AGRL4_MOUSE
ID AGRL4_MOUSE Reviewed; 739 AA.
AC Q923X1; E9QLT4; Q91W44;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Adhesion G protein-coupled receptor L4;
DE AltName: Full=EGF, latrophilin seven transmembrane domain-containing protein 1;
DE Flags: Precursor;
GN Name=Adgrl4; Synonyms=Eltd1;
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].
RC STRAIN=AKR/J;
RX PubMed=11438738; DOI=10.1073/pnas.131200898;
RA Terskikh A.V., Easterday M.C., Li L., Hood L., Kornblum H.I.,
RA Geschwind D.H., Weissman I.L.;
RT "From hematopoiesis to neuropoiesis: evidence of overlapping genetic
RT programs.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7934-7939(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 DISRUPTION PHENOTYPE.
RX PubMed=22606234; DOI=10.1371/journal.pone.0035779;
RA Xiao J., Jiang H., Zhang R., Fan G., Zhang Y., Jiang D., Li H.;
RT "Augmented cardiac hypertrophy in response to pressure overload in mice
RT lacking ELTD1.";
RL PLoS ONE 7:E35779-E35779(2012).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=23871637; DOI=10.1016/j.ccr.2013.06.004;
RA Masiero M., Simoes F.C., Han H.D., Snell C., Peterkin T., Bridges E.,
RA Mangala L.S., Wu S.Y., Pradeep S., Li D., Han C., Dalton H.,
RA Lopez-Berestein G., Tuynman J.B., Mortensen N., Li J.L., Patient R.,
RA Sood A.K., Banham A.H., Harris A.L., Buffa F.M.;
RT "A core human primary tumor angiogenesis signature identifies the
RT endothelial orphan receptor ELTD1 as a key regulator of angiogenesis.";
RL Cancer Cell 24:229-241(2013).
CC -!- FUNCTION: Endothelial orphan receptor that acts as a key regulator of
CC angiogenesis. {ECO:0000250|UniProtKB:Q9HBW9,
CC ECO:0000269|PubMed:23871637}.
CC -!- SUBUNIT: Heterodimer of 2 chains generated by proteolytic processing;
CC the large extracellular N-terminal fragment and the membrane-bound C-
CC terminal fragment predominantly remain associated and non-covalently
CC linked. {ECO:0000250|UniProtKB:Q9ESC1}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23871637};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Induced by VEGF and FGF2. {ECO:0000269|PubMed:23871637}.
CC -!- DOMAIN: The transmembrane domain is not required for cleavage, but it
CC is required for dimer formation. {ECO:0000250|UniProtKB:Q9ESC1}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q9HBW9}.
CC -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular alpha
CC subunit and a seven-transmembrane subunit.
CC {ECO:0000250|UniProtKB:Q9ESC1}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype but deficient mice present
CC increased cardiac hypertrophy in response to pressure overload.
CC {ECO:0000269|PubMed:22606234}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
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DR EMBL; AF385682; AAK62363.1; -; mRNA.
DR EMBL; AC127233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017134; AAH17134.1; -; mRNA.
DR CCDS; CCDS17910.1; -.
DR RefSeq; NP_573485.2; NM_133222.3.
DR AlphaFoldDB; Q923X1; -.
DR SMR; Q923X1; -.
DR BioGRID; 228419; 6.
DR STRING; 10090.ENSMUSP00000041939; -.
DR MEROPS; P02.013; -.
DR GlyGen; Q923X1; 8 sites.
DR PhosphoSitePlus; Q923X1; -.
DR CPTAC; non-CPTAC-3686; -.
DR MaxQB; Q923X1; -.
DR PaxDb; Q923X1; -.
DR PRIDE; Q923X1; -.
DR ProteomicsDB; 296141; -.
DR ABCD; Q923X1; 6 sequenced antibodies.
DR Antibodypedia; 9366; 226 antibodies from 30 providers.
DR DNASU; 170757; -.
