ID ICAM2_MOUSE Reviewed; 277 AA.
AC P35330; Q9D8Q4;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 24-JAN-2024, entry version 188.
DE RecName: Full=Intercellular adhesion molecule 2;
DE Short=ICAM-2;
DE AltName: Full=Lymphocyte function-associated AG-1 counter-receptor;
DE AltName: CD_antigen=CD102;
DE Flags: Precursor;
GN Name=Icam2; Synonyms=Icam-2;
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 [GENOMIC DNA / MRNA].
RC STRAIN=AKR/J; TISSUE=B-cell;
RX PubMed=1401904;
RA Xu H., Tong I.L., de Fougerolles A.R., Springer T.A.;
RT "Isolation, characterization, and expression of mouse ICAM-2 complementary
RT and genomic DNA.";
RL J. Immunol. 149:2650-2655(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [4]
RP INTERACTION WITH EZR; MSN AND RDX, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 253-ARG--ARG-255.
RX PubMed=9472040; DOI=10.1083/jcb.140.4.885;
RA Yonemura S., Hirao M., Doi Y., Takahashi N., Kondo T., Tsukita S.,
RA Tsukita S.;
RT "Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino
RT acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and
RT ICAM-2.";
RL J. Cell Biol. 140:885-895(1998).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Lung, and Spleen;
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).
CC -!- FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein
CC LFA-1 (integrin alpha-L/beta-2). ICAM2 may play a role in lymphocyte
CC recirculation by blocking LFA-1-dependent cell adhesion. It mediates
CC adhesive interactions important for antigen-specific immune response,
CC NK-cell mediated clearance, lymphocyte recirculation, and other
CC cellular interactions important for immune response and surveillance.
CC -!- SUBUNIT: Interacts with RDX, EZR and MSN. {ECO:0000269|PubMed:9472040}.
CC -!- INTERACTION:
CC P35330; P26043: Rdx; NbExp=2; IntAct=EBI-1035485, EBI-647737;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}. Cell projection, microvillus
CC {ECO:0000269|PubMed:9472040}. Note=Co-localizes with RDX, EZR and MSN
CC in microvilli. {ECO:0000269|PubMed:9472040}.
CC -!- TISSUE SPECIFICITY: Expressed in endothelial cells and leukocytes. High
CC levels found in lung.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=ICAM-2;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Itlect_189";
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DR EMBL; X65493; CAA46474.1; -; mRNA.
DR EMBL; X65490; CAA46473.1; -; Genomic_DNA.
DR EMBL; X65491; CAA46473.1; JOINED; Genomic_DNA.
DR EMBL; X65492; CAA46473.1; JOINED; Genomic_DNA.
DR EMBL; AK007801; BAB25266.1; -; mRNA.
DR EMBL; BC039128; AAH39128.1; -; mRNA.
DR EMBL; BC039970; AAH39970.1; -; mRNA.
DR CCDS; CCDS25555.1; -.
DR PIR; A46510; A46510.
DR RefSeq; NP_034624.1; NM_010494.2.
DR RefSeq; XP_006532366.1; XM_006532303.1.
DR PDB; 1J19; X-ray; 2.40 A; B=253-268.
DR PDBsum; 1J19; -.
DR AlphaFoldDB; P35330; -.
DR SMR; P35330; -.
DR DIP; DIP-29094N; -.
DR IntAct; P35330; 1.
DR STRING; 10090.ENSMUSP00000001055; -.
DR GlyCosmos; P35330; 5 sites, No reported glycans.
DR GlyGen; P35330; 5 sites.
DR iPTMnet; P35330; -.
DR PhosphoSitePlus; P35330; -.
DR SwissPalm; P35330; -.
DR CPTAC; non-CPTAC-3315; -.
DR EPD; P35330; -.
DR jPOST; P35330; -.
DR MaxQB; P35330; -.
DR PaxDb; 10090-ENSMUSP00000001055; -.
DR ProteomicsDB; 273258; -.
DR ABCD; P35330; 22 sequenced antibodies.
