TTYH2_MOUSE
ID TTYH2_MOUSE Reviewed; 532 AA.
AC Q3TH73; Q3U103; Q3U8L3; Q6P9J3; Q920A8;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Protein tweety homolog 2;
DE Short=mTTY2;
GN Name=Ttyh2;
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 [MRNA] (ISOFORM 1).
RX PubMed=11597145; DOI=10.1006/geno.2001.6629;
RA Rae F.K., Hooper J.D., Eyre H.J., Sutherland G.R., Nicol D.L.,
RA Clements J.A.;
RT "TTYH2, a human homologue of the Drosophila melanogaster gene tweety, is
RT located on 17q24 and upregulated in renal cell carcinoma.";
RL Genomics 77:200-207(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Heart, and Spleen;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-504, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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. May be involved in cell
CC proliferation and cell aggregation (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=Q3TH73-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TH73-2; Sequence=VSP_029768;
CC -!- SIMILARITY: Belongs to the tweety family. {ECO:0000305}.
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DR EMBL; AF329682; AAL16785.1; -; mRNA.
DR EMBL; AK152172; BAE31004.1; -; mRNA.
DR EMBL; AK155166; BAE33089.1; -; mRNA.
DR EMBL; AK156393; BAE33698.1; -; mRNA.
DR EMBL; AK168408; BAE40325.1; -; mRNA.
DR EMBL; AL645484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL663079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC060740; AAH60740.1; -; mRNA.
DR CCDS; CCDS25608.1; -. [Q3TH73-1]
DR RefSeq; NP_444503.2; NM_053273.2. [Q3TH73-1]
DR PDB; 7RTT; EM; 3.50 A; A/B=2-532.
DR PDB; 7RTU; EM; 3.89 A; A/B=2-532.
DR PDB; 7RTV; EM; 3.96 A; A=2-532.
DR PDBsum; 7RTT; -.
DR PDBsum; 7RTU; -.
DR PDBsum; 7RTV; -.
DR AlphaFoldDB; Q3TH73; -.
DR SMR; Q3TH73; -.
DR STRING; 10090.ENSMUSP00000037821; -.
DR GlyGen; Q3TH73; 1 site.
DR iPTMnet; Q3TH73; -.
DR PhosphoSitePlus; Q3TH73; -.
DR SwissPalm; Q3TH73; -.
DR jPOST; Q3TH73; -.
DR MaxQB; Q3TH73; -.
DR PaxDb; Q3TH73; -.
DR PeptideAtlas; Q3TH73; -.
DR PRIDE; Q3TH73; -.
DR ProteomicsDB; 300056; -. [Q3TH73-1]
DR ProteomicsDB; 300057; -. [Q3TH73-2]
DR Antibodypedia; 61709; 26 antibodies from 16 providers.
DR DNASU; 117160; -.
DR Ensembl; ENSMUST00000045779; ENSMUSP00000037821; ENSMUSG00000034714. [Q3TH73-1]
DR GeneID; 117160; -.
DR KEGG; mmu:117160; -.
DR UCSC; uc007mfm.1; mouse. [Q3TH73-1]
DR UCSC; uc011yhf.1; mouse. [Q3TH73-2]
DR CTD; 94015; -.
DR MGI; MGI:2157091; Ttyh2.
DR VEuPathDB; HostDB:ENSMUSG00000034714; -.
DR eggNOG; KOG4433; Eukaryota.
DR GeneTree; ENSGT00950000183060; -.
DR HOGENOM; CLU_023758_0_1_1; -.
DR InParanoid; Q3TH73; -.
DR OMA; HYSGEFP; -.
DR OrthoDB; 725378at2759; -.
DR PhylomeDB; Q3TH73; -.
DR TreeFam; TF319025; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 117160; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Ttyh2; mouse.
DR PRO; PR:Q3TH73; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q3TH73; protein.
DR Bgee; ENSMUSG00000034714; Expressed in lumbar subsegment of spinal cord and 231 other tissues.
DR Genevisible; Q3TH73; MM.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; ISS:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IBA:GO_Central.
DR GO; GO:0072320; F:volume-sensitive chloride channel activity; IBA:GO_Central.
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..532
FT /note="Protein tweety homolog 2"
FT /id="PRO_0000312247"
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..385
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..532
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 199
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSA4"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 421..482
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029768"
FT CONFLICT 29..31
FT /note="RVD -> DEY (in Ref. 1; AAL16785)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="G -> V (in Ref. 2; BAE31004)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="H -> R (in Ref. 2; BAE33698)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="A -> E (in Ref. 4; AAH60740)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="S -> F (in Ref. 4; AAH60740)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="D -> R (in Ref. 1; AAL16785)"
FT /evidence="ECO:0000305"
FT CONFLICT 358..363
FT /note="LHQLTA -> CTVDR (in Ref. 1; AAL16785)"
FT /evidence="ECO:0000305"
FT HELIX 12..18
FT /evidence="ECO:0007829|PDB:7RTT"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:7RTT"
FT HELIX 39..71
FT /evidence="ECO:0007829|PDB:7RTT"
FT HELIX 90..157
FT /evidence="ECO:0007829|PDB:7RTT"
FT HELIX 166..187
FT /evidence="ECO:0007829|PDB:7RTT"
FT HELIX 192..234
FT /evidence="ECO:0007829|PDB:7RTT"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:7RTT"
FT HELIX 240..269
FT /evidence="ECO:0007829|PDB:7RTT"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:7RTT"
FT HELIX 277..284
FT /evidence="ECO:0007829|PDB:7RTT"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:7RTT"
FT HELIX 291..298
FT /evidence="ECO:0007829|PDB:7RTT"
FT HELIX 309..329
FT /evidence="ECO:0007829|PDB:7RTT"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:7RTT"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:7RTT"
FT HELIX 341..364
FT /evidence="ECO:0007829|PDB:7RTT"
FT HELIX 367..382
FT /evidence="ECO:0007829|PDB:7RTT"
FT HELIX 385..409
FT /evidence="ECO:0007829|PDB:7RTT"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:7RTT"
SQ SEQUENCE 532 AA; 59008 MW; FC5B882F5FB7573A CRC64;
MPAARVEYIA PWWVVWLHSV PHLGLRLQRV DSTFSPGDET YQESLLFLGV LAAIGLGLNL
IFLTVYLVCT CCCRRDHTVQ TKQQESCCVT WTAVVAGLLC CAAVGVGFYG NSETNDGMHQ
LIYSLDNANH TFSGMDELVS ANTQRMKVDL EQHLARLSEI IAARGDYIQT LKFMQQMAGN
VVSQLSGLPV WREVTTQLTK LSHQTAYVEY YRWLSYLLLF ILDLVICLVT CLGLARRSKC
LLASMLCCGI LTLILSWASL AADAAAAVGT SDFCMAPDIY ILNNTGSQIN SEVTRYYLHC
SQSLISPFQQ SLTTFQRSLT TMQIQVGGLL QFAVPLFPTA EKDLLGIQLL LNNSEISLHQ
LTAMLDCRGL HKDYLDALTG ICYDGIEGLL FLGLFSLLAA LAFSTLTCAG PRAWKYFINR
DRDYDDIDDD DPFNPQARRI AAHNPTRGQL HSFCSYSSGL GSQCSLQPPS QTISNAPVSE
YMNQAILFGG NPRYENVPLI GRGSPPPTYS PSMRPTYMSV ADEHLRHYEF PS
