TTYH3_XENLA
ID TTYH3_XENLA Reviewed; 522 AA.
AC Q6GPA5;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Protein tweety homolog 3;
GN Name=ttyh3;
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=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable large-conductance Ca(2+)-activated chloride channel.
CC {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; BC073236; AAH73236.1; -; mRNA.
DR RefSeq; NP_001085713.1; NM_001092244.1.
DR AlphaFoldDB; Q6GPA5; -.
DR SMR; Q6GPA5; -.
DR GeneID; 444139; -.
DR KEGG; xla:444139; -.
DR CTD; 444139; -.
DR Xenbase; XB-GENE-941475; ttyh3.S.
DR OMA; RIDLYDW; -.
DR OrthoDB; 725378at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 444139; Expressed in spleen and 19 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 Calcium; Cell membrane; Chloride; Chloride channel; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..522
FT /note="Protein tweety homolog 3"
FT /id="PRO_0000312254"
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..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..211
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..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..386
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..522
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 483..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 522 AA; 58981 MW; F53029D8859159F1 CRC64;
MAAAISYTPP WWVNLLHRLP HLNLQWESLN GDFRPEDPDY QQSLMLLACV ALSCLALDLL
FLLFYSFWFC CRHRKTEENT NADCCCTVWC VIVATLVCSA GIAVGFYGNG ETSDGIHRVT
YSIRHVNRTM AGIHDRVSDT TTSLNQTVEP CLQNLEVMFT KQTDYLRIVQ RLQSLLYTLV
QQTSEIPFWK NHYLLDEFAA QVDLFDWYRW LGYLGLLLFH VFICLLVLFG LIRNSKGTLI
CVCFLGMMAL IISWASMGLE LAVAVGSSDF CVNPDTFVSK MVEEKSVLRA DILNYYLVCN
TGSPNPFQQM LSSGHKALVE MQDDVRDLLR SAVKEYPNSK DYLVCIQGVL NSTEINLQHL
TALVDCRGLH LDYVQSLTGF CYDGVEGLIY LVLFSFVTAL MFSSIVCSVP HTWQQRRANY
EEGDEETTTP GTRQTHDNLY RVHMPSLYSC GSSYGSETSI PAAAHTVSNA PVTEYMSQNA
NFQNPRCENT PLIGRESPPP SYTSSMRAKY LATNRPETDP VH