ICAM5_MOUSE
ID ICAM5_MOUSE Reviewed; 917 AA.
AC Q60625; G5E826; Q2KHL7; Q3UY19;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Intercellular adhesion molecule 5;
DE Short=ICAM-5;
DE AltName: Full=Telencephalin;
DE Flags: Precursor;
GN Name=Icam5; Synonyms=Icam3, Tlcn;
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, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=7794412; DOI=10.1016/0896-6273(94)90211-9;
RA Yoshihara Y., Oka S., Nemoto Y., Watanabe Y., Nagata S., Kagamiyama H.,
RA Mori K.;
RT "An ICAM-related neuronal glycoprotein, telencephalin, with brain segment-
RT specific expression.";
RL Neuron 12:541-553(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RC STRAIN=C57BL/CBA;
RX PubMed=9244438; DOI=10.1006/geno.1997.4812;
RA Sugino H., Yoshihara Y., Copeland N.G., Gilbert D.J., Jenkins N.A.,
RA Mori K.;
RT "Genomic organization and chromosomal localization of the mouse
RT telencephalin gene, a neuronal member of the ICAM family.";
RL Genomics 43:209-215(1997).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [8]
RP GLYCOSYLATION AT ASN-54, AND MUTAGENESIS OF ASN-54.
RX PubMed=22187327; DOI=10.1007/s10719-011-9363-0;
RA Ohgomori T., Nanao T., Morita A., Ikekita M.;
RT "Asn54-linked glycan is critical for functional folding of intercellular
RT adhesion molecule-5.";
RL Glycoconj. J. 29:47-55(2012).
CC -!- FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein
CC LFA-1 (integrin alpha-L/beta-2). {ECO:0000269|PubMed:7794412}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:7794412}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:7794412}.
CC -!- TISSUE SPECIFICITY: Expressed on neurons in the most rostral segment of
CC the mammalian brain, the telencephalon. {ECO:0000269|PubMed:7794412}.
CC -!- PTM: Glycosylation at Asn-54 is critical for functional folding.
CC {ECO:0000269|PubMed:22187327}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM family.
CC {ECO:0000305}.
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DR EMBL; U06483; AAA67204.1; -; mRNA.
DR EMBL; AK135040; BAE22394.1; -; mRNA.
DR EMBL; AC159314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466522; EDL25153.1; -; Genomic_DNA.
DR EMBL; BC113140; AAI13141.1; -; mRNA.
DR EMBL; U89893; AAC53308.1; -; Genomic_DNA.
DR CCDS; CCDS22891.1; -.
DR PIR; I48950; I48950.
DR RefSeq; NP_032345.2; NM_008319.2.
DR AlphaFoldDB; Q60625; -.
DR SMR; Q60625; -.
DR BioGRID; 200503; 5.
DR IntAct; Q60625; 4.
DR STRING; 10090.ENSMUSP00000019616; -.
DR CarbonylDB; Q60625; -.
DR GlyConnect; 2409; 15 N-Linked glycans (10 sites).
DR GlyGen; Q60625; 14 sites, 15 N-linked glycans (10 sites).
DR iPTMnet; Q60625; -.
DR PhosphoSitePlus; Q60625; -.
DR PaxDb; Q60625; -.
DR PeptideAtlas; Q60625; -.
DR PRIDE; Q60625; -.
DR ProteomicsDB; 267086; -.
DR Antibodypedia; 2298; 288 antibodies from 37 providers.
DR DNASU; 15898; -.
DR Ensembl; ENSMUST00000019616; ENSMUSP00000019616; ENSMUSG00000032174.
DR GeneID; 15898; -.
DR KEGG; mmu:15898; -.
DR UCSC; uc009oka.2; mouse.
DR CTD; 7087; -.
DR MGI; MGI:109430; Icam5.
DR VEuPathDB; HostDB:ENSMUSG00000032174; -.
DR eggNOG; ENOG502QS16; Eukaryota.
DR GeneTree; ENSGT00940000162184; -.
DR HOGENOM; CLU_014560_0_0_1; -.
DR InParanoid; Q60625; -.
DR OMA; GCPSNWT; -.
DR OrthoDB; 731140at2759; -.
DR PhylomeDB; Q60625; -.
DR TreeFam; TF333745; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR BioGRID-ORCS; 15898; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Icam5; mouse.
DR PRO; PR:Q60625; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q60625; protein.
DR Bgee; ENSMUSG00000032174; Expressed in entorhinal cortex and 41 other tissues.
