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Protein

Short transient receptor potential channel 4

Gene

TRPC4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Form a receptor-activated non-selective calcium permeant cation channel. Acts as a cell-cell contact-dependent endothelial calcium entry channel. Probably operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Mediates cation entry, with an enhanced permeability to barium over calcium. May also be activated by intracellular calcium store depletion.2 Publications

GO - Molecular functioni

  1. beta-catenin binding Source: BHF-UCL
  2. cadherin binding Source: BHF-UCL
  3. inositol 1,4,5 trisphosphate binding Source: GO_Central
  4. store-operated calcium channel activity Source: UniProtKB

GO - Biological processi

  1. axon guidance Source: Reactome
  2. calcium ion import Source: BHF-UCL
  3. calcium ion transmembrane transport Source: GO_Central
  4. calcium ion transport Source: ProtInc
  5. cytosolic calcium ion homeostasis Source: GO_Central
  6. gamma-aminobutyric acid secretion Source: Ensembl
  7. ion transmembrane transport Source: Reactome
  8. manganese ion transport Source: GO_Central
  9. oligodendrocyte differentiation Source: Ensembl
  10. transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_169333. TRP channels.
REACT_22228. Role of second messengers in netrin-1 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Short transient receptor potential channel 4
Short name:
TrpC4
Alternative name(s):
Trp-related protein 4
Short name:
hTrp-4
Short name:
hTrp4
Gene namesi
Name:TRPC4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:12336. TRPC4.

Subcellular locationi

  1. Membrane; Multi-pass membrane protein
  2. Cell membrane; Multi-pass membrane protein

  3. Note: Enhanced insertion into the cell membrane after activation of the EGF receptor.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 329329CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei330 – 35021HelicalSequence AnalysisAdd
BLAST
Topological domaini351 – 36212ExtracellularSequence AnalysisAdd
BLAST
Transmembranei363 – 38321HelicalSequence AnalysisAdd
BLAST
Topological domaini384 – 43653CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei437 – 45721HelicalSequence AnalysisAdd
BLAST
Topological domaini458 – 46912ExtracellularSequence AnalysisAdd
BLAST
Transmembranei470 – 49021HelicalSequence AnalysisAdd
BLAST
Topological domaini491 – 51121CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei512 – 53221HelicalSequence AnalysisAdd
BLAST
Topological domaini533 – 59967ExtracellularSequence AnalysisAdd
BLAST
Transmembranei600 – 62021HelicalSequence AnalysisAdd
BLAST
Topological domaini621 – 977357CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. basolateral plasma membrane Source: BHF-UCL
  2. calcium channel complex Source: UniProtKB
  3. caveola Source: Ensembl
  4. cell surface Source: BHF-UCL
  5. cortical cytoskeleton Source: UniProtKB
  6. integral component of plasma membrane Source: GO_Central
  7. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi959 – 9591Y → F: Reduced EGF-induced phosphorylation and decreased association with SLC9A3R1/NHERF. Loss of EGF-induced phosphorylation and decreased association with SLC9A3R1/NHERF; when associated with F-972. 1 Publication
Mutagenesisi972 – 9721Y → F: Reduced EGF-induced phosphorylation and decreased association with SLC9A3R1/NHERF. Loss of EGF-induced phosphorylation and decreased association with SLC9A3R1/NHERF; when associated with F-959. 1 Publication
Mutagenesisi975 – 9773Missing : Loss of interaction with SLC9A3R1/NHERF. 1 Publication

Organism-specific databases

PharmGKBiPA37009.

Polymorphism and mutation databases

BioMutaiTRPC4.
DMDMi13633994.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 977977Short transient receptor potential channel 4PRO_0000215314Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei959 – 9591Phosphotyrosine; by FYN1 Publication
Modified residuei972 – 9721Phosphotyrosine; by FYN1 Publication

Post-translational modificationi

Phosphorylation modulates TRPC channel function by regulating the level of TRPC4 at the cell surface and by increasing the association with SLC9A3R1/NHERF.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9UBN4.
PRIDEiQ9UBN4.

PTM databases

PhosphoSiteiQ9UBN4.

Expressioni

Tissue specificityi

Strongly expressed in placenta. Expressed at lower levels in heart, pancreas, kidney and brain. Expressed in endothelial cells. Isoform alpha was found to be the predominant isoform. Isoform beta was not found in pancreas and brain.1 Publication

Gene expression databases

BgeeiQ9UBN4.
CleanExiHS_TRPC4.
ExpressionAtlasiQ9UBN4. baseline and differential.
GenevestigatoriQ9UBN4.

