FXYD5_HUMAN
ID FXYD5_HUMAN Reviewed; 178 AA.
AC Q96DB9; B7WNZ8; Q6UW44; Q9HC34; Q9P039;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=FXYD domain-containing ion transport regulator 5;
DE AltName: Full=Dysadherin;
DE Flags: Precursor;
GN Name=FXYD5; Synonyms=DYSAD, IWU1; ORFNames=HSPC113, UNQ2561/PRO6241;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT HIS-176.
RC TISSUE=Bone marrow;
RX PubMed=11342114; DOI=10.1016/s0167-4781(00)00251-7;
RA Omasa T., Chen Y.G., Mantalaris A., Wu J.H.D.;
RT "A cDNA from human bone marrow encoding a protein exhibiting homology to
RT the ATP11/PLM/MAT8 family of transmembrane proteins.";
RL Biochim. Biophys. Acta 1517:307-310(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, GLYCOSYLATION, AND
RP VARIANT HIS-176.
RC TISSUE=Leukocyte;
RX PubMed=11756660; DOI=10.1073/pnas.012425299;
RA Ino Y., Gotoh M., Sakamoto M., Tsukagoshi K., Hirohashi S.;
RT "Dysadherin, a cancer-associated cell membrane glycoprotein, down-regulates
RT E-cadherin and promotes metastasis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:365-370(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-176.
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-176.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-176.
RC TISSUE=Pancreas;
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).
CC -!- FUNCTION: Involved in down-regulation of E-cadherin which results in
CC reduced cell adhesion. Promotes metastasis.
CC {ECO:0000269|PubMed:11756660}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96DB9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96DB9-2; Sequence=VSP_001584;
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:11756660}.
CC -!- SIMILARITY: Belongs to the FXYD family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FXYD5ID40652ch19q13.html";
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DR EMBL; AF177940; AAG09301.1; -; mRNA.
DR EMBL; AB072911; BAB83766.1; -; mRNA.
DR EMBL; AF161462; AAF29077.1; -; mRNA.
DR EMBL; AY358991; AAQ89350.1; -; mRNA.
DR EMBL; BT007343; AAP36007.1; -; mRNA.
DR EMBL; AC002390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020907; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009642; AAH09642.1; -; mRNA.
DR CCDS; CCDS12447.1; -. [Q96DB9-1]
DR RefSeq; NP_001158077.1; NM_001164605.1. [Q96DB9-1]
DR RefSeq; NP_001307842.1; NM_001320913.1.
DR RefSeq; NP_054883.3; NM_014164.5. [Q96DB9-1]
DR RefSeq; NP_659003.1; NM_144779.2. [Q96DB9-1]
DR AlphaFoldDB; Q96DB9; -.
DR SMR; Q96DB9; -.
DR BioGRID; 119800; 1.
DR IntAct; Q96DB9; 1.
DR STRING; 9606.ENSP00000344254; -.
DR TCDB; 1.A.27.3.1; the phospholemman (plm) family.
DR GlyGen; Q96DB9; 3 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q96DB9; -.
DR PhosphoSitePlus; Q96DB9; -.
DR SwissPalm; Q96DB9; -.
DR BioMuta; FXYD5; -.
DR DMDM; 311033386; -.
DR EPD; Q96DB9; -.
DR jPOST; Q96DB9; -.
DR MassIVE; Q96DB9; -.
DR MaxQB; Q96DB9; -.
DR PaxDb; Q96DB9; -.
DR PeptideAtlas; Q96DB9; -.
DR PRIDE; Q96DB9; -.
DR ProteomicsDB; 76270; -. [Q96DB9-1]
DR Antibodypedia; 2277; 206 antibodies from 33 providers.
DR DNASU; 53827; -.
