FXYD5_MOUSE
ID FXYD5_MOUSE Reviewed; 178 AA.
AC P97808;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=FXYD domain-containing ion transport regulator 5;
DE AltName: Full=EF-8;
DE AltName: Full=Ion channel homolog RIC;
DE AltName: Full=Oncoprotein-induced protein 2;
DE Flags: Precursor;
GN Name=Fxyd5; Synonyms=Oit2;
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].
RC STRAIN=BALB/cJ;
RX PubMed=9032278; DOI=10.1128/mcb.17.3.1503;
RA Fu X., Kamps M.P.;
RT "E2a-Pbx1 induces aberrant expression of tissue-specific and
RT developmentally regulated genes when expressed in NIH 3T3 fibroblasts.";
RL Mol. Cell. Biol. 17:1503-1512(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: Involved in down-regulation of E-cadherin which results in
CC reduced cell adhesion. Promotes metastasis (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Spleen, lung, skeletal muscle, and testis.
CC -!- DEVELOPMENTAL STAGE: Exhibits biphasic expression during development.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FXYD family. {ECO:0000305}.
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DR EMBL; U72680; AAB51040.1; -; mRNA.
DR EMBL; AK003068; BAB22545.1; -; mRNA.
DR CCDS; CCDS21121.1; -.
DR RefSeq; NP_001104543.1; NM_001111073.2.
DR RefSeq; NP_001274142.1; NM_001287213.1.
DR RefSeq; NP_032787.1; NM_008761.4.
DR AlphaFoldDB; P97808; -.
DR SMR; P97808; -.
DR STRING; 10090.ENSMUSP00000125285; -.
DR iPTMnet; P97808; -.
DR PhosphoSitePlus; P97808; -.
DR SwissPalm; P97808; -.
DR EPD; P97808; -.
DR PaxDb; P97808; -.
DR PeptideAtlas; P97808; -.
DR PRIDE; P97808; -.
DR ProteomicsDB; 267547; -.
DR DNASU; 18301; -.
DR Ensembl; ENSMUST00000159924; ENSMUSP00000124219; ENSMUSG00000009687.
DR Ensembl; ENSMUST00000161684; ENSMUSP00000125285; ENSMUSG00000009687.
DR Ensembl; ENSMUST00000161805; ENSMUSP00000125398; ENSMUSG00000009687.
DR Ensembl; ENSMUST00000162087; ENSMUSP00000125065; ENSMUSG00000009687.
DR Ensembl; ENSMUST00000162116; ENSMUSP00000124203; ENSMUSG00000009687.
DR GeneID; 18301; -.
DR KEGG; mmu:18301; -.
DR UCSC; uc009ghp.3; mouse.
DR CTD; 53827; -.
DR MGI; MGI:1201785; Fxyd5.
DR VEuPathDB; HostDB:ENSMUSG00000009687; -.
DR eggNOG; ENOG502TDJN; Eukaryota.
DR GeneTree; ENSGT00990000203831; -.
DR InParanoid; P97808; -.
DR OMA; ATPNQME; -.
DR PhylomeDB; P97808; -.
DR TreeFam; TF338182; -.
DR BioGRID-ORCS; 18301; 6 hits in 72 CRISPR screens.
DR ChiTaRS; Fxyd5; mouse.
DR PRO; PR:P97808; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P97808; protein.
DR Bgee; ENSMUSG00000009687; Expressed in granulocyte and 204 other tissues.
DR ExpressionAtlas; P97808; baseline and differential.
DR Genevisible; P97808; MM.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0045296; F:cadherin binding; ISO:MGI.
DR GO; GO:0099106; F:ion channel regulator activity; IEA:InterPro.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0043269; P:regulation of ion transport; IEA:InterPro.
DR InterPro; IPR000272; Ion-transport_regulator_FXYD.
DR Pfam; PF02038; ATP1G1_PLM_MAT8; 1.
DR PROSITE; PS01310; FXYD; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..178
FT /note="FXYD domain-containing ion transport regulator 5"
FT /id="PRO_0000388996"
FT TOPO_DOM 22..145
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 21..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 178 AA; 19454 MW; 466FBF1E05D861C5 CRC64;
MSLSSRLCLL TIVALILPSR GQTPKKPTSI FTADQTSATT RDNVPDPDQT SPGVQTTPLI
WTREEATGSQ TAAQTETQQL TKMATSNPVS DPGPHTSSKK GTPAVSRIEP LSPSKNFMPP
SYIEHPLDSN ENNPFYYDDT TLRKRGLLVA AVLFITGIII LTSGKCRQLS QFCLNRHR
