LOCUS       NP_001034274             521 aa            linear   ROD 04-MAR-2025
DEFINITION  cell adhesion molecule CEACAM1 isoform 1 precursor [Mus musculus].
ACCESSION   NP_001034274
VERSION     NP_001034274.1
DBSOURCE    REFSEQ: accession NM_001039185.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Muturi,H.T., Ghadieh,H.E., Asalla,S., Lester,S.G., Belew,G.D.,
            Zaidi,S., Abdolahipour,R., Shrestha,A.P., Portuphy,A.O.,
            Stankus,H.L., Helal,R.A., Verhulst,S., Duarte,S., Zarrinpar,A., van
            Grunsven,L.A., Friedman,S.L., Schwabe,R.F., Hinds,T.D. Jr.,
            Kumarasamy,S. and Najjar,S.M.
  TITLE     Conditional deletion of CEACAM1 in hepatic stellate cells causes
            their activation
  JOURNAL   Mol Metab 88, 102010 (2024)
   PUBMED   39168268
  REMARK    GeneRIF: Conditional deletion of CEACAM1 in hepatic stellate cells
            causes their activation.
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Patel,V.N., Aure,M.H., Choi,S.H., Ball,J.R., Lane,E.D., Wang,Z.,
            Xu,Y., Zheng,C., Liu,X., Martin,D., Pailin,J.Y., Prochazkova,M.,
            Kulkarni,A.B., van Kuppevelt,T.H., Ambudkar,I.S., Liu,J. and
            Hoffman,M.P.
  TITLE     Specific 3-O-sulfated heparan sulfate domains regulate salivary
            gland basement membrane metabolism and epithelial differentiation
  JOURNAL   Nat Commun 15 (1), 7584 (2024)
   PUBMED   39217171
  REMARK    Erratum:[Nat Commun. 2024 Oct 10;15(1):8784. doi:
            10.1038/s41467-024-53230-4. PMID: 39389981]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Sasner,M., Preuss,C., Pandey,R.S., Uyar,A., Garceau,D.,
            Kotredes,K.P., Williams,H., Oblak,A.L., Lin,P.B., Perkins,B.,
            Soni,D., Ingraham,C., Lee-Gosselin,A., Lamb,B.T., Howell,G.R. and
            Carter,G.W.
  TITLE     In vivo validation of late-onset Alzheimer's disease genetic risk
            factors
  JOURNAL   Alzheimers Dement 20 (7), 4970-4984 (2024)
   PUBMED   38687251
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Zaidi,S., Asalla,S., Muturi,H.T., Russo,L., Abdolahipour,R.,
            Belew,G.D., Iglesias,M.B., Feraudo,M., Leon,L., Kuo,E., Liu,X.,
            Kumarasamy,S., Ghadieh,H.E., Gatto-Weis,C., Zarrinpar,A., Duarte,S.
            and Najjar,S.M.
  TITLE     Loss of CEACAM1 in hepatocytes causes hepatic fibrosis
  JOURNAL   Eur J Clin Invest 54 (7), e14177 (2024)
   PUBMED   38381498
  REMARK    GeneRIF: Loss of CEACAM1 in hepatocytes causes hepatic fibrosis.
REFERENCE   5  (residues 1 to 521)
  AUTHORS   Dery,K.J., Kojima,H., Kageyama,S., Kadono,K., Hirao,H., Cheng,B.,
            Zhai,Y., Farmer,D.G., Kaldas,F.M., Yuan,X., Eltzschig,H.K. and
            Kupiec-Weglinski,J.W.
  TITLE     Alternative splicing of CEACAM1 by hypoxia-inducible factor-1alpha
            enhances tolerance to hepatic ischemia in mice and humans
  JOURNAL   Sci Transl Med 15 (707), eadf2059 (2023)
   PUBMED   37531413
  REMARK    GeneRIF: Alternative splicing of CEACAM1 by hypoxia-inducible
            factor-1alpha enhances tolerance to hepatic ischemia in mice and
            humans.
REFERENCE   6  (residues 1 to 521)
  AUTHORS   Yokomori,K. and Lai,M.M.
