NALF2_HUMAN
ID NALF2_HUMAN Reviewed; 472 AA.
AC O75949; B1ALV6; B9EGK1; D3DVU1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=NALCN channel auxiliary factor 2 {ECO:0000312|HGNC:HGNC:30701};
DE AltName: Full=Protein TED;
DE AltName: Full=Transmembrane protein 28;
DE AltName: Full=Transmembrane protein FAM155B;
GN Name=NALF2 {ECO:0000312|HGNC:HGNC:30701}; Synonyms=FAM155B, TED, TMEM28;
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], AND VARIANT PRO-172.
RA Zonana J., Gault J.;
RT "Isolation and characterization of a human X-linked gene mapping to the
RT Xq13.1 region.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP PROBABLE FUNCTION.
RX PubMed=32494638; DOI=10.1126/sciadv.aaz3154;
RA Chua H.C., Wulf M., Weidling C., Rasmussen L.P., Pless S.A.;
RT "The NALCN channel complex is voltage sensitive and directly modulated by
RT extracellular calcium.";
RL Sci. Adv. 6:eaaz3154-eaaz3154(2020).
CC -!- FUNCTION: Probable component of the NALCN channel complex, a channel
CC that regulates the resting membrane potential and controls neuronal
CC excitability. {ECO:0000305|PubMed:32494638}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the NALF family. {ECO:0000305}.
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DR EMBL; AF087142; AAC62086.1; -; mRNA.
DR EMBL; AL158069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471132; EAX05363.1; -; Genomic_DNA.
DR EMBL; CH471132; EAX05364.1; -; Genomic_DNA.
DR EMBL; BC136518; AAI36519.1; -; mRNA.
DR EMBL; BC136519; AAI36520.1; -; mRNA.
DR CCDS; CCDS35317.1; -.
DR RefSeq; NP_056501.2; NM_015686.2.
DR AlphaFoldDB; O75949; -.
DR SMR; O75949; -.
DR STRING; 9606.ENSP00000252338; -.
DR GlyGen; O75949; 2 sites.
DR iPTMnet; O75949; -.
DR PhosphoSitePlus; O75949; -.
DR BioMuta; FAM155B; -.
DR MassIVE; O75949; -.
DR PaxDb; O75949; -.
DR PeptideAtlas; O75949; -.
DR PRIDE; O75949; -.
DR Antibodypedia; 27337; 87 antibodies from 14 providers.
DR DNASU; 27112; -.
DR Ensembl; ENST00000252338.5; ENSP00000252338.5; ENSG00000130054.5.
DR GeneID; 27112; -.
DR KEGG; hsa:27112; -.
DR MANE-Select; ENST00000252338.5; ENSP00000252338.5; NM_015686.3; NP_056501.2.
DR UCSC; uc004dxk.4; human.
DR CTD; 27112; -.
DR DisGeNET; 27112; -.
DR GeneCards; FAM155B; -.
DR HGNC; HGNC:30701; NALF2.
DR HPA; ENSG00000130054; Tissue enriched (heart).
DR neXtProt; NX_O75949; -.
DR OpenTargets; ENSG00000130054; -.
DR VEuPathDB; HostDB:ENSG00000130054; -.
DR eggNOG; ENOG502QQKW; Eukaryota.
DR GeneTree; ENSGT00940000161362; -.
DR HOGENOM; CLU_058453_0_0_1; -.
DR InParanoid; O75949; -.
DR OMA; GTCGPRY; -.
DR OrthoDB; 1585247at2759; -.
DR PhylomeDB; O75949; -.
DR TreeFam; TF331752; -.
DR PathwayCommons; O75949; -.
DR BioGRID-ORCS; 27112; 6 hits in 687 CRISPR screens.
DR ChiTaRS; FAM155B; human.
DR GenomeRNAi; 27112; -.
DR Pharos; O75949; Tbio.
DR PRO; PR:O75949; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O75949; protein.
DR Bgee; ENSG00000130054; Expressed in cardiac muscle of right atrium and 111 other tissues.
DR Genevisible; O75949; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR InterPro; IPR029604; NALF1/2.
DR PANTHER; PTHR15819:SF8; PTHR15819:SF8; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..472
FT /note="NALCN channel auxiliary factor 2"
FT /id="PRO_0000072598"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 77..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..111
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 172
FT /note="L -> P (in dbSNP:rs1171942)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_043975"
FT CONFLICT 99
FT /note="L -> V (in Ref. 1; AAC62086)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="K -> KK (in Ref. 1; AAC62086)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 52477 MW; 709FAB4CEF99B54C CRC64;
MFRGAWMWPG KDAAALTICC CCCCWAPRPS DKPCADSERA QRWRLSLASL LFFTVLLADH
LWLCAGARPR ARELSSAMRP PWGAGRERQP VPPRAVLPLP PPPPGEPSAP PGTCGPRYSN
LTKAAPAAGS RPVCGGVPEP TGLDAACTKL QSLQRLFEPT TPAPPLRPPD SLSRAPAEFP
SAKKNLLKGH FRNFTLSFCD TYTVWDLLLG MDRPDSLDCS LDTLMGDLLA VVASPGSGAW
EACSNCIEAY QRLDRHAQEK YDEFDLVLHK YLQAEEYSIR SCTKGCKAVY KAWLCSEYFS
VTQQECQRWV PCKQYCLEVQ TRCPFILPDN EEMVYGGLPG FICTGLLDTS PKRLETKCCD
VQWVSCEAKK KKFKESEAPK THQQQFHHSY FHHYHQQYHH YHPHHDPPGR VSNKPALLPV
SGGSRLSPSR IRLCVLVLML LHTVVSFSSN QGGGGLGLET LPALEEGLTR EE