ASIC2_RAT
ID ASIC2_RAT Reviewed; 512 AA.
AC Q62962; O55163;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Acid-sensing ion channel 2;
DE Short=ASIC2;
DE AltName: Full=Amiloride-sensitive brain sodium channel;
DE AltName: Full=Amiloride-sensitive brain sodium channel 2;
DE AltName: Full=Amiloride-sensitive cation channel 1, neuronal;
DE AltName: Full=Amiloride-sensitive cation channel neuronal 1;
DE AltName: Full=Brain sodium channel 1;
DE Short=BNC1;
DE Short=BNaC1;
DE AltName: Full=Mammalian degenerin homolog {ECO:0000303|PubMed:8631835};
DE Short=MDEG {ECO:0000303|PubMed:8631835};
GN Name=Asic2; Synonyms=Accn1, Bnac1, Mdeg;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, MUTAGENESIS OF
RP GLY-430 AND SER-443, AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=8631835; DOI=10.1074/jbc.271.18.10433;
RA Waldmann R., Champigny G., Voilley N., Lauritzen I., Lazdunski M.;
RT "The mammalian degenerin MDEG, an amiloride-sensitive cation channel
RT activated by mutations causing neurodegeneration in Caenorhabditis
RT elegans.";
RL J. Biol. Chem. 271:10433-10436(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY,
RP OLIGOMERIZATION, AND INTERACTION WITH ASIC3.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=9368048; DOI=10.1074/jbc.272.47.29778;
RA Lingueglia E., de Weille J.R., Bassilana F., Heurteaux C., Sakai H.,
RA Waldmann R., Lazdunski M.;
RT "A modulatory subunit of acid sensing ion channels in brain and dorsal root
RT ganglion cells.";
RL J. Biol. Chem. 272:29778-29783(1997).
RN [3]
RP TISSUE SPECIFICITY, INTERACTION WITH ASIC2, AND FUNCTION.
RX PubMed=9360943; DOI=10.1074/jbc.272.46.28819;
RA Bassilana F., Champigny G., Waldmann R., de Weille J.R., Heurteaux C.,
RA Lazdunski M.;
RT "The acid-sensitive ionic channel subunit ASIC and the mammalian degenerin
RT MDEG form a heteromultimeric H+-gated Na+ channel with novel properties.";
RL J. Biol. Chem. 272:28819-28822(1997).
RN [4]
RP MUTAGENESIS OF HIS-72; HIS-109; HIS-127; HIS-145; HIS-158; HIS-162;
RP HIS-180; HIS-249; HIS-326; HIS-339 AND GLY-430, AND REGULATION BY PROTONS
RP AND ZINC.
RX PubMed=11457851; DOI=10.1074/jbc.m105208200;
RA Baron A., Schaefer L., Lingueglia E., Champigny G., Lazdunski M.;
RT "Zn2+ and H+ are coactivators of acid-sensing ion channels.";
RL J. Biol. Chem. 276:35361-35367(2001).
RN [5]
RP INDUCTION, AND INHIBITION BY DRUGS.
RX PubMed=11588175; DOI=10.1523/jneurosci.21-20-08026.2001;
RA Voilley N., de Weille J.R., Mamet J., Lazdunski M.;
RT "Nonsteroid anti-inflammatory drugs inhibit both the activity and the
RT inflammation-induced expression of acid-sensing ion channels in
RT nociceptors.";
RL J. Neurosci. 21:8026-8033(2001).
RN [6]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11842212; DOI=10.1073/pnas.042688199;
RA Alvarez de la Rosa D., Zhang P., Shao D., White F., Canessa C.M.;
RT "Functional implications of the localization and activity of acid-sensitive
RT channels in rat peripheral nervous system.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2326-2331(2002).
RN [7]
RP INTERACTION WITH ASIC3.
RX PubMed=14976185; DOI=10.1074/jbc.m313078200;
RA Deval E., Salinas M., Baron A., Lingueglia E., Lazdunski M.;
RT "ASIC2b-dependent regulation of ASIC3, an essential acid-sensing ion
RT channel subunit in sensory neurons via the partner protein PICK-1.";
RL J. Biol. Chem. 279:19531-19539(2004).
RN [8]
RP GLYCOSYLATION AT ASN-365 AND ASN-392, MUTAGENESIS OF LYS-4; ASN-22; PRO-37;
RP ARG-63; TYR-67; HIS-72; ALA-81; ASN-365; ASN-392; TYR-414;
RP 423-TYR--VAL-425; 453-TYR--TYR-455; ASN-478 AND ASN-487, AND TOPOLOGY.
