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Database: UniProt
Entry: J9P9P7_CANLF
LinkDB: J9P9P7_CANLF
Original site: J9P9P7_CANLF 
ID   J9P9P7_CANLF            Unreviewed;       925 AA.
AC   J9P9P7;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   30-AUG-2017, entry version 35.
DE   SubName: Full=Transient receptor potential cation channel subfamily C member 3 {ECO:0000313|Ensembl:ENSCAFP00000042480};
GN   Name=TRPC3 {ECO:0000313|Ensembl:ENSCAFP00000042480};
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:ENSCAFP00000042480, ECO:0000313|Proteomes:UP000002254};
RN   [1] {ECO:0000313|Ensembl:ENSCAFP00000042480, ECO:0000313|Proteomes:UP000002254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000042480,
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:ENSCAFP00000042480}
RP   IDENTIFICATION.
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000042480};
RG   Ensembl;
RL   Submitted (SEP-2012) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
CC       {ECO:0000256|SAAS:SAAS00788929}.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSCAFP00000042480}.
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DR   EMBL; AAEX03011800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_540964.3; XM_540964.5.
DR   STRING; 9615.ENSCAFP00000042480; -.
DR   PaxDb; J9P9P7; -.
DR   Ensembl; ENSCAFT00000050091; ENSCAFP00000042480; ENSCAFG00000004110.
DR   GeneID; 483844; -.
DR   CTD; 7222; -.
DR   eggNOG; KOG3609; Eukaryota.
DR   eggNOG; ENOG410XQ0Y; LUCA.
DR   GeneTree; ENSGT00760000119180; -.
DR   InParanoid; J9P9P7; -.
DR   OMA; CMEKQRH; -.
DR   OrthoDB; EOG091G01FB; -.
DR   Reactome; R-CFA-114508; Effects of PIP2 hydrolysis.
DR   Reactome; R-CFA-139853; Elevation of cytosolic Ca2+ levels.
DR   Reactome; R-CFA-3295583; TRP channels.
DR   Proteomes; UP000002254; Chromosome 19.
DR   Bgee; ENSCAFG00000004110; -.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IEA:Ensembl.
DR   GO; GO:0015279; F:store-operated calcium channel activity; IBA:GO_Central.
DR   GO; GO:0006828; P:manganese ion transport; IBA:GO_Central.
DR   GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IEA:Ensembl.
DR   GO; GO:1903244; P:positive regulation of cardiac muscle hypertrophy in response to stress; IEA:Ensembl.
DR   GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR   GO; GO:0033198; P:response to ATP; IEA:Ensembl.
DR   GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR   GO; GO:0007338; P:single fertilization; IBA:GO_Central.
DR   CDD; cd00204; ANK; 1.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR004729; TRP_channel.
DR   InterPro; IPR013555; TRP_dom.
DR   InterPro; IPR005459; TRPC3_channel.
DR   InterPro; IPR002153; TRPC_channel.
DR   PANTHER; PTHR10117; PTHR10117; 1.
DR   PANTHER; PTHR10117:SF63; PTHR10117:SF63; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF08344; TRP_2; 1.
DR   PRINTS; PR01097; TRNSRECEPTRP.
DR   PRINTS; PR01644; TRPCHANNEL3.
DR   SMART; SM00248; ANK; 3.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   TIGRFAMs; TIGR00870; trp; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
PE   3: Inferred from homology;
KW   ANK repeat {ECO:0000256|SAAS:SAAS00844120};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002254};
KW   Ion channel {ECO:0000256|SAAS:SAAS00816195};
KW   Ion transport {ECO:0000256|SAAS:SAAS00816776};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002254};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|SAAS:SAAS00816535}.
FT   TRANSMEM    423    447       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    459    479       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    511    528       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    548    567       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    654    676       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    725    744       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      123    173       ANK_REP_REGION. {ECO:0000259|PROSITE:
FT                                PS50297}.
SQ   SEQUENCE   925 AA;  105789 MW;  2617E31E81CDE692 CRC64;
     MSTKGRKCKE QARVTFPAPE EEEEEEEEEG EDGGSEPQRR RRGWRGVNGG LEPRSAPSQR
     EPHGCRPPPF SPGLDPSMEG SPSLRRKTVM REKGRRQAVR GPAFMFNDRG TSLTAEEERF
     LDAAEYGNIP VVRKMLEESK TLNVNCVDYM GQNALQLAVG NEHLEVTELL LKKENLARIG
     DALLLAISKG YVRIVEAILN HPGFAASKRL TLSPCEQELQ DDDFYAYDED GTRFSPDITP
     IILAAHCQKY EVVHMLLMKG ARIERPHDYF CKCGDCMEKQ RHDSFSHSRS RINAYKGLAS
     PAYLSLSSED PVLTALELSN ELAKLANIEK EFKNDYRKLS MQCKDFVVGV LDLCRDSEEV
     EAILNGDLES AEPLEVHRHK ASLSRVKLAI KYEVKKFVAH PNCQQQLLTI WYENLSGLRE
     QTIAIKCLVV LVVALGLPFL AIGYWIAPCS RLGKILRSPF MKFVAHAASF IIFLGLLVFN
     ASDRFEGITT LPNITVIDYP KQIFRVKTTQ FTWTEMLIMV WVLGMMWSEC KELWLEGPRE
     YILQLWNVLD FGMLSIFIAA FTARFLAFLQ ATKAQQYVDS YVQESDLSEV TLPPEIQYFT
     YARDKWLPSD PQIISEGLYA IAVVLSFSRI AYILPANESF GPLQISLGRT VKDIFKFMVL
     FIMVFLAFMI GMFILYSYYL GAKVNAAFTT VEESFKTLFW SIFGLSEVTS VVLKYDHKFI
     ENIGYVLYGI YNVTMVVVLL NMLIAMINSS YQEIEDDSDV EWKFARSKLW LSYFDDGKTL
     PPPFSLVPSP KSFVYFVMRI INFSKCRRSR LQKDIEMGMG NSKSRLNLFT QSNSRVFESH
     SFNSILNQPT RYQQIMKRLI KRYVLKAQVD KENDEVNEGE LKEIKQDISS LRYELLEDKS
     QATEELAVLI HKLSEKLNPS MPRCE
//
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