Interactioni

Subunit structurei

Interacts with TRPC4AP (By similarity). Homotetramer and heterotetramer with TRPC1 and/or TRPC5. Isoform alpha but not isoform beta associates with inositol 1,4,5-trisphosphate receptor (ITPR). Interacts with (via PDZ-binding domain) with SLC9A3R1/NHERF. Interacts with MX1 and RNF24. Interacts (via CIRB domain) with SESTD1 (via spectrin 1 repeat). Interacts with CDH5 and CTNNB1. Interacts with SPTAN1 (via C-terminal spectrin repeats) and SPTBN5 (via C-terminus). Interacts (via protein 4.1-binding domain) with EPB41L2.By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MX1P205912EBI-929504,EBI-929476

Protein-protein interaction databases

BioGridi113074. 13 interactions.
IntActiQ9UBN4. 2 interactions.
MINTiMINT-157838.
STRINGi9606.ENSP00000369003.

Structurei

3D structure databases

ProteinModelPortaliQ9UBN4.
SMRiQ9UBN4. Positions 36-167.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati31 – 6030ANK 1Add
BLAST
Repeati69 – 9729ANK 2Add
BLAST
Repeati98 – 12427ANK 3Add
BLAST
Repeati141 – 17030ANK 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni87 – 17286Multimerization domainBy similarityAdd
BLAST
Regioni254 – 30451Multimerization domainBy similarityAdd
BLAST
Regioni615 – 977363Binds to ITPR1, ITPR2 and ITPR3Add
BLAST
Regioni975 – 9773PDZ-binding domain

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili223 – 26038Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi377 – 3826Poly-Leu

Domaini

The protein 4.1-binding domain (654-685) is required for binding to EPB41L2 and channel activation.
The calmodulin- and inositol 1,4,5-trisphosphate receptor-binding (CIRB) domain (695-724) is sufficient for the interaction with SESTD1.
The spectrin-binding domain (730-758) is required for binding to SPTAN1 and SPTBN5.

Sequence similaritiesi

Contains 4 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Coiled coil, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG254238.
GeneTreeiENSGT00760000119180.
HOGENOMiHOG000151279.
HOVERGENiHBG068337.
InParanoidiQ9UBN4.
KOiK04967.
OMAiEYVHDMW.
OrthoDBiEOG72G17P.
PhylomeDBiQ9UBN4.
TreeFamiTF313147.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR013555. TRP_dom.
IPR005460. TRPC4_channel.
IPR002153. TRPC_channel.
[Graphical view]
PANTHERiPTHR10117. PTHR10117. 1 hit.
PTHR10117:SF25. PTHR10117:SF25. 1 hit.
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
PF08344. TRP_2. 1 hit.
[Graphical view]
PRINTSiPR01097. TRNSRECEPTRP.
PR01645. TRPCHANNEL4.
SMARTiSM00248. ANK. 2 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
TIGRFAMsiTIGR00870. trp. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Alpha (identifier: Q9UBN4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAQFYYKRNV NAPYRDRIPL RIVRAESELS PSEKAYLNAV EKGDYASVKK
60 70 80 90 100
SLEEAEIYFK ININCIDPLG RTALLIAIEN ENLELIELLL SFNVYVGDAL
110 120 130 140 150
LHAIRKEVVG AVELLLNHKK PSGEKQVPPI LLDKQFSEFT PDITPIILAA
160 170 180 190 200
HTNNYEIIKL LVQKGVSVPR PHEVRCNCVE CVSSSDVDSL RHSRSRLNIY
210 220 230 240 250
KALASPSLIA LSSEDPFLTA FQLSWELQEL SKVENEFKSE YEELSRQCKQ
260 270 280 290 300
FAKDLLDQTR SSRELEIILN YRDDNSLIEE QSGNDLARLK LAIKYRQKEF
310 320 330 340 350
VAQPNCQQLL ASRWYDEFPG WRRRHWAVKM VTCFIIGLLF PVFSVCYLIA
360 370 380 390 400
PKSPLGLFIR KPFIKFICHT ASYLTFLFLL LLASQHIDRS DLNRQGPPPT
410 420 430 440 450
IVEWMILPWV LGFIWGEIKQ MWDGGLQDYI HDWWNLMDFV MNSLYLATIS
460 470 480 490 500
LKIVAFVKYS ALNPRESWDM WHPTLVAEAL FAIANIFSSL RLISLFTANS
510 520 530 540 550
HLGPLQISLG RMLLDILKFL FIYCLVLLAF ANGLNQLYFY YEETKGLTCK
560 570 580 590 600
GIRCEKQNNA FSTLFETLQS LFWSIFGLIN LYVTNVKAQH EFTEFVGATM
610 620 630 640 650
FGTYNVISLV VLLNMLIAMM NNSYQLIADH ADIEWKFART KLWMSYFEEG
660 670 680 690 700
GTLPTPFNVI PSPKSLWYLI KWIWTHLCKK KMRRKPESFG TIGRRAADNL
710 720 730 740 750
RRHHQYQEVM RNLVKRYVAA MIRDAKTEEG LTEENFKELK QDISSFRFEV
760 770 780 790 800
LGLLRGSKLS TIQSANASKE SSNSADSDEK SDSEGNSKDK KKNFSLFDLT
810 820 830 840 850
TLIHPRSAAI ASERHNISNG SALVVQEPPR EKQRKVNFVT DIKNFGLFHR
860 870 880 890 900
RSKQNAAEQN ANQIFSVSEE VARQQAAGPL ERNIQLESRG LASRGDLSIP
910 920 930 940 950
GLSEQCVLVD HRERNTDTLG LQVGKRVCPF KSEKVVVEDT VPIIPKEKHA
960 970
KEEDSSIDYD LNLPDTVTHE DYVTTRL
Length:977
Mass (Da):112,101
Last modified:May 1, 2000 - v1
Checksum:i77E4D27C374D660E
GO
Isoform Beta (identifier: Q9UBN4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     785-868: Missing.

