Q9UBN4 (TRPC4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

TRPC4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	977 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.12 Ref.16
Subunit structure	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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16
Subcellular location	Membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Note: Enhanced insertion into the cell membrane after activation of the EGF receptor. Ref.8 Ref.10 Ref.12
Tissue specificity	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. Ref.16
Domain	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.
Post-translational modification	Phosphorylation modulates TRPC channel function by regulating the level of TRPC4 at the cell surface and by increasing the association with SLC9A3R1/NHERF.
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.
Sequence similarities	Belongs to the transient receptor (TC 1.A.4) family. STrpC subfamily. TRPC4 sub-subfamily. [View classification] Contains 4 ANK repeats.

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	ANK repeat Coiled coil Repeat Transmembrane Transmembrane helix
Ligand	Calcium
Molecular function	Calcium channel Ion channel
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Traceable author statement. Source: Reactome calcium ion import Inferred from direct assay Ref.16. Source: BHF-UCL gamma-aminobutyric acid secretion Inferred from electronic annotation. Source: Compara
Cellular_component	basolateral plasma membrane Inferred from direct assay Ref.16. Source: BHF-UCL calcium channel complex Inferred from direct assay Ref.15. Source: UniProtKB caveola Inferred from electronic annotation. Source: Compara cell surface Inferred from direct assay Ref.16. Source: BHF-UCL cortical cytoskeleton Inferred from direct assay Ref.10. Source: UniProtKB
Molecular_function	inositol 1,4,5 trisphosphate binding Inferred from electronic annotation. Source: Compara store-operated calcium channel activity Inferred from mutant phenotype Ref.10. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MX1	P20591	2	EBI-929504,EBI-929476

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform Alpha (identifier: Q9UBN4-1)

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.

Isoform Beta (identifier: Q9UBN4-2)

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

Isoform Delta (identifier: Q9UBN4-3)

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

Isoform Gamma (identifier: Q9UBN4-4)

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

Isoform Epsilon (identifier: Q9UBN4-5)