DR Ensembl; ENST00000342879.7; ENSP00000344254.3; ENSG00000089327.15. [Q96DB9-1]
DR Ensembl; ENST00000392217.3; ENSP00000376051.3; ENSG00000089327.15. [Q96DB9-2]
DR Ensembl; ENST00000392219.7; ENSP00000376053.2; ENSG00000089327.15. [Q96DB9-1]
DR Ensembl; ENST00000423817.7; ENSP00000393848.2; ENSG00000089327.15. [Q96DB9-1]
DR Ensembl; ENST00000541435.6; ENSP00000443390.1; ENSG00000089327.15. [Q96DB9-1]
DR Ensembl; ENST00000590686.5; ENSP00000465667.1; ENSG00000089327.15. [Q96DB9-1]
DR GeneID; 53827; -.
DR KEGG; hsa:53827; -.
DR MANE-Select; ENST00000392219.7; ENSP00000376053.2; NM_014164.6; NP_054883.3.
DR UCSC; uc002nyg.3; human. [Q96DB9-1]
DR CTD; 53827; -.
DR DisGeNET; 53827; -.
DR GeneCards; FXYD5; -.
DR HGNC; HGNC:4029; FXYD5.
DR HPA; ENSG00000089327; Low tissue specificity.
DR MIM; 606669; gene.
DR neXtProt; NX_Q96DB9; -.
DR OpenTargets; ENSG00000089327; -.
DR PharmGKB; PA28445; -.
DR VEuPathDB; HostDB:ENSG00000089327; -.
DR eggNOG; ENOG502SA05; Eukaryota.
DR GeneTree; ENSGT00940000153062; -.
DR HOGENOM; CLU_109413_0_0_1; -.
DR InParanoid; Q96DB9; -.
DR OMA; ATPNQME; -.
DR PhylomeDB; Q96DB9; -.
DR TreeFam; TF338182; -.
DR PathwayCommons; Q96DB9; -.
DR SignaLink; Q96DB9; -.
DR BioGRID-ORCS; 53827; 10 hits in 1072 CRISPR screens.
DR ChiTaRS; FXYD5; human.
DR GeneWiki; FXYD5; -.
DR GenomeRNAi; 53827; -.
DR Pharos; Q96DB9; Tbio.
DR PRO; PR:Q96DB9; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96DB9; protein.
DR Bgee; ENSG00000089327; Expressed in granulocyte and 167 other tissues.
DR ExpressionAtlas; Q96DB9; baseline and differential.
DR Genevisible; Q96DB9; HS.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; IDA:UniProtKB.
DR GO; GO:0099106; F:ion channel regulator activity; IEA:InterPro.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0030033; P:microvillus assembly; NAS:UniProtKB.
DR GO; GO:0046588; P:negative regulation of calcium-dependent cell-cell adhesion; NAS:UniProtKB.
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 Alternative splicing; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Reference proteome; 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_0000010369"
FT TOPO_DOM 22..145
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 23..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..97
FT /note="MSPSGRLCLLTIVGLILPTRGQTLKDTTSSSSADSTIMDIQVPTRAPDAVYT
FT ELQPTSPTPTWPADETPQPQTQTQQLEGTDGPLVTDPETHKSTKA -> MQTLSNIPCF
FT CLHGSLLPSTDLATLS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11342114"
FT /id="VSP_001584"
FT VARIANT 35
FT /note="S -> A (in dbSNP:rs1688005)"
FT /id="VAR_012349"
FT VARIANT 176
FT /note="R -> H (in dbSNP:rs12110)"
FT /evidence="ECO:0000269|PubMed:11042152,
FT ECO:0000269|PubMed:11342114, ECO:0000269|PubMed:11756660,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.5"
FT /id="VAR_027959"
FT CONFLICT 140..141
FT /note="HT -> SH (in Ref. 3; AAF29077)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 178 AA; 19472 MW; 7429C04838B75AA1 CRC64;
MSPSGRLCLL TIVGLILPTR GQTLKDTTSS SSADSTIMDI QVPTRAPDAV YTELQPTSPT
PTWPADETPQ PQTQTQQLEG TDGPLVTDPE THKSTKAAHP TDDTTTLSER PSPSTDVQTD
PQTLKPSGFH EDDPFFYDEH TLRKRGLLVA AVLFITGIII LTSGKCRQLS RLCRNRCR