RX PubMed=15504740; DOI=10.1074/jbc.m411849200;
RA Saugstad J.A., Roberts J.A., Dong J., Zeitouni S., Evans R.J.;
RT "Analysis of the membrane topology of the acid-sensing ion channel 2a.";
RL J. Biol. Chem. 279:55514-55519(2004).
RN [9]
RP FUNCTION, INTERACTION WITH STOM, AND SUBCELLULAR LOCATION.
RX PubMed=22850675; DOI=10.1038/emboj.2012.203;
RA Brand J., Smith E.S., Schwefel D., Lapatsina L., Poole K., Omerbasic D.,
RA Kozlenkov A., Behlke J., Lewin G.R., Daumke O.;
RT "A stomatin dimer modulates the activity of acid-sensing ion channels.";
RL EMBO J. 31:3635-3646(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-11, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [11]
RP INTERACTION WITH SNAKE VENOM MAMBALGIN-1 AND MAMBALGIN-2, AND SUBUNIT.
RC TISSUE=Venom, and Venom gland;
RX PubMed=23034652; DOI=10.1038/nature11494;
RA Diochot S., Baron A., Salinas M., Douguet D., Scarzello S.,
RA Dabert-Gay A.-S., Debayle D., Friend V., Alloui A., Lazdunski M.,
RA Lingueglia E.;
RT "Black mamba venom peptides target acid-sensing ion channels to abolish
RT pain.";
RL Nature 490:552-555(2012).
RN [12]
RP INTERACTION WITH MAMBALGIN-1; MAMBALGIN-2 AND MAMBALGIN-3, SUBUNIT, AND
RP REVIEW.
RX PubMed=23624383; DOI=10.1016/j.toxicon.2013.04.008;
RA Baron A., Diochot S., Salinas M., Deval E., Noel J., Lingueglia E.;
RT "Venom toxins in the exploration of molecular, physiological and
RT pathophysiological functions of acid-sensing ion channels.";
RL Toxicon 75:187-204(2013).
CC -!- FUNCTION: Cation channel with high affinity for sodium, which is gated
CC by extracellular protons and inhibited by the diuretic amiloride. Also
CC permeable for Li(+) and K(+). Activation by an extracellular pH drop is
CC followed by a rapid pH-independent inactivation. Heteromeric channel
CC assembly seems to modulate channel properties.
CC {ECO:0000269|PubMed:22850675, ECO:0000269|PubMed:8631835,
CC ECO:0000269|PubMed:9360943}.
CC -!- SUBUNIT: Homotrimer or heterotrimer with other ASIC proteins (By
CC similarity). Interacts with PRKCABP (By similarity). Interacts with
CC STOM; this regulates channel activity. Interacts with ASIC1. Isoform 2
CC interacts with ASIC3. Heterotrimer of Asic1a-Asic2a interacts with the
CC snake venom mambalgin-1, mambalgin-2 and mambalgin-3 (PubMed:23034652,
CC PubMed:23624383). Heterotrimer of Asic1a-Asic2b interacts with the
CC snake venom mambalgin-1 and mambalgin-2 (PubMed:23034652).
CC {ECO:0000250, ECO:0000269|PubMed:14976185, ECO:0000269|PubMed:22850675,
CC ECO:0000269|PubMed:9360943, ECO:0000269|PubMed:9368048}.
CC -!- INTERACTION:
CC Q62962-1; D4A100: Stoml3; NbExp=2; IntAct=EBI-15615798, EBI-15615743;
CC Q62962-2; D4A100: Stoml3; NbExp=2; IntAct=EBI-15615759, EBI-15615743;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11842212,
CC ECO:0000269|PubMed:22850675}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11842212, ECO:0000269|PubMed:22850675}.
CC Note=Localized at the plasma membrane of neurons, in the soma and
CC punctated peripheral processes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Mdeg1 {ECO:0000303|PubMed:9368048}, Asic2a;
CC IsoId=Q62962-1; Sequence=Displayed;
CC Name=2; Synonyms=Mdeg2 {ECO:0000303|PubMed:9368048}, Asic2b;
CC IsoId=Q62962-2; Sequence=VSP_015594, VSP_015595;
CC -!- TISSUE SPECIFICITY: Expressed in sciatic nerve and dorsal root ganglion
CC (DRG) (at protein level). Both isoforms display the same expression
CC pattern except in DRG where isoform 2 is more abundantly expressed.