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

Isoform Zeta (identifier: Q9UBN4-6)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 977	977	Short transient receptor potential channel 4		PRO_0000215314
Regions
	Topological domain	1 – 329	329	Cytoplasmic Potential
	Transmembrane	330 – 350	21	Helical; Potential
	Topological domain	351 – 362	12	Extracellular Potential
	Transmembrane	363 – 383	21	Helical; Potential
	Topological domain	384 – 436	53	Cytoplasmic Potential
	Transmembrane	437 – 457	21	Helical; Potential
	Topological domain	458 – 469	12	Extracellular Potential
	Transmembrane	470 – 490	21	Helical; Potential
	Topological domain	491 – 511	21	Cytoplasmic Potential
	Transmembrane	512 – 532	21	Helical; Potential
	Topological domain	533 – 599	67	Extracellular Potential
	Transmembrane	600 – 620	21	Helical; Potential
	Topological domain	621 – 977	357	Cytoplasmic Potential
	Repeat	31 – 60	30	ANK 1
	Repeat	69 – 97	29	ANK 2
	Repeat	98 – 124	27	ANK 3
	Repeat	141 – 170	30	ANK 4
	Region	87 – 172	86	Multimerization domain By similarity
	Region	254 – 304	51	Multimerization domain By similarity
	Region	615 – 977	363	Binds to ITPR1, ITPR2 and ITPR3
	Region	975 – 977	3	PDZ-binding domain
	Coiled coil	223 – 260	38	Potential
	Compositional bias	377 – 382	6	Poly-Leu
Amino acid modifications
	Modified residue	959	1	Phosphotyrosine; by FYN Ref.12
	Modified residue	972	1	Phosphotyrosine; by FYN Ref.12
Natural variations
	Alternative sequence	127 – 299	173	Missing in isoform Zeta.		VSP_041439
	Alternative sequence	629 – 693	65	Missing in isoform Gamma.		VSP_006567
	Alternative sequence	693	1	G → GVRTQH in isoform Epsilon.		VSP_041262
	Alternative sequence	730 – 870	141	Missing in isoform Delta.		VSP_006568
	Alternative sequence	785 – 868	84	Missing in isoform Beta and isoform Gamma.		VSP_006569
	Natural variant	138	1	E → K in a breast cancer sample; somatic mutation. Ref.17		VAR_036452
Experimental info
	Mutagenesis	959	1	Y → 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. Ref.12
	Mutagenesis	972	1	Y → 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. Ref.12
	Mutagenesis	975 – 977	3	Missing: Loss of interaction with SLC9A3R1/NHERF. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 77E4D27C374D660E	FASTA	977	112,101
	10 20 30 40 50 60 MAQFYYKRNV NAPYRDRIPL RIVRAESELS PSEKAYLNAV EKGDYASVKK SLEEAEIYFK 70 80 90 100 110 120 ININCIDPLG RTALLIAIEN ENLELIELLL SFNVYVGDAL LHAIRKEVVG AVELLLNHKK 130 140 150 160 170 180 PSGEKQVPPI LLDKQFSEFT PDITPIILAA HTNNYEIIKL LVQKGVSVPR PHEVRCNCVE 190 200 210 220 230 240 CVSSSDVDSL RHSRSRLNIY KALASPSLIA LSSEDPFLTA FQLSWELQEL SKVENEFKSE 250 260 270 280 290 300 YEELSRQCKQ FAKDLLDQTR SSRELEIILN YRDDNSLIEE QSGNDLARLK LAIKYRQKEF 310 320 330 340 350 360 