TTYH3_MOUSE
ID TTYH3_MOUSE Reviewed; 524 AA.
AC Q6P5F7; Q69ZD3; Q6PCX0; Q8C789;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protein tweety homolog 3;
DE Short=mTTY3;
GN Name=Ttyh3; Synonyms=Kiaa1691;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 139-524 (ISOFORM 1).
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=15010458; DOI=10.1074/jbc.m313813200;
RA Suzuki M., Mizuno A.;
RT "A novel human Cl(-) channel family related to Drosophila flightless
RT locus.";
RL J. Biol. Chem. 279:22461-22468(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496; SER-504 AND SER-522, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Probable large-conductance Ca(2+)-activated chloride channel.
CC May play a role in Ca(2+) signal transduction (By similarity).
CC {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=Q6P5F7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P5F7-2; Sequence=VSP_029771, VSP_029772;
CC -!- TISSUE SPECIFICITY: Expressed in excitable tissues. Expressed in the
CC brain, heart, skeletal muscle, colon, spleen, kidney and peripheral
CC blood leukocytes. Also expressed in fat, the pancreas, thymus, and
CC uterus. {ECO:0000269|PubMed:15010458}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tweety family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH59083.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK052340; BAC34944.1; -; mRNA.
DR EMBL; BC059083; AAH59083.1; ALT_SEQ; mRNA.
DR EMBL; BC062917; AAH62917.1; -; mRNA.
DR EMBL; AK173233; BAD32511.1; -; mRNA.
DR CCDS; CCDS19822.1; -. [Q6P5F7-1]
DR CCDS; CCDS80450.1; -. [Q6P5F7-2]
DR RefSeq; NP_001294969.1; NM_001308040.1. [Q6P5F7-2]
DR RefSeq; NP_780483.2; NM_175274.5. [Q6P5F7-1]
DR PDB; 7RTW; EM; 3.23 A; A/B=2-524.
DR PDBsum; 7RTW; -.
DR AlphaFoldDB; Q6P5F7; -.
DR SMR; Q6P5F7; -.
DR STRING; 10090.ENSMUSP00000037447; -.
DR GlyConnect; 2646; 2 N-Linked glycans (2 sites).
DR GlyGen; Q6P5F7; 3 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; Q6P5F7; -.
DR PhosphoSitePlus; Q6P5F7; -.
DR SwissPalm; Q6P5F7; -.
DR EPD; Q6P5F7; -.
DR MaxQB; Q6P5F7; -.
DR PaxDb; Q6P5F7; -.
DR PeptideAtlas; Q6P5F7; -.
DR PRIDE; Q6P5F7; -.
DR ProteomicsDB; 300058; -. [Q6P5F7-1]
DR ProteomicsDB; 300059; -. [Q6P5F7-2]
DR Antibodypedia; 43641; 26 antibodies from 11 providers.
DR DNASU; 78339; -.
DR Ensembl; ENSMUST00000042661; ENSMUSP00000037447; ENSMUSG00000036565. [Q6P5F7-1]
DR Ensembl; ENSMUST00000197452; ENSMUSP00000142655; ENSMUSG00000036565. [Q6P5F7-2]
DR GeneID; 78339; -.
DR KEGG; mmu:78339; -.
DR UCSC; uc009ahw.2; mouse. [Q6P5F7-1]
DR UCSC; uc012egc.1; mouse. [Q6P5F7-2]
DR CTD; 80727; -.
DR MGI; MGI:1925589; Ttyh3.
DR VEuPathDB; HostDB:ENSMUSG00000036565; -.
DR eggNOG; KOG4433; Eukaryota.
DR GeneTree; ENSGT00950000183060; -.
DR HOGENOM; CLU_023758_0_1_1; -.
DR InParanoid; Q6P5F7; -.
DR OMA; PHTWQAR; -.
DR OrthoDB; 725378at2759; -.
DR PhylomeDB; Q6P5F7; -.