CC Widely distributed throughout the brain. Highly expressed in the main
CC olfactory bulb, neo- and allo-cortical regions, hippocampal formation,
CC habenula, basolateral amygdaloid nuclei, and cerebellum. In the
CC olfactory system, expressed in the glomerular cell layer, the internal
CC granular layer, and the mitral and internal plexiform cell layers.
CC Within the glomerular layer, restricted to the periglomerular cells. In
CC the neocortex, strongly expressed in the large pyramidal neurons in all
CC cortical layers as well as in the oligo-, astro-, or micro-glia cells.
CC In the hippocampal formation, expressed in dentate granule cells and
CC hilar neurons, as well as in pyramidal cells of CA1-CA3 subfields.
CC Expressed in stratum oriens and radiatum of all subfields. Within the
CC thalamus, expressed moderately in the medial and lateral habenula. In
CC the cerebellar cortex expressed in Purkinje cells and granule cells.
CC Expressed at low levels in choroid plexus.
CC {ECO:0000269|PubMed:11842212, ECO:0000269|PubMed:8631835,
CC ECO:0000269|PubMed:9360943, ECO:0000269|PubMed:9368048}.
CC -!- DEVELOPMENTAL STAGE: Appears just before birth, reaches maximum levels
CC after birth, then declines slightly until adulthood.
CC -!- INDUCTION: Up-regulation upon tissues inflammation is abolished by
CC anti-inflammatory drugs. {ECO:0000269|PubMed:11588175}.
CC -!- MISCELLANEOUS: Regulated by Zn(2+). Inhibited by anti-inflammatory
CC drugs like salicylic acid.
CC -!- MISCELLANEOUS: [Isoform 2]: Seems to be inactive as monomer or in a
CC monomeric assembly and is not activated by mutagenesis of Gly-430.
CC Mutagenesis of Ser-60 into Gly reduces activation by PKC through
CC PRKCABP/PICK-1 of a ASIC3/ACCN3-ASIC2/ASIC2b channel. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC 1.A.6) family. ASIC2 subfamily. {ECO:0000305}.
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DR EMBL; U53211; AAC52588.1; -; mRNA.
DR EMBL; Y14635; CAA74979.1; -; mRNA.
DR RefSeq; NP_001029186.1; NM_001034014.1. [Q62962-1]
DR RefSeq; NP_037024.2; NM_012892.2. [Q62962-2]
DR AlphaFoldDB; Q62962; -.
DR SMR; Q62962; -.
DR DIP; DIP-41193N; -.
DR IntAct; Q62962; 1.
DR MINT; Q62962; -.
DR ChEMBL; CHEMBL3562171; -.
DR TCDB; 1.A.6.1.2; the epithelial na(+) channel (enac) family.
DR GlyGen; Q62962; 2 sites.
DR iPTMnet; Q62962; -.
DR PhosphoSitePlus; Q62962; -.
DR DNASU; 25364; -.
DR Ensembl; ENSRNOT00000086961; ENSRNOP00000068763; ENSRNOG00000058308. [Q62962-2]
DR Ensembl; ENSRNOT00000112270; ENSRNOP00000080191; ENSRNOG00000058308. [Q62962-1]
DR GeneID; 25364; -.
DR KEGG; rno:25364; -.
DR CTD; 40; -.
DR RGD; 2017; Asic2.
DR GeneTree; ENSGT00940000154991; -.
DR InParanoid; Q62962; -.
DR OrthoDB; 686369at2759; -.
DR PhylomeDB; Q62962; -.
DR TreeFam; TF330663; -.
DR Reactome; R-RNO-2672351; Stimuli-sensing channels.
DR PRO; PR:Q62962; -.
DR Proteomes; UP000002494; Chromosome 10.
DR GO; GO:0043197; C:dendritic spine; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0005261; F:cation channel activity; ISO:RGD.
DR GO; GO:0005216; F:ion channel activity; IDA:RGD.
DR GO; GO:0022839; F:ion gated channel activity; ISO:RGD.
DR GO; GO:0015280; F:ligand-gated sodium channel activity; ISO:RGD.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:RGD.
DR GO; GO:0006812; P:cation transport; ISO:RGD.
DR GO; GO:0071468; P:cellular response to acidic pH; IDA:RGD.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:RGD.
DR GO; GO:0050974; P:detection of mechanical stimulus involved in sensory perception; ISO:RGD.
DR GO; GO:0034220; P:ion transmembrane transport; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0007602; P:phototransduction; ISO:RGD.
