adhesion molecule CEACAM1 isoform 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_001029032
VERSION     NP_001029032.1
DBSOURCE    REFSEQ: accession NM_001033860.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Huff,L.P., Kikuchi,D.S., Faidley,E., Forrester,S.J., Tsai,M.Z.,
            Lassegue,B. and Griendling,K.K.
  TITLE     Polymerase-delta-interacting protein 2 activates the RhoGEF
            epithelial cell transforming sequence 2 in vascular smooth muscle
            cells
  JOURNAL   Am J Physiol Cell Physiol 316 (5), C621-C631 (2019)
   PUBMED   30726115
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Bonsor,D.A., Gunther,S., Beadenkopf,R., Beckett,D. and
            Sundberg,E.J.
  TITLE     Diverse oligomeric states of CEACAM IgV domains
  JOURNAL   Proc Natl Acad Sci U S A 112 (44), 13561-13566 (2015)
   PUBMED   26483485
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Huang,Y.H., Zhu,C., Kondo,Y., Anderson,A.C., Gandhi,A., Russell,A.,
            Dougan,S.K., Petersen,B.S., Melum,E., Pertel,T., Clayton,K.L.,
            Raab,M., Chen,Q., Beauchemin,N., Yazaki,P.J., Pyzik,M.,
            Ostrowski,M.A., Glickman,J.N., Rudd,C.E., Ploegh,H.L., Franke,A.,
            Petsko,G.A., Kuchroo,V.K. and Blumberg,R.S.
  TITLE     CEACAM1 regulates TIM-3-mediated tolerance and exhaustion
  JOURNAL   Nature 517 (7534), 386-390 (2015)
   PUBMED   25363763
  REMARK    Erratum:[Nature. 2016 Aug 18;536(7616):359. doi:
            10.1038/nature17421.. PMID: 26982724]
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Heckt,T., Bickert,T., Jeschke,A., Seitz,S., Schulze,J., Ito,W.D.,
            Zimmermann,W., Amling,M., Schinke,T., Horst,A.K. and Keller,J.
  TITLE     Increased osteoclastogenesis in mice lacking the carcinoembryonic
            antigen-related cell adhesion molecule 1
  JOURNAL   PLoS One 9 (12), e114360 (2014)
   PUBMED   25490771
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 519)
  AUTHORS   Singer,B.B., Opp,L., Heinrich,A., Schreiber,F.,
            Binding-Liermann,R., Berrocal-Almanza,L.C., Heyl,K.A., Muller,M.M.,
            Weimann,A., Zweigner,J. and Slevogt,H.
  TITLE     Soluble CEACAM8 interacts with CEACAM1 inhibiting TLR2-triggered
            immune responses
  JOURNAL   PLoS One 9 (4), e94106 (2014)
   PUBMED   24743304
  REMARK    GeneRIF: CEACAM8 interacts with CEACAM1 inhibiting TLR2-triggered
            immune responses
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 519)
  AUTHORS   Culic,O., Huang,Q.H., Flanagan,D., Hixson,D. and Lin,S.H.
  TITLE     Molecular cloning and expression of a new rat liver cell-CAM105
            isoform. Differential phosphorylation of isoforms
  JOURNAL   Biochem J 285 (Pt 1) (Pt 1), 47-53 (1992)
   PUBMED   1637321
REFERENCE   7  (residues 1 to 519)
  AUTHORS   McCuaig,K., Turbide,C. and Beauchemin,N.
  TITLE     mmCGM1a: a mouse carcinoembryonic antigen gene family member,
            generated by alternative splicing, functions as an adhesion
            molecule
  JOURNAL   Cell Growth Differ 3 (3), 165-174 (1992)
   PUBMED   1633107
REFERENCE   8  (residues 1 to 519)
  AUTHORS   Dveksler,G.S., Pensiero,M.N., Cardellichio,C.B., Williams,R.K.,
            Jiang,G.S., Holmes,K.V. and Dieffenbach,C.W.
  TITLE     Cloning of the mouse hepatitis virus (MHV) receptor: expression in
            human and hamster cell lines confers susceptibility to MHV
  JOURNAL   J Virol 65 (12), 6881-6891 (1991)
   PUBMED   1719235
REFERENCE   9  (residues 1 to 519)
  AUTHORS   Lin,S.H., Culic,O., Flanagan,D. and Hixson,D.C.
