Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P16573

- CEAM1_RAT

UniProt

P16573 - CEAM1_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Carcinoembryonic antigen-related cell adhesion molecule 1

Gene

Ceacam1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

This protein is a calcium-independent cell adhesion molecule with homophilic binding properties. May play a role in the formation and maintenance of the specialized membrane structure of the apical surface of the hepatocytes.

GO - Molecular functioni

  1. protein homodimerization activity Source: UniProtKB
  2. protein kinase binding Source: RGD

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. positive regulation of MAP kinase activity Source: MGI
  3. protein homotrimerization Source: UniProtKB
  4. signal transduction Source: RGD
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Protein family/group databases

TCDBi8.A.23.1.4. the basigin (basigin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Carcinoembryonic antigen-related cell adhesion molecule 1
Alternative name(s):
ATP-dependent taurocolate-carrier protein
Cell-CAM 105
Short name:
C-CAM 105
Ecto-ATPase
GP110
pp120
CD_antigen: CD66a
Gene namesi
Name:Ceacam1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi67396. Ceacam1.

Subcellular locationi

Cell membrane; Single-pass type I membrane protein
Note: Canalicular domain of hepatocyte plasma membranes.

GO - Cellular componenti

  1. integral component of plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3434By similarityAdd
BLAST
Chaini35 – 519485Carcinoembryonic antigen-related cell adhesion molecule 1PRO_0000014564Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351Pyrrolidone carboxylic acidBy similarity
Glycosylationi87 – 871N-linked (GlcNAc...)
Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence Analysis
Glycosylationi148 – 1481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi152 – 1521N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi167 ↔ 215PROSITE-ProRule annotation
Glycosylationi172 – 1721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi173 – 1731N-linked (GlcNAc...)Sequence Analysis
Glycosylationi197 – 1971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi224 – 2241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi256 – 2561N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi259 ↔ 299PROSITE-ProRule annotation
Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi292 – 2921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi302 – 3021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi315 – 3151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi331 – 3311N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi344 ↔ 392PROSITE-ProRule annotation
Glycosylationi374 – 3741N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Phosphorylated on serine residues in both isoforms. On serine and tyrosine residues in cytoplasmic region of the long isoform.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP16573.
PRIDEiP16573.

PTM databases

PhosphoSiteiP16573.

Expressioni

Tissue specificityi

Expressed in epithelia, vessel endothelia, leukocytes and platelets.

Gene expression databases

ExpressionAtlasiP16573. baseline and differential.
GenevestigatoriP16573.

Interactioni

Protein-protein interaction databases

MINTiMINT-220849.

Structurei

3D structure databases

ProteinModelPortaliP16573.
SMRiP16573. Positions 280-415.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini35 – 422388ExtracellularSequence AnalysisAdd
BLAST
Topological domaini449 – 51971CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei423 – 44826HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 14099Ig-like V-typeAdd
BLAST
Domaini147 – 23286Ig-like C2-type 1Add
BLAST
Domaini237 – 31781Ig-like C2-type 2Add
BLAST
Domaini325 – 40379Ig-like C2-type 3Add
BLAST

