AGRL4_RAT
ID AGRL4_RAT Reviewed; 738 AA.
AC Q9ESC1; Q9ESC0;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Adhesion G protein-coupled receptor L4;
DE AltName: Full=EGF,latrophilin and seven transmembrane domain-containing protein 1;
DE AltName: Full=EGF-TM7-latrophilin-related protein;
DE Short=ETL protein;
DE Flags: Precursor;
GN Name=Adgrl4; Synonyms=Eltd1, Etl;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), MUTAGENESIS OF THR-455,
RP SUBUNIT, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP PROTEOLYTIC PROCESSING.
RX PubMed=11050079; DOI=10.1074/jbc.m004814200;
RA Nechiporuk T., Urness L.D., Keating M.T.;
RT "ETL, a novel seven-transmembrane receptor that is developmentally
RT regulated in the heart.";
RL J. Biol. Chem. 276:4150-4157(2001).
CC -!- FUNCTION: Endothelial orphan receptor that acts as a key regulator of
CC angiogenesis. {ECO:0000250|UniProtKB:Q9HBW9}.
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:0000269|PubMed:11050079}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11050079};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ESC1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ESC1-2; Sequence=VSP_009415, VSP_009416;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in heart, lung, and kidney.
CC Less evident expression is observed in brain, skeletal muscle, liver
CC and spleen. No expression is detected in testis.
CC {ECO:0000269|PubMed:11050079}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated in the adult heart.
CC {ECO:0000269|PubMed:11050079}.
CC -!- DOMAIN: The transmembrane domain is not required for cleavage, but it
CC is required for dimer formation. {ECO:0000269|PubMed:11050079}.
CC -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular alpha
CC subunit and a seven-transmembrane subunit.
CC {ECO:0000269|PubMed:11050079}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q9HBW9}.
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; AF192401; AAG33019.1; -; mRNA.
DR EMBL; AF192402; AAG33020.1; -; mRNA.
DR RefSeq; NP_071630.1; NM_022294.1. [Q9ESC1-1]
DR AlphaFoldDB; Q9ESC1; -.
DR SMR; Q9ESC1; -.
DR STRING; 10116.ENSRNOP00000045890; -.
DR MEROPS; P02.013; -.
DR GlyGen; Q9ESC1; 8 sites.
DR PhosphoSitePlus; Q9ESC1; -.
DR PaxDb; Q9ESC1; -.
DR Ensembl; ENSRNOT00000047564; ENSRNOP00000045890; ENSRNOG00000033940. [Q9ESC1-2]
DR GeneID; 64124; -.
DR KEGG; rno:64124; -.
DR CTD; 64123; -.
DR RGD; 621136; Adgrl4.
DR VEuPathDB; HostDB:ENSRNOG00000033940; -.
DR eggNOG; KOG4193; Eukaryota.
DR GeneTree; ENSGT00940000158252; -.
DR InParanoid; Q9ESC1; -.
DR OMA; SKMKHIH; -.
DR OrthoDB; 388923at2759; -.
DR PhylomeDB; Q9ESC1; -.
DR TreeFam; TF316380; -.
DR PRO; PR:Q9ESC1; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000033940; Expressed in lung and 19 other tissues.
DR Genevisible; Q9ESC1; RN.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA: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; IDA:RGD.
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 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..738
FT /note="Adhesion G protein-coupled receptor L4"
FT /id="PRO_0000012872"
FT TOPO_DOM 20..480
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 481..501
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 502..522
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 523..543
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 544..547
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 548..568
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..580
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 581..601
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 602..621
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 622..642
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 643..666
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 667..687
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 688..694
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 695..715
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 716..738
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 20..56
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 57..106
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 107..156
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 414..466
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT SITE 454..455
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:11050079"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
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 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 22..32
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 26..41
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 43..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 61..73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 67..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 84..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 111..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 117..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 134..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 632..662
FT /note="VNLLAFGVIIYKVFRHTAGLKPEVSCYENIR -> IYILVSFTSHIPLNMCA
FT ECRRMVSASLHVRL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11050079"
FT /id="VSP_009415"
FT VAR_SEQ 663..738
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11050079"
FT /id="VSP_009416"
FT MUTAGEN 455
FT /note="T->A: Abolishes cleavage."
FT /evidence="ECO:0000269|PubMed:11050079"
SQ SEQUENCE 738 AA; 82451 MW; 680D3731FE60EF95 CRC64;
MRLLLLLVGL STLLNHSYTQ NCKTPCLPNA KCEVLDEVAA CFCSTGYTGN GITICEDVDE
CNETSVCGDH AVCENTNGGF SCFCVEGYQT STGKTQFTPN DGSYCQDVDE CNETSVCGDH
AVCENTNGGF SCFCVEGYQT STGKTQFTPN DGSYCQEIVN SNCHLEHDCI AANINKTLKR
IGPITEQLTL LHEIYKNSEA ELSLVDIVTY IEILTESSSL QGYIKNTTSP KDAYFGSALT
EFGKTVNNFV EKNTHEMWDQ LPTNRRRLHL TKLMHAAEHV TLQISQNIQK NTQFDMNSTD
LALKVFVFDS VHMKHTHPHM NVDGGYVKIS PRRKSAYDPN GNVIVAFLCY RSIGPLLSSS
DDFLLGAQSD NSKGKEKVIS SVISASISSN PPTLYELEKI TFTLSHVKLS DKHQTQCAFW
NYSVDDMNNG SWSSEGCELT YSNDTHTSCR CSHLTHFAIL MSPSTSIEVK DYNILTRITQ
LGIIISLICL AICIFTFWFF SEIQSTRTTI HKNLCCSLFL AQLVFLVGIN INTNKLVCSI
IAGLLHYFFL AAFAWMCIEG IYLYLIVVGL IYNKGFLHKN FYIFGYLSPA VVVGFSASLG
YRYYGTTKVC WLSTENNFIW SFIGPACLII LVNLLAFGVI IYKVFRHTAG LKPEVSCYEN
IRSCARGALA LLFLLGTTWT FGVLHVVHAS VVTAYLFTVS NAFQGMFIFL FLCVLSRKIQ
EEYYRLFKNV PCCFECLR
