NKAIN_DROME
ID NKAIN_DROME Reviewed; 658 AA.
AC A6MHQ4; Q8MMC8; Q961Q4;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit beta-1-interacting protein;
DE Short=Na(+)/K(+)-transporting ATPase subunit beta-1-interacting protein;
DE Short=dNKAIN;
GN Name=NKAIN; ORFNames=CG34413;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH NRV1,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17606467; DOI=10.1093/hmg/ddm167;
RA Gorokhova S., Bibert S., Geering K., Heintz N.;
RT "A novel family of transmembrane proteins interacting with beta subunits of
RT the Na,K-ATPase.";
RL Hum. Mol. Genet. 16:2394-2410(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291; SER-308; SER-398 AND
RP SER-399, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Induces a small but significant sodium conductance when
CC expressed in Xenopus oocytes. {ECO:0000269|PubMed:17606467}.
CC -!- SUBUNIT: Interacts with nrv1. {ECO:0000269|PubMed:17606467}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=F, G, H;
CC IsoId=A6MHQ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A6MHQ4-2; Sequence=VSP_029303, VSP_029304;
CC -!- TISSUE SPECIFICITY: Expressed in the brain.
CC {ECO:0000269|PubMed:17606467}.
CC -!- DISRUPTION PHENOTYPE: Flies are not viable. However, the decreased
CC expression due to gene disruption leads to a temperature-sensitive
CC phenotype with paralysis at 38 degrees Celsius.
CC {ECO:0000269|PubMed:17606467}.
CC -!- SIMILARITY: Belongs to the NKAIN family. {ECO:0000305}.
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DR EMBL; EF058058; ABN51176.1; -; mRNA.
DR EMBL; AE013599; AAF47286.4; -; Genomic_DNA.
DR EMBL; AE013599; AAM70797.3; -; Genomic_DNA.
DR EMBL; AE013599; AAN16122.2; -; Genomic_DNA.
DR EMBL; AY051438; AAK92862.1; -; mRNA.
DR RefSeq; NP_001246506.1; NM_001259577.2. [A6MHQ4-1]
DR RefSeq; NP_611975.3; NM_138131.4. [A6MHQ4-1]
DR RefSeq; NP_726492.2; NM_166693.3. [A6MHQ4-1]
DR RefSeq; NP_726493.2; NM_166694.3. [A6MHQ4-1]
DR AlphaFoldDB; A6MHQ4; -.
DR BioGRID; 63547; 3.
DR STRING; 7227.FBpp0291061; -.
DR TCDB; 8.A.118.1.1; the na+k+-atpase beta-subunit interacting nkain (nkain) family.
DR GlyGen; A6MHQ4; 8 sites.
DR iPTMnet; A6MHQ4; -.
DR PaxDb; A6MHQ4; -.
DR PRIDE; A6MHQ4; -.
DR DNASU; 37979; -.
DR EnsemblMetazoa; FBtr0301847; FBpp0291061; FBgn0085442. [A6MHQ4-1]
DR EnsemblMetazoa; FBtr0301848; FBpp0291062; FBgn0085442. [A6MHQ4-1]
DR EnsemblMetazoa; FBtr0301849; FBpp0291063; FBgn0085442. [A6MHQ4-1]
DR EnsemblMetazoa; FBtr0305056; FBpp0293593; FBgn0085442. [A6MHQ4-1]
DR GeneID; 37979; -.
DR KEGG; dme:Dmel_CG34413; -.
DR CTD; 37979; -.
DR FlyBase; FBgn0085442; NKAIN.
DR VEuPathDB; VectorBase:FBgn0085442; -.
DR eggNOG; KOG4556; Eukaryota.
DR HOGENOM; CLU_027600_0_0_1; -.
DR InParanoid; A6MHQ4; -.
DR PhylomeDB; A6MHQ4; -.
DR BioGRID-ORCS; 37979; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 37979; -.
DR PRO; PR:A6MHQ4; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0085442; Expressed in capitellum (Drosophila) and 37 other tissues.
DR ExpressionAtlas; A6MHQ4; baseline and differential.
DR Genevisible; A6MHQ4; DM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002028; P:regulation of sodium ion transport; IMP:UniProtKB.
DR InterPro; IPR008516; Na/K-Atpase_Interacting.
DR PANTHER; PTHR13084; PTHR13084; 2.
DR Pfam; PF05640; NKAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..658
FT /note="Sodium/potassium-transporting ATPase subunit beta-1-
FT interacting protein"
FT /id="PRO_0000310473"
FT TRANSMEM 1..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 222..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 394..452
FT /note="GGNISSPVRPLDRLSRSLEDDEDNFSLQKFAPGEHGVTYVPFQSPTPNSLFL
FT GENNNSQ -> AALAPLLSLTHAFCLGRMAVTNSTRITRSLNTYKKFHIHRCCCFFVVP
FT NQPANLAKNRS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_029303"
FT VAR_SEQ 453..658
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_029304"
SQ SEQUENCE 658 AA; 73671 MW; F8E7AEFF6ABC2715 CRC64;
MGSCSCTRRH FLLSICFLQV ITIIERQVFD FLGYMWAPIL VNFFHILFII FGFYGAYHFR
VKYIITYLIW NFLWIGWNTF LICFYLNVGQ LNRDSDLLNL GTGSVSWFEA NGYGCKPTYN
MAADDTFRPQ RPERVEGCLL DYPLVEITHS GVQCALALLG ILGAILISCI FLDEDDRFDF
MNGDAKSPQH TVVHPMYVSY TSIPTTSASA TMQSNKHLQL QHQQPQQNSL KLYHHQQQQQ
PKLHHFNKNY QLSGSNNNTL NNNLHQRAPA LLPPNTTNNR SASFQTQSHP SNNHVTQRTG
GEGSNCSSLR RHRQHHSKAL VSPSPMSPQT TPSLSYASLQ NSSPYLAGNS LSNSNYSIFQ
SPDSLQGSSH FARIHHKPKP PKSDYPVSGE FNPGGNISSP VRPLDRLSRS LEDDEDNFSL
QKFAPGEHGV TYVPFQSPTP NSLFLGENNN SQPHLVFHTN SRSSPNNNAY PYDQSGLPSS
LRMGSNSNAR RPTHIPLPTV PMHNCQEVEN DEDADGESEQ DHDQMLTPPP PPLVRPHIHQ
RLGQAPYLDL SPEVAERYAI PSKLGPSLPI QVPLPVPHGS PMVRRSNRRP RPSNPVNFCD
QIRATPPGYV VRAQSDDRLM EQVEADAAPH VNRRSGRGGS GQKTRPRSFC NSIVGVQG