DR GO; GO:2001259; P:positive regulation of cation channel activity; IDA:RGD.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISO:RGD.
DR GO; GO:0035418; P:protein localization to synapse; ISO:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; ISO:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0003026; P:regulation of systemic arterial blood pressure by aortic arch baroreceptor feedback; ISO:RGD.
DR GO; GO:0019229; P:regulation of vasoconstriction; ISO:RGD.
DR GO; GO:0010447; P:response to acidic pH; ISO:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR GO; GO:0050915; P:sensory perception of sour taste; ISO:RGD.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; IDA:RGD.
DR InterPro; IPR001873; ENaC.
DR InterPro; IPR004724; ENaC_chordates.
DR InterPro; IPR020903; ENaC_CS.
DR PANTHER; PTHR11690; PTHR11690; 1.
DR Pfam; PF00858; ASC; 1.
DR PRINTS; PR01078; AMINACHANNEL.
DR TIGRFAMs; TIGR00859; ENaC; 1.
DR PROSITE; PS01206; ASC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Sodium; Sodium channel; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..512
FT /note="Acid-sensing ion channel 2"
FT /id="PRO_0000181292"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15504740"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..427
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:15504740"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..512
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15504740"
FT SITE 478
FT /note="Not glycosylated"
FT SITE 487
FT /note="Not glycosylated"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15504740"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15504740"
FT DISULFID 92..193
FT /evidence="ECO:0000250"
FT DISULFID 171..178
FT /evidence="ECO:0000250"
FT DISULFID 289..364
FT /evidence="ECO:0000250"
FT DISULFID 307..360
FT /evidence="ECO:0000250"
FT DISULFID 311..358
FT /evidence="ECO:0000250"
FT DISULFID 320..342
FT /evidence="ECO:0000250"
FT DISULFID 322..334
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..184
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9368048"
FT /id="VSP_015594"
FT VAR_SEQ 185
FT /note="T -> MSRSGGARLPATALSGPGRFRMAREQPAPVAVAAARQPGGDRSGDPA
FT LQGPGVARRGRPSLSRTKLHGLRHMCAGRTAAGGSFQRRALWVLAFCTSLGLLLSWSSN
FT RLLYWLSFPSHTRVHREWSRQLPFPAVTVCNNNPLRFPRLSKGDLYYAGHWLGLLLPNR
FT TARPLVSELLRGDEPRRQWFRKLADFRLFLPPRHFEGISAAFMDRLGHQLEDMLLSCKY
FT RGELCGPHNFSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9368048"
FT /id="VSP_015595"
FT MUTAGEN 4
FT /note="K->N: No effect on N-glycosylation."
FT /evidence="ECO:0000269|PubMed:15504740"
FT MUTAGEN 22
FT /note="N->S: No effect on N-glycosylation."
FT /evidence="ECO:0000269|PubMed:15504740"
FT MUTAGEN 37
FT /note="P->N: No effect on N-glycosylation."
FT /evidence="ECO:0000269|PubMed:15504740"
FT MUTAGEN 63
FT /note="R->N: No effect on N-glycosylation."
FT /evidence="ECO:0000269|PubMed:15504740"
FT MUTAGEN 67
FT /note="Y->N: No effect on N-glycosylation."
FT /evidence="ECO:0000269|PubMed:15504740"
FT MUTAGEN 72
FT /note="H->A: Inactive. Active at lower pH; when associated
FT with V-430."
FT /evidence="ECO:0000269|PubMed:11457851,
FT ECO:0000269|PubMed:15504740"
FT MUTAGEN 72
FT /note="H->N: Increases N-glycosylation."
FT /evidence="ECO:0000269|PubMed:11457851,
FT ECO:0000269|PubMed:15504740"
FT MUTAGEN 81
FT /note="A->N: Increases N-glycosylation."
FT /evidence="ECO:0000269|PubMed:15504740"
FT MUTAGEN 109
FT /note="H->A: No effect on pH dependence and function."
FT /evidence="ECO:0000269|PubMed:11457851"
FT MUTAGEN 127
FT /note="H->A: No effect on pH dependence and function."
FT /evidence="ECO:0000269|PubMed:11457851"
FT MUTAGEN 145
FT /note="H->A: No effect on pH dependence and function."
FT /evidence="ECO:0000269|PubMed:11457851"
FT MUTAGEN 158
FT /note="H->A: No effect on pH dependence and function."
FT /evidence="ECO:0000269|PubMed:11457851"
FT MUTAGEN 162
FT /note="H->A: Loss of potentiation by Zn(2+)."
