ESAM_RAT
ID ESAM_RAT Reviewed; 394 AA.
AC Q6AYD4;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Endothelial cell-selective adhesion molecule;
DE Flags: Precursor;
GN Name=Esam;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-348, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Can mediate aggregation most likely through a homophilic
CC molecular interaction. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MAGI1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000250}.
CC Cell junction, tight junction {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
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DR EMBL; BC079093; AAH79093.1; -; mRNA.
DR RefSeq; NP_001004245.1; NM_001004245.1.
DR AlphaFoldDB; Q6AYD4; -.
DR STRING; 10116.ENSRNOP00000051485; -.
DR GlyGen; Q6AYD4; 4 sites.
DR iPTMnet; Q6AYD4; -.
DR PhosphoSitePlus; Q6AYD4; -.
DR PaxDb; Q6AYD4; -.
DR Ensembl; ENSRNOT00000050609; ENSRNOP00000051485; ENSRNOG00000033217.
DR GeneID; 300519; -.
DR KEGG; rno:300519; -.
DR UCSC; RGD:1303286; rat.
DR CTD; 90952; -.
DR RGD; 1303286; Esam.
DR eggNOG; ENOG502QRZ4; Eukaryota.
DR GeneTree; ENSGT00940000157231; -.
DR InParanoid; Q6AYD4; -.
DR OMA; CFINLEI; -.
DR OrthoDB; 831462at2759; -.
DR PhylomeDB; Q6AYD4; -.
DR TreeFam; TF330875; -.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR PRO; PR:Q6AYD4; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000033217; Expressed in lung and 19 other tissues.
DR ExpressionAtlas; Q6AYD4; baseline and differential.
DR Genevisible; Q6AYD4; RN.
DR GO; GO:0005912; C:adherens junction; ISO:RGD.
DR GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; ISO:RGD.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISO:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:RGD.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:RGD.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; ISO:RGD.
DR GO; GO:0030833; P:regulation of actin filament polymerization; ISO:RGD.
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_0000014755"
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 156..243
FT /note="Ig-like C2-type"
FT REGION 300..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 336
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q925F2"
FT MOD_RES 338
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q925F2"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q925F2"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q925F2"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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; 41936 MW; 9CA7402EA46F1195 CRC64;
MILPARTPET SLLRVLFLGL STLAAFSLAQ MELHVPPGLN KLEAVEGEEV VLPAWYTMAR
EESSSHPWEA PFLIWFLEQE GKEPKQVLSY FKGSLSNKPG VTLVHSISTR NVSLRLDALQ
EGDSGTYRCS VNAYDSDGKN IGHSIKTIEL KVLVPPAPPS CSFQGVPYVG TNVTLNCKSP
RSKPTAQYQW ERLAPSSQVF FGPALDTVRG SLKLTNISTA MSGVYVCKAQ NRVGFAQCNV
TLDVMTGSKA AVVAGAVVGT FVGLVLIAGL VLLYQRRSKT LEELANDIKE DAIAPRTLPW
TKGSDTISKN GTLSSVTSAR ALRPPKAAPP RPGTFTPTPS VSSQALSSPR LPRTDGPPPQ
AVSLTPGGVS SSTLNRMGAV PVMVPAQSQA GSLV