VAQPNCQQLL ASRWYDEFPG WRRRHWAVKM VTCFIIGLLF PVFSVCYLIA PKSPLGLFIR 370 380 390 400 410 420 KPFIKFICHT ASYLTFLFLL LLASQHIDRS DLNRQGPPPT IVEWMILPWV LGFIWGEIKQ 430 440 450 460 470 480 MWDGGLQDYI HDWWNLMDFV MNSLYLATIS LKIVAFVKYS ALNPRESWDM WHPTLVAEAL 490 500 510 520 530 540 FAIANIFSSL RLISLFTANS HLGPLQISLG RMLLDILKFL FIYCLVLLAF ANGLNQLYFY 550 560 570 580 590 600 YEETKGLTCK GIRCEKQNNA FSTLFETLQS LFWSIFGLIN LYVTNVKAQH EFTEFVGATM 610 620 630 640 650 660 FGTYNVISLV VLLNMLIAMM NNSYQLIADH ADIEWKFART KLWMSYFEEG GTLPTPFNVI 670 680 690 700 710 720 PSPKSLWYLI KWIWTHLCKK KMRRKPESFG TIGRRAADNL RRHHQYQEVM RNLVKRYVAA 730 740 750 760 770 780 MIRDAKTEEG LTEENFKELK QDISSFRFEV LGLLRGSKLS TIQSANASKE SSNSADSDEK 790 800 810 820 830 840 SDSEGNSKDK KKNFSLFDLT TLIHPRSAAI ASERHNISNG SALVVQEPPR EKQRKVNFVT 850 860 870 880 890 900 DIKNFGLFHR RSKQNAAEQN ANQIFSVSEE VARQQAAGPL ERNIQLESRG LASRGDLSIP 910 920 930 940 950 960 GLSEQCVLVD HRERNTDTLG LQVGKRVCPF KSEKVVVEDT VPIIPKEKHA KEEDSSIDYD 970 LNLPDTVTHE DYVTTRL
	Isoform Beta [UniParc]. Checksum: 20E5FE3C93B47BB5	FASTA	893	102,640
	10 20 30 40 50 60 MAQFYYKRNV NAPYRDRIPL RIVRAESELS PSEKAYLNAV EKGDYASVKK SLEEAEIYFK 70 80 90 100 110 120 ININCIDPLG RTALLIAIEN ENLELIELLL SFNVYVGDAL LHAIRKEVVG AVELLLNHKK 130 140 150 160 170 180 PSGEKQVPPI LLDKQFSEFT PDITPIILAA HTNNYEIIKL LVQKGVSVPR PHEVRCNCVE 190 200 210 220 230 240 CVSSSDVDSL RHSRSRLNIY KALASPSLIA LSSEDPFLTA FQLSWELQEL SKVENEFKSE 250 260 270 280 290 300 YEELSRQCKQ FAKDLLDQTR SSRELEIILN YRDDNSLIEE QSGNDLARLK LAIKYRQKEF 310 320 330 340 350 360 VAQPNCQQLL ASRWYDEFPG WRRRHWAVKM VTCFIIGLLF PVFSVCYLIA PKSPLGLFIR 370 380 390 400 410 420 KPFIKFICHT ASYLTFLFLL LLASQHIDRS DLNRQGPPPT IVEWMILPWV LGFIWGEIKQ 430 440 450 460 470 480 MWDGGLQDYI HDWWNLMDFV MNSLYLATIS LKIVAFVKYS ALNPRESWDM WHPTLVAEAL 490 500 510 520 530 540 FAIANIFSSL RLISLFTANS HLGPLQISLG RMLLDILKFL FIYCLVLLAF ANGLNQLYFY 550 560 570 580 590 600 YEETKGLTCK GIRCEKQNNA FSTLFETLQS LFWSIFGLIN LYVTNVKAQH EFTEFVGATM 610 620 630 640 650 660 FGTYNVISLV VLLNMLIAMM NNSYQLIADH ADIEWKFART KLWMSYFEEG GTLPTPFNVI 670 680 690 700 710 720 PSPKSLWYLI KWIWTHLCKK KMRRKPESFG TIGRRAADNL RRHHQYQEVM RNLVKRYVAA 730 740 750 760 770 780 MIRDAKTEEG LTEENFKELK QDISSFRFEV LGLLRGSKLS TIQSANASKE SSNSADSDEK 790 800 810 820 830 840 SDSEEEVARQ QAAGPLERNI QLESRGLASR GDLSIPGLSE QCVLVDHRER NTDTLGLQVG 850 860 870 880 890 KRVCPFKSEK VVVEDTVPII PKEKHAKEED SSIDYDLNLP DTVTHEDYVT TRL
	Isoform Delta [UniParc]. Checksum: 1BAE1CA946ED6DAF	FASTA	836	96,389
