TTYH1_MACFA
ID TTYH1_MACFA Reviewed; 450 AA.
AC Q9MZZ8; Q4R4N3;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Protein tweety homolog 1;
GN Name=TTYH1; ORFNames=QccE-16395, QccE-16959;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain cortex;
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA Suzuki Y., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable chloride channel. May be involved in cell adhesion
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9MZZ8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9MZZ8-2; Sequence=VSP_029761;
CC -!- SIMILARITY: Belongs to the tweety family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB046649; BAB03567.1; -; mRNA.
DR EMBL; AB169861; BAE01942.1; -; mRNA.
DR RefSeq; NP_001270987.1; NM_001284058.1.
DR AlphaFoldDB; Q9MZZ8; -.
DR SMR; Q9MZZ8; -.
DR STRING; 9541.XP_005590378.1; -.
DR GeneID; 101866113; -.
DR CTD; 57348; -.
DR eggNOG; KOG4433; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
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 GO; GO:0007155; P:cell adhesion; 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 Alternative splicing; Cell adhesion; Cell membrane; Chloride;
KW Chloride channel; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..450
FT /note="Protein tweety homolog 1"
FT /id="PRO_0000312240"
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..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..214
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..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..390
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 428..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D3A9"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 437
FT /note="P -> PQ (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_029761"
FT CONFLICT 138
FT /note="H -> L (in Ref. 1; BAE01942)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="L -> P (in Ref. 1; BAE01942)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="M -> T (in Ref. 1; BAE01942)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="Y -> C (in Ref. 1; BAE01942)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 450 AA; 49043 MW; FB17B0C6F9722B64 CRC64;
MGAPPGYRPS AWVHLLHQLP RADFQLRPVP SGFAPQEQEY QQALLLVAAL AGLGLGLSLI
FIAVYLIRFC CCRPPEPPGS KTPSPGGGCV TWSCIVALLA GCIGIGIGFY GNSETSDGVS
QLSSALLHAN HTLSAIDHLV LETVERLGEA VRTELTTLEE VLEPRTELVA AARGARRQAE
AVAQQLQGLA FWQGVPLSPL QVAEDVSFVE EYRWLAYVLL LLLELLVCLF TLLGLAKQSK
WLVIVMTVMS LLVLVLSWGS MGLEAATAVG LSDFYSNPDP YVLNLTQEET GLSSDILSYY
FLCNQAVSNP FQQRLTLSQR ALANIHSQLL GLEREAVPQF PSAQKPLLSL EETLNVTEGN
FHQLVALLHC RGLHKDYGAA LRGLCEDALE GLLFLLLFSL LSAGALATAL CSLPRAWALF
PPSDDYDDTD DDDPFNPQES KRFVQWQSSI