Show »
Length:893
Mass (Da):102,640
Checksum:i20E5FE3C93B47BB5
GO
Isoform Delta (identifier: Q9UBN4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     730-870: Missing.

Show »
Length:836
Mass (Da):96,389
Checksum:i1BAE1CA946ED6DAF
GO
Isoform Gamma (identifier: Q9UBN4-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     629-693: Missing.
     785-868: Missing.

Show »
Length:828
Mass (Da):94,859
Checksum:iC01141A15CCA516C
GO
Isoform Epsilon (identifier: Q9UBN4-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     693-693: G → GVRTQH

Show »
Length:982
Mass (Da):112,723
Checksum:i7F4500A57F38B8BD
GO
Isoform Zeta (identifier: Q9UBN4-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     127-299: Missing.

Show »
Length:804
Mass (Da):92,221
Checksum:i30F8E11810A76888
GO
Isoform Eta (identifier: Q9UBN4-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     300-323: FVAQPNCQQLLASRWYDEFPGWRR → ASYGEKLNRCGMADFRTTSMIGGI
     324-977: Missing.

Show »
Length:323
Mass (Da):36,759
Checksum:i39B4E28D03534CDD
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti138 – 1381E → K in a breast cancer sample; somatic mutation. 1 Publication
VAR_036452