	10 20 30 40 50 60 MAQFYYKRNV NAPYRDRIPL RIVRAESELS PSEKAYLNAV EKGDYASVKK SLEEAEIYFK 70 80 90 100 110 120 ININCIDPLG RTALLIAIEN ENLELIELLL SFNVYVGDAL LHAIRKEVVG AVELLLNHKK 130 140 150 160 170 180 PSGEKQVPPI LLDKQFSEFT PDITPIILAA HTNNYEIIKL LVQKGVSVPR PHEVRCNCVE 190 200 210 220 230 240 CVSSSDVDSL RHSRSRLNIY KALASPSLIA LSSEDPFLTA FQLSWELQEL SKVENEFKSE 250 260 270 280 290 300 YEELSRQCKQ FAKDLLDQTR SSRELEIILN YRDDNSLIEE QSGNDLARLK LAIKYRQKEF 310 320 330 340 350 360 VAQPNCQQLL ASRWYDEFPG WRRRHWAVKM VTCFIIGLLF PVFSVCYLIA PKSPLGLFIR 370 380 390 400 410 420 KPFIKFICHT ASYLTFLFLL LLASQHIDRS DLNRQGPPPT IVEWMILPWV LGFIWGEIKQ 430 440 450 460 470 480 MWDGGLQDYI HDWWNLMDFV MNSLYLATIS LKIVAFVKYS ALNPRESWDM WHPTLVAEAL 490 500 510 520 530 540 FAIANIFSSL RLISLFTANS HLGPLQISLG RMLLDILKFL FIYCLVLLAF ANGLNQLYFY 550 560 570 580 590 600 YEETKGLTCK GIRCEKQNNA FSTLFETLQS LFWSIFGLIN LYVTNVKAQH EFTEFVGATM 610 620 630 640 650 660 FGTYNVISLV VLLNMLIAMM NNSYQLIADH ADIEWKFART KLWMSYFEEG GTLPTPFNVI 670 680 690 700 710 720 PSPKSLWYLI KWIWTHLCKK KMRRKPESFG TIGRRAADNL RRHHQYQEVM RNLVKRYVAA 730 740 750 760 770 780 MIRDAKTEEV ARQQAAGPLE RNIQLESRGL ASRGDLSIPG LSEQCVLVDH RERNTDTLGL 790 800 810 820 830 QVGKRVCPFK SEKVVVEDTV PIIPKEKHAK EEDSSIDYDL NLPDTVTHED YVTTRL
	Isoform Gamma [UniParc]. Checksum: C01141A15CCA516C	FASTA	828	94,859
	10 20 30 40 50 60 MAQFYYKRNV NAPYRDRIPL RIVRAESELS PSEKAYLNAV EKGDYASVKK SLEEAEIYFK 70 80 90 100 110 120 ININCIDPLG RTALLIAIEN ENLELIELLL SFNVYVGDAL LHAIRKEVVG AVELLLNHKK 130 140 150 160 170 180 PSGEKQVPPI LLDKQFSEFT PDITPIILAA HTNNYEIIKL LVQKGVSVPR PHEVRCNCVE 190 200 210 220 230 240 CVSSSDVDSL RHSRSRLNIY KALASPSLIA LSSEDPFLTA FQLSWELQEL SKVENEFKSE 250 260 270 280 290 300 YEELSRQCKQ FAKDLLDQTR SSRELEIILN YRDDNSLIEE QSGNDLARLK LAIKYRQKEF 310 320 330 340 350 360 VAQPNCQQLL ASRWYDEFPG WRRRHWAVKM VTCFIIGLLF PVFSVCYLIA PKSPLGLFIR 370 380 390 400 410 420 KPFIKFICHT ASYLTFLFLL LLASQHIDRS DLNRQGPPPT IVEWMILPWV LGFIWGEIKQ 430 440 450 460 470 480 MWDGGLQDYI HDWWNLMDFV MNSLYLATIS LKIVAFVKYS ALNPRESWDM WHPTLVAEAL 490 500 510 520 530 540 FAIANIFSSL RLISLFTANS HLGPLQISLG RMLLDILKFL FIYCLVLLAF ANGLNQLYFY 550 560 570 580 590 600 YEETKGLTCK GIRCEKQNNA FSTLFETLQS LFWSIFGLIN LYVTNVKAQH EFTEFVGATM 610 620 630 640 650 660 FGTYNVISLV VLLNMLIAMM NNSYQLIARR AADNLRRHHQ YQEVMRNLVK RYVAAMIRDA 670 680 690 700 710 720 KTEEGLTEEN FKELKQDISS FRFEVLGLLR GSKLSTIQSA NASKESSNSA DSDEKSDSEE 730 740 750 760 770 780 EVARQQAAGP LERNIQLESR GLASRGDLSI PGLSEQCVLV DHRERNTDTL GLQVGKRVCP 790 800 810 820 FKSEKVVVED TVPIIPKEKH AKEEDSSIDY DLNLPDTVTH EDYVTTRL
	Isoform Epsilon [UniParc]. Checksum: 7F4500A57F38B8BD	FASTA	982	112,723
