NALF1_MOUSE
ID NALF1_MOUSE Reviewed; 467 AA.
AC Q8CCS2; Q149R3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=NALCN channel auxiliary factor 1;
DE AltName: Full=Transmembrane protein FAM155A;
GN Name=Nalf1 {ECO:0000312|MGI:MGI:2142765}; Synonyms=Fam155a;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3] {ECO:0007744|PDB:7CU3}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.65 ANGSTROMS) OF NALF1 IN COMPLEX WITH
RP RAT NALCN, AND SUBUNIT.
RX PubMed=33273469; DOI=10.1038/s41467-020-20002-9;
RA Kang Y., Wu J.X., Chen L.;
RT "Structure of voltage-modulated sodium-selective NALCN-FAM155A channel
RT complex.";
RL Nat. Commun. 11:6199-6199(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:0000250|UniProtKB:B1AL88}.
CC -!- SUBUNIT: Component of the NALCN channel complex (PubMed:33273469).
CC NALCN complex consists of NALCN and auxiliary subunits, UNC79, UNC80
CC and NACL1. These auxiliary subunits are essential for the NALCN channel
CC function (By similarity). {ECO:0000250|UniProtKB:B1AL88,
CC ECO:0000269|PubMed:33273469}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:B1AL88};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CCS2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CCS2-2; Sequence=VSP_034162, VSP_034163;
CC -!- SIMILARITY: Belongs to the NALF family. {ECO:0000305}.
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DR EMBL; AK032202; BAC27755.1; -; mRNA.
DR EMBL; BC117535; AAI17536.1; -; mRNA.
DR CCDS; CCDS40216.1; -. [Q8CCS2-1]
DR CCDS; CCDS85497.1; -. [Q8CCS2-2]
DR RefSeq; NP_001334056.1; NM_001347127.1. [Q8CCS2-2]
DR RefSeq; NP_775622.1; NM_173446.2. [Q8CCS2-1]
DR PDB; 7CU3; EM; 2.65 A; B=1-467.
DR PDBsum; 7CU3; -.
DR AlphaFoldDB; Q8CCS2; -.
DR SMR; Q8CCS2; -.
DR IntAct; Q8CCS2; 1.
DR STRING; 10090.ENSMUSP00000106596; -.
DR GlyGen; Q8CCS2; 4 sites.
DR PhosphoSitePlus; Q8CCS2; -.
DR PaxDb; Q8CCS2; -.
DR PRIDE; Q8CCS2; -.
DR ProteomicsDB; 275567; -. [Q8CCS2-1]
DR ProteomicsDB; 275568; -. [Q8CCS2-2]
DR Antibodypedia; 48568; 101 antibodies from 14 providers.
DR DNASU; 270028; -.
DR Ensembl; ENSMUST00000110969; ENSMUSP00000106596; ENSMUSG00000079157. [Q8CCS2-1]
DR Ensembl; ENSMUST00000208933; ENSMUSP00000146609; ENSMUSG00000079157. [Q8CCS2-2]
DR GeneID; 270028; -.
DR KEGG; mmu:270028; -.
DR UCSC; uc009kuj.1; mouse. [Q8CCS2-1]
DR UCSC; uc009kuk.1; mouse. [Q8CCS2-2]
DR CTD; 728215; -.
DR MGI; MGI:2142765; Nalf1.
DR VEuPathDB; HostDB:ENSMUSG00000079157; -.
DR eggNOG; ENOG502QQKW; Eukaryota.
DR GeneTree; ENSGT00940000155696; -.
DR HOGENOM; CLU_058453_0_0_1; -.
DR InParanoid; Q8CCS2; -.
DR OMA; DMNCTLD; -.
DR OrthoDB; 1585247at2759; -.
DR PhylomeDB; Q8CCS2; -.
DR TreeFam; TF331752; -.
DR BioGRID-ORCS; 270028; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Fam155a; mouse.
DR PRO; PR:Q8CCS2; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8CCS2; protein.
DR Bgee; ENSMUSG00000079157; Expressed in subiculum and 111 other tissues.
DR ExpressionAtlas; Q8CCS2; baseline and differential.
DR Genevisible; Q8CCS2; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS: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; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..467
FT /note="NALCN channel auxiliary factor 1"
FT /id="PRO_0000339374"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 121..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 200..270
FT /evidence="ECO:0000269|PubMed:33273469,
FT ECO:0007744|PDB:7CU3"
FT DISULFID 235..322
FT /evidence="ECO:0000269|PubMed:33273469,
FT ECO:0007744|PDB:7CU3"
FT DISULFID 255..270
FT /evidence="ECO:0000269|PubMed:33273469,
FT ECO:0007744|PDB:7CU3"
FT DISULFID 313..350
FT /evidence="ECO:0000269|PubMed:33273469,
FT ECO:0007744|PDB:7CU3"
FT DISULFID 333..386
FT /evidence="ECO:0000269|PubMed:33273469,
FT ECO:0007744|PDB:7CU3"
FT DISULFID 339..385
FT /evidence="ECO:0000269|PubMed:33273469,
FT ECO:0007744|PDB:7CU3"
FT DISULFID 343..370
FT /evidence="ECO:0000269|PubMed:33273469,
FT ECO:0007744|PDB:7CU3"
FT VAR_SEQ 373..378
FT /note="LYETFL -> EGEVYL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034162"
FT VAR_SEQ 379..467
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034163"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:7CU3"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 240..244
FT /evidence="ECO:0007829|PDB:7CU3"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 268..296
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 310..325
FT /evidence="ECO:0007829|PDB:7CU3"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 341..349
FT /evidence="ECO:0007829|PDB:7CU3"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:7CU3"
SQ SEQUENCE 467 AA; 52739 MW; 3DFC917DC35E2289 CRC64;
MTRGAWMCRQ YDDGLKIWLA APRENEKPFI DSERAQKWRL SLASLLFFTV LLSDHLWFCA
EAKLTRTRDK EHHQQQQQQQ QQQQQQQQQQ QQQQQRQQQR QRQQQRQRQQ EPSWPALLAS
MGESSPAAQA HRLLSASSSP TLPPSPGGGG GSKGNRGKNN RSRALFLGNS AKPVWRLETC
YPQGASSGQC FTVESADAVC ARNWSRGAAA GEEQSSRGSR PTPLWNLSDF YLSFCNSYTL
WELFSGLSSP STLNCSLDVV LTEGGEMTTC RQCIEAYQDY DHHAQEKYEE FESVLHKYLQ
SDEYSVKSCP EDCKIVYKAW LCSQYFEVTQ FNCRKTIPCK QYCLEVQTRC PFILPDNDEV
IYGGLSSFIC TGLYETFLTN DEPECCDIRS EEQTAPRPKG TVDRRDSCPR TSLTVSSATR
LCPGRLKLCV LVLILLHTVL TASAAQNSTG LGLGGLPTLE DNSTRED
