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AGRD2_HUMAN
ID   AGRD2_HUMAN             Reviewed;         963 AA.
AC   Q7Z7M1; Q86SL4; Q8NH12;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Adhesion G-protein coupled receptor D2 {ECO:0000303|PubMed:25713288};
DE   AltName: Full=G-protein coupled receptor 144;
DE   AltName: Full=G-protein coupled receptor PGR24;
GN   Name=ADGRD2; Synonyms=GPR144, PGR24;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15203201; DOI=10.1016/j.ygeno.2003.12.004;
RA   Bjarnadottir T.K., Fredriksson R., Hoeglund P.J., Gloriam D.E.,
RA   Lagerstroem M.C., Schioeth H.B.;
RT   "The human and mouse repertoire of the adhesion family of G-protein-coupled
RT   receptors.";
RL   Genomics 84:23-33(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA   Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT   "Genome-wide discovery and analysis of human seven transmembrane helix
RT   receptor genes.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 619-897.
RX   PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA   Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA   Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA   Bergmann J.E., Gaitanaris G.A.;
RT   "The G protein-coupled receptor repertoires of human and mouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
RN   [5]
RP   NOMENCLATURE.
RX   PubMed=25713288; DOI=10.1124/pr.114.009647;
RA   Hamann J., Aust G., Arac D., Engel F.B., Formstone C., Fredriksson R.,
RA   Hall R.A., Harty B.L., Kirchhoff C., Knapp B., Krishnan A., Liebscher I.,
RA   Lin H.H., Martinelli D.C., Monk K.R., Peeters M.C., Piao X., Promel S.,
RA   Schoneberg T., Schwartz T.W., Singer K., Stacey M., Ushkaryov Y.A.,
RA   Vallon M., Wolfrum U., Wright M.W., Xu L., Langenhan T., Schioth H.B.;
RT   "International union of basic and clinical pharmacology. XCIV. Adhesion G
RT   protein-coupled receptors.";
RL   Pharmacol. Rev. 67:338-367(2015).
RN   [6]
RP   VARIANTS SER-170 AND THR-630.
RX   PubMed=28585349; DOI=10.1002/humu.23270;
RA   Poirier K., Hubert L., Viot G., Rio M., Billuart P., Besmond C.,
RA   Bienvenu T.;
RT   "CSNK2B splice site mutations in patients cause intellectual disability
RT   with or without myoclonic epilepsy.";
RL   Hum. Mutat. 38:932-941(2017).
CC   -!- FUNCTION: Orphan receptor.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
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=BAC05829.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY278562; AAP35064.1; -; mRNA.
DR   EMBL; AB065601; BAC05829.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL137846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY255620; AAO85132.1; -; mRNA.
DR   AlphaFoldDB; Q7Z7M1; -.
DR   STRING; 9606.ENSP00000335156; -.
DR   ChEMBL; CHEMBL4523880; -.
DR   MEROPS; P02.015; -.
DR   GlyGen; Q7Z7M1; 2 sites.
DR   iPTMnet; Q7Z7M1; -.
DR   PhosphoSitePlus; Q7Z7M1; -.
DR   BioMuta; ADGRD2; -.
DR   DMDM; 59797942; -.
DR   PaxDb; Q7Z7M1; -.
DR   PRIDE; Q7Z7M1; -.
DR   Antibodypedia; 52848; 53 antibodies from 16 providers.
DR   Ensembl; ENST00000334810.5; ENSP00000335156.2; ENSG00000180264.11.
DR   UCSC; uc033dhj.2; human.
DR   GeneCards; ADGRD2; -.
DR   HGNC; HGNC:18651; ADGRD2.
DR   HPA; ENSG00000180264; Tissue enhanced (brain, pituitary gland, seminal vesicle).
DR   neXtProt; NX_Q7Z7M1; -.
DR   PharmGKB; PA134882616; -.
DR   VEuPathDB; HostDB:ENSG00000180264; -.
DR   eggNOG; KOG4193; Eukaryota.
DR   HOGENOM; CLU_015074_0_0_1; -.
DR   InParanoid; Q7Z7M1; -.
DR   OrthoDB; 388923at2759; -.
DR   PhylomeDB; Q7Z7M1; -.