DR Ensembl; ENSMUST00000046977; ENSMUSP00000041939; ENSMUSG00000039167.
DR GeneID; 170757; -.
DR KEGG; mmu:170757; -.
DR UCSC; uc008rsj.2; mouse.
DR CTD; 64123; -.
DR MGI; MGI:2655562; Adgrl4.
DR VEuPathDB; HostDB:ENSMUSG00000039167; -.
DR eggNOG; KOG4193; Eukaryota.
DR eggNOG; KOG4291; Eukaryota.
DR GeneTree; ENSGT00940000158252; -.
DR HOGENOM; CLU_002753_3_8_1; -.
DR InParanoid; Q923X1; -.
DR OMA; SKMKHIH; -.
DR OrthoDB; 388923at2759; -.
DR PhylomeDB; Q923X1; -.
DR TreeFam; TF316380; -.
DR BioGRID-ORCS; 170757; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Adgrl4; mouse.
DR PRO; PR:Q923X1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q923X1; protein.
DR Bgee; ENSMUSG00000039167; Expressed in brain blood vessel and 203 other tissues.
DR ExpressionAtlas; Q923X1; baseline and differential.
DR Genevisible; Q923X1; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR Gene3D; 2.60.220.50; -; 1.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
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; 2.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF01825; GPS; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00303; GPS; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell membrane; Disulfide bond; EGF-like domain;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..739
FT /note="Adhesion G protein-coupled receptor L4"
FT /id="PRO_0000012871"
FT TOPO_DOM 20..481
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 482..502
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 503..513
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 514..534
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 535..548
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 549..569
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 570..581
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 582..602
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 603..622
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 623..643
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 644..667
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 668..688
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 689..695
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 696..716
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 717..739
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 20..57
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 58..107
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 108..157
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 415..467
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT SITE 455..456
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q9ESC1"
FT CARBOHYD 21
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 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 22..33
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 27..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 44..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 62..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 68..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 85..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 112..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 118..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 135..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 289
FT /note="T -> I (in Ref. 1; AAK62363)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="Missing (in Ref. 3; AAH17134)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 739 AA; 82246 MW; 1AEB95CCCB73B095 CRC64;
MRLLPLLVGF STLLNCSYTQ NCSKTTCLPN AKCEVHNGVE ACFCSQGYSG NGVTICEDID
ECSESSVCGD HAVCENVNGG FSCFCREGYQ TATGKSQFTP NDGSYCQDID ECSESSVCGD
HAVCENVNGG FSCFCREGYQ TATGKSQFTP NDGSYCQESM NSNCHLEHAC IAANINKTLK
RIGPITEQTT LLQEIYRNSE AELSLMDIVT YIEILTESSS LLGHPNSTTS YKDAHFNSTL
TEFGETINNF VERSTHKMWD QLPTNHRRLH LTKLMHTAEL VTLQIAQNTQ KNSQFDMNST
DLALKVFAFD STHMKHAHPH MNVDGGYVKI SPRRKAAHGT TGNVVVAFLC YKSIGPLLSS
SDNFLLDTQN DNSEGKEKVI SSVISASISS NPPTLYELEK ITFTLSHVKL SDKHRTQCAF
WNYSVDAMNN GSWSTEGCEL THSNDTHTSC RCSHLTHFAI LMSSTSSIGI KDYNILTRIT
QLGIIISLIC LAICIFTFWF FSEIQSTRTT IHKNLCCSLF LAELVFLIGI NINTNKLVCS
IIAGLLHYFF LAAFAWMCIE GIHLYLIVVG VIYNKGFLHK NFYIFGYLSP AVVVGFSASL
GYRYYGTTKV CWLSTENNFI WSFIGPACLI ILVNLLAFGV IIYKVFRHTA GLKPEVSCYE
NIRSCARGAL ALLFLLGTTW IFGVLHVVHA SVVTAYLFTV SNAFQGMFIF LFLCVLSRKI
QEEYYRLFKN VPCCFGCLR
