AGRE4_MOUSE
ID AGRE4_MOUSE Reviewed; 689 AA.
AC Q91ZE5; Q3U1I7; Q8BYX0; Q8VIM3;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Adhesion G protein-coupled receptor E4;
DE AltName: Full=EGF-like module receptor 4;
DE AltName: Full=EGF-like module-containing mucin-like hormone receptor-like 4;
DE AltName: Full=F4/80-like-receptor;
DE AltName: Full=Seven-span membrane protein FIRE;
DE Flags: Precursor;
GN Name=Adgre4; Synonyms=Emr4;
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], PROTEIN SEQUENCE OF 327-336, FUNCTION, TISSUE
RP SPECIFICITY, INDUCTION, AND GLYCOSYLATION.
RC STRAIN=BALB/cJ;
RX PubMed=12023293; DOI=10.1074/jbc.m204306200;
RA Stacey M., Chang G.-W., Sanos S.L., Chittenden L.R., Stubbs L., Gordon S.,
RA Lin H.-H.;
RT "EMR4, a novel epidermal growth factor (EGF)-TM7 molecule up-regulated in
RT activated mouse macrophages, binds to a putative cellular ligand on B
RT lymphoma cell line A20.";
RL J. Biol. Chem. 277:29283-29293(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=11564768; DOI=10.4049/jimmunol.167.7.3570;
RA Caminschi I., Lucas K.M., O'Keeffe M.A., Hochrein H., Laabi Y.,
RA Koentgen F., Lew A.M., Shortman K., Wright M.D.;
RT "Molecular cloning of F4/80-like-receptor, a seven-span membrane protein
RT expressed differentially by dendritic cell and monocyte-macrophage
RT subpopulations.";
RL J. Immunol. 167:3570-3576(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, and Thymus;
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: May mediate the cellular interaction between myeloid cells
CC and B-cells. {ECO:0000269|PubMed:12023293}.
CC -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular
CC region (alpha subunit) non-covalently linked to a seven-transmembrane
CC moiety (beta subunit). {ECO:0000269|PubMed:12023293}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12023293};
CC Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in myeloid cells.
CC Predominantly expressed on resident macrophages.
CC {ECO:0000269|PubMed:11564768, ECO:0000269|PubMed:12023293}.
CC -!- INDUCTION: Up-regulated following macrophage activation.
CC {ECO:0000269|PubMed:12023293}.
CC -!- DOMAIN: The second EGF domain mediates the interaction with the
CC putative ligand. {ECO:0000269|PubMed:12023293}.
CC -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular alpha
CC subunit and a seven-transmembrane subunit.
CC {ECO:0000269|PubMed:12023293}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:12023293}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL31879.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY032690; AAK51125.1; -; mRNA.
DR EMBL; AF396935; AAL31879.1; ALT_INIT; mRNA.
DR EMBL; AK037483; BAC29816.1; -; mRNA.
DR EMBL; AK155935; BAE33510.1; -; mRNA.
DR CCDS; CCDS50148.1; -.
DR RefSeq; NP_631877.2; NM_139138.3.
DR AlphaFoldDB; Q91ZE5; -.
DR SMR; Q91ZE5; -.
DR STRING; 10090.ENSMUSP00000025004; -.
DR MEROPS; P02.005; -.
DR GlyGen; Q91ZE5; 8 sites.
DR PhosphoSitePlus; Q91ZE5; -.
DR MaxQB; Q91ZE5; -.
DR PaxDb; Q91ZE5; -.
DR PRIDE; Q91ZE5; -.
DR ProteomicsDB; 282032; -.
DR DNASU; 52614; -.
DR Ensembl; ENSMUST00000025004; ENSMUSP00000025004; ENSMUSG00000032915.
DR GeneID; 52614; -.
DR KEGG; mmu:52614; -.
DR UCSC; uc008dae.2; mouse.
DR CTD; 52614; -.
DR MGI; MGI:1196464; Adgre4.
DR VEuPathDB; HostDB:ENSMUSG00000032915; -.
DR eggNOG; KOG4193; Eukaryota.
DR GeneTree; ENSGT00940000162163; -.
DR HOGENOM; CLU_002753_3_7_1; -.
DR InParanoid; Q91ZE5; -.
DR OMA; MLHYLYL; -.
DR OrthoDB; 124090at2759; -.
DR PhylomeDB; Q91ZE5; -.
DR TreeFam; TF316380; -.
DR BioGRID-ORCS; 52614; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q91ZE5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q91ZE5; protein.
DR Bgee; ENSMUSG00000032915; Expressed in spleen and 65 other tissues.
DR Genevisible; Q91ZE5; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISA:MGI.
DR Gene3D; 2.60.220.50; -; 1.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR001740; GPCR_2_EMR1-like_rcpt.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF01825; GPS; 1.
DR PRINTS; PR01128; EMR1HORMONER.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00303; GPS; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Repeat; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT CHAIN 38..689
FT /note="Adhesion G protein-coupled receptor E4"
FT /id="PRO_0000012878"
FT TOPO_DOM 38..350
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..407
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 429..455
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..476
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 477..499
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 521..544
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 545..565
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 566..570
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 571..591
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 592..689
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 38..76
FT /note="EGF-like 1"
FT DOMAIN 77..127
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255"
FT DOMAIN 289..338
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT SITE 326..327
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:12023293"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..47
FT /evidence="ECO:0000250"
FT DISULFID 41..53
FT /evidence="ECO:0000250"
FT DISULFID 55..75
FT /evidence="ECO:0000250"
FT DISULFID 81..94
FT /evidence="ECO:0000250"
FT DISULFID 88..103
FT /evidence="ECO:0000250"
FT DISULFID 105..126
FT /evidence="ECO:0000250"
FT CONFLICT 666
FT /note="P -> H (in Ref. 3; BAC29816)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 689 AA; 77045 MW; D9469A095CBC2088 CRC64;
MLMGATRDMG SRCLLHASVP GMLLIWSILQ MMNISASCPQ CNENASCFNS THCVCKEGFW
TGSENRRIIE PHEKCQDINE CLLKELVCKD VSYCRNKIGT YICSCVVKYP LFNWVAGIIN
IDHPDCYVNK SKNTGSKTHT LGVLSEFKSK EEVAKGATKL LRKVEHHILN ENSDIPKKDE
NPLLDIVYET KRCKTMTLLE AGNNTMKVDC TSGFKEHNSG GETAVAFIAY KSLGNLLNGS
FFSNEEGFQE VTLNSHIVSG AIRSEVKPVL SEPVLLTLQN IQPIDSRAEH LCVHWEGSEE
GGSWSTKGCS HVYTNNSYTI CKCFHLSSFA VLMALPHEED GVLSALSVIT YVGLSLSLLC
LFLAAITFLL CRPIQNTSTT LHLQLSICLF LADLLFLTGI NRTKPKVLCS IIAGMLHYLY
LASFMWMFLE GLHLFLTVSN LKVANYSNSG RFKKRFMYPV GYGLPAFIVA VSAIAGHKNY
GTHNHCWLSL HRGFIWSFLG PAAAIILINL VFYFLIIWIL RSKLSSLNKE VSTLQDTKVM
TFKAIVQLFV LGCSWGIGLF IFIEVGKTVR LIVAYLFTII NVLQGVLIFM VHCLLNRQVR
MEYKKWFHRL RKEVESESTE VSHSTTHTKM GLSLNLENFC PTGNLHDPSD SILPSTEVAG
VYLSTPRSHM GAEDVNSGTH AYWSRTISD