FT /evidence="ECO:0000269|PubMed:11457851"
FT MUTAGEN 180
FT /note="H->A: No effect on pH dependence and function."
FT /evidence="ECO:0000269|PubMed:11457851"
FT MUTAGEN 249
FT /note="H->A: No effect on pH dependence and function."
FT /evidence="ECO:0000269|PubMed:11457851"
FT MUTAGEN 326
FT /note="H->A: No effect on pH dependence and function."
FT /evidence="ECO:0000269|PubMed:11457851"
FT MUTAGEN 339
FT /note="H->A: Loss of potentiation by Zn(2+)."
FT /evidence="ECO:0000269|PubMed:11457851"
FT MUTAGEN 365
FT /note="N->S: Reduces N-glycosylation. Abolishes N-
FT glycosylation; when associated with S-392."
FT /evidence="ECO:0000269|PubMed:15504740"
FT MUTAGEN 392
FT /note="N->S: Reduces N-glycosylation. Abolishes N-
FT glycosylation; when associated with S-365."
FT /evidence="ECO:0000269|PubMed:15504740"
FT MUTAGEN 414
FT /note="Y->N: Increases N-glycosylation."
FT /evidence="ECO:0000269|PubMed:15504740"
FT MUTAGEN 423..425
FT /note="YEV->NES: Increases N-glycosylation."
FT /evidence="ECO:0000269|PubMed:15504740"
FT MUTAGEN 430
FT /note="G->C: Partial activation."
FT /evidence="ECO:0000269|PubMed:11457851,
FT ECO:0000269|PubMed:8631835"
FT MUTAGEN 430
FT /note="G->F: Constitutive activation causing cell death.
FT Inactive; when associated with F-443."
FT /evidence="ECO:0000269|PubMed:11457851,
FT ECO:0000269|PubMed:8631835"
FT MUTAGEN 430
FT /note="G->K,T: Constitutive activation causing cell death."
FT /evidence="ECO:0000269|PubMed:11457851,
FT ECO:0000269|PubMed:8631835"
FT MUTAGEN 430
FT /note="G->S: No constitutive activation."
FT /evidence="ECO:0000269|PubMed:11457851,
FT ECO:0000269|PubMed:8631835"
FT MUTAGEN 430
FT /note="G->V: Constitutive activation causing cell death.
FT Activated at lower pH; when associated with A-72."
FT /evidence="ECO:0000269|PubMed:11457851,
FT ECO:0000269|PubMed:8631835"
FT MUTAGEN 443
FT /note="S->F: Loss of function. Inactive; when associated
FT with F-430."
FT /evidence="ECO:0000269|PubMed:8631835"
FT MUTAGEN 453..455
FT /note="YIY->NIS: No effect on N-glycosylation."
FT /evidence="ECO:0000269|PubMed:15504740"
FT MUTAGEN 478
FT /note="N->S: No effect on N-glycosylation."
FT /evidence="ECO:0000269|PubMed:15504740"
FT MUTAGEN 487
FT /note="N->S: No effect on N-glycosylation."
FT /evidence="ECO:0000269|PubMed:15504740"
SQ SEQUENCE 512 AA; 57739 MW; 38D0A77C3C430B03 CRC64;
MDLKESPSEG SLQPSSIQIF ANTSTLHGIR HIFVYGPLTI RRVLWAVAFV GSLGLLLVES
SERVSYYFSY QHVTKVDEVV AQSLVFPAVT LCNLNGFRFS RLTTNDLYHA GELLALLDVN
LQIPDPHLAD PTVLEALRQK ANFKHYKPKQ FSMLEFLHRV GHDLKDMMLY CKFKGQECGH
QDFTTVFTKY GKCYMFNSGE DGKPLLTTVK GGTGNGLEIM LDIQQDEYLP IWGETEETTF
EAGVKVQIHS QSEPPFIQEL GFGVAPGFQT FVATQEQRLT YLPPPWGECR SSEMGLDFFP
VYSITACRID CETRYIVENC NCRMVHMPGD APFCTPEQHK ECAEPALGLL AEKDSNYCLC
RTPCNLTRYN KELSMVKIPS KTSAKYLEKK FNKSEKYISE NILVLDIFFE ALNYETIEQK
KAYEVAALLG DIGGQMGLFI GASLLTILEL FDYIYELIKE KLLDLLGKEE EEGSHDENMS
TCDTMPNHSE TISHTVNVPL QTALGTLEEI AC