	10 20 30 40 50 60 MAQFYYKRNV NAPYRDRIPL RIVRAESELS PSEKAYLNAV EKGDYASVKK SLEEAEIYFK 70 80 90 100 110 120 ININCIDPLG RTALLIAIEN ENLELIELLL SFNVYVGDAL LHAIRKEVVG AVELLLNHKK 130 140 150 160 170 180 PSGEKQVPPI LLDKQFSEFT PDITPIILAA HTNNYEIIKL LVQKGVSVPR PHEVRCNCVE 190 200 210 220 230 240 CVSSSDVDSL RHSRSRLNIY KALASPSLIA LSSEDPFLTA FQLSWELQEL SKVENEFKSE 250 260 270 280 290 300 YEELSRQCKQ FAKDLLDQTR SSRELEIILN YRDDNSLIEE QSGNDLARLK LAIKYRQKEF 310 320 330 340 350 360 VAQPNCQQLL ASRWYDEFPG WRRRHWAVKM VTCFIIGLLF PVFSVCYLIA PKSPLGLFIR 370 380 390 400 410 420 KPFIKFICHT ASYLTFLFLL LLASQHIDRS DLNRQGPPPT IVEWMILPWV LGFIWGEIKQ 430 440 450 460 470 480 MWDGGLQDYI HDWWNLMDFV MNSLYLATIS LKIVAFVKYS ALNPRESWDM WHPTLVAEAL 490 500 510 520 530 540 FAIANIFSSL RLISLFTANS HLGPLQISLG RMLLDILKFL FIYCLVLLAF ANGLNQLYFY 550 560 570 580 590 600 YEETKGLTCK GIRCEKQNNA FSTLFETLQS LFWSIFGLIN LYVTNVKAQH EFTEFVGATM 610 620 630 640 650 660 FGTYNVISLV VLLNMLIAMM NNSYQLIADH ADIEWKFART KLWMSYFEEG GTLPTPFNVI 670 680 690 700 710 720 PSPKSLWYLI KWIWTHLCKK KMRRKPESFG TIGVRTQHRR AADNLRRHHQ YQEVMRNLVK 730 740 750 760 770 780 RYVAAMIRDA KTEEGLTEEN FKELKQDISS FRFEVLGLLR GSKLSTIQSA NASKESSNSA 790 800 810 820 830 840 DSDEKSDSEG NSKDKKKNFS LFDLTTLIHP RSAAIASERH NISNGSALVV QEPPREKQRK 850 860 870 880 890 900 VNFVTDIKNF GLFHRRSKQN AAEQNANQIF SVSEEVARQQ AAGPLERNIQ LESRGLASRG 910 920 930 940 950 960 DLSIPGLSEQ CVLVDHRERN TDTLGLQVGK RVCPFKSEKV VVEDTVPIIP KEKHAKEEDS 970 980 SIDYDLNLPD TVTHEDYVTT RL
	Isoform Zeta [UniParc]. Checksum: 30F8E11810A76888	FASTA	804	92,221
	10 20 30 40 50 60 MAQFYYKRNV NAPYRDRIPL RIVRAESELS PSEKAYLNAV EKGDYASVKK SLEEAEIYFK 70 80 90 100 110 120 ININCIDPLG RTALLIAIEN ENLELIELLL SFNVYVGDAL LHAIRKEVVG AVELLLNHKK 130 140 150 160 170 180 PSGEKQFVAQ PNCQQLLASR WYDEFPGWRR RHWAVKMVTC FIIGLLFPVF SVCYLIAPKS 190 200 210 220 230 240 PLGLFIRKPF IKFICHTASY LTFLFLLLLA SQHIDRSDLN RQGPPPTIVE WMILPWVLGF 250 260 270 280 290 300 IWGEIKQMWD GGLQDYIHDW WNLMDFVMNS LYLATISLKI VAFVKYSALN PRESWDMWHP 310 320 330 340 350 360 TLVAEALFAI ANIFSSLRLI SLFTANSHLG PLQISLGRML LDILKFLFIY CLVLLAFANG 370 380 390 400 410 420 LNQLYFYYEE TKGLTCKGIR CEKQNNAFST LFETLQSLFW SIFGLINLYV TNVKAQHEFT 430 440 450 460 470 480 EFVGATMFGT YNVISLVVLL NMLIAMMNNS YQLIADHADI EWKFARTKLW MSYFEEGGTL 490 500 510 520 530 540 PTPFNVIPSP KSLWYLIKWI WTHLCKKKMR RKPESFGTIG RRAADNLRRH HQYQEVMRNL 550 560 570 580 590 600 VKRYVAAMIR DAKTEEGLTE ENFKELKQDI SSFRFEVLGL LRGSKLSTIQ SANASKESSN 610 620 630 640 650 660 SADSDEKSDS EGNSKDKKKN FSLFDLTTLI HPRSAAIASE RHNISNGSAL VVQEPPREKQ 670 680 690 700 710 720 RKVNFVTDIK NFGLFHRRSK QNAAEQNANQ IFSVSEEVAR QQAAGPLERN IQLESRGLAS 730 740 750 760 770 780 RGDLSIPGLS EQCVLVDHRE RNTDTLGLQV GKRVCPFKSE KVVVEDTVPI IPKEKHAKEE 790 800 DSSIDYDLNL PDTVTHEDYV TTRL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Functional differences between TRPC4 splice variants." Schaefer M., Plant T.D., Stresow N., Albrecht N., Schultz G. J. Biol. Chem. 277:3752-3759(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA; EPSILON AND ZETA).