DR Genevisible; Q60625; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:InterPro.
DR GO; GO:0006909; P:phagocytosis; IDA:MGI.
DR Gene3D; 2.60.40.10; -; 9.
DR InterPro; IPR003988; ICAM.
DR InterPro; IPR013768; ICAM_N.
DR InterPro; IPR003987; ICAM_VCAM_N.
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 Pfam; PF03921; ICAM_N; 1.
DR PRINTS; PR01473; ICAM.
DR PRINTS; PR01472; ICAMVCAM1.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 9.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 1: Evidence at protein level;
KW Cell adhesion; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..917
FT /note="Intercellular adhesion molecule 5"
FT /id="PRO_0000014800"
FT TOPO_DOM 32..833
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 834..854
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 855..917
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 48..130
FT /note="Ig-like C2-type 1"
FT DOMAIN 135..235
FT /note="Ig-like C2-type 2"
FT DOMAIN 242..329
FT /note="Ig-like C2-type 3"
FT DOMAIN 337..402
FT /note="Ig-like C2-type 4"
FT DOMAIN 408..486
FT /note="Ig-like C2-type 5"
FT DOMAIN 491..567
FT /note="Ig-like C2-type 6"
FT DOMAIN 572..651
FT /note="Ig-like C2-type 7"
FT DOMAIN 665..738
FT /note="Ig-like C2-type 8"
FT DOMAIN 745..828
FT /note="Ig-like C2-type 9"
FT REGION 884..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMF0"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:22187327"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 645
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 762
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 793
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 794
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 59..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 142..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 249..302
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 344..383
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 415..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 498..551
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 579..644
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 672..724
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 767..812
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 54
FT /note="N->Q: Fails to form disulfide bonds and to induce
FT filopodia-like protrusions."
FT /evidence="ECO:0000269|PubMed:22187327"
FT CONFLICT 47
FT /note="R -> P (in Ref. 1; AAA67204)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="S -> T (in Ref. 1; AAA67204)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="H -> P (in Ref. 1; AAA67204)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="R -> Q (in Ref. 2; BAE22394)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="P -> R (in Ref. 2; BAE22394)"
FT /evidence="ECO:0000305"
FT CONFLICT 859
FT /note="Q -> L (in Ref. 5; AAI13141)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 917 AA; 96946 MW; C2E98892A190F59C CRC64;
MPGPSPGLRR ALLGLWAALG LGILGISAVA LEPFWADLQP RVALVERGGS LWLNCSTNCP
RPERGGLETS LRRNGTQRGL RWLARQLVDI REPETQPVCF FRCARRTLQA RGLIRTFQRP
DRVELVPLPS WQPVGENFTL SCRVPGAGPR ASLTLTLLRG GQELIRRSFV GEPPRARGAM
LTARVLARRE DHRVNFSCLA ELDLRPHGLG LFANSSAPRQ LRTFAMPPHS PSLIAPRVLE
VDSERPVTCT LDGLFPAPEA GVYLSLGDQR LNPNVTLDGD SLVATATATA SAEQEGTKQL
MCVVTLGGES RETQENLTVY SFPTPLLTLS EPEAPEGKMV TISCWAGARA LVTLEGIPAA
VPGQPAELQL NVTKNDDKRG FFCDAALDVD GETLRKNQSS ELRVLYAPRL DDLDCPRSWT
WPEGPEQTLH CEARGNPEPS VHCARPEGGA VLALGLLGPV TRALAGTYRC TAVNGQGQAV
KDVTLTVEYA PALDSVGCPE HITWLEGTEA SLSCVAHGVP PPSVSCVRSG KEEVMEGPLR
VAREHAGTYR CEAINARGSA AKNVAVTVEY GPSFEELGCP SNWTWVEGSG KLFSCEVDGK
PEPRVECVGS EGASEGIVLP LVSSNSGPRN SMTPGNLSPG IYLCNATNRH GSTVKTVVVS
AESPPQMDES SCPSHQTWLE GAEATALACS ARGRPSPRVH CSREGAARLE RLQVSREDAG
TYRCVATNAH GTDSRTVTVG VEYRPVVAEL AASPPSVRPG GNFTLTCRAE AWPPAQISWR
APPGALNLGL SSNNSTLSVA GAMGSHGGEY ECAATNAHGR HARRITVRVA GPWLWVAVGG
AAGGAALLAA GAGLAFYVQS TACKKGEYNV QEAESSGEAV CLNGAGGTPG AEGGAETPGT
AESPADGEVF AIQLTSS