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei127 – 299173Missing in isoform Zeta. 1 PublicationVSP_041439Add
BLAST
Alternative sequencei300 – 32324FVAQP…PGWRR → ASYGEKLNRCGMADFRTTSM IGGI in isoform Eta. 1 PublicationVSP_047747Add
BLAST
Alternative sequencei324 – 977654Missing in isoform Eta. 1 PublicationVSP_047748Add
BLAST
Alternative sequencei629 – 69365Missing in isoform Gamma. 1 PublicationVSP_006567Add
BLAST
Alternative sequencei693 – 6931G → GVRTQH in isoform Epsilon. 1 PublicationVSP_041262
Alternative sequencei730 – 870141Missing in isoform Delta. 1 PublicationVSP_006568Add
BLAST
Alternative sequencei785 – 86884Missing in isoform Beta and isoform Gamma. 2 PublicationsVSP_006569Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF063822 mRNA. Translation: AAF22927.1.
AF063823 mRNA. Translation: AAF22928.1.
AF063824 mRNA. Translation: AAF22929.1.
AF063825 mRNA. Translation: AAF22930.1.
AF175406 mRNA. Translation: AAD51736.1.
AF421358 mRNA. Translation: AAL24549.1.
AF421359 mRNA. Translation: AAL24550.1.
AF421360 mRNA. Translation: AAL24551.1.
AF421361 mRNA. Translation: AAL24552.1.
AF421362 mRNA. Translation: AAL24553.1.
AL138679, AL354802 Genomic DNA. Translation: CAH70109.1.
AL138679, AL354802 Genomic DNA. Translation: CAH70110.1.
AL138679, AL354802 Genomic DNA. Translation: CAH70111.1.
AL138679, AL354802 Genomic DNA. Translation: CAH70114.1.
AL354802, AL138679 Genomic DNA. Translation: CAI15556.1.
AL354802, AL138679 Genomic DNA. Translation: CAI15557.1.
AL354802, AL138679 Genomic DNA. Translation: CAI15558.1.
AL354802, AL138679 Genomic DNA. Translation: CAI15560.1.
AL138679, AL354802 Genomic DNA. Translation: CAH70112.1.
AL354802, AL138679 Genomic DNA. Translation: CAI15561.1.
CH471075 Genomic DNA. Translation: EAX08595.1.
CH471075 Genomic DNA. Translation: EAX08596.1.
CH471075 Genomic DNA. Translation: EAX08597.1.
CH471075 Genomic DNA. Translation: EAX08598.1.
CH471075 Genomic DNA. Translation: EAX08600.1.
CH471075 Genomic DNA. Translation: EAX08601.1.
BC104725 mRNA. Translation: AAI04726.1.
U40983 mRNA. Translation: AAC50630.1.
CCDSiCCDS45035.1. [Q9UBN4-6]
CCDS45036.1. [Q9UBN4-4]
CCDS45038.1. [Q9UBN4-2]
CCDS45039.1. [Q9UBN4-3]
CCDS9365.1. [Q9UBN4-1]
RefSeqiNP_001129427.1. NM_001135955.1. [Q9UBN4-2]
NP_001129428.1. NM_001135956.1. [Q9UBN4-4]
NP_001129429.1. NM_001135957.1. [Q9UBN4-3]
NP_001129430.1. NM_001135958.1. [Q9UBN4-6]
NP_003297.1. NM_003306.1. [Q9UBN4-5]
NP_057263.1. NM_016179.2. [Q9UBN4-1]
UniGeneiHs.262960.

Genome annotation databases

EnsembliENST00000338947; ENSP00000342580; ENSG00000133107. [Q9UBN4-6]
ENST00000355779; ENSP00000348025; ENSG00000133107. [Q9UBN4-3]
ENST00000358477; ENSP00000351264; ENSG00000133107. [Q9UBN4-2]
ENST00000379673; ENSP00000368995; ENSG00000133107. [Q9UBN4-4]
ENST00000379679; ENSP00000369001; ENSG00000133107. [Q9UBN4-6]
ENST00000379705; ENSP00000369027; ENSG00000133107. [Q9UBN4-1]
ENST00000488717; ENSP00000435969; ENSG00000133107. [Q9UBN4-7]
GeneIDi7223.
KEGGihsa:7223.
UCSCiuc001uws.3. human. [Q9UBN4-1]
uc001uwt.3. human. [Q9UBN4-2]
uc010abw.3. human. [Q9UBN4-6]
uc010abx.3. human. [Q9UBN4-5]
uc010aby.3. human. [Q9UBN4-4]
uc010tey.2. human. [Q9UBN4-3]

Polymorphism and mutation databases

BioMutaiTRPC4.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF063822 mRNA. Translation: AAF22927.1.
AF063823 mRNA. Translation: AAF22928.1.
AF063824 mRNA. Translation: AAF22929.1.
AF063825 mRNA. Translation: AAF22930.1.
AF175406 mRNA. Translation: AAD51736.1.
AF421358 mRNA. Translation: AAL24549.1.
AF421359 mRNA. Translation: AAL24550.1.
AF421360 mRNA. Translation: AAL24551.1.
AF421361 mRNA. Translation: AAL24552.1.
AF421362 mRNA. Translation: AAL24553.1.
AL138679, AL354802 Genomic DNA. Translation: CAH70109.1.
AL138679, AL354802 Genomic DNA. Translation: CAH70110.1.
AL138679, AL354802 Genomic DNA. Translation: CAH70111.1.
AL138679, AL354802 Genomic DNA. Translation: CAH70114.1.
AL354802, AL138679 Genomic DNA. Translation: CAI15556.1.
AL354802, AL138679 Genomic DNA. Translation: CAI15557.1.
AL354802, AL138679 Genomic DNA. Translation: CAI15558.1.
AL354802, AL138679 Genomic DNA. Translation: CAI15560.1.
AL138679, AL354802 Genomic DNA. Translation: CAH70112.1.
AL354802, AL138679 Genomic DNA. Translation: CAI15561.1.
CH471075 Genomic DNA. Translation: EAX08595.1.
CH471075 Genomic DNA. Translation: EAX08596.1.
CH471075 Genomic DNA. Translation: EAX08597.1.
CH471075 Genomic DNA. Translation: EAX08598.1.
CH471075 Genomic DNA. Translation: EAX08600.1.
CH471075 Genomic DNA. Translation: EAX08601.1.
BC104725 mRNA. Translation: AAI04726.1.
U40983 mRNA. Translation: AAC50630.1.
CCDSiCCDS45035.1. [Q9UBN4-6]
CCDS45036.1. [Q9UBN4-4]
CCDS45038.1. [Q9UBN4-2]
CCDS45039.1. [Q9UBN4-3]
CCDS9365.1. [Q9UBN4-1]
RefSeqiNP_001129427.1. NM_001135955.1. [Q9UBN4-2]
NP_001129428.1. NM_001135956.1. [Q9UBN4-4]
NP_001129429.1. NM_001135957.1. [Q9UBN4-3]
NP_001129430.1. NM_001135958.1. [Q9UBN4-6]
NP_003297.1. NM_003306.1. [Q9UBN4-5]
NP_057263.1. NM_016179.2. [Q9UBN4-1]
UniGeneiHs.262960.