  TITLE     The receptor for mouse hepatitis virus in the resistant mouse
            strain SJL is functional: implications for the requirement of a
            second factor for viral infection
  JOURNAL   J Virol 66 (12), 6931-6938 (1992)
   PUBMED   1279194
REFERENCE   7  (residues 1 to 521)
  AUTHORS   Yokomori,K. and Lai,M.M.
  TITLE     Mouse hepatitis virus utilizes two carcinoembryonic antigens as
            alternative receptors
  JOURNAL   J Virol 66 (10), 6194-6199 (1992)
   PUBMED   1326665
REFERENCE   8  (residues 1 to 521)
  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   9  (residues 1 to 521)
  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
REFERENCE   10 (residues 1 to 521)
  AUTHORS   Robbins,J., Robbins,P.F., Kozak,C.A. and Callahan,R.
  TITLE     The mouse biliary glycoprotein gene (Bgp): partial nucleotide
            sequence, expression, and chromosomal assignment
  JOURNAL   Genomics 10 (3), 583-587 (1991)
   PUBMED   1653760
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AAHY01060000.1, M77196.1 and AB236328.2.
            
            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 :: X67279.1, X67281.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Mus musculus"
                     /strain="BALB/c"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 13.84 cM"
     Protein         1..521
                     /product="cell adhesion molecule CEACAM1 isoform 1
                     precursor"
                     /note="hepatitis virus receptor; BGP-1; MHV-R; biliary
                     glycoprotein D; murine hepatitis virus receptor;
                     CEA-related cell adhesion molecule 1; biliary glycoprotein
                     1; carcinoembryonic antigen 1; carcinoembryonic antigen 7;
                     hepatitis virus (MHV-4) susceptibility; carcinoembryonic
                     antigen-related cell adhesion molecule 1; cell adhesion
                     molecule CEACAM1"
                     /calculated_mol_wt=53488
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3516
     mat_peptide     35..521
                     /product="Cell adhesion molecule CEACAM1.
                     /id=PRO_0000014563"
                     /note="propagated from UniProtKB/Swiss-Prot (P31809.1)"
                     /calculated_mol_wt=53488
     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:0000250|UniProtKB:P16573"
                     /note="propagated from UniProtKB/Swiss-Prot (P31809.1)"
     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"
     Site            71
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498,
                     ECO:0000269|PubMed:11980704, ECO:0000269|PubMed:19349973;
                     propagated from UniProtKB/Swiss-Prot (P31809.1)"
     Region          78..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409430"
     Region          88..91
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409430"
     Site            89
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498,
                     ECO:0000269|PubMed:11980704, ECO:0000269|PubMed:19349973;
                     propagated from UniProtKB/Swiss-Prot (P31809.1)"
     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,
                     ECO:0000269|PubMed:11980704; propagated from
                     UniProtKB/Swiss-Prot (P31809.1)"
     Region          105..109
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409430"
     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..236
                     /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 (P31809.1)"
     Site            152
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:P13688,
                     ECO:0000255|PROSITE-ProRule:PRU00498; propagated from
                     UniProtKB/Swiss-Prot (P31809.1)"
     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"
     Region          178..183
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409402"
     Region          185..188
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409402"
     Region          192..196
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409402"
     Region          199..204
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409402"
     Site            199
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P31809.1)"
     Site            206
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498,
                     ECO:0000269|PubMed:16944957; propagated from
                     UniProtKB/Swiss-Prot (P31809.1)"
     Site            210
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:P13688,
                     ECO:0000255|PROSITE-ProRule:PRU00498; propagated from
                     UniProtKB/Swiss-Prot (P31809.1)"
     Region          214..222
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409402"
     Region          226..235
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409402"
     Site            226
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:P13688,
                     ECO:0000255|PROSITE-ProRule:PRU00498; propagated from
                     UniProtKB/Swiss-Prot (P31809.1)"
     Region          245..320
                     /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          245..251
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409540"
     Region          256..263
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409540"
     Site            258
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P31809.1)"
     Region          269..275
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409540"
     Region          278..283
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409540"
     Region          286..292
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409540"
     Site            290
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P31809.1)"
     Site            294
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P31809.1)"
     Region          295..306
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409540"
     Site            304
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P31809.1)"
     Region          309..320
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409540"
     Site            317
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498,
                     ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P31809.1)"
     Region          326..413
                     /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          326..330
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409402"
     Region          333..337
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409402"
     Site            333
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498,
                     ECO:0000269|PubMed:11980704, ECO:0000269|PubMed:19349973;
                     propagated from UniProtKB/Swiss-Prot (P31809.1)"
     Region          342..348
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409402"
     Region          355..360
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409402"
     Region          362..365
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409402"
     Region          369..373
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409402"
     Site            375
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498,
                     ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P31809.1)"
     Region          376..381
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409402"
     Region          391..399
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409402"
     Region          403..412
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409402"
     Region          416..452
                     /region_name="TM_EphA1"
                     /note="Transmembrane domain of Ephrin Receptor A1 Protein
                     Tyrosine Kinase; cl25995"
                     /db_xref="CDD:474744"
     Site            order(422,424..425,428..429,431..433,436..437,440..441,
                     445,450)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:214014"
     Site            429..447
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31809.1)"
     Region          445..457
                     /region_name="Interaction with calmodulin.
