AGRL4_DANRE
ID AGRL4_DANRE Reviewed; 727 AA.
AC Q7SY09; F1QUS5;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Adhesion G protein-coupled receptor L4;
DE Flags: Precursor;
GN Name=adgrl4 {ECO:0000312|ZFIN:ZDB-GENE-040426-2689};
GN Synonyms=eltd1 {ECO:0000312|ZFIN:ZDB-GENE-040426-2689},
GN zgc:63629 {ECO:0000312|EMBL:AAH55171.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|EMBL:AAH55171.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
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: Orphan receptor that plays a role in vessel formation.
CC {ECO:0000269|PubMed:23871637}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9HBW9};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: During gastrulation, expression is ubiquitously
CC detected throughout the embryo. During development is detected in
CC epithelial cells, blood precursor cells and developing vessels. By 48
CC hpf, weaker expression is still detected in epithelials cells.
CC {ECO:0000269|PubMed:23871637}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes
CC dramatic vascular impairment in embryos. {ECO:0000269|PubMed:23871637}.
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; CU464206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC055171; AAH55171.1; -; mRNA.
DR AlphaFoldDB; Q7SY09; -.
DR SMR; Q7SY09; -.
DR STRING; 7955.ENSDARP00000014501; -.
DR MEROPS; P02.013; -.
DR PaxDb; Q7SY09; -.
DR PRIDE; Q7SY09; -.
DR ZFIN; ZDB-GENE-040426-2689; adgrl4.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG4193; Eukaryota.
DR PhylomeDB; Q7SY09; -.
DR TreeFam; TF316380; -.
DR PRO; PR:Q7SY09; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
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; PS50026; EGF_3; 2.
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; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..726
FT /note="Adhesion G protein-coupled receptor L4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433794"
FT TOPO_DOM 20..467
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 468..488
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 489..496
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 497..517
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 518..535
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 536..556
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 557..568
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 569..589
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 590..609
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 610..630
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 631..654
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 655..675
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 676..682
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 683..703
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT DOMAIN 52..90
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 102..139
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 404..454
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT DISULFID 56..69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 63..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 106..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 112..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 153
FT /note="Missing (in Ref. 2; AAH55171)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="S -> F (in Ref. 2; AAH55171)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="M -> K (in Ref. 2; AAH55171)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="F -> S (in Ref. 2; AAH55171)"
FT /evidence="ECO:0000305"
FT CONFLICT 615
FT /note="A -> P (in Ref. 2; AAH55171)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 727 AA; 81948 MW; 8054707A793E39A9 CRC64;
MKLLLFAAWF SSLLDPCRFL DICQSCHPNA DCDDICKCRT GYTGNGISDC RDDNECETVP
EICGLHANCT NYVGGYYCNC LSGFISNGTE QFQTNDGTSC NDINECEEDR KCGPNSKCHN
NIGSFICSCL RGYTSPAGPW FMPNHGTDCI ENSKIHCHQD HKCTKETVNS TLERMTNLSI
SERLKEIRYQ TSAALSPVLL ISYIEAMVSS KLNSGDVSKD SKEHVNETIT NLVFSVNNLV
EKDEKVEWKK INEDLRMYYV TKLLHTAEKE TLALSAGYTH ATQMQVHAGD VEMKLYTFEP
RQAQKHPLSA NIQGNSISLS TKKARHANNN GSTSVVFLIY HSIGDLLKPA DDPGVADYSR
YAAAGEITVN SPVIAAAISN QKTLPLNDVT FTLKHTQEID PARDETKCAF WEYSPSMMGH
WSLDGCIRTR VNTTHTSCSC NHLTHFAILM SSARANLLAH YNVLTRITQL GMVISLICLS
MCIFTFWFFR DIQNTRTTIH KNLCCSLFMA QFIFLIGINK SAHKWFCSLI AGLLHYFFLA
AFAWMCIEGI HLYLIVVGVI YNKGFLHRNF YAFGYGSPAV VVAISATLGY KYYGTSSVCW
LSTENNFIWS FIGPAILIIL VNLLAFAVII YKVYRHTAVK KPEISHYENI RSCARGAIAL
LFVLGVTWAF GVMYILYETT LTAYLFTFAN VFQGMFIFIF LCVLSRRIQE EYYRLFKNMP
CCFECLR
