NALF1_HUMAN
ID NALF1_HUMAN Reviewed; 458 AA.
AC B1AL88; B2RUV1; B7Z334;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=NALCN channel auxiliary factor 1;
DE AltName: Full=Transmembrane protein FAM155A;
GN Name=NALF1 {ECO:0000312|HGNC:HGNC:33877}; Synonyms=FAM155A, NLF-1;
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 [LARGE SCALE MRNA].
RC TISSUE=Corpus callosum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
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 [4]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
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).
RN [5] {ECO:0007744|PDB:6XIW}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) IN COMPLEX WITH NALCN,
RP DISULFIDE BONDS, AND SUBUNIT.
RX PubMed=32698188; DOI=10.1038/s41586-020-2570-8;
RA Kschonsak M., Chua H.C., Noland C.L., Weidling C., Clairfeuille T.,
RA Bahlke O.O., Ameen A.O., Li Z.R., Arthur C.P., Ciferri C., Pless S.A.,
RA Payandeh J.;
RT "Structure of the human sodium leak channel NALCN.";
RL Nature 587:313-318(2020).
RN [6] {ECO:0007744|PDB:7CM3}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) IN COMPLEX WITH NALCN,
RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-217.
RX PubMed=33203861; DOI=10.1038/s41467-020-19667-z;
RA Xie J., Ke M., Xu L., Lin S., Huang J., Zhang J., Yang F., Wu J., Yan Z.;
RT "Structure of the human sodium leak channel NALCN in complex with
RT FAM155A.";
RL Nat. Commun. 11:5831-5831(2020).
CC -!- FUNCTION: Auxillary component of the NALCN sodium channel complex, a
CC channel that regulates the resting membrane potential and controls
CC neuronal excitability. {ECO:0000269|PubMed:32494638}.
CC -!- SUBUNIT: Component of the NALCN channel complex. NALCN complex consists
CC of NALCN and auxiliary subunits, UNC79, UNC80 and NACL1. These
CC auxiliary subunits are essential for the NALCN channel function.
CC {ECO:0000269|PubMed:32494638, ECO:0000269|PubMed:32698188,
CC ECO:0000269|PubMed:33203861}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32494638};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the NALF family. {ECO:0000305}.
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DR EMBL; AK295445; BAH12070.1; -; mRNA.
DR EMBL; AL138914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445204; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC146878; AAI46879.1; -; mRNA.
DR EMBL; BC157830; AAI57831.1; -; mRNA.
DR EMBL; BC157855; AAI57856.1; -; mRNA.
DR EMBL; BC157862; AAI57863.1; -; mRNA.
DR CCDS; CCDS32006.1; -.
DR RefSeq; NP_001073865.1; NM_001080396.2.
DR PDB; 6XIW; EM; 2.80 A; B=1-458.
DR PDB; 7CM3; EM; 3.10 A; B=1-458.
DR PDB; 7SX3; EM; 3.10 A; B=1-458.
DR PDB; 7SX4; EM; 3.50 A; B=1-458.
DR PDBsum; 6XIW; -.
DR PDBsum; 7CM3; -.
DR PDBsum; 7SX3; -.
DR PDBsum; 7SX4; -.
DR AlphaFoldDB; B1AL88; -.
DR SMR; B1AL88; -.
DR STRING; 9606.ENSP00000365080; -.
DR GlyGen; B1AL88; 1 site.
DR iPTMnet; B1AL88; -.
DR PhosphoSitePlus; B1AL88; -.
DR BioMuta; FAM155A; -.
DR EPD; B1AL88; -.
DR MassIVE; B1AL88; -.
DR PaxDb; B1AL88; -.
DR PeptideAtlas; B1AL88; -.
DR PRIDE; B1AL88; -.
DR ProteomicsDB; 3138; -.
DR Antibodypedia; 48568; 101 antibodies from 14 providers.
DR DNASU; 728215; -.
DR Ensembl; ENST00000375915.4; ENSP00000365080.1; ENSG00000204442.4.
DR GeneID; 728215; -.
DR KEGG; hsa:728215; -.
DR MANE-Select; ENST00000375915.4; ENSP00000365080.1; NM_001080396.3; NP_001073865.1.
DR UCSC; uc001vql.4; human.
DR CTD; 728215; -.
DR DisGeNET; 728215; -.
DR GeneCards; FAM155A; -.
DR HGNC; HGNC:33877; NALF1.
DR HPA; ENSG00000204442; Tissue enhanced (brain, pituitary gland).
DR neXtProt; NX_B1AL88; -.