3D structure databases

ProteinModelPortaliQ9UBN4.
SMRiQ9UBN4. Positions 36-167.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113074. 13 interactions.
IntActiQ9UBN4. 2 interactions.
MINTiMINT-157838.
STRINGi9606.ENSP00000369003.

Chemistry

GuidetoPHARMACOLOGYi489.

PTM databases

PhosphoSiteiQ9UBN4.

Polymorphism and mutation databases

BioMutaiTRPC4.
DMDMi13633994.

Proteomic databases

PaxDbiQ9UBN4.
PRIDEiQ9UBN4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000338947; ENSP00000342580; ENSG00000133107. [Q9UBN4-6]
ENST00000355779; ENSP00000348025; ENSG00000133107. [Q9UBN4-3]
ENST00000358477; ENSP00000351264; ENSG00000133107. [Q9UBN4-2]
ENST00000379673; ENSP00000368995; ENSG00000133107. [Q9UBN4-4]
ENST00000379679; ENSP00000369001; ENSG00000133107. [Q9UBN4-6]
ENST00000379705; ENSP00000369027; ENSG00000133107. [Q9UBN4-1]
ENST00000488717; ENSP00000435969; ENSG00000133107. [Q9UBN4-7]
GeneIDi7223.
KEGGihsa:7223.
UCSCiuc001uws.3. human. [Q9UBN4-1]
uc001uwt.3. human. [Q9UBN4-2]
uc010abw.3. human. [Q9UBN4-6]
uc010abx.3. human. [Q9UBN4-5]
uc010aby.3. human. [Q9UBN4-4]
uc010tey.2. human. [Q9UBN4-3]

Organism-specific databases

CTDi7223.
GeneCardsiGC13M038210.
HGNCiHGNC:12336. TRPC4.
MIMi603651. gene.
neXtProtiNX_Q9UBN4.
PharmGKBiPA37009.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG254238.
GeneTreeiENSGT00760000119180.
HOGENOMiHOG000151279.
HOVERGENiHBG068337.
InParanoidiQ9UBN4.
KOiK04967.
OMAiEYVHDMW.
OrthoDBiEOG72G17P.
PhylomeDBiQ9UBN4.
TreeFamiTF313147.

Enzyme and pathway databases

ReactomeiREACT_169333. TRP channels.
REACT_22228. Role of second messengers in netrin-1 signaling.