  TITLE     Immunochemical characterization of two isoforms of rat liver
            ecto-ATPase that show an immunological and structural identity with
            a glycoprotein cell-adhesion molecule with Mr 105,000
  JOURNAL   Biochem J 278 (Pt 1) (Pt 1), 155-161 (1991)
   PUBMED   1831973
REFERENCE   10 (residues 1 to 519)
  AUTHORS   Williams,R.K., Jiang,G.S. and Holmes,K.V.
  TITLE     Receptor for mouse hepatitis virus is a member of the
            carcinoembryonic antigen family of glycoproteins
  JOURNAL   Proc Natl Acad Sci U S A 88 (13), 5533-5536 (1991)
   PUBMED   1648219
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            M92848.1, J04963.1, BC061740.1 and JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061740.1, J04963.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN16676784,
                                           SAMN16676785 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..519
                     /product="cell adhesion molecule CEACAM1 isoform 1
                     precursor"
                     /note="GP110; pp120; C-CAM 105; ecto-ATPase; cell-CAM 105;
                     ATP-dependent taurocolate-carrier protein; bone
                     gamma-carboxyglutamic acid (Gla) protein; osteocalcin;
                     CEA-related cell adhesion molecule 1 (bone
                     gamma-carboxyglutamic acid (Gla) protein) (osteocalcin);
                     carcinoembryonic antigen-related cell adhesion molecule 1
                     (biliary glycoprotein); pp120/ecto-ATPase;
                     carcinoembryonic antigen related cell adhesion molecule 1;
                     cell adhesion molecule CEACAM1"
                     /calculated_mol_wt=53628
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3801
     mat_peptide     35..519
                     /product="Cell adhesion molecule CEACAM1.
                     /id=PRO_0000014564"
                     /note="propagated from UniProtKB/Swiss-Prot (P16573.4)"
                     /calculated_mol_wt=53628
     Site            35
                     /site_type="pyrrolidone-carboxylic-acid"
                     /note="Pyrrolidone carboxylic acid.
                     /evidence=ECO:0000250|UniProtKB:P13688; propagated from
                     UniProtKB/Swiss-Prot (P16573.4)"
     Region          36..140
                     /region_name="IgV_CEACAM_D1"
                     /note="First immunoglobulin (Ig)-like domain of
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule (CEACAM); cd05774"
                     /db_xref="CDD:409430"
     Region          37..55
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409430"
     Region          37..39
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409430"
     Region          39..142
                     /region_name="Required for homophilic binding.
                     /evidence=ECO:0000269|PubMed:8831574"
                     /note="propagated from UniProtKB/Swiss-Prot (P16573.4)"
     Region          44..46
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409430"
     Region          49..56
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409430"
     Region          56..63
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409430"
     Region          64..69
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409430"
     Region          64..68
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409430"
     Region          70..91
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409430"
     Region          78..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409430"
     Site            87
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          88..91
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409430"
     Region          98..124
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409430"
     Region          98..103
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409430"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          105..109
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409430"
     Site            113
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          119..124
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409430"
     Region          125..132
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409430"
     Region          133..140
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409430"
     Region          133..139
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409430"
     Region          146..234
                     /region_name="IgI_hCEACAM_2_4_6_like"
                     /note="Immunoglobulin (Ig)-like domain of human
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule (CEACAM) domains 2, 4, and 6, and similar
                     domains; cd05740"
                     /db_xref="CDD:409402"
     Region          146..150
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409402"
     Site            148
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Site            152
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          153..158
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409402"
     Region          163..169
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409402"
     Site            173
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          176..181
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409402"
     Region          183..186
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409402"
     Region          190..194
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409402"
     Region          197..202
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409402"
     Site            197
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          212..220
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409402"
     Region          224..233
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409402"
     Site            224
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          243..318
                     /region_name="IgC2_CEACAM5-like"
                     /note="Fifth immunoglobulin (Ig)-like domain of the
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule 5 (CEACAM5) and similar domains; member of the
                     C2-set IgSF domains; cd20948"
                     /db_xref="CDD:409540"
     Region          243..249
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409540"
     Region          254..261
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409540"
     Site            256
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          267..273
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409540"
     Region          276..281
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409540"
     Region          284..290
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409540"
     Site            288
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Site            292
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          293..304
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409540"
     Site            302
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          307..318
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409540"
     Site            315
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          324..411
                     /region_name="IgI_hCEACAM_2_4_6_like"
                     /note="Immunoglobulin (Ig)-like domain of human
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule (CEACAM) domains 2, 4, and 6, and similar
                     domains; cd05740"
                     /db_xref="CDD:409402"
     Region          324..328
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409402"
     Region          331..335
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409402"
     Site            331
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          340..346
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409402"
     Region          353..358
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409402"
     Region          360..363
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409402"
     Region          367..371
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409402"
     Region          374..379
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409402"
     Site            374
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine, atypical.
