ID   ESAM_MACFA              Reviewed;         390 AA.
AC   Q95KI3;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Endothelial cell-selective adhesion molecule;
DE   Flags: Precursor;
GN   Name=ESAM; ORFNames=QtrA-11419;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Temporal cortex;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA   Suzuki Y., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
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; AB060855; BAB46874.1; -; mRNA.
DR   RefSeq; NP_001274219.1; NM_001287290.1.
DR   AlphaFoldDB; Q95KI3; -.
DR   SMR; Q95KI3; -.
DR   STRING; 9541.XP_005580092.1; -.
DR   GeneID; 102122049; -.
DR   CTD; 90952; -.
DR   VEuPathDB; HostDB:ENSMFAG00000000739; -.
DR   eggNOG; ENOG502QRZ4; Eukaryota.
DR   OMA; CFINLEI; -.
DR   OrthoDB; 831462at2759; -.
DR   Proteomes; UP000233100; Chromosome 14.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098609; P:cell-cell adhesion; IEA:InterPro.
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   2: Evidence at transcript 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..390
FT                   /note="Endothelial cell-selective adhesion molecule"
FT                   /id="PRO_0000014753"
FT   TOPO_DOM        30..248
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        249..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        270..390
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          30..143
FT                   /note="Ig-like V-type"
FT   DOMAIN          156..242
FT                   /note="Ig-like C2-type"
FT   REGION          316..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         301
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q925F2"
FT   MOD_RES         332
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q925F2"
FT   MOD_RES         334
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q925F2"
FT   MOD_RES         336
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q925F2"
FT   MOD_RES         339
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q925F2"
FT   MOD_RES         344
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q925F2"
FT   MOD_RES         371
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q925F2"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        213
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        236
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        174..224
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   390 AA;  40946 MW;  CDBF63F2BD464EF5 CRC64;
     MISLPGPLVT NLLRFLFLGL SALAPPSRAE LQLHLPANQL QAVEGGEVVL PAWYTLHAEV
     SSAQPGEVPF VMWFFKDKEK EDQVLSYING VTTSKPGVSL VYSMPSRNLS LRLEGLQEKD
     SGPYSCSVNV QDKNGQASGH SIKTLELNVL VPPAPPSCRL QGVPRVGANV TLSCQSPRSK
     PAVQYQWDRQ LPSFQTFFAP VLDVIRGSLS LTNLSSSMAG VYVCKAHNEV GTAQCNVTLE
     VSTGPGAAVV AGAVVGTLVG LGLLAGLVLL YHRRGKALEE PANDIKEDAI APRTLPWPKS
     SDTISKNGTL SSVTSARALR PPHGPPRPGA LTPTPSLSSQ ALPSPRLPTT DGANPQPISL
     IPGGVSSSGL SRMGAVPVMV PAQSQAGSLV