                     /evidence=ECO:0000250|UniProtKB:P16573"
                     /note="propagated from UniProtKB/Swiss-Prot (P31809.1)"
     Region          447..521
                     /region_name="Interaction with FLNA.
                     /evidence=ECO:0000250|UniProtKB:P16573"
                     /note="propagated from UniProtKB/Swiss-Prot (P31809.1)"
     Region          455..521
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P31809.1)"
     Region          484..521
                     /region_name="Required for interaction with PTPN11 and
                     PTPN6 and for control of phosphorylation level.
                     /evidence=ECO:0000269|PubMed:9867848"
                     /note="propagated from UniProtKB/Swiss-Prot (P31809.1)"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC, LCK, INSR and EGFR.
                     /evidence=ECO:0000269|PubMed:21081647,
                     ECO:0000269|PubMed:9867848; propagated from
                     UniProtKB/Swiss-Prot (P31809.1)"
     Site            503
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P16573; propagated from
                     UniProtKB/Swiss-Prot (P31809.1)"
     Region          515..518
                     /region_name="Essential for interaction with PTPN11 and
                     PTPN6. /evidence=ECO:0000269|PubMed:9867848"
                     /note="propagated from UniProtKB/Swiss-Prot (P31809.1)"
     Site            515
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by INSR, SRC and LCK.
                     /evidence=ECO:0000269|PubMed:21081647,
                     ECO:0000269|PubMed:9867848; propagated from
                     UniProtKB/Swiss-Prot (P31809.1)"
     CDS             1..521
                     /gene="Ceacam1"
                     /gene_synonym="bb-1; Bgp; Bgp1; C-CAM; Cc1; CD66a; Cea-1;
                     Cea-7; Cea1; Cea7; Hv-2; Hv2; mCEA1; Mhv-1; MHVR; MHVR1;
                     mmCGM1; mmCGM1a; mmCGM2"
                     /coded_by="NM_001039185.1:92..1657"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS20984.1"
                     /db_xref="GeneID:26365"
                     /db_xref="MGI:MGI:1347245"
ORIGIN      
        1 melasahlhk gqvpwgglll tasllaswsp attaevtiea vppqvaednn vlllvhnlpl
       61 algafawykg nttaidkeia rfvpnsnmnf tgqaysgrei iysngsllfq mitmkdmgvy
      121 tldmtdenyr rtqatvrfhv hpillkpnit snnsnpvegd dsvsltcdsy tdpdninylw
      181 srngeslseg drlklsegnr tltllnvtrn dtgpyvcetr npvsvnrsdp fslniiygpd
      241 tpiispsdiy lhpgsnlnls chaasnppaq yfwlinekph assqelfipn ittnnsgtyt
      301 cfvnnsvtgl srttvknitv lepvtqpflq vtnttvkeld svtltclsnd iganiqwlfn
      361 sqslqlterm tlsqnnsilr idpikredag eyqceisnpv svrrsnsikl diifdptqgg
      421 lsdgaiagiv igvvagvali aglayflysr ksgggsdqrd ltehkpsasn hnlapsdnsp
      481 nkvddvaytv lnfnsqqpnr ptsapsspra tetvysevkk k
//
