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DIHR_MANSE
ID   DIHR_MANSE              Reviewed;         395 AA.
AC   P35464;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Diuretic hormone receptor;
DE            Short=DH-R;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8276884; DOI=10.1016/s0021-9258(17)42299-x;
RA   Reagan J.D.;
RT   "Expression cloning of an insect diuretic hormone receptor. A member of the
RT   calcitonin/secretin receptor family.";
RL   J. Biol. Chem. 269:9-12(1994).
CC   -!- FUNCTION: Receptor for the insect diurectic hormone. The activity of
CC       this receptor is mediated by G proteins which activate adenylyl
CC       cyclase.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in Malpighian tubules.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       {ECO:0000305}.
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DR   EMBL; U03489; AAC46469.1; -; mRNA.
DR   AlphaFoldDB; P35464; -.
DR   SMR; P35464; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008036; F:diuretic hormone receptor activity; IEA:InterPro.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   Gene3D; 4.10.1240.10; -; 1.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR002001; GPCR_2_diuretic_rcpt.
DR   InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR   InterPro; IPR001879; GPCR_2_extracellular_dom.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF02793; HRM; 1.
DR   PRINTS; PR01127; DIUHORMONER.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   SMART; SM00008; HormR; 1.
DR   SUPFAM; SSF111418; SSF111418; 1.
DR   PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1.
DR   PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR   PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Receptor; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..395
FT                   /note="Diuretic hormone receptor"
FT                   /id="PRO_0000070330"
FT   TOPO_DOM        1..87
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..111
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        112..119
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        141..155
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        177..195
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..217
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        218..248
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        249..272
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        273..295
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        296..314
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        315..329
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        330..349
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        350..395
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          369..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..395
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        11
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        69
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        144
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   395 AA;  45421 MW;  3F8C1A3EFEA01B2D CRC64;
     MAEECLARKF NLSDNYCPAY FDGLLCWDPT PWNTLAVQKC FKELYGIQYD DTQNASRLCL
     DGVWHNYTNY TNCTERIANG SPTDVASLIY LAGYSLSLAV LSLAVFVFLY FKDLRCLRNT
     IHTNLMSTYI LSACSWILNL VLQNWSDESQ QDQTSCMILV ICMNYFYLTN FFWMLVEGLY
     LYMLVVETFT AENIKLKVYT TIGWGAPAVF ITIWVISRCF VNVLPSTGPD GLAMFPEAKM
     CIWMHEHQVD WIHKAPALVG LALNLFFLIR IMWVLITKLR SANTLETEQY RKATKALLVL
     IPLLGITNLL VLCGPSDDSW FAYAFDYTRA LMLSTQGFTV ALFYCFMNTE VRHAIRYHVE
     RWKTGRTIGG GRRRGASYSK DWSPRSRTES IRLTV
 
 
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