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TM114_MOUSE
ID   TM114_MOUSE             Reviewed;         222 AA.
AC   Q9D563;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Transmembrane protein 114 {ECO:0000250|UniProtKB:B3SHH9};
DE   AltName: Full=Claudin-26;
GN   Name=Tmem114 {ECO:0000250|UniProtKB:B3SHH9}; Synonyms=Cldn26;
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] {ECO:0000312|EMBL:BAB29961.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB29961.1};
RC   TISSUE=Testis {ECO:0000312|EMBL:BAB29961.1};
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] {ECO:0000312|EMBL:EDK97288.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000312|EMBL:AAH27071.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH27071.1};
RC   TISSUE=Brain {ECO:0000312|EMBL:AAI47191.1}, and
RC   Eye {ECO:0000312|EMBL:AAH27071.1};
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   [4] {ECO:0000305}
RP   DEVELOPMENTAL STAGE.
RX   PubMed=17492639; DOI=10.1002/humu.20545;
RA   Jamieson R.V., Farrar N., Stewart K., Perveen R., Mihelec M., Carette M.,
RA   Grigg J.R., McAvoy J.W., Lovicu F.J., Tam P.P.L., Scambler P., Lloyd I.C.,
RA   Donnai D., Black G.C.M.;
RT   "Characterization of a familial t(16;22) balanced translocation associated
RT   with congenital cataract leads to identification of a novel gene, TMEM114,
RT   expressed in the lens and disrupted by the translocation.";
RL   Hum. Mutat. 28:968-977(2007).
RN   [5]
RP   IDENTIFICATION BY 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).
RN   [6]
RP   SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-54 AND ASN-88, AND MUTAGENESIS
RP   OF ASN-54 AND ASN-88.
RX   PubMed=21689651; DOI=10.1016/j.febslet.2011.05.060;
RA   Maher G.J., Hilton E.N., Urquhart J.E., Davidson A.E., Spencer H.L.,
RA   Black G.C., Manson F.D.;
RT   "The cataract-associated protein TMEM114, and TMEM235, are glycosylated
RT   transmembrane proteins that are distinct from claudin family members.";
RL   FEBS Lett. 585:2187-2192(2011).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21689651};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:21689651}. Note=N-
CC       glycosylation at Asn-54 and Asn-88 is required for plasma membrane
CC       localization.
CC   -!- DEVELOPMENTAL STAGE: Expressed weakly in the eye from as early as 13.5
CC       dpc, with ocular expression up-regulated postnatally. By 10 weeks,
CC       expressed strongly in the lens epithelial cells and weakly in lens
CC       fibers. In adult, expressed in eye, brain and testis.
CC       {ECO:0000269|PubMed:17492639}.
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DR   EMBL; AK015757; BAB29961.1; -; mRNA.
DR   EMBL; CH466521; EDK97288.1; -; Genomic_DNA.
DR   EMBL; BC027071; AAH27071.1; -; mRNA.
DR   EMBL; BC147190; AAI47191.1; -; mRNA.
DR   EMBL; BC147191; AAI47192.1; -; mRNA.
DR   CCDS; CCDS27937.1; -.
DR   RefSeq; NP_083346.1; NM_029070.2.
DR   AlphaFoldDB; Q9D563; -.
DR   IntAct; Q9D563; 1.
DR   MINT; Q9D563; -.
DR   STRING; 10090.ENSMUSP00000023400; -.
DR   TCDB; 8.A.16.2.7; the ca(+) channel auxiliary subunit Gama1-Gama8 (ccaGama) family.
DR   GlyGen; Q9D563; 2 sites.
DR   iPTMnet; Q9D563; -.
DR   PhosphoSitePlus; Q9D563; -.
DR   PaxDb; Q9D563; -.
DR   PRIDE; Q9D563; -.
DR   ProteomicsDB; 259211; -.
DR   Antibodypedia; 51871; 12 antibodies from 10 providers.
DR   DNASU; 74720; -.
DR   Ensembl; ENSMUST00000023400; ENSMUSP00000023400; ENSMUSG00000022715.
DR   GeneID; 74720; -.
DR   KEGG; mmu:74720; -.
DR   UCSC; uc007yck.1; mouse.
DR   CTD; 283953; -.
DR   MGI; MGI:1921970; Tmem114.
DR   VEuPathDB; HostDB:ENSMUSG00000022715; -.
DR   eggNOG; ENOG502QR97; Eukaryota.
DR   GeneTree; ENSGT00390000011615; -.
DR   HOGENOM; CLU_102991_0_0_1; -.
DR   InParanoid; Q9D563; -.
DR   OMA; CYPLINP; -.
DR   OrthoDB; 1265742at2759; -.
DR   PhylomeDB; Q9D563; -.
DR   TreeFam; TF327980; -.
DR   BioGRID-ORCS; 74720; 4 hits in 71 CRISPR screens.
DR   ChiTaRS; Tmem114; mouse.
DR   PRO; PR:Q9D563; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q9D563; protein.
DR   Bgee; ENSMUSG00000022715; Expressed in primary oocyte and 27 other tissues.
DR   Genevisible; Q9D563; MM.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0016327; C:apicolateral plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   InterPro; IPR039951; TMEM114/TMEM235.
DR   PANTHER; PTHR20516; PTHR20516; 1.
DR   Pfam; PF13903; Claudin_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..222
FT                   /note="Transmembrane protein 114"
FT                   /id="PRO_0000352760"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        188..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          44..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:21689651"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:21689651"
FT   MUTAGEN         54
FT                   /note="N->K: Complete loss of glycosylation; when
FT                   associated with K-88."
FT                   /evidence="ECO:0000269|PubMed:21689651"
FT   MUTAGEN         88
FT                   /note="N->K: Complete loss of glycosylation; when
FT                   associated with K-54."
FT                   /evidence="ECO:0000269|PubMed:21689651"
SQ   SEQUENCE   222 AA;  24388 MW;  8AB6E66C94ECAD52 CRC64;
     MRVRLGALAG AAALSGALSF VLLAAAIGTD FWYIIDTERL ERSSQRMRDQ GPANRSQQEP
     LSSHSGLWRT CRVQSSCTPL MNPFWQENVT VSDSSRQLLT MHGTFVILLP LSLIVMVFGG
     MTGFLSFLLR AHLLLLLTGI LFLFGAMVTL TGISIYIAYS AVAFREAVCL LEERALLDQV
     DIRFGWSLAL GWISFVSELL TGVVFLAAAR ALSLSQRQDQ AI
 
 
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