Sequence similaritiesi

Belongs to the immunoglobulin superfamily. CEA family.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG149650.
GeneTreeiENSGT00760000119187.
HOGENOMiHOG000233417.
HOVERGENiHBG007922.
InParanoidiP16573.
KOiK06499.
OrthoDBiEOG74BJS7.
PhylomeDBiP16573.
TreeFamiTF336859.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR013151. Immunoglobulin.
[Graphical view]
PfamiPF00047. ig. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 2 hits.
SM00408. IGc2. 2 hits.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Long (identifier: P16573) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MELASARLLR GQIPWRGLLL TASLLTYWSP LTTAQVTVDA VPPNVVEESS
60 70 80 90 100
VLLLTHNLPQ EFQVFYWYKV TTTGLNSEIA RYIRSSNTSQ TEPAYSGRVT
110 120 130 140 150
IYSNGSLFFQ NVNKTDEGPY TLSVIDKQFN PIQTSVQFRV YPALQKPNVT
160 170 180 190 200
GNNSNPMEGE PFVSLMCEPY TNNTSYLWSR NGESLSEGDR VTFSEGNRTL
210 220 230 240 250
TLLNVRRTDK GYYECEARNP ATFNRSDPFN LDVIYGPDAP VISPPDIYLH
260 270 280 290 300
QGSNLNLSCH ADSNPPAQYF WLINEKLQTS SQELFISNIT TNNSGTYACF
310 320 330 340 350
VNNTVTGLSR TTVKNITVFE PVTQPSIQIT NTTVKELGSV TLTCFSKDTG
360 370 380 390 400
VSVRWLFNSQ SLQLTDRMTL SQDNSTLRID PIKREDAGDY QCEISNPVSF
410 420 430 440 450
RISHPIKLDV IPDPTQGNSG LSEGAIAGIV IGSVAGVALI AALAYFLYSR
460 470 480 490 500
KTGGGSDHRD LTEHKPSTSS HNLGPSDDSP NKVDDVSYSV LNFNAQQSKR
510
PTSASSSPTE TVYSVVKKK
Length:519
Mass (Da):57,264
Last modified:October 1, 1994 - v3
Checksum:i04143928D7975776
GO
Isoform Short (identifier: P16573-2) [UniParc]FASTAAdd to Basket

Also known as: C-CAM3

The sequence of this isoform differs from the canonical sequence as follows:
     455-458: GSDH → SGSF
     459-519: Missing.

Show »
Length:458
Mass (Da):50,614
Checksum:i0C7709DFBFA72FA0
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti49 – 491S → K.
Natural varianti55 – 551T → A.
Natural varianti70 – 701V → G.
Natural varianti73 – 764TGLN → LNPD.
Natural varianti86 – 861S → D.
Natural varianti88 – 881T → M.
Natural varianti90 – 901Q → K.
Natural varianti92 – 921E → G.
Natural varianti99 – 991V → E.
Natural varianti118 – 1192GP → RA.
Natural varianti125 – 1251I → F.
Natural varianti127 – 1271K → Q.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei455 – 4584GSDH → SGSF in isoform Short. 2 PublicationsVSP_002504
Alternative sequencei459 – 51961Missing in isoform Short. 2 PublicationsVSP_002505Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04963 mRNA. Translation: AAA41104.1.
X71122 mRNA. Translation: CAA50435.1.
Z12019 mRNA. Translation: CAA78054.1.
M92848 mRNA. Translation: AAA16783.1. Different termination.
BC061740 mRNA. Translation: AAH61740.1.
PIRiA44783.
S23969.
RefSeqiNP_001029032.1. NM_001033860.1.
NP_001029033.1. NM_001033861.1.
NP_001029034.1. NM_001033862.1.
NP_113943.1. NM_031755.2.
UniGeneiRn.91235.

Genome annotation databases

EnsembliENSRNOT00000051892; ENSRNOP00000046654; ENSRNOG00000020578.
GeneIDi81613.
KEGGirno:81613.
UCSCiRGD:67396. rat. [P16573-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04963 mRNA. Translation: AAA41104.1 .
X71122 mRNA. Translation: CAA50435.1 .
Z12019 mRNA. Translation: CAA78054.1 .
M92848 mRNA. Translation: AAA16783.1 . Different termination.
BC061740 mRNA. Translation: AAH61740.1 .
PIRi A44783.
S23969.
RefSeqi NP_001029032.1. NM_001033860.1.
NP_001029033.1. NM_001033861.1.
NP_001029034.1. NM_001033862.1.
NP_113943.1. NM_031755.2.
UniGenei Rn.91235.

3D structure databases

ProteinModelPortali P16573.
SMRi P16573. Positions 280-415.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-220849.

Protein family/group databases

TCDBi 8.A.23.1.4. the basigin (basigin) family.

PTM databases

PhosphoSitei P16573.

