TTYH3
entrez
80727
canonical
uniprot
Q9C0H2
canonical
ensembl
ENSG00000136295
resolver
ensp
ENSP00000258796
resolver
genesymbol
TTYH3
resolver
genesymbol_syn
KIAA1691
resolver
hgnc
HGNC:22222
resolver
uniprot
A4D201
resolver
uniprot
B7WP98
resolver
uniprot
Q6L749
resolver
uniprot
Q6ZVG3
resolver
uniprot
Q8TEG6
resolver
uniprot_entry
TTYH3_HUMAN
resolver
uniprot_sec
A4D201
resolver
uniprot_sec
B7WP98
resolver
uniprot_sec
Q6L749
resolver
uniprot_sec
Q6ZVG3
resolver
uniprot_sec
Q8TEG6
resolver
amino_acid_sequence
MAGVSYAAPWWVSLLHRLPHFDLSWEATSSQFRPEDTDYQQALLLLGAAALACLALDLLFLLFYSFWLCCRRRKSEEHLDADCCCTAWCVIIATLVCSAGIAVGFYGNGETSDGIHRATYSLRHANRTVAGVQDRVWDTAVGLNHTAEPSLQTLERQLAGRPEPLRAVQRLQGLLETLLGYTAAIPFWRNTAVSLEVLAEQVDLYDWYRWLGYLGLLLLDVIICLLVLVGLIRSSKGILVGVCLLGVLALVISWGALGLELAVSVGSSDFCVDPDAYVTKMVEEYSVLSGDILQYYLACSPRAANPFQQKLSGSHKALVEMQDVVAELLRTVPWEQPATKDPLLRVQEVLNGTEVNLQHLTALVDCRSLHLDYVQALTGFCYDGVEGLIYLALFSFVTALMFSSIVCSVPHTWQQKRGPDEDGEEEAAPGPRQAHDSLYRVHMPSLYSCGSSYGSETSIPAAAHTVSNAPVTEYMSQNANFQNPRCENTPLIGRESPPPSYTSSMRAKYLATSQPRPDSSGSH
uniprot
proteins
function
FUNCTION: Calcium-independent, swelling-dependent volume-regulated anion channel (VRAC-swell) which plays a pivotal role in the process of regulatory volume decrease (RVD) in the brain through the efflux of anions like chloride and organic osmolytes like glutamate (By similarity). Probable large-conductance Ca(2+)-activated chloride channel (PubMed:15010458). {ECO:0000250|UniProtKB:Q6P5F7, ECO:0000269|PubMed:15010458}.
uniprot
proteins
mass_dalton
57545
uniprot
proteins
mutagenesis
MUTAGEN 128; /note="T->A: Does not affect N-glycosylation state."; /evidence="ECO:0000269|PubMed:15010458"; MUTAGEN 146; /note="T->A: Does not affect N-glycosylation state."; /evidence="ECO:0000269|PubMed:15010458"; MUTAGEN 351; /note="N->Q: Loss of N-glycosylation."; /evidence="ECO:0000269|PubMed:18260827"; MUTAGEN 353; /note="T->A: Abolishes N-glycosylation."; /evidence="ECO:0000269|PubMed:15010458, ECO:0000269|PubMed:18260827"; MUTAGEN 367; /note="R->Q: Induces a stronger permeability to cations."; /evidence="ECO:0000269|PubMed:15010458"; MUTAGEN 370; /note="H->D: Shows a different ion selectivity."; /evidence="ECO:0000269|PubMed:15010458
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by NEDD4L. {ECO:0000269|PubMed:18577513}.; PTM: N-Glycosylated (PubMed:15010458, PubMed:18260827, PubMed:19159218). Contains high-mannose, hybrid and complex oligosaccharides (PubMed:18260827). {ECO:0000269|PubMed:15010458, ECO:0000269|PubMed:18260827, ECO:0000269|PubMed:19159218}.
uniprot
proteins
protein_family
Tweety family
uniprot
proteins
pubmed
11214970
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
12690205
uniprot
proteins
pubmed
12693554
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15010458
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18260827
uniprot
proteins
pubmed
18577513
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
34385445
uniprot
proteins
sequence_length
523
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15010458, ECO:0000269|PubMed:34385445}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 43..63; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 87..107; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 212..232; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 237..257; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 387..407; /note="Helical; Name=5"; /evidence="ECO:0000255
uniprot
proteins