ICAM4_MOUSE
ID ICAM4_MOUSE Reviewed; 262 AA.
AC Q9ERM2; Q8K4L7; Q9CU00;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Intercellular adhesion molecule 4;
DE Short=ICAM-4;
DE AltName: CD_antigen=CD242;
DE Flags: Precursor;
GN Name=Icam4;
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] (ISOFORMS 1 AND 2), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Spleen;
RX PubMed=12406883; DOI=10.1182/blood-2002-08-2529;
RA Lee G., Spring F.A., Parsons S.F., Mankelow T.J., Peters L.L., Koury M.J.,
RA Mohandas N., Anstee D.J., Chasis J.A.;
RT "Novel secreted isoform of adhesion molecule ICAM-4: potential regulator of
RT membrane-associated ICAM-4 interactions.";
RL Blood 101:1790-1797(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 74-262 (ISOFORM 1).
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).
CC -!- FUNCTION: Adhesion molecule that binds to leukocyte adhesion LFA-1
CC protein LFA-1 (integrin alpha-L/beta-2). ICAM4 is also a ligand for
CC alpha-4/beta-1 and alpha-V integrins (By similarity). Isoform 2 may
CC modulate binding of membrane-associated ICAM4. {ECO:0000250,
CC ECO:0000269|PubMed:12406883}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:12406883}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted
CC {ECO:0000269|PubMed:12406883}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ERM2-1; Sequence=Displayed;
CC Name=2; Synonyms=ICAM-4S;
CC IsoId=Q9ERM2-2; Sequence=VSP_013464;
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM family.
CC {ECO:0000305}.
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DR EMBL; AF296282; AAG30953.1; -; mRNA.
DR EMBL; AF296283; AAM97787.1; -; mRNA.
DR EMBL; AK019013; BAB31510.1; -; mRNA.
DR CCDS; CCDS22890.1; -. [Q9ERM2-1]
DR CCDS; CCDS90509.1; -. [Q9ERM2-2]
DR RefSeq; NP_076381.1; NM_023892.2. [Q9ERM2-1]
DR AlphaFoldDB; Q9ERM2; -.
DR SMR; Q9ERM2; -.
DR CORUM; Q9ERM2; -.
DR STRING; 10090.ENSMUSP00000001040; -.
DR GlyGen; Q9ERM2; 3 sites.
DR PaxDb; Q9ERM2; -.
DR PRIDE; Q9ERM2; -.
DR ProteomicsDB; 267084; -. [Q9ERM2-1]
DR ProteomicsDB; 267085; -. [Q9ERM2-2]
DR TopDownProteomics; Q9ERM2-1; -. [Q9ERM2-1]
DR Antibodypedia; 25271; 276 antibodies from 30 providers.
DR DNASU; 78369; -.
DR Ensembl; ENSMUST00000001040; ENSMUSP00000001040; ENSMUSG00000001014. [Q9ERM2-1]
DR Ensembl; ENSMUST00000215077; ENSMUSP00000151013; ENSMUSG00000001014. [Q9ERM2-2]
DR GeneID; 78369; -.
DR KEGG; mmu:78369; -.
DR UCSC; uc009ojy.1; mouse. [Q9ERM2-2]
DR UCSC; uc009ojz.1; mouse. [Q9ERM2-1]
DR CTD; 3386; -.
DR MGI; MGI:1925619; Icam4.
DR VEuPathDB; HostDB:ENSMUSG00000001014; -.
DR eggNOG; ENOG502TF7V; Eukaryota.
DR GeneTree; ENSGT00940000162431; -.
DR HOGENOM; CLU_1165526_0_0_1; -.
DR InParanoid; Q9ERM2; -.
DR OMA; APFWVRI; -.
DR PhylomeDB; Q9ERM2; -.
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; 78369; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q9ERM2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9ERM2; protein.
DR Bgee; ENSMUSG00000001014; Expressed in fetal liver hematopoietic progenitor cell and 55 other tissues.
DR ExpressionAtlas; Q9ERM2; baseline and differential.
DR Genevisible; Q9ERM2; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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 Gene3D; 2.60.40.10; -; 2.
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 Pfam; PF03921; ICAM_N; 1.
DR PRINTS; PR01472; ICAMVCAM1.
DR SUPFAM; SSF48726; SSF48726; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Reference proteome; Repeat;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..262
FT /note="Intercellular adhesion molecule 4"
FT /id="PRO_0000014797"
FT TOPO_DOM 23..231
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 54..116
FT /note="Ig-like C2-type 1"
FT DOMAIN 138..209
FT /note="Ig-like C2-type 2"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 61..109
FT /evidence="ECO:0000250"
FT DISULFID 61..105
FT /evidence="ECO:0000250|UniProtKB:P32942,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 65..109
FT /evidence="ECO:0000250|UniProtKB:P32942"
FT DISULFID 145..202
FT /evidence="ECO:0000250"
FT VAR_SEQ 226..262
FT /note="ALSPASIALASTSIATLVGILLAVGAVYVRKYLAVQT -> GEASCNPREWV
FT RERGCCHSKGACRTGVGSTLGGPQTS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12406883"
FT /id="VSP_013464"
SQ SEQUENCE 262 AA; 28495 MW; E2F26890C04738DE CRC64;
MESALLLPSL LLVAAYPRGG SPQQEWMQSP PAPSVTSAPF WVRLNPELEA VPPGGSAWLN
CSHNCPLPVH SSLRTQLRQG KIVNGSGWVS YQLLDVRAWN SKVRCVVTCA GETREATARI
TAYKRPRSVI LEPPVLVGHK YTLRCYVTHV FPVGFLVVSL RRGGRVIYHE SLERFTGSDL
ANVTLTYVMR AGLNDLWQPL TCHARLNLDG LVVRSSSAPV MLTVLALSPA SIALASTSIA
TLVGILLAVG AVYVRKYLAV QT
