TRPC6_BOVIN
ID TRPC6_BOVIN Reviewed; 931 AA.
AC Q9MYW0; F1MND4;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Short transient receptor potential channel 6 {ECO:0000250|UniProtKB:Q9Y210};
DE Short=TrpC6 {ECO:0000250|UniProtKB:Q9Y210};
GN Name=TRPC6 {ECO:0000250|UniProtKB:Q9Y210};
GN Synonyms=TRP6 {ECO:0000250|UniProtKB:Q9Y210};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 640-728.
RC TISSUE=Brain;
RX PubMed=10816590; DOI=10.1074/jbc.m003408200;
RA Philipp S., Trost C., Warnat J., Rautmann J., Himmerkus N., Schroth G.,
RA Kretz O., Nastainczyk W., Cavalie A., Hoth M., Flockerzi V.;
RT "TRP4 (CCE1) protein is part of native calcium release-activated Ca2+-like
RT channels in adrenal cells.";
RL J. Biol. Chem. 275:23965-23972(2000).
CC -!- FUNCTION: Thought to form a receptor-activated non-selective calcium
CC permeant cation channel. Probably is operated by a phosphatidylinositol
CC second messenger system activated by receptor tyrosine kinases or G-
CC protein coupled receptors. Activated by diacylglycerol (DAG) in a
CC membrane-delimited fashion, independently of protein kinase C. Seems
CC not to be activated by intracellular calcium store depletion.
CC {ECO:0000250|UniProtKB:Q9Y210}.
CC -!- SUBUNIT: Homodimer; forms channel complex. Interacts with MX1 and
CC RNF24. {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9Y210};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y210}.
CC -!- PTM: Phosphorylated by FYN, leading to an increase of TRPC6 channel
CC activity. {ECO:0000250|UniProtKB:Q61143}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. STrpC
CC subfamily. TRPC6 sub-subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DAAA02039923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02039924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02039925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ271069; CAC01677.1; -; mRNA.
DR RefSeq; NP_001160044.1; NM_001166572.1.
DR RefSeq; XP_015330068.1; XM_015474582.1.
DR AlphaFoldDB; Q9MYW0; -.
DR SMR; Q9MYW0; -.
DR IntAct; Q9MYW0; 1.
DR STRING; 9913.ENSBTAP00000053428; -.
DR PaxDb; Q9MYW0; -.
DR Ensembl; ENSBTAT00000061311; ENSBTAP00000053428; ENSBTAG00000011227.
DR GeneID; 407151; -.
DR KEGG; bta:407151; -.
DR CTD; 7225; -.
DR VEuPathDB; HostDB:ENSBTAG00000011227; -.
DR VGNC; VGNC:36386; TRPC6.
DR eggNOG; KOG3609; Eukaryota.
DR GeneTree; ENSGT01050000244831; -.
DR HOGENOM; CLU_005716_4_2_1; -.
DR InParanoid; Q9MYW0; -.
DR OMA; WISELFW; -.
DR OrthoDB; 1018075at2759; -.
DR TreeFam; TF313147; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000011227; Expressed in neutrophil and 90 other tissues.
DR GO; GO:0034703; C:cation channel complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0036057; C:slit diaphragm; IEA:Ensembl.
DR GO; GO:0005261; F:cation channel activity; ISS:UniProtKB.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0015279; F:store-operated calcium channel activity; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006828; P:manganese ion transport; IBA:GO_Central.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; IEA:Ensembl.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:0032414; P:positive regulation of ion transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0007338; P:single fertilization; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR013555; TRP_dom.
DR InterPro; IPR005462; TRPC6_channel.
DR InterPro; IPR002153; TRPC_channel.
DR PANTHER; PTHR10117; PTHR10117; 1.
DR PANTHER; PTHR10117:SF7; PTHR10117:SF7; 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; PR01647; TRPCHANNEL6.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; Calcium; Calcium channel; Calcium transport; Cell membrane;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..931
FT /note="Short transient receptor potential channel 6"
FT /id="PRO_0000215321"
FT TOPO_DOM 1..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..438
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..487
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 509..521
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 543..592
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 593..613
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 614..636
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 637..657
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 658..674
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 675..695
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 696..706
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 707..727
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 728..931
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 131..160
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 162..188
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 217..246
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 618..647
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 815
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y210"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 931 AA; 106351 MW; 8E2E7E964043E339 CRC64;
MNQSPAAFGP RRGGSPAVVA GAGARRNESQ DYLLMDSELG DDAQPPLPAY GYYPCLRGTD
SRLTHRRQTV LREKGRRLAN RGPAYMFNDH STSLSIEEER FLDAAEYGNI PVVRKMLEEC
LSLNVNCVDY MGQNALQLAV ANEHLEITEL LLKKENLSRV GDALLLAISK GYVRIVEAIL
SHPAFAEGKR LATSPSQSEL QQDDFYAYDE DGTRFSHDVT PIILAAHCQE YEIVHTLLRK
GARIERPHDY FCKCSECNQK QKHDSFSHSR SRINAYKGLA SPAYLSLSSE DPVMTALELS
NELAVLANIE KEFKNDYKKL SMQCKDFVVG LLDLCRNTEE VEAILNGDVE IHHSGGDHYR
PNLSRLKLAI KYDVKKFVAH PNCQQQLLSI WYENLSGLRQ QTMAVKFLVV LAVAVGLPFL
ALVYWFAPCS KMGKIMRGPF MKFVAHAASF TIFLGLLVMN AADRFEGTKI LPNETSTDHA
KQLFRMKTSC FSWMEMLIIS WVIGMIWAEC KEIWTQGPKE YLFELWNMLD FGMLAIFAAS
FIARFMAFWH ASKAQSIIDA NDTLKDLTKV TLGDNVKYYN LARIKWDPSD PQIISEGLYA
IAVVLSFSRI AYILPANESF GPLQISLGRT VKDIFKFMVI FIMVFVAFMI GMFNLYSYYI
GAKQNEAFTT VEESFKTLFW AIFGLSEVKS VVINYNHKFI ENIGYVLYGV YNVTMVIVLL
NMLIAMINSS FQEIEDDADV EWKFARAKLW FSYFEEGRTL PVPFNLVPSP KSLFYLLLRL
KKWISELFQG HKKGFQEDAE MNKRNEGKKF GILGSHEDLS KLSLDRKQFA HSKQSSIRSS
EDFQLNSFTN PPRQYQKIMK RLIKRYVLQA QIDKESDEVN EGELKEIKQD ISSLRYELLE
EKTQNSEDLA ELIRKLGEKL SMEPNQEESN R
