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Ig-like domain-containing protein

 W5Q263_SHEEP            Unreviewed;       536 AA.
W5Q263;
16-APR-2014, integrated into UniProtKB/TrEMBL.
16-APR-2014, sequence version 1.
26-FEB-2020, entry version 39.
RecName: Full=Ig-like domain-containing protein {ECO:0000259|PROSITE:PS50835};
Name=ICAM1 {ECO:0000313|Ensembl:ENSOARP00000016801};
Ovis aries (Sheep).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
Caprinae; Ovis.
NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000016801, ECO:0000313|Proteomes:UP000002356};
[1] {ECO:0000313|Ensembl:ENSOARP00000016801, ECO:0000313|Proteomes:UP000002356}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000016801,
ECO:0000313|Proteomes:UP000002356};
PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
Wang W., Xun X.;
"The sheep genome reference sequence: a work in progress.";
Anim. Genet. 41:449-453(2010).
[2] {ECO:0000313|Ensembl:ENSOARP00000016801}
IDENTIFICATION.
Ensembl;
Submitted (FEB-2014) to UniProtKB.
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EMBL; AMGL01091308; -; NOT_ANNOTATED_CDS; Genomic_DNA.
STRING; 9940.ENSOARP00000016801; -.
Ensembl; ENSOART00000017039; ENSOARP00000016801; ENSOARG00000015656.
GeneTree; ENSGT00940000162311; -.
HOGENOM; CLU_036160_1_1_1; -.
OMA; TFLTVYW; -.
Proteomes; UP000002356; Chromosome 5.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005178; F:integrin binding; IEA:Ensembl.
GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:Ensembl.
GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:0061028; P:establishment of endothelial barrier; IEA:Ensembl.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IEA:Ensembl.
GO; GO:0022614; P:membrane to membrane docking; IEA:Ensembl.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IEA:Ensembl.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
GO; GO:0002693; P:positive regulation of cellular extravasation; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IEA:Ensembl.
GO; GO:1900027; P:regulation of ruffle assembly; IEA:Ensembl.
GO; GO:0002291; P:T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; IEA:Ensembl.
GO; GO:0002457; P:T cell antigen processing and presentation; IEA:Ensembl.
GO; GO:0072683; P:T cell extravasation; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR003988; ICAM.
InterPro; IPR013768; ICAM_N.
InterPro; IPR003987; ICAM_VCAM_N.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
Pfam; PF03921; ICAM_N; 1.
PRINTS; PR01473; ICAM.
PRINTS; PR01472; ICAMVCAM1.
SMART; SM00409; IG; 3.
SUPFAM; SSF48726; SSF48726; 5.
PROSITE; PS50835; IG_LIKE; 1.
4: Predicted;
Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
Reference proteome {ECO:0000313|Proteomes:UP000002356};
Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAM:Phobius}.
SIGNAL 1..30
/evidence="ECO:0000256|SAM:SignalP"
CHAIN 31..536
/note="Ig-like domain-containing protein"
/evidence="ECO:0000256|SAM:SignalP"
/id="PRO_5004869749"
TRANSMEM 486..507
/note="Helical"
/evidence="ECO:0000256|SAM:Phobius"
DOMAIN 398..476
/note="Ig-like"
/evidence="ECO:0000259|PROSITE:PS50835"
COILED 506..526
/evidence="ECO:0000256|SAM:Coils"
SEQUENCE 536 AA; 58577 MW; E8604BC4B87D833D CRC64;
PAMAPPPGAA PAALLALLVL LGTLLPGSGG AEISIHPPKA IIPRGGSLRV NCSISCDRKT
TFGLETVLNK EEVSRGPNWK VFELSDVQEE INPLCYSNCH GEQIVASMNL TIYWFPERVE
LAPLPLWQPV GEELNLSCQV SGGGPRHHLS MVLLRGEEEL DRQPVGKEEP AKVTFMVQPR
REDHGTSFSC RWELDLRSQG LELFQNTSAP RKLQTYVLPS TDPHLEAPPV VEVGSRWPVK
CTLDGLFPAS DAEVYVQLGD QKLESNITYN GDSVLAEAWT EENEEGTHSL RCSVSLGEKI
RRTRGSVTMY SFPLPTLTLS PPEVSEWTTV TVECVTRDGA VVRLNGVSAE PPGPRAQLKL
NVSADDHGSN FSCSAALKIA GQEVHKIQTR ELHVLYGPRL DQRDCLGNWT WQEGSEQTLK
CAARGNPIPK LNCSRKGDGA SLPIGDLRPV TREVAGTYLC WATSARGGVT REVVLNVLYG
QNILDIVIPV VAVTLILGTL GTAGYIYNYQ RKIQKYELQK AQKEAALKLN AQSTPP


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Pathways :
WP1689: Porphyrin and chlorophyll metabolism
WP2371: Parkinsons Disease Pathway
WP540: Cytoplasmic Ribosomal Proteins
WP1049: G Protein Signaling Pathways
WP1713: Two-component system
WP163: Cytoplasmic Ribosomal Proteins
WP1659: Glycine, serine and threonine metabolism
WP1789: Binding of RNA by Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs)
WP1665: Limonene and pinene degradation
WP525: Mitochondrial Unfolded-Protein Response
WP914: NLR proteins
WP1438: Influenza A virus infection
WP1892: Protein folding
WP1531: Vitamin D synthesis
WP2032: TSH signaling pathway
WP1887: Post-translational modification: synthesis of GPI-anchored proteins
WP1675: Nitrogen metabolism
WP813: G Protein Signaling Pathways
WP1685: Peptidoglycan biosynthesis
WP1032: NLR proteins
WP1616: ABC transporters
WP2199: Seed Development
WP1963: The effect of Glucocorticoids on target gene expression
WP1644: DNA replication
WP2272: Pathogenic Escherichia coli infection

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Bibliography :
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[28785060] Angulin proteins ILDR1 and ILDR2 regulate alternative pre-mRNA splicing through binding to splicing factors TRA2A, TRA2B, or SRSF1.
[28739804] Role of the disulfide bond in stabilizing and folding of the fimbrial protein DraE from uropathogenic .
[28461473] ILDR1 is important for paracellular water transport and urine concentration mechanism.