DR Antibodypedia; 796; 998 antibodies from 43 providers.
DR DNASU; 15896; -.
DR Ensembl; ENSMUST00000001055.15; ENSMUSP00000001055.9; ENSMUSG00000001029.16.
DR GeneID; 15896; -.
DR KEGG; mmu:15896; -.
DR UCSC; uc007lyx.1; mouse.
DR AGR; MGI:96394; -.
DR CTD; 3384; -.
DR MGI; MGI:96394; Icam2.
DR VEuPathDB; HostDB:ENSMUSG00000001029; -.
DR eggNOG; ENOG502RZRA; Eukaryota.
DR GeneTree; ENSGT00940000161654; -.
DR HOGENOM; CLU_088446_0_0_1; -.
DR InParanoid; P35330; -.
DR OMA; QVYEPVQ; -.
DR OrthoDB; 4014106at2759; -.
DR PhylomeDB; P35330; -.
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 Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling.
DR BioGRID-ORCS; 15896; 2 hits in 76 CRISPR screens.
DR EvolutionaryTrace; P35330; -.
DR PRO; PR:P35330; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P35330; Protein.
DR Bgee; ENSMUSG00000001029; Expressed in right lung lobe and 181 other cell types or tissues.
DR ExpressionAtlas; P35330; baseline and differential.
DR Genevisible; P35330; MM.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0032154; C:cleavage furrow; ISO:MGI.
DR GO; GO:0005902; C:microvillus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0001931; C:uropod; IDA:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:InterPro.
DR CDD; cd20995; IgI_N_ICAM-2; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR IDEAL; IID50119; -.
DR InterPro; IPR013768; ICAM_N.
DR InterPro; IPR047012; ICAM_VCAM.
DR InterPro; IPR003987; ICAM_VCAM_N.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR13771; INTERCELLULAR ADHESION MOLECULE; 1.
DR PANTHER; PTHR13771:SF3; INTERCELLULAR ADHESION MOLECULE 2; 1.
DR Pfam; PF03921; ICAM_N; 1.
DR PRINTS; PR01472; ICAMVCAM1.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell projection; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..277
FT /note="Intercellular adhesion molecule 2"
FT /id="PRO_0000014791"
FT TOPO_DOM 23..222
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 39..98
FT /note="Ig-like C2-type 1"
FT DOMAIN 127..196
FT /note="Ig-like C2-type 2"
FT REGION 250..277
FT /note="Required for interaction with EZR, MSN and RDX and
FT co-localization to microvilli"
FT /evidence="ECO:0000269|PubMed:9472040"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..91
FT /evidence="ECO:0000250|UniProtKB:P13598"
FT DISULFID 50..95
FT /evidence="ECO:0000250|UniProtKB:P13598"
FT DISULFID 134..189
FT /evidence="ECO:0000250|UniProtKB:P13598"
FT MUTAGEN 253..255
FT /note="RRR->GGA: Loss of interaction with EZR, MSN and RDX
FT and co-localization to microvilli."
FT /evidence="ECO:0000269|PubMed:9472040"
FT CONFLICT 272
FT /note="F -> S (in Ref. 2; BAB25266)"
FT /evidence="ECO:0000305"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:1J19"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:1J19"
SQ SEQUENCE 277 AA; 31390 MW; CBB2FFBCF207DA48 CRC64;
MSSFACWSLS LLILFYSPGS GEKAFEVYIW SEKQIVEATE SWKINCSTNC AAPDMGGLET
PTNKIMLEEH PQGKWKQFLV SNVSKDTVFF CHFTCSGKQH SESLNIRVYQ PPAQVTLKLQ
PPRVFVGEDF TIECTVSPVQ PLERLTLSLL RGRETLKNQT FGGAETVPQE ATATFNSTAL
KKDGLNFSCQ AELDLRPHGG YIIRSISEYQ ILEVYEPMQD NQMVIIIVVV SILLFLFVTS
VLLCFIFGQH WHRRRTGTYG VLAAWRRLPR AFRARPV
//
