TTYH2_XENLA
ID TTYH2_XENLA Reviewed; 534 AA.
AC Q7ZWN9;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Protein tweety homolog 2;
GN Name=ttyh2;
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 (FEB-2003) 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; BC046859; AAH46859.1; -; mRNA.
DR RefSeq; NP_001080592.1; NM_001087123.1.
DR AlphaFoldDB; Q7ZWN9; -.
DR SMR; Q7ZWN9; -.
DR DNASU; 380284; -.
DR GeneID; 380284; -.
DR KEGG; xla:380284; -.
DR CTD; 380284; -.
DR Xenbase; XB-GENE-866564; ttyh2.S.
DR OMA; HYSGEFP; -.
DR OrthoDB; 725378at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 380284; Expressed in neurula embryo and 14 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..534
FT /note="Protein tweety homolog 2"
FT /id="PRO_0000312249"
FT TOPO_DOM 1..44
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..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..213
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..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..534
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 534 AA; 59299 MW; 2757C0EA358BF0F4 CRC64;
MATARVEYIA PWWVYWLHNL PHVDFSLQRE SGDFNPKDPG YQQTLLFVAL FIALCAAVNL
LFVSGYLICL CCCKKEDETE TKMTSSCCVT WTAAVSGLLC CAAVGIGFYG NSETNDGVYQ
LTYSLDNANH TLAGIDSLVS NTNAKMKEDL DQHLFRLNEI FAARGDYIQS LRFMQQMAGN
IIQQLTSLPN WQGTSVNFSE IARNASIIEY YRWLSYLILF ITDVVICLVT CLGLAKKSKC
LLLTMLCCGL IALMLSWASL ALETSSAVGT SDFCVAPDKF ILNMTPDQIT ADVVHYYLYC
SQSQRNPFQQ ALTVFQRSLT TMQIQIQGLL QFAVPLFPTA QKDLLGIQLL LNTSESNLHQ
ITALLDCRGL HKDYLEALIG ICYDGVEGLL YLSLFSLLAA VAFTAMVCAM PRAWKHLAAR
DRDYNDVDDE DPFNPQARRI AVHNPNRGQL RSFCSYSSSL GSQASLQPPA QTVSNAQAAE
YMNQAALFGG NPRYENVPLI GRGSPPPTYS PTMRATYLSM NEESPNIYSN VFPA