ESAM_HUMAN
ID ESAM_HUMAN Reviewed; 390 AA.
AC Q96AP7; B4DVN8; Q96T50;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Endothelial cell-selective adhesion molecule;
DE Flags: Precursor;
GN Name=ESAM; ORFNames=UNQ220/PRO246;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
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] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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 [6]
RP PROTEIN SEQUENCE OF 30-44.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-169.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
CC -!- FUNCTION: Can mediate aggregation most likely through a homophilic
CC molecular interaction. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MAGI1. {ECO:0000250}.
CC -!- INTERACTION:
CC Q96AP7; P55061: TMBIM6; NbExp=3; IntAct=EBI-4314670, EBI-1045825;
CC Q96AP7; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-4314670, EBI-10243654;
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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96AP7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96AP7-2; Sequence=VSP_055594, VSP_055595, VSP_055596;
CC -!- TISSUE SPECIFICITY: Highly expressed in endothelial cells.
CC {ECO:0000269|PubMed:11279107}.
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DR EMBL; AF361746; AAK51065.1; -; mRNA.
DR EMBL; AY358382; AAQ88748.1; -; mRNA.
DR EMBL; AK075396; BAC11594.1; -; mRNA.
DR EMBL; AK301160; BAG62750.1; -; mRNA.
DR EMBL; AP000866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016868; AAH16868.1; -; mRNA.
DR CCDS; CCDS8453.1; -. [Q96AP7-1]
DR RefSeq; NP_620411.2; NM_138961.2. [Q96AP7-1]
DR AlphaFoldDB; Q96AP7; -.
DR SMR; Q96AP7; -.
DR BioGRID; 124781; 10.
DR IntAct; Q96AP7; 7.
DR STRING; 9606.ENSP00000278927; -.
DR GlyConnect; 1935; 7 N-Linked glycans (3 sites).
DR GlyGen; Q96AP7; 5 sites, 7 N-linked glycans (3 sites).
DR iPTMnet; Q96AP7; -.
DR PhosphoSitePlus; Q96AP7; -.
DR BioMuta; ESAM; -.
DR DMDM; 68052240; -.
DR jPOST; Q96AP7; -.
DR MassIVE; Q96AP7; -.
DR MaxQB; Q96AP7; -.
DR PaxDb; Q96AP7; -.
DR PeptideAtlas; Q96AP7; -.
DR PRIDE; Q96AP7; -.
DR ProteomicsDB; 5285; -.
DR ProteomicsDB; 75983; -. [Q96AP7-1]
DR Antibodypedia; 32908; 489 antibodies from 32 providers.
DR DNASU; 90952; -.
DR Ensembl; ENST00000278927.10; ENSP00000278927.5; ENSG00000149564.12. [Q96AP7-1]
DR Ensembl; ENST00000444566.5; ENSP00000406689.1; ENSG00000149564.12. [Q96AP7-2]
DR GeneID; 90952; -.
DR KEGG; hsa:90952; -.
DR MANE-Select; ENST00000278927.10; ENSP00000278927.5; NM_138961.3; NP_620411.2.
DR UCSC; uc001qav.5; human. [Q96AP7-1]
DR CTD; 90952; -.
DR DisGeNET; 90952; -.
DR GeneCards; ESAM; -.
DR HGNC; HGNC:17474; ESAM.
DR HPA; ENSG00000149564; Low tissue specificity.
DR MIM; 614281; gene.
DR neXtProt; NX_Q96AP7; -.
DR OpenTargets; ENSG00000149564; -.
DR PharmGKB; PA134954912; -.
DR VEuPathDB; HostDB:ENSG00000149564; -.
DR eggNOG; ENOG502QRZ4; Eukaryota.
DR GeneTree; ENSGT00940000157231; -.
DR HOGENOM; CLU_1824658_0_0_1; -.
DR InParanoid; Q96AP7; -.
DR OMA; WYTLEGE; -.
DR OrthoDB; 831462at2759; -.
DR PhylomeDB; Q96AP7; -.
DR TreeFam; TF330875; -.
DR PathwayCommons; Q96AP7; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR SignaLink; Q96AP7; -.
DR BioGRID-ORCS; 90952; 8 hits in 1069 CRISPR screens.
DR GeneWiki; ESAM_(gene); -.
DR GenomeRNAi; 90952; -.
DR Pharos; Q96AP7; Tbio.
DR PRO; PR:Q96AP7; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96AP7; protein.
DR Bgee; ENSG00000149564; Expressed in right lung and 160 other tissues.
DR ExpressionAtlas; Q96AP7; baseline and differential.
DR Genevisible; Q96AP7; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; IDA:ARUK-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0032991; C:protein-containing complex; IDA:ARUK-UCL.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IDA:ARUK-UCL.
DR GO; GO:0070830; P:bicellular tight junction assembly; IMP:ARUK-UCL.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:ARUK-UCL.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; NAS:ARUK-UCL.
DR GO; GO:0008104; P:protein localization; IDA:ARUK-UCL.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IDA:ARUK-UCL.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IDA:ARUK-UCL.
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 Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
KW Direct protein sequencing; 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:0000269|PubMed:15340161"
FT CHAIN 30..390
FT /note="Endothelial cell-selective adhesion molecule"
FT /id="PRO_0000014752"
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 153..242
FT /note="Ig-like C2-type"
FT REGION 316..368
FT /note="Disordered"
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:0000269|PubMed:19159218"
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"
FT VAR_SEQ 22..200
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055594"
FT VAR_SEQ 287..320
FT /note="EDAIAPRTLPWPKSSDTISKNGTLSSVTSARALR -> VRSPLGLSFSAPKM
FT EWLWKWRDAHFYRDSYLSKW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055595"
FT VAR_SEQ 321..390
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055596"
FT VARIANT 273
FT /note="R -> C (in dbSNP:rs12792040)"
FT /id="VAR_049872"
FT CONFLICT 380
FT /note="V -> M (in Ref. 1; AAK51065)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 41176 MW; C5E3F302F41B6EEC CRC64;
MISLPGPLVT NLLRFLFLGL SALAPPSRAQ LQLHLPANRL QAVEGGEVVL PAWYTLHGEV
SSSQPWEVPF VMWFFKQKEK EDQVLSYING VTTSKPGVSL VYSMPSRNLS LRLEGLQEKD
SGPYSCSVNV QDKQGKSRGH SIKTLELNVL VPPAPPSCRL QGVPHVGANV TLSCQSPRSK
PAVQYQWDRQ LPSFQTFFAP ALDVIRGSLS LTNLSSSMAG VYVCKAHNEV GTAQCNVTLE
VSTGPGAAVV AGAVVGTLVG LGLLAGLVLL YHRRGKALEE PANDIKEDAI APRTLPWPKS
SDTISKNGTL SSVTSARALR PPHGPPRPGA LTPTPSLSSQ ALPSPRLPTT DGAHPQPISP
IPGGVSSSGL SRMGAVPVMV PAQSQAGSLV
