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Intercellular adhesion molecule 2 (ICAM-2) (Lymphocyte function-associated AG-1 counter-receptor) (CD antigen CD102)

 ICAM2_MOUSE             Reviewed;         277 AA.
P35330; Q9D8Q4;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
28-MAR-2018, entry version 157.
RecName: Full=Intercellular adhesion molecule 2;
Short=ICAM-2;
AltName: Full=Lymphocyte function-associated AG-1 counter-receptor;
AltName: CD_antigen=CD102;
Flags: Precursor;
Name=Icam2; Synonyms=Icam-2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=AKR/J; TISSUE=B-cell;
PubMed=1401904;
Xu H., Tong I.L., de Fougerolles A.R., Springer T.A.;
"Isolation, characterization, and expression of mouse ICAM-2
complementary and genomic DNA.";
J. Immunol. 149:2650-2655(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Pancreas;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH EZR; MSN AND RDX, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF 253-ARG--ARG-255.
PubMed=9472040;
Yonemura S., Hirao M., Doi Y., Takahashi N., Kondo T., Tsukita S.,
Tsukita S.;
"Ezrin/radixin/moesin (ERM) proteins bind to a positively charged
amino acid cluster in the juxta-membrane cytoplasmic domain of CD44,
CD43, and ICAM-2.";
J. Cell Biol. 140:885-895(1998).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: ICAM proteins are ligands for the leukocyte adhesion
protein LFA-1 (integrin alpha-L/beta-2). ICAM2 may play a role in
lymphocyte recirculation by blocking LFA-1-dependent cell
adhesion. It mediates adhesive interactions important for antigen-
specific immune response, NK-cell mediated clearance, lymphocyte
recirculation, and other cellular interactions important for
immune response and surveillance.
-!- SUBUNIT: Interacts with RDX, EZR and MSN.
{ECO:0000269|PubMed:9472040}.
-!- INTERACTION:
P26043:Rdx; NbExp=2; IntAct=EBI-1035485, EBI-647737;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
membrane protein {ECO:0000255}. Cell projection, microvillus
{ECO:0000269|PubMed:9472040}. Note=Co-localizes with RDX, EZR and
MSN in microvilli. {ECO:0000269|PubMed:9472040}.
-!- TISSUE SPECIFICITY: Expressed in endothelial cells and leukocytes.
High levels found in lung.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=ICAM-2;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Itlect_189";
-----------------------------------------------------------------------
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EMBL; X65493; CAA46474.1; -; mRNA.
EMBL; X65490; CAA46473.1; -; Genomic_DNA.
EMBL; X65491; CAA46473.1; JOINED; Genomic_DNA.
EMBL; X65492; CAA46473.1; JOINED; Genomic_DNA.
EMBL; AK007801; BAB25266.1; -; mRNA.
EMBL; BC039128; AAH39128.1; -; mRNA.
EMBL; BC039970; AAH39970.1; -; mRNA.
CCDS; CCDS25555.1; -.
PIR; A46510; A46510.
RefSeq; NP_034624.1; NM_010494.2.
RefSeq; XP_006532366.1; XM_006532303.1.
UniGene; Mm.394; -.
PDB; 1J19; X-ray; 2.40 A; B=253-268.
PDBsum; 1J19; -.
ProteinModelPortal; P35330; -.
SMR; P35330; -.
DIP; DIP-29094N; -.
IntAct; P35330; 1.
STRING; 10090.ENSMUSP00000001055; -.
iPTMnet; P35330; -.
PhosphoSitePlus; P35330; -.
SwissPalm; P35330; -.
EPD; P35330; -.
MaxQB; P35330; -.
PaxDb; P35330; -.
PRIDE; P35330; -.
Ensembl; ENSMUST00000001055; ENSMUSP00000001055; ENSMUSG00000001029.
GeneID; 15896; -.
KEGG; mmu:15896; -.
UCSC; uc007lyx.1; mouse.
CTD; 3384; -.
MGI; MGI:96394; Icam2.
eggNOG; ENOG410IH57; Eukaryota.
eggNOG; ENOG410Z9H1; LUCA.
GeneTree; ENSGT00530000063246; -.
HOGENOM; HOG000049136; -.
HOVERGEN; HBG052075; -.
InParanoid; P35330; -.
KO; K06523; -.
OMA; NFSCLAV; -.
OrthoDB; EOG091G022Y; -.
PhylomeDB; P35330; -.
TreeFam; TF333745; -.
Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-MMU-216083; Integrin cell surface interactions.
Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling.
EvolutionaryTrace; P35330; -.
PRO; PR:P35330; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000001029; -.
CleanEx; MM_ICAM2; -.
ExpressionAtlas; P35330; baseline and differential.
Genevisible; P35330; MM.
GO; GO:0071944; C:cell periphery; IDA:MGI.
GO; GO:0032154; C:cleavage furrow; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
GO; GO:0005902; C:microvillus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0001931; C:uropod; IDA:MGI.
GO; GO:0005178; F:integrin binding; ISO:MGI.
GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
GO; GO:0098609; P:cell-cell adhesion; IEA:InterPro.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR015653; ICAM2.
InterPro; IPR013768; ICAM_N.
InterPro; IPR003987; ICAM_VCAM_N.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
PANTHER; PTHR13771:SF3; PTHR13771:SF3; 1.
Pfam; PF03921; ICAM_N; 1.
PRINTS; PR01472; ICAMVCAM1.
SUPFAM; SSF48726; SSF48726; 2.
1: Evidence at protein level;
3D-structure; Cell adhesion; Cell projection; Complete proteome;
Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 22 {ECO:0000250}.
CHAIN 23 277 Intercellular adhesion molecule 2.
/FTId=PRO_0000014791.
TOPO_DOM 23 222 Extracellular. {ECO:0000255}.
TRANSMEM 223 247 Helical. {ECO:0000255}.
TOPO_DOM 248 277 Cytoplasmic. {ECO:0000255}.
DOMAIN 39 98 Ig-like C2-type 1.
DOMAIN 127 196 Ig-like C2-type 2.
REGION 250 277 Required for interaction with EZR, MSN
and RDX and co-localization to
microvilli. {ECO:0000269|PubMed:9472040}.
CARBOHYD 45 45 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 82 82 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 158 158 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 176 176 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 186 186 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 46 91 {ECO:0000250|UniProtKB:P13598}.
DISULFID 50 95 {ECO:0000250|UniProtKB:P13598}.
DISULFID 134 189 {ECO:0000250|UniProtKB:P13598}.
MUTAGEN 253 255 RRR->GGA: Loss of interaction with EZR,
MSN and RDX and co-localization to
microvilli. {ECO:0000269|PubMed:9472040}.
CONFLICT 272 272 F -> S (in Ref. 2; BAB25266).
{ECO:0000305}.
STRAND 256 259 {ECO:0000244|PDB:1J19}.
HELIX 262 264 {ECO:0000244|PDB:1J19}.
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


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