Miscellaneous databases

ChiTaRSiTRPC4. human.
GeneWikiiTRPC4.
GenomeRNAii7223.
NextBioi28287.
PROiQ9UBN4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UBN4.
CleanExiHS_TRPC4.
ExpressionAtlasiQ9UBN4. baseline and differential.
GenevestigatoriQ9UBN4.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR013555. TRP_dom.
IPR005460. TRPC4_channel.
IPR002153. TRPC_channel.
[Graphical view]
PANTHERiPTHR10117. PTHR10117. 1 hit.
PTHR10117:SF25. PTHR10117:SF25. 1 hit.
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
PF08344. TRP_2. 1 hit.
[Graphical view]
PRINTSiPR01097. TRNSRECEPTRP.
PR01645. TRPCHANNEL4.
SMARTiSM00248. ANK. 2 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
TIGRFAMsiTIGR00870. trp. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of the human transient receptor potential 4 (TRP4) gene: localization and functional expression of human TRP4 and TRP3."
    McKay R.R., Szymeczek-Seay C.L., Lievremont J.-P., Bird G.S., Zitt C., Juengling E., Lueckhoff A., Putney J.W. Jr.
    Biochem. J. 351:735-746(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
    Tissue: Kidney.
  2. "Alternative splice variants of hTrp4 differentially interact with the C-terminal portion of the inositol 1,4,5-trisphosphate receptors."
    Mery L., Magnino F., Schmidt K., Krause K.-H., Dufour J.-F.
    FEBS Lett. 487:377-383(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA; DELTA AND GAMMA).
    Tissue: Embryonic kidney.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA; EPSILON; ETA AND ZETA), SUBCELLULAR LOCATION.
  4. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
  7. "trp, a novel mammalian gene family essential for agonist-activated capacitative Ca2+ entry."
    Zhu X., Jiang M., Peyton M., Boulay G., Hurst R., Stefani E., Birnbaumer L.
    Cell 85:661-671(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 514-633.
    Tissue: Kidney.
  8. "The PDZ-interacting domain of TRPC4 controls its localization and surface expression in HEK293 cells."
    Mery L., Strauss B., Dufour J.F., Krause K.H., Hoth M.
    J. Cell Sci. 115:3497-3508(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 975-THR--LEU-977, INTERACTION WITH SLC9A3R1, SUBCELLULAR LOCATION.
  9. "Subunit composition of mammalian transient receptor potential channels in living cells."
    Hofmann T., Schaefer M., Schultz G., Gudermann T.
    Proc. Natl. Acad. Sci. U.S.A. 99:7461-7466(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  10. "Activation of the endothelial store-operated ISOC Ca2+ channel requires interaction of protein 4.1 with TRPC4."
    Cioffi D.L., Wu S., Alexeyev M., Goodman S.R., Zhu M.X., Stevens T.
    Circ. Res. 97:1164-1172(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EPB41L2.
  11. "MxA, a member of the dynamin superfamily, interacts with the ankyrin-like repeat domain of TRPC."
    Lussier M.P., Cayouette S., Lepage P.K., Bernier C.L., Francoeur N., St-Hilaire M., Pinard M., Boulay G.
    J. Biol. Chem. 280:19393-19400(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MX1.
  12. "Epidermal growth factor induces tyrosine phosphorylation, membrane insertion, and activation of transient receptor potential channel 4."
    Odell A.F., Scott J.L., Van Helden D.F.
    J. Biol. Chem. 280:37974-37987(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-959 AND TYR-972, MUTAGENESIS OF TYR-959 AND TYR-972.
  13. "RNF24, a new TRPC interacting protein, causes the intracellular retention of TRPC."
    Lussier M.P., Lepage P.K., Bousquet S.M., Boulay G.
    Cell Calcium 43:432-443(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF24.
  14. "The spectrin cytoskeleton influences the surface expression and activation of human transient receptor potential channel 4 channels."
    Odell A.F., Van Helden D.F., Scott J.L.
    J. Biol. Chem. 283:4395-4407(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPTAN1 AND SPTBN5.
  15. "The phospholipid-binding protein SESTD1 is a novel regulator of the transient receptor potential channels TRPC4 and TRPC5."
    Miehe S., Bieberstein A., Arnould I., Ihdene O., Rutten H., Strubing C.
    J. Biol. Chem. 285:12426-12434(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SESTD1.
  16. "Cell-cell contact formation governs Ca2+ signaling by TRPC4 in the vascular endothelium: evidence for a regulatory TRPC4-beta-catenin interaction."
    Graziani A., Poteser M., Heupel W.M., Schleifer H., Krenn M., Drenckhahn D., Romanin C., Baumgartner W., Groschner K.
    J. Biol. Chem. 285:4213-4223(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH CDH5 AND CTNNB1.
  17. Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-138.

Entry informationi

Entry nameiTRPC4_HUMAN
AccessioniPrimary (citable) accession number: Q9UBN4
Secondary accession number(s): B1ALE0
, B1ALE1, B1ALE2, Q15721, Q3SWS6, Q96P03, Q96P04, Q96P05, Q9UIB0, Q9UIB1, Q9UIB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2000
Last modified: April 29, 2015
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

The interaction with spectrin is important in controlling the translocation of TRPC4 channels to the plasma membrane following EGF stimulation.
The cell membrane presentation, the calcium entry function and the interaction with junctional proteins (CTNNB1 and CDH5) are controlled by endothelial cell-cell contacts.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.