Proteomic databases

PaxDbi P16573.
PRIDEi P16573.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000051892 ; ENSRNOP00000046654 ; ENSRNOG00000020578 .
GeneIDi 81613.
KEGGi rno:81613.
UCSCi RGD:67396. rat. [P16573-1 ]

Organism-specific databases

CTDi 634.
RGDi 67396. Ceacam1.

Phylogenomic databases

eggNOGi NOG149650.
GeneTreei ENSGT00760000119187.
HOGENOMi HOG000233417.
HOVERGENi HBG007922.
InParanoidi P16573.
KOi K06499.
OrthoDBi EOG74BJS7.
PhylomeDBi P16573.
TreeFami TF336859.

Miscellaneous databases

NextBioi 615097.

Gene expression databases

ExpressionAtlasi P16573. baseline and differential.
Genevestigatori P16573.

Family and domain databases

Gene3Di 2.60.40.10. 4 hits.
InterProi IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR013151. Immunoglobulin.
[Graphical view ]
Pfami PF00047. ig. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view ]
SMARTi SM00409. IG. 2 hits.
SM00408. IGc2. 2 hits.
[Graphical view ]
PROSITEi PS50835. IG_LIKE. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of a cDNA coding for a rat liver plasma membrane ecto-ATPase. The primary structure of the ecto-ATPase is similar to that of the human biliary glycoprotein I."
    Lin S.-H., Guidotti G.
    J. Biol. Chem. 264:14408-14414(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), PROTEIN SEQUENCE OF 50-68.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "Different isoforms and stock-specific variants of the cell adhesion molecule C-CAM (cell-CAM 105) in rat liver."
    Edlund M., Gaardsvoll H., Bock E., Oebrink B.
    Eur. J. Biochem. 213:1109-1116(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
    Strain: Sprague-Dawley and Wistar.
    Tissue: Liver.
  3. "Molecular cloning and expression of a new rat liver cell-CAM105 isoform. Differential phosphorylation of isoforms."
    Culic O., Huang Q., Flanagan D., Hixon D., Lin S.-H.
    Biochem. J. 285:47-53(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
    Strain: Sprague-Dawley.
    Tissue: Liver.
  4. "The cytoplasmic domain of C-CAM is required for C-CAM-mediated adhesion function: studies of a C-CAM transcript containing an unspliced intron."
    Cheung P.H., Culic O., Qiu Y., Earley K., Thompson N., Hixson D.C., Lin S.-H.
    Biochem. J. 295:427-435(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Intestine.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
    Tissue: Prostate.
  6. "The cell adhesion molecule Cell-CAM 105 is an ecto-ATPase and a member of the immunoglobulin superfamily."
    Aurivillius M., Hansen O.C., Lazrek M.B.S., Bock E., Oebrink B.
    FEBS Lett. 264:267-269(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 58-66 AND 119-138.
  7. "Characterisation of the ATP-dependent taurocholate-carrier protein (gp110) of the hepatocyte canalicular membrane."
    Becker A., Lucka L., Kilian C., Kannicht C., Reutter W.
    Eur. J. Biochem. 214:539-548(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Strain: Wistar.
    Tissue: Liver.
  8. "The rat liver ecto-ATPase is also a canalicular bile acid transport protein."
    Sippel C.J., Suchy F.J., Ananthanarayanan M., Perlmutter D.H.
    J. Biol. Chem. 268:2083-2091(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 110-138 AND 148-150, PHOSPHORYLATION.
  9. "pp120/ecto-ATPase, an endogenous substrate of the insulin receptor tyrosine kinase, is expressed as two variably spliced isoforms."
    Najjae S.M., Accili D., Philippe N., Jernberg J., Margolis R., Taylor S.I.
    J. Biol. Chem. 268:1201-1206(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  10. "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."
    Lin S.-H., Culic O., Flanagan D., Hixson D.C.
    Biochem. J. 278:155-161(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.

Entry informationi

Entry nameiCEAM1_RAT
AccessioniPrimary (citable) accession number: P16573
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: October 1, 1994
Last modified: October 29, 2014
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3