DR TreeFam; TF319025; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 78339; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Ttyh3; mouse.
DR PRO; PR:Q6P5F7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6P5F7; protein.
DR Bgee; ENSMUSG00000036565; Expressed in ventricular zone and 214 other tissues.
DR ExpressionAtlas; Q6P5F7; baseline and differential.
DR Genevisible; Q6P5F7; MM.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005254; F:chloride channel activity; ISO:MGI.
DR GO; GO:0005229; F:intracellular calcium activated chloride channel activity; ISO:MGI.
DR GO; GO:0072320; F:volume-sensitive chloride channel activity; IBA:GO_Central.
DR GO; GO:0006821; P:chloride transport; ISO:MGI.
DR CDD; cd07912; Tweety_N; 1.
DR InterPro; IPR006990; Tweety.
DR PANTHER; PTHR12424; PTHR12424; 1.
DR Pfam; PF04906; Tweety; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell membrane; Chloride;
KW Chloride channel; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..524
FT /note="Protein tweety homolog 3"
FT /id="PRO_0000312252"
FT TOPO_DOM 1..42
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..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..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..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..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..524
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 413..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 475..479
FT /note="MSQNA -> ITPPA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029771"
FT VAR_SEQ 480..524
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029772"
FT CONFLICT 60
FT /note="F -> L (in Ref. 1; BAC34944)"
FT /evidence="ECO:0000305"
FT HELIX 10..16
FT /evidence="ECO:0007829|PDB:7RTW"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:7RTW"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:7RTW"
FT HELIX 49..62
FT /evidence="ECO:0007829|PDB:7RTW"
FT HELIX 88..146
FT /evidence="ECO:0007829|PDB:7RTW"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:7RTW"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:7RTW"
FT HELIX 162..182
FT /evidence="ECO:0007829|PDB:7RTW"
FT HELIX 195..232
FT /evidence="ECO:0007829|PDB:7RTW"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:7RTW"
FT HELIX 241..272
FT /evidence="ECO:0007829|PDB:7RTW"
FT HELIX 274..285
FT /evidence="ECO:0007829|PDB:7RTW"
FT HELIX 290..296
FT /evidence="ECO:0007829|PDB:7RTW"
FT HELIX 307..328
FT /evidence="ECO:0007829|PDB:7RTW"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:7RTW"
FT HELIX 340..363
FT /evidence="ECO:0007829|PDB:7RTW"
FT HELIX 366..408
FT /evidence="ECO:0007829|PDB:7RTW"
SQ SEQUENCE 524 AA; 57714 MW; 95B499209DBC6D51 CRC64;
MAGVSYAAPW WVSLLHRLPH FDLRWEATSS QFRPEDADYQ QALLLLGATA LACLALDLLF
LLFYSFWLCC RRRKTDEHLD ADCCCTAWCV IITTLVCSAG IAVGFYGNGE TSDGIHRATY
SLRHANRTVA GVQDRVWDTA AALNRTAEPN LQSLERQLAG RQEPLRAVQR LQTLLGTLLG
YTAAIPFWRN PGVSLEVLAE QVDLYDWYRW LGYLGLLLLD VIICLLVLVG LIRSSKGILV
GVCLLGVLAL VISWGALGLE LAVSVGSSDF CVDPDTFVTK MVEEHSVLSG DILQYYLACS
PRATNPFQQK LSGSHKALVE MQDVVAELLR NVPREHPATK DPLLRVQEVL NGTEVNLQHL
TALVDCRSLH LDYVQALTGF CYDGVEGLIY LALFSFVTAL MFSSIVCSIP HTWQQKRGPD
DDGEEETAPG PRQAHDSLYR VHMPSLYSCG SSYGSEASIP AAAHTVSNAP VTEYMSQNAN
FQNPRCENTP LIGRESPPPS YTSSMRAKYL ATSQPRPDSS GSGH
