TTY1A_XENLA
ID TTY1A_XENLA Reviewed; 449 AA.
AC Q6AX57;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Protein tweety homolog 1-A;
GN Name=ttyh1-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable chloride channel. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tweety family. {ECO:0000305}.
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DR EMBL; BC079745; AAH79745.1; -; mRNA.
DR RefSeq; NP_001087415.1; NM_001093946.1.
DR AlphaFoldDB; Q6AX57; -.
DR SMR; Q6AX57; -.
DR DNASU; 447239; -.
DR GeneID; 447239; -.
DR KEGG; xla:447239; -.
DR CTD; 447239; -.
DR Xenbase; XB-GENE-940455; ttyh1.L.
DR OMA; PREREYQ; -.
DR OrthoDB; 725378at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 447239; Expressed in brain and 11 other tissues.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR CDD; cd07912; Tweety_N; 1.
DR InterPro; IPR006990; Tweety.
DR PANTHER; PTHR12424; PTHR12424; 1.
DR Pfam; PF04906; Tweety; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Chloride; Chloride channel; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..449
FT /note="Protein tweety homolog 1-A"
FT /id="PRO_0000312243"
FT TOPO_DOM 1..43
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..212
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..388
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 449 AA; 50941 MW; 57EF725D9ADBECAD CRC64;
MSTSHGYRAS WWTNILHQVP HTNFQFEVVD NQFAPQEWPY QQALLFLASI AGLCLAISLI
LICVYLIRFC CCASQEDDDS KNHRVCCVTW SCVAAVIICC AGIGIGFYGN SETNDGVYQV
TYSLMNTNHT LTSINLLVSD TVELLSSVVK SDLTQLEEIF SKRTEFLVMI RNTRRQVESV
AQQLAEISFW KGTELNPNVL AEQVNFIEDY RWLAYILLLL LDLIICLFTL LGLAKRIKWL
VIVMTVVSFF VLLLSWGSMG LEMATAVGLS DFCSNPDGYV MNQTQMITNI NPDILQYYIS
CNQDVANPFR QRLTTSQRAL SNIHSQLHGL EREAVPQFPT AEKNLLAVQG MLNTTEGNFH
HLVALLNCRG LHKDYVDALK GLCYDGMEGI LFLLLFSFLS ALSFTAAVCS LPRAWKRFQN
RDLDYDDMDE DDPFNPQESK RFVQWQSSI