ESAM_MOUSE
ID ESAM_MOUSE Reviewed; 394 AA.
AC Q925F2;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Endothelial cell-selective adhesion molecule;
DE Flags: Precursor;
GN Name=Esam; Synonyms=Esam1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Swiss Webster / NIH;
RX PubMed=11279107; DOI=10.1074/jbc.m100630200;
RA Hirata K., Ishida T., Penta K., Rezaee M., Yang E., Wohlgemuth J.,
RA Quertermous T.;
RT "Cloning of an immunoglobulin family adhesion molecule selectively
RT expressed by endothelial cells.";
RL J. Biol. Chem. 276:16223-16231(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11847224; DOI=10.1074/jbc.m111999200;
RA Nasdala I., Wolburg-Buchholz K., Wolburg H., Kuhn A., Ebnet K.,
RA Brachtendorf G., Samulowitz U., Kuster B., Engelhardt B., Vestweber D.,
RA Butz S.;
RT "A transmembrane tight junction protein selectively expressed on
RT endothelial cells and platelets.";
RL J. Biol. Chem. 277:16294-16303(2002).
RN [4]
RP INTERACTION WITH MAGI1.
RX PubMed=15383320; DOI=10.1016/j.yexcr.2004.07.010;
RA Wegmann F., Ebnet K., Du Pasquier L., Vestweber D., Butz S.;
RT "Endothelial adhesion molecule ESAM binds directly to the multidomain
RT adaptor MAGI-1 and recruits it to cell contacts.";
RL Exp. Cell Res. 300:121-133(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; THR-336; THR-338;
RP SER-340; SER-343; SER-348 AND SER-375, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Can mediate aggregation most likely through a homophilic
CC molecular interaction. {ECO:0000269|PubMed:11279107,
CC ECO:0000269|PubMed:11847224}.
CC -!- SUBUNIT: Interacts with MAGI1. {ECO:0000269|PubMed:15383320}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000305}.
CC Cell junction, tight junction {ECO:0000305}. Cell membrane
CC {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the heart and lung. Weakly
CC expressed in the kidney and skin. Expression is restricted to the
CC vascular endothelial cells. Expressed in the kidney, heart and tongue
CC (at protein level). Also expressed on megakaryocytes and activated
CC platelets. {ECO:0000269|PubMed:11279107, ECO:0000269|PubMed:11847224}.
CC -!- DEVELOPMENTAL STAGE: Expression in 8.5 dpc-9.5 dpc embryos is observed
CC in embryonic blood vessels including the dorsal aorta, intersomitic
CC arteries and the forming vascular plexus in the head as well as the
CC cardiac outflow tract. By 10.5 dpc-11.5 dpc embryos expression is found
CC in association with the all recognizable blood vessels and in
CC association with cells lining the heart chambers. At 10.5-days embryos
CC expression is associated with syncytiotrophoblasts and cytotrophoblasts
CC as well as endothelial cells associated with blood vessels in the
CC decidua. Expression decreased after mid-gestation from 15.5-day
CC embryos. {ECO:0000269|PubMed:11279107}.
CC -!- INDUCTION: Up-regulated on the surface of platelets upon activation.
CC {ECO:0000269|PubMed:11847224}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF361882; AAK51504.1; -; mRNA.
DR EMBL; BC049249; AAH49249.1; -; mRNA.
DR CCDS; CCDS22979.1; -.
DR RefSeq; NP_081378.1; NM_027102.3.
DR AlphaFoldDB; Q925F2; -.
DR SMR; Q925F2; -.
DR BioGRID; 213501; 1.
DR STRING; 10090.ENSMUSP00000002011; -.
DR GlyConnect; 2288; 1 N-Linked glycan (1 site).
DR GlyGen; Q925F2; 4 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q925F2; -.
DR PhosphoSitePlus; Q925F2; -.
DR jPOST; Q925F2; -.
DR MaxQB; Q925F2; -.
DR PaxDb; Q925F2; -.
DR PRIDE; Q925F2; -.
DR ProteomicsDB; 275781; -.
DR ABCD; Q925F2; 44 sequenced antibodies.
DR Antibodypedia; 32908; 489 antibodies from 32 providers.
DR DNASU; 69524; -.
DR Ensembl; ENSMUST00000002011; ENSMUSP00000002011; ENSMUSG00000001946.
DR GeneID; 69524; -.
DR KEGG; mmu:69524; -.
DR UCSC; uc009ouz.2; mouse.
DR CTD; 90952; -.
DR MGI; MGI:1916774; Esam.
DR VEuPathDB; HostDB:ENSMUSG00000001946; -.
DR eggNOG; ENOG502QRZ4; Eukaryota.
DR GeneTree; ENSGT00940000157231; -.
DR HOGENOM; CLU_040549_3_1_1; -.
DR InParanoid; Q925F2; -.
DR OMA; WYTLEGE; -.
DR OrthoDB; 831462at2759; -.
DR PhylomeDB; Q925F2; -.
DR TreeFam; TF330875; -.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR BioGRID-ORCS; 69524; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q925F2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q925F2; protein.
DR Bgee; ENSMUSG00000001946; Expressed in brain blood vessel and 231 other tissues.
DR ExpressionAtlas; Q925F2; baseline and differential.
DR Genevisible; Q925F2; MM.
DR GO; GO:0005912; C:adherens junction; IDA:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; ISO:MGI.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISO:MGI.
DR GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; TAS:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:MGI.
DR GO; GO:0008104; P:protein localization; ISO:MGI.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:0030833; P:regulation of actin filament polymerization; ISO:MGI.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR042757; ESAM.
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 PANTHER; PTHR44549; PTHR44549; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Tight junction; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000250"
FT CHAIN 30..394
FT /note="Endothelial cell-selective adhesion molecule"
FT /id="PRO_0000014754"
FT TOPO_DOM 30..251
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 37..146
FT /note="Ig-like V-type"
FT DOMAIN 159..243
FT /note="Ig-like C2-type"
FT REGION 304..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 336
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 338
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 177..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 394 AA; 41810 MW; 3D2B354943A2227D CRC64;
MILQAGTPET SLLRVLFLGL STLAAFSRAQ MELHVPPGLN KLEAVEGEEV VLPAWYTMAR
EESWSHPREV PILIWFLEQE GKEPNQVLSY INGVMTNKPG TALVHSISSR NVSLRLGALQ
EGDSGTYRCS VNVQNDEGKS IGHSIKSIEL KVLVPPAPPS CSLQGVPYVG TNVTLNCKSP
RSKPTAQYQW ERLAPSSQVF FGPALDAVRG SLKLTNLSIA MSGVYVCKAQ NRVGFAKCNV
TLDVMTGSKA AVVAGAVVGT FVGLVLIAGL VLLYQRRSKT LEELANDIKE DAIAPRTLPW
TKGSDTISKN GTLSSVTSAR ALRPPKAAPP RPGTFTPTPS VSSQALSSPR LPRVDEPPPQ
AVSLTPGGVS SSALSRMGAV PVMVPAQSQA GSLV