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-138.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. 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: 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.
IPI	IPI00002689. IPI00044147. IPI00219492. IPI00219494. IPI00219495. IPI00643379.
RefSeq	NP_001129427.1. NM_001135955.1. NP_001129428.1. NM_001135956.1. NP_001129429.1. NM_001135957.1. NP_001129430.1. NM_001135958.1. NP_003297.1. NM_003306.1. NP_057263.1. NM_016179.2.
UniGene	Hs.262960.
3D structure databases
ProteinModelPortal	Q9UBN4.
SMR	Q9UBN4. Positions 36-167.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UBN4. 1 interaction.
MINT	MINT-157838.
STRING	9606.ENSP00000369003.
PTM databases
PhosphoSite	Q9UBN4.
Polymorphism databases
DMDM	13633994.
Proteomic databases
PaxDb	Q9UBN4.
PRIDE	Q9UBN4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000338947; ENSP00000342580; ENSG00000133107. ENST00000355779; ENSP00000348025; ENSG00000133107. ENST00000358477; ENSP00000351264; ENSG00000133107. ENST00000379673; ENSP00000368995; ENSG00000133107. ENST00000379679; ENSP00000369001; ENSG00000133107. ENST00000379681; ENSP00000369003; ENSG00000133107. ENST00000379705; ENSP00000369027; ENSG00000133107. ENST00000447043; ENSP00000414316; ENSG00000133107.
GeneID	7223.
KEGG	hsa:7223.
UCSC	uc001uws.3. human. uc001uwt.3. human. uc010abw.3. human. uc010abx.3. human. uc010aby.3. human. uc010tey.2. human.
Organism-specific databases
CTD	7223.
GeneCards	GC13M038210.
HGNC	HGNC:12336. TRPC4.
MIM	603651. gene.
neXtProt	NX_Q9UBN4.
PharmGKB	PA37009.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG254238.
HOVERGEN	HBG068337.
KO	K04967.
OMA	NMAQFYY.
OrthoDB	EOG4V6ZG2.
PhylomeDB	Q9UBN4.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology.
Gene expression databases
ArrayExpress	Q9UBN4.
Bgee	Q9UBN4.
CleanEx	HS_TRPC4.
Genevestigator	Q9UBN4.
GermOnline	ENSG00000133107. Homo sapiens.
Family and domain databases
Gene3D	1.25.40.20. 1 hit.
InterPro	IPR002110. 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]
PANTHER	PTHR10117. PTHR10117. 1 hit. PTHR10117:SF25. PTHR10117:SF25. 1 hit.
Pfam	PF00023. Ank. 1 hit. PF12796. Ank_2. 1 hit. PF00520. Ion_trans. 1 hit. PF08344. TRP_2. 1 hit. [Graphical view]
PRINTS	PR01097. TRNSRECEPTRP. PR01645. TRPCHANNEL4.
SMART	SM00248. ANK. 2 hits. [Graphical view]
SUPFAM	SSF48403. ANK. 1 hit.
TIGRFAMs	TIGR00870. trp. 1 hit.
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	TRPC4. human.
GenomeRNAi	7223.
NextBio	28287.
SOURCE	Search...

Entry information

Entry name

TRPC4_HUMAN

Accession

Primary (citable) accession number: Q9UBN4
Secondary accession number(s): B1ALE0 , B1ALE1, B1ALE2, Q15721, Q3SWS6, Q96P03, Q96P05, Q9UIB0, Q9UIB1, Q9UIB2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 127 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.