DR   TreeFam; TF351999; -.
DR   GeneWiki; GPR144; -.
DR   Pharos; Q7Z7M1; Tdark.
DR   PRO; PR:Q7Z7M1; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q7Z7M1; protein.
DR   Bgee; ENSG00000180264; Expressed in parotid gland and 136 other tissues.
DR   ExpressionAtlas; Q7Z7M1; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; TAS:GDB.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0007186; P:G protein-coupled receptor signaling pathway; TAS:GDB.
DR   Gene3D; 2.60.220.50; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR046338; GAIN_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR000203; GPS.
DR   InterPro; IPR001759; Pentraxin-related.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF00354; Pentaxin; 1.
DR   PRINTS; PR00895; PENTAXIN.
DR   SMART; SM00303; GPS; 1.
DR   SMART; SM00159; PTX; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
DR   PROSITE; PS51828; PTX_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..963
FT                   /note="Adhesion G-protein coupled receptor D2"
FT                   /id="PRO_0000070338"
FT   TOPO_DOM        1..662
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        663..683
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        684..691
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        692..712
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        713..720
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        721..741
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        742..762
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        763..783
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        784..800
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        801..821
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        822..857
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        858..878
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        879..880
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        881..901
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        902..963
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          116..325
FT                   /note="Pentraxin (PTX)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   DOMAIN          572..648
FT                   /note="GPS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT   REGION          18..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        634
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        146..212
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   VARIANT         170
FT                   /note="P -> S"
FT                   /evidence="ECO:0000269|PubMed:28585349"
FT                   /id="VAR_083658"
FT   VARIANT         630
FT                   /note="A -> T"
FT                   /evidence="ECO:0000269|PubMed:28585349"
FT                   /id="VAR_083659"
SQ   SEQUENCE   963 AA;  104087 MW;  EA7BEE0663F7A54C CRC64;
     MDAPWGAGER WLHGAAVDRS GVSLGPPPTP QVNQGTLGPQ VAPVAAGEVV KTAGGVCKFS
     GQRLSWWQAQ ESCEQQFGHL ALQPPDGVLA SRLRDPVWVG QREAPLRRPP QRRARTTAVL
     VFDERTADRA ARLRSPLPEL AALTACTHVQ WDCASPDPAA LFSVAAPALP NALQLRAFAE
     PGGVVRAALV VRGQHAPFLA AFRADGRWHH VCATWEQRGG RWALFSDGRR RAGARGLGAG
     HPVPSGGILV LGQDQDSLGG GFSVRHALSG NLTDFHLWAR ALSPAQLHRA RACAPPSEGL
     LFRWDPGALD VTPSLLPTVW VRLLCPVPSE ECPTWNPGPR SEGSELCLEP QPFLCCYRTE
     PYRRLQDAQS WPGQDVISRV NALANDIVLL PDPLSEVHGA LSPAEASSFL GLLEHVLAME
     MAPLGPAALL AVVRFLKRVV ALGAGDPELL LTGPWEQLSQ GVVSVASLVL EEQVADTWLS
     LREVIGGPMA LVASVQRLAP LLSTSMTSER PRMRIQHRHA GLSGVTVIHS WFTSRVFQHT
     LEGPDLEPQA PASSEEANRV QRFLSTQVGS AIISSEVWDV TGEVNVAMTF HLQHRAQSPL
     FPPHPPSPYT GGAWATTGCS VAALYLDSTA CFCNHSTSFA ILLQIYEVQR GPEEESLLRT
     LSFVGCGVSF CALTTTFLLF LVAGVPKSER TTVHKNLTFS LASAEGFLMT SEWAKANEVA
     CVAVTVAMHF LFLVAFSWML VEGLLLWRKV VAVSMHPGPG MRLYHATGWG VPVGIVAVTL
     AMLPHDYVAP GHCWLNVHTN AIWAFVGPVL FVLTANTCIL ARVVMITVSS ARRRARMLSP
     QPCLQQQIWT QIWATVKPVL VLLPVLGLTW LAGILVHLSP AWAYAAVGLN SIQGLYIFLV
     YAACNEEVRS ALQRMAEKKV AEVLRALGVW GGAAKEHSLP FSVLPLFLPP KPSTPRHPLK
     APA
 
 
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