9OLM: Human TRPC3 cerebellar splice variant

Structure of human TRPC3 cerebellar splice variant (isoform c). Determined by electron microscopy at 2.5 Å resolution. Released 25 Mar 2026.

Method: Electron microscopy
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 4
Atoms: 24,528
Mol. weight: 376.73 kDa
Released: 25 Mar 2026

Explore 9OLM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9OLM contains 172 α-helices and 24 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chains A, B, C and D: 43 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	35-37	3
α-helix	38-48	11
α-helix	52-61	10
α-helix	77-83	7
α-helix	87-93	7
α-helix	102-112	11
α-helix	115-122	8
α-helix	125-128	4
α-helix	137-141	5
β-strand	149	1	1
β-strand	155	1	1
α-helix	163-170	8
α-helix	173-181	9
α-helix	197-205	9
α-helix	209-221	13
α-helix	224-230	7
α-helix	234-251	18
α-helix	256-274	19
α-helix	280-288	9
α-helix	307-314	8
α-helix	318-321	4
α-helix	324-334	11
α-helix	339-342	4
α-helix	348-369	22
α-helix	373-379	7
α-helix	382-402	21
α-helix	405-407	3
α-helix	427-432	6
α-helix	436-458	23
α-helix	461-464	4
α-helix	470-504	35
α-helix	517-520	4
α-helix	521-523	3
α-helix	526-528	3
α-helix	534-549	16
α-helix	552-555	4
α-helix	557-559	3
α-helix	564-598	35
β-strand	606	1	2
α-helix	614-623	10
α-helix	631-634	4
β-strand	636	1	2
α-helix	641-674	34
α-helix	680-694	15
α-helix	746-795	22
β-strand	798	1	3
α-helix	799	1
β-strand	800	1	4
α-helix	801-837	37

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Short transient receptor potential channel 3	A, B, C, D	protein	820	Homo sapiens	Q13507 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>9OLM_1 Short transient receptor potential channel 3 (chains A, B, C, D)
MEGSPSLRRMTVMREKGRRQAVRGPAFMFNDRGTSLTAEEERFLDAAEYGNIPVVRKMLE
ESKTLNVNCVDYMGQNALQLAVGNEHLEVTELLLKKENLARIGDALLLAISKGYVRIVEA
ILNHPGFAASKRLTLSPCEQELQDDDFYAYDEDGTRFSPDITPIILAAHCQKYEVVHMLL
MKGARIERPHDYFCKCGDCMEKQRHDSFSHSRSRINAYKGLASPAYLSLSSEDPVLTALE
LSNELAKLANIEKEFKNDYRKLSMQCKDFVVGVLDLCRDSEEVEAILNGDLESAEPLEVH
RHKASLSRVKLAIKYEVKKFVAHPNCQQQLLTIWYENLSGLREQTIAIKCLVVLVVALGL
PFLAIGYWIAPCSRLGKILRSPFMKFVAHAASFIIFLGLLVFNASDRFEGITTLPNITVT
DYPKQIFRVKTTQFTWTEMLIMVWVLGMMWSECKELWLEGPREYILQLWNVLDFGMLSIF
IAAFTARFLAFLQATKAQQYVDSYVQESDLSEVTLPPEIQYFTYARDKWLPSDPQIISEG
LYAIAVVLSFSRIAYILPANESFGPLQISLGRTVKDIFKFMVLFIMVFFAFMIGMFILYS
YYLGAKVNAAFTTVEESFKTLFWSIFGLSEVTSVVLKYDHKFIENIGYVLYGIYNVTMVV
VLLNMLIAMINSSYQEIEDDSDVEWKFARSKLWLSYFDDGKTLPPPFSLVPSPKSFVYFI
MRIVNFPKCRRRRLQKDIEMGMGNSKSRQIMKRLIKRYVLKAQVDKENDEVNEGELKEIK
QDISSLRYELLEDKSQATEELAILIHKLSEISSLRYELLE

Primary citation

Functional and structural basis of a hypermorphic TRPC3 variant. Bell, B., Jaramillo-Granada, A.M., Romero, L.O. et al. Sci Adv (2026) 12:eaec9284-eaec9284. DOI 10.1126/sciadv.aec9284 · PubMed

Other PDB entries of the same protein (UniProt Q13507 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9U5C 2.25 Å, Structure of hTRPC3 in complex with Nb1-94 at 2.25 angstrom
9KDB 2.67 Å, Structure of hTRPC3 in complex with Nb1-25 at 2.67 angstrom
7DXB 2.7 Å, Structure of TRPC3 at 2.7 angstrom in high calcium state
9KDD 2.7 Å, Structure of GSK1702934A-bound TRPC3 at 3.3 angstrom
9VFI 2.72 Å, Structure of hTRPC3 solubilized with 4F peptide at 2.72 angstrom
9OLK 2.8 Å, Structure of wild-type human TRPC3
9KDC 3.01 Å, Structure of hTRPC3 in complex with Nb3-37 at 3.01 angstrom
7DXC 3.06 Å, Structure of TRPC3 at 3.06 angstrom in low calcium state
9OLL 3.1 Å, Structure of human TRPC3 T573A mutant
7DXE 3.2 Å, Structure of TRPC3 gain of function mutation R803C at 3.2 angstrom in 1340nM free…
6CUD 3.3 Å, Structure of the human TRPC3 in a lipid-occupied, closed state
9OLX 3.3 Å, Structure of a constitutively open human TRPC3 mutant in the inhibited state

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