GenomeNet

Database: UniProt
Entry: J9P2S3_CANLF
LinkDB: J9P2S3_CANLF
Original site: J9P2S3_CANLF 
ID   J9P2S3_CANLF            Unreviewed;       348 AA.
AC   J9P2S3;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   08-MAY-2019, entry version 38.
DE   SubName: Full=5-hydroxytryptamine receptor 3B {ECO:0000313|Ensembl:ENSCAFP00000039851};
GN   Name=HTR3B {ECO:0000313|Ensembl:ENSCAFP00000039851,
GN   ECO:0000313|VGNC:VGNC:41830};
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000039851, ECO:0000313|Proteomes:UP000002254};
RN   [1] {ECO:0000313|Ensembl:ENSCAFP00000039851, ECO:0000313|Proteomes:UP000002254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000039851,
RC   ECO:0000313|Proteomes:UP000002254};
RX   PubMed=16341006; DOI=10.1038/nature04338;
RG   Broad Sequencing Platform;
RA   Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA   Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C.,
RA   Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A.,
RA   Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F.,
RA   Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A.,
RA   Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M.,
RA   Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L.,
RA   Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J.,
RA   Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA   Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA   Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L.,
RA   Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A.,
RA   Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N.,
RA   Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A.,
RA   Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N.,
RA   Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N.,
RA   Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K.,
RA   Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G.,
RA   Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E.,
RA   Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C.,
RA   Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L.,
RA   Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C.,
RA   Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T.,
RA   Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J.,
RA   Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J.,
RA   Marabella R., Maru K., Matthews C., McDonough S., Mehta T.,
RA   Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K.,
RA   Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J.,
RA   Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA   Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K.,
RA   Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F.,
RA   Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C.,
RA   Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S.,
RA   Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J.,
RA   Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S.,
RA   Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S.,
RA   Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T.,
RA   Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T.,
RA   Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X.,
RA   Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.;
RT   "Genome sequence, comparative analysis and haplotype structure of the
RT   domestic dog.";
RL   Nature 438:803-819(2005).
RN   [2] {ECO:0000313|Ensembl:ENSCAFP00000039851}
RP   IDENTIFICATION.
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000039851};
RG   Ensembl;
RL   Submitted (SEP-2012) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
CC       family. {ECO:0000256|SAAS:SAAS00978283}.
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DR   EMBL; AAEX03003482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSCAFT00000043605; ENSCAFP00000039851; ENSCAFG00000013576.
DR   VGNC; VGNC:41830; HTR3B.
DR   eggNOG; KOG3645; Eukaryota.
DR   eggNOG; ENOG410XQGR; LUCA.
DR   GeneTree; ENSGT00940000158478; -.
DR   Proteomes; UP000002254; Chromosome 5.
DR   Bgee; ENSCAFG00000013576; Expressed in 3 organ(s), highest expression level in liver.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:InterPro.
DR   GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   Gene3D; 2.70.170.10; -; 1.
DR   InterPro; IPR008132; 5HT3_rcpt.
DR   InterPro; IPR008134; 5HT3_rcpt_B.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   PANTHER; PTHR18945; PTHR18945; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR01710; 5HT3BRECEPTR.
DR   PRINTS; PR01708; 5HT3RECEPTOR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF63712; SSF63712; 1.
DR   SUPFAM; SSF90112; SSF90112; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002254};
KW   Membrane {ECO:0000256|SAAS:SAAS00978300, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002254};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00978734,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00978768,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    142    165       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    203    230       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    316    339       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        2    141       Neur_chan_LBD. {ECO:0000259|Pfam:
FT                                PF02931}.
FT   DOMAIN      148    228       Neur_chan_memb. {ECO:0000259|Pfam:
FT                                PF02932}.
SQ   SEQUENCE   348 AA;  39666 MW;  AAB804BD917C9F0E CRC64;
     MFDEIREISL PLSDIWAPDI IINELVDVEG SPDLPYVYVN SSGTIKNSKP MQVVTTCSLE
     TYAFPFDIQN CSLTFSSILH TVEDVNLAFL RSREDIKQDK KEFLNDSEWE LLSVSSTYNI
     LQSSAGDFAQ IQFNVVIRRR PLVYIVSLLI PSIFLMLVDL GSFYLPPTCR ARIMFKTSVL
     VGYTVFRVNM SDEMPRSAVS TPLIGVFFTV CMAFLVISLF KSILLVKLLY DERNSGQERP
     LFCLQGDTDV DGPRVDPRAQ LAGVPEPICR EHLAPTGTLE EVWFQLKSIS TYFQTWDQSD
     QQEVKWLALL ERFDRLLFQA YTIILGLYAI TLCSLWALWG SSWRLRAG
//
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