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ICAM2_MOUSE
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   03-AUG-2022, entry version 180.
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   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; P35330; -.
DR   PRIDE; P35330; -.
DR   ProteomicsDB; 273258; -.
DR   ABCD; P35330; 22 sequenced antibodies.
DR   Antibodypedia; 796; 923 antibodies from 43 providers.
DR   DNASU; 15896; -.
DR   Ensembl; ENSMUST00000001055; ENSMUSP00000001055; ENSMUSG00000001029.
DR   GeneID; 15896; -.
DR   KEGG; mmu:15896; -.
DR   UCSC; uc007lyx.1; mouse.
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; 731140at2759; -.
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 71 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 178 other 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:0005887; C:integral component of plasma membrane; IDA: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   Gene3D; 2.60.40.10; -; 2.
DR   IDEAL; IID50119; -.
DR   InterPro; IPR015653; ICAM2.
DR   InterPro; IPR013768; ICAM_N.
DR   InterPro; IPR003987; ICAM_VCAM_N.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR13771:SF3; PTHR13771:SF3; 1.
DR   Pfam; PF03921; ICAM_N; 1.
DR   PRINTS; PR01472; ICAMVCAM1.
DR   SUPFAM; SSF48726; SSF48726; 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
 
 
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