TTYH1_MOUSE
ID TTYH1_MOUSE Reviewed; 450 AA.
AC Q9D3A9; Q6L751; Q6P0A7; Q8BRL4; Q8C7M4; Q9D5D1; Q9EQN7; Q9ESC3;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Protein tweety homolog 1;
DE Short=mTTY1;
GN Name=Ttyh1;
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 [GENOMIC DNA / MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ;
RX PubMed=10950931; DOI=10.1006/geno.2000.6259;
RA Campbell H.D., Kamei M., Claudianos C., Woollatt E., Sutherland G.R.,
RA Suzuki Y., Hida M., Sugano S., Young I.G.;
RT "Human and mouse homologues of the Drosophila melanogaster tweety (tty)
RT gene: a novel gene family encoding predicted transmembrane proteins.";
RL Genomics 68:89-92(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC STRAIN=C57BL/6J;
RC TISSUE=Brain cortex, Head, Hippocampus, Medulla oblongata, and Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Olfactory epithelium;
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=17116230; DOI=10.1111/j.1471-4159.2006.04237.x;
RA Matthews C.A., Shaw J.E., Hooper J.A., Young I.G., Crouch M.F.,
RA Campbell H.D.;
RT "Expression and evolution of the mammalian brain gene Ttyh1.";
RL J. Neurochem. 100:693-707(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 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=3;
CC Name=1;
CC IsoId=Q9D3A9-1; Sequence=Displayed;
CC Name=4;
CC IsoId=Q9D3A9-4; Sequence=VSP_029765;
CC Name=5;
CC IsoId=Q9D3A9-5; Sequence=VSP_029762, VSP_029763;
CC -!- TISSUE SPECIFICITY: Restricted mainly to neural tissues. Strongly
CC expressed in brain and eye. {ECO:0000269|PubMed:17116230}.
CC -!- SIMILARITY: Belongs to the tweety family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG15842.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 4]:
CC Sequence=BAD20188.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF190991; AAG15842.1; ALT_SEQ; mRNA.
DR EMBL; AF190699; AAG02615.1; -; mRNA.
DR EMBL; DQ104403; AAZ06803.1; -; Genomic_DNA.
DR EMBL; AB162929; BAD20188.1; ALT_FRAME; mRNA.
DR EMBL; AK015486; BAB29865.1; -; mRNA.
DR EMBL; AK018148; BAB31094.1; -; mRNA.
DR EMBL; AK043998; BAC31730.1; -; mRNA.
DR EMBL; AK048413; BAC33329.1; -; mRNA.
DR EMBL; AK049903; BAC33980.1; -; mRNA.
DR EMBL; BC046310; AAH46310.1; -; mRNA.
DR EMBL; BC065694; AAH65694.1; -; mRNA.
DR CCDS; CCDS20730.1; -. [Q9D3A9-1]
DR CCDS; CCDS51970.1; -. [Q9D3A9-4]
DR RefSeq; NP_001001454.2; NM_001001454.4. [Q9D3A9-4]
DR RefSeq; NP_001103235.1; NM_001109765.2. [Q9D3A9-1]
DR RefSeq; NP_001292751.1; NM_001305822.1.
DR RefSeq; NP_067299.2; NM_021324.6. [Q9D3A9-1]
DR AlphaFoldDB; Q9D3A9; -.
DR SMR; Q9D3A9; -.
DR STRING; 10090.ENSMUSP00000078384; -.
DR ChEMBL; CHEMBL4739703; -.
DR GlyGen; Q9D3A9; 3 sites.
DR iPTMnet; Q9D3A9; -.
DR PhosphoSitePlus; Q9D3A9; -.
DR SwissPalm; Q9D3A9; -.
DR MaxQB; Q9D3A9; -.
DR PaxDb; Q9D3A9; -.
DR PeptideAtlas; Q9D3A9; -.
DR PRIDE; Q9D3A9; -.
DR ProteomicsDB; 300053; -. [Q9D3A9-1]
DR ProteomicsDB; 300054; -. [Q9D3A9-4]
DR ProteomicsDB; 300055; -. [Q9D3A9-5]
DR Antibodypedia; 32911; 169 antibodies from 25 providers.