DR OpenTargets; ENSG00000204442; -.
DR VEuPathDB; HostDB:ENSG00000204442; -.
DR eggNOG; ENOG502QQKW; Eukaryota.
DR GeneTree; ENSGT00940000155696; -.
DR HOGENOM; CLU_058453_0_0_1; -.
DR InParanoid; B1AL88; -.
DR OMA; DMNCTLD; -.
DR OrthoDB; 1585247at2759; -.
DR PhylomeDB; B1AL88; -.
DR TreeFam; TF331752; -.
DR PathwayCommons; B1AL88; -.
DR BioGRID-ORCS; 728215; 11 hits in 1074 CRISPR screens.
DR ChiTaRS; FAM155A; human.
DR GenomeRNAi; 728215; -.
DR Pharos; B1AL88; Tdark.
DR PRO; PR:B1AL88; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; B1AL88; protein.
DR Bgee; ENSG00000204442; Expressed in endothelial cell and 138 other tissues.
DR Genevisible; B1AL88; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR InterPro; IPR029604; NALF1/2.
DR PANTHER; PTHR15819:SF9; PTHR15819:SF9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..458
FT /note="NALCN channel auxiliary factor 1"
FT /id="PRO_0000339373"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 70..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:33203861,
FT ECO:0007744|PDB:7CM3"
FT DISULFID 191..261
FT /evidence="ECO:0000250|UniProtKB:Q8CCS2"
FT DISULFID 226..313
FT /evidence="ECO:0000269|PubMed:32698188,
FT ECO:0000269|PubMed:33203861, ECO:0007744|PDB:6XIW,
FT ECO:0007744|PDB:7CM3"
FT DISULFID 246..261
FT /evidence="ECO:0000269|PubMed:33203861,
FT ECO:0007744|PDB:7CM3"
FT DISULFID 304..341
FT /evidence="ECO:0000269|PubMed:32698188,
FT ECO:0000269|PubMed:33203861, ECO:0007744|PDB:6XIW,
FT ECO:0007744|PDB:7CM3"
FT DISULFID 324..377
FT /evidence="ECO:0000269|PubMed:32698188,
FT ECO:0000269|PubMed:33203861, ECO:0007744|PDB:6XIW,
FT ECO:0007744|PDB:7CM3"
FT DISULFID 330..376
FT /evidence="ECO:0000269|PubMed:32698188,
FT ECO:0000269|PubMed:33203861, ECO:0007744|PDB:6XIW,
FT ECO:0007744|PDB:7CM3"
FT DISULFID 334..361
FT /evidence="ECO:0000269|PubMed:32698188,
FT ECO:0000269|PubMed:33203861, ECO:0007744|PDB:6XIW,
FT ECO:0007744|PDB:7CM3"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:7SX3"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:7CM3"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:6XIW"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:7CM3"
FT HELIX 231..236
FT /evidence="ECO:0007829|PDB:6XIW"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:7CM3"
FT HELIX 262..287
FT /evidence="ECO:0007829|PDB:6XIW"
FT TURN 290..294
FT /evidence="ECO:0007829|PDB:6XIW"
FT HELIX 301..316
FT /evidence="ECO:0007829|PDB:6XIW"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:6XIW"
FT HELIX 330..340
FT /evidence="ECO:0007829|PDB:6XIW"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:7CM3"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:6XIW"
SQ SEQUENCE 458 AA; 51493 MW; FA15D8280AE497D9 CRC64;
MTRGAWMCRQ YDDGLKIWLA APRENEKPFI DSERAQKWRL SLASLLFFTV LLSDHLWFCA
EAKLTRARDK EHQQQQRQQQ QQQQQQRQRQ QQQQQRRQQE PSWPALLASM GESSPAAQAH
RLLSASSSPT LPPSPGDGGG GGGKGNRGKD DRGKALFLGN SAKPVWRLET CYPQGASSGQ
CFTVENADAV CARNWSRGAA GGDGQEVRSK HPTPLWNLSD FYLSFCNSYT LWELFSGLSS
PNTLNCSLDV VLKEGGEMTT CRQCVEAYQD YDHHAQEKYE EFESVLHKYL QSEEYSVKSC
PEDCKIVYKA WLCSQYFEVT QFNCRKTIPC KQYCLEVQTR CPFILPDNDE VIYGGLSSFI
CTGLYETFLT NDEPECCDVR REEKSNNPSK GTVEKSGSCH RTSLTVSSAT RLCNSRLKLC
VLVLILLHTV LTASAAQNTA GLSFGGINTL EENSTNEE