                     /evidence=ECO:0000250|UniProtKB:P31809,
                     ECO:0000255|PROSITE-ProRule:PRU00498; propagated from
                     UniProtKB/Swiss-Prot (P16573.4)"
     Region          389..397
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409402"
     Region          401..410
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409402"
     Site            426..446
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P16573.4)"
     Region          445..457
                     /region_name="Interaction with calmodulin.
                     /evidence=ECO:0000269|PubMed:8576129"
                     /note="propagated from UniProtKB/Swiss-Prot (P16573.4)"
     Region          447..519
                     /region_name="Interaction with FLNA.
                     /evidence=ECO:0000269|PubMed:16291724"
                     /note="propagated from UniProtKB/Swiss-Prot (P16573.4)"
     Region          455..519
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P16573.4)"
     Region          484..519
                     /region_name="Required for interaction with PTPN11 and
                     PTPN6 and for control of phosphorylation level.
                     /evidence=ECO:0000250|UniProtKB:P31809"
                     /note="propagated from UniProtKB/Swiss-Prot (P16573.4)"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC, LCK, INSR and EGFR.
                     /evidence=ECO:0000269|PubMed:15467833,
                     ECO:0000269|PubMed:16054098, ECO:0000269|PubMed:7518458,
                     ECO:0000269|PubMed:7626603, ECO:0000269|PubMed:9712832;
                     propagated from UniProtKB/Swiss-Prot (P16573.4)"
     Site            503
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16054098,
                     ECO:0000269|PubMed:7518458; propagated from
                     UniProtKB/Swiss-Prot (P16573.4)"
     Region          513..516
                     /region_name="Essential for interaction with PTPN11 and
                     PTPN6. /evidence=ECO:0000250|UniProtKB:P31809"
                     /note="propagated from UniProtKB/Swiss-Prot (P16573.4)"
     Site            513
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by INSR, SRC and LCK.
                     /evidence=ECO:0000269|PubMed:16054098; propagated from
                     UniProtKB/Swiss-Prot (P16573.4)"
     CDS             1..519
                     /gene="Ceacam1"
                     /gene_synonym="Bgp; BGPR; Ccam1; CD66a"
                     /coded_by="NM_001033860.1:58..1617"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:81613"
                     /db_xref="RGD:67396"
ORIGIN      
        1 melasarllr gqipwrglll taslltywsp lttaqvtvda vppnvveeks vlllahnlpq
       61 efqvfywykg ttlnpdseia ryirsdnmsk tgpaysgret iysngslffq nvnktderay
      121 tlsvfdqqfn piqtsvqfrv ypalqkpnvt gnnsnpmege pfvslmcepy tnntsylwsr
      181 ngeslsegdr vtfsegnrtl tllnvrrtdk gyyecearnp atfnrsdpfn ldviygpdap
      241 visppdiylh qgsnlnlsch adsnppaqyf wlineklqts sqelfisnit tnnsgtyacf
      301 vnntvtglsr ttvknitvfe pvtqpsiqit nttvkelgsv tltcfskdtg vsvrwlfnsq
      361 slqltdrmtl sqdnstlrid pikredagdy qceisnpvsf rishpikldv ipdptqgnsg
      421 lsegaiagiv igsvagvali aalayflysr ktgggsdhrd ltehkpstss hnlgpsddsp
      481 nkvddvsysv lnfnaqqskr ptsassspte tvysvvkkk
//