DR DNASU; 57776; -.
DR Ensembl; ENSMUST00000079415; ENSMUSP00000078384; ENSMUSG00000030428. [Q9D3A9-4]
DR Ensembl; ENSMUST00000119661; ENSMUSP00000113937; ENSMUSG00000030428. [Q9D3A9-1]
DR Ensembl; ENSMUST00000129423; ENSMUSP00000120182; ENSMUSG00000030428. [Q9D3A9-1]
DR GeneID; 57776; -.
DR KEGG; mmu:57776; -.
DR UCSC; uc009eww.3; mouse. [Q9D3A9-1]
DR UCSC; uc012ewq.2; mouse. [Q9D3A9-4]
DR CTD; 57348; -.
DR MGI; MGI:1889007; Ttyh1.
DR VEuPathDB; HostDB:ENSMUSG00000030428; -.
DR eggNOG; KOG4433; Eukaryota.
DR GeneTree; ENSGT00950000183060; -.
DR HOGENOM; CLU_023758_1_0_1; -.
DR InParanoid; Q9D3A9; -.
DR OMA; SYSPSIW; -.
DR OrthoDB; 725378at2759; -.
DR PhylomeDB; Q9D3A9; -.
DR TreeFam; TF319025; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 57776; 2 hits in 55 CRISPR screens.
DR ChiTaRS; Ttyh1; mouse.
DR PRO; PR:Q9D3A9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9D3A9; protein.
DR Bgee; ENSMUSG00000030428; Expressed in visual cortex and 196 other tissues.
DR ExpressionAtlas; Q9D3A9; baseline and differential.
DR Genevisible; Q9D3A9; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0031527; C:filopodium membrane; IDA:MGI.
DR GO; GO:0032433; C:filopodium tip; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030868; C:smooth endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IBA:GO_Central.
DR GO; GO:0072320; F:volume-sensitive chloride channel activity; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:MGI.
DR GO; GO:0031589; P:cell-substrate adhesion; IDA:MGI.
DR GO; GO:0006821; P:chloride transport; ISO:MGI.
DR GO; GO:0046847; P:filopodium assembly; IDA:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; IMP: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 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_0000312241"
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:0007744|PubMed:21183079"
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 1..96
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029762"
FT VAR_SEQ 97..102
FT /note="ALLVGC -> MQRSNS (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029763"
FT VAR_SEQ 423..450
FT /note="SDDYDDTDDDDPFNPQESKRFVQWQSSI -> RNPNALCSGSLPSEPPLQSG
FT ACLSSMLLSWLLEKAPLT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15010458,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_029765"
FT CONFLICT 15
FT /note="L -> P (in Ref. 1; AAG02615/AAG15842)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="R -> L (in Ref. 3; BAC31730)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="S -> T (in Ref. 3; BAB29865)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="V -> M (in Ref. 3; BAB29865)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="E -> G (in Ref. 1; AAG02615/AAG15842 and 2;
FT BAD20188)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="D -> Y (in Ref. 3; BAB29865)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 450 AA; 49032 MW; 53A93E0EC7D16EB8 CRC64;
MGAPPGYRPS AWVHLLHQLP RADFQLRPVP SGFAPRDQEY QQALLLVAAL AGLGLGLSLI
FIAVYLIRFC CCRPPEPHGA KSPPPGGGCV TWSCIAALLV GCAGIGIGFY GNSETSDGVS
QLSSALLHAN HTLSTIDDVV LETVERLGEA VKTELTTLEE VLSVRMELVA ATRGARRQAE
AAAQYLQGLA FWQGVSLSPV QVAEDVTFVE EYRWLAYVLL LLLVLLVCLF TLLGLAKQSK
WLVVVMTAMS LLVLVLSWGS MGLEAATAVG LSDFCSNPDT YVLNLTQEET GLSSDILSYY
FLCNQAVSNP FQQRLTLSQR ALASIHSQLQ GLEREAIPQF SAAQKPLLSL EETLNVTERS
FHQLVALLHC RSLHKDYGSA LRGLCEDALE GLLFLMLFSL LSAGALATTL CSLPRAWALF
PPSDDYDDTD DDDPFNPQES KRFVQWQSSI
