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TTYH1_RAT
ID   TTYH1_RAT               Reviewed;         450 AA.
AC   P0C5X8;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Protein tweety homolog 1;
GN   Name=Ttyh1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   SUBCELLULAR LOCATION.
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Probable chloride channel. May be involved in cell adhesion.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17116230};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:17116230}.
CC   -!- SIMILARITY: Belongs to the tweety family. {ECO:0000305}.
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DR   EMBL; AABR03001833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001099695.1; NM_001106225.1.
DR   RefSeq; XP_006228278.1; XM_006228216.3.
DR   AlphaFoldDB; P0C5X8; -.
DR   SMR; P0C5X8; -.
DR   STRING; 10116.ENSRNOP00000062088; -.
DR   GlyGen; P0C5X8; 3 sites.
DR   iPTMnet; P0C5X8; -.
DR   PhosphoSitePlus; P0C5X8; -.
DR   SwissPalm; P0C5X8; -.
DR   PaxDb; P0C5X8; -.
DR   PRIDE; P0C5X8; -.
DR   Ensembl; ENSRNOT00000068459; ENSRNOP00000062088; ENSRNOG00000032699.
DR   GeneID; 292597; -.
DR   KEGG; rno:292597; -.
DR   UCSC; RGD:1310103; rat.
DR   CTD; 57348; -.
DR   RGD; 1310103; Ttyh1.
DR   eggNOG; KOG4433; Eukaryota.
DR   GeneTree; ENSGT00950000183060; -.
DR   HOGENOM; CLU_023758_1_0_1; -.
DR   InParanoid; P0C5X8; -.
DR   OMA; SYSPSIW; -.
DR   OrthoDB; 725378at2759; -.
DR   PhylomeDB; P0C5X8; -.
DR   Reactome; R-RNO-2672351; Stimuli-sensing channels.
DR   PRO; PR:P0C5X8; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000032699; Expressed in Ammon's horn and 20 other tissues.
DR   ExpressionAtlas; P0C5X8; baseline and differential.
DR   Genevisible; P0C5X8; RN.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0031527; C:filopodium membrane; ISO:RGD.
DR   GO; GO:0032433; C:filopodium tip; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0030868; C:smooth endoplasmic reticulum membrane; ISO:RGD.
DR   GO; GO:0045202; C:synapse; ISO:RGD.
DR   GO; GO:0005509; F:calcium ion binding; ISO:RGD.
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:RGD.
DR   GO; GO:0098609; P:cell-cell adhesion; ISO:RGD.
DR   GO; GO:0031589; P:cell-substrate adhesion; ISO:RGD.
DR   GO; GO:0006821; P:chloride transport; ISO:RGD.
DR   GO; GO:0046847; P:filopodium assembly; ISO:RGD.
DR   GO; GO:0000278; P:mitotic cell cycle; ISO:RGD.
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   Cell adhesion; Cell membrane; Chloride; Chloride channel; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..450
FT                   /note="Protein tweety homolog 1"
FT                   /id="PRO_0000312242"
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"
SQ   SEQUENCE   450 AA;  49032 MW;  25BC429B4D7BFCF3 CRC64;
     MGAPPGYRPS AWVHLLHQLP RADFQLRPVP SGFAPRDQEY QQALLLVAAL AGLGLGLSLI
     FIAVYLIRFC CCRPPEPPGA KSPPPGGGCV TWSCIAALLV GCAGIGIGFY GNSETSDGVS
     QLSSALQHAN HTLSTIDDLV LETVERLGEA VRTELTTLEE VLSERVELVA ATRGARRQAE
     AAAQHLQGLA FWQGVSLSPV QVAEDVTFVE EYRWLAYVLL LLLVLLVCLF TLLGLAKQSK
     WLVVVMTAMS LLVLVLSWGS MGLEAATAVG LSDFCSNPDT YVLNLTQEET GISSDILNYY
     FLCNQAVSNP FQQRLTLSQR ALASIHSQLQ GLEREASPQF PAAQKPLLSL EETLNVTERS
     FHQLVALLHC RSLHKDYGSA LRGLCEDALE GLLFLMLFSL LSAGALATTL CSLPRAWALF
     PPSDDYDDTD DDDPFNPQES KRFVQWQSSI
 
 
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