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5HTR_HELVI
ID   5HTR_HELVI              Reviewed;         466 AA.
AC   Q25190;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=5-hydroxytryptamine receptor;
DE            Short=5-HT receptor;
DE   AltName: Full=Serotonin receptor;
OS   Heliothis virescens (Tobacco budworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Heliothis.
OX   NCBI_TaxID=7102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Antenna;
RX   PubMed=9014328; DOI=10.1016/s0965-1748(96)00031-8;
RA   von Nickisch-Rosenegk E., Krieger J., Kubick S., Laage R., Strobel J.,
RA   Strotmann J., Breer H.;
RT   "Cloning of biogenic amine receptors from moths (Bombyx mori and Heliothis
RT   virescens).";
RL   Insect Biochem. Mol. Biol. 26:817-827(1996).
CC   -!- FUNCTION: This is a receptor for 5-hydroxytryptamine (serotonin), a
CC       biogenic hormone that function as a neurotransmitter, a hormone, and a
CC       mitogen. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; X95605; CAA64863.1; -; mRNA.
DR   AlphaFoldDB; Q25190; -.
DR   SMR; Q25190; -.
DR   PRIDE; Q25190; -.
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:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..466
FT                   /note="5-hydroxytryptamine receptor"
FT                   /id="PRO_0000068986"
FT   TOPO_DOM        1..66
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        67..89
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        90..99
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        100..121
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        122..136
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        137..158
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        159..177
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        178..200
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        201..228
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        229..250
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        251..386
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        387..410
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        411..419
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        420..442
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        443..466
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          255..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..357
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        2
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        10
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        135..215
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   466 AA;  52094 MW;  AD29A38EC37106EB CRC64;
     MNASRLPGFN DTSQDQPYPT SSEWFDGSNC SWVDAVSWGC NVTINGTSTN ATSTDVTSFV
     LMAVTSVVLA LIILATIVGN VFVIAAIIIE RNLQNVANYL VASLAVADLM VACLVMPLGA
     VYEVSQGWIL GPELCDMWTS SDVLCSSASI LHLVAIATDR YWAVTDVDYI HIRNEKRIFT
     MIVLVWGAAL VVSLAPQLGW KDPDYLARIT QQQKCLVSQD LAYQIFATMS TFYVPLAVIL
     ILYWKIFQTA RRRIRRRRDP PPPRPTSADG ATPSGRPVQS ARDRRFVKKR FLNLKKCNQR
     TRAETLAAAL LLTEGQSTST VDTLDEEPRT TAFTINEKVP PSVSPEKSSS TVTNGSKPER
     AIVPAPTHRE KKESLEAKRE RKAAKTLAII TGAFVFCWLP FFIMALVMPI CQTCVISDYL
     ASFFLWLGYF NSTLNPVIYT IFSPDFRQAF ARILFGTHRR RRYKKF
 
 
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