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Acid ceramidase (AC) (ACDase) (Acid CDase) (EC 3.5.1.23) (Acylsphingosine deacylase) (N-acylsphingosine amidohydrolase) (Putative 32 kDa heart protein) (PHP32) [Cleaved into: Acid ceramidase subunit alpha; Acid ceramidase subunit beta]

 ASAH1_HUMAN             Reviewed;         395 AA.
Q13510; E9PDS0; Q6W898; Q96AS2;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
16-JUN-2009, sequence version 5.
20-JUN-2018, entry version 183.
RecName: Full=Acid ceramidase;
Short=AC;
Short=ACDase;
Short=Acid CDase;
EC=3.5.1.23 {ECO:0000269|PubMed:7744740};
AltName: Full=Acylsphingosine deacylase;
AltName: Full=N-acylsphingosine amidohydrolase;
AltName: Full=Putative 32 kDa heart protein;
Short=PHP32;
Contains:
RecName: Full=Acid ceramidase subunit alpha;
Contains:
RecName: Full=Acid ceramidase subunit beta;
Flags: Precursor;
Name=ASAH1; Synonyms=ASAH; ORFNames=HSD-33, HSD33;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE,
VARIANT FRBRL LYS-222, AND VARIANTS MET-72; VAL-93 AND ALA-246.
TISSUE=Fibroblast, Pituitary, and Urine;
PubMed=8955159; DOI=10.1074/jbc.271.51.33110;
Koch J., Gaertner S., Li C.M., Quintern L.E., Bernardo K., Levran O.,
Schnabel D., Desnick R.J., Schuchman E.H., Sandhoff K.;
"Molecular cloning and characterization of a full-length complementary
DNA encoding human acid ceramidase. Identification of the first
molecular lesion causing Farber disease.";
J. Biol. Chem. 271:33110-33115(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS MET-72; VAL-93
AND ALA-246.
Churchill J.R., Wieland S.J., Hoffman S., Gallin E.K., Murphy P.M.;
"A new gene family predicted by a novel human heart cDNA.";
Mol. Biol. Cell 6:418-418(1995).
[3]
SEQUENCE REVISION.
Wieland S.J., Hoffman S., Churchill J.R., Gallin E.K., Murphy P.M.;
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
Fan M.M., Miao S.Y., Zhang X.D., Qiao Y., Liang G., Wang L.F.;
"A new spermatogenesis related gene.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS FRBRL HIS-22; ASP-23;
VAL-138; LYS-222 AND ASP-320, AND VARIANTS MET-72; VAL-93 AND ALA-246.
PubMed=10993717; DOI=10.1006/mgme.2000.3029;
Zhang Z., Mandal A.K., Mital A., Popescu N., Zimonjic D., Moser A.,
Moser H., Mukherjee A.B.;
"Human acid ceramidase gene: novel mutations in Farber disease.";
Mol. Genet. Metab. 70:301-309(2000).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS FRBRL VAL-138; GLY-254
AND ARG-362.
PubMed=10610716; DOI=10.1006/geno.1999.5940;
Li C.M., Park J.H., He X., Levy B., Chen F., Arai K., Adler D.A.,
Disteche C.M., Koch J., Sandhoff K., Schuchman E.H.;
"The human acid ceramidase gene (ASAH): structure, chromosomal
location, mutation analysis, and expression.";
Genomics 62:223-231(1999).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND
VARIANTS MET-72; VAL-93 AND ALA-246.
TISSUE=Bone marrow, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
SUBUNIT.
PubMed=7744740; DOI=10.1074/jbc.270.19.11098;
Bernardo K., Hurwitz R., Zenk T., Desnick R.J., Ferlinz K.,
Schuchman E.H., Sandhoff K.;
"Purification, characterization, and biosynthesis of human acid
ceramidase.";
J. Biol. Chem. 270:11098-11102(1995).
[10]
GLYCOSYLATION AT ASN-259 AND ASN-286.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-259.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-259.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-259 AND ASN-286.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[17]
VARIANTS FRBRL CYS-36 AND ASP-320.
PubMed=11241842; DOI=10.1002/humu.5;
Bar J., Linke T., Ferlinz K., Neumann U., Schuchman E.H., Sandhoff K.;
"Molecular analysis of acid ceramidase deficiency in patients with
Farber disease.";
Hum. Mutat. 17:199-209(2001).
[18]
VARIANTS FRBRL VAL-96 DEL; GLU-97 AND ARG-235, AND VARIANT ILE-369.
PubMed=12638942; DOI=10.1023/A:1022047408477;
Muramatsu T., Sakai N., Yanagihara L., Yamada M., Nishigaki T.,
Kokubu C., Tsukamoto H., Ito M., Inui K.;
"Mutation analysis of the acid ceramidase gene in Japanese patients
with Farber disease.";
J. Inherit. Metab. Dis. 25:585-592(2002).
[19]
VARIANT FRBRL VAL-182.
PubMed=16951918; DOI=10.1007/s10038-006-0019-z;
Devi A.R.R., Gopikrishna M., Ratheesh R., Savithri G., Swarnalata G.,
Bashyam M.;
"Farber lipogranulomatosis: clinical and molecular genetic analysis
reveals a novel mutation in an Indian family.";
J. Hum. Genet. 51:811-814(2006).
[20]
VARIANT FRBRL TRP-168.
PubMed=20609603; DOI=10.1016/j.ejpn.2010.06.002;
Cvitanovic-Sojat L., Gjergja Juraski R., Sabourdy F., Fensom A.H.,
Fumic K., Paschke E., Levade T.;
"Farber lipogranulomatosis type 1--late presentation and early death
in a Croatian boy with a novel homozygous ASAH1 mutation.";
Eur. J. Paediatr. Neurol. 15:171-173(2011).
[21]
VARIANT SMAPME MET-42, AND CHARACTERIZATION OF VARIANT SMAPME MET-42.
PubMed=22703880; DOI=10.1016/j.ajhg.2012.05.001;
Zhou J., Tawk M., Tiziano F.D., Veillet J., Bayes M., Nolent F.,
Garcia V., Servidei S., Bertini E., Castro-Giner F., Renda Y.,
Carpentier S., Andrieu-Abadie N., Gut I., Levade T., Topaloglu H.,
Melki J.;
"Spinal muscular atrophy associated with progressive myoclonic
epilepsy is caused by mutations in ASAH1.";
Am. J. Hum. Genet. 91:5-14(2012).
[22]
VARIANT FRBRL GLY-97.
PubMed=21893389; DOI=10.1016/j.braindev.2011.07.003;
Chedrawi A.K., Al-Hassnan Z.N., Al-Muhaizea M., Colak D.,
Al-Younes B., Albakheet A., Tulba S., Kaya N.;
"Novel V97G ASAH1 mutation found in Farber disease patients: unique
appearance of the disease with an intermediate severity, and marked
early involvement of central and peripheral nervous system.";
Brain Dev. 34:400-404(2012).
[23]
VARIANTS FRBRL ARG-185 AND GLN-382 (ISOFORM 2).
PubMed=21982811; DOI=10.1016/j.braindev.2011.09.006;
Al Jasmi F.;
"A novel mutation in an atypical presentation of the rare infantile
Farber disease.";
Brain Dev. 34:533-535(2012).
[24]
VARIANT SMAPME ASN-152.
PubMed=24164096; DOI=10.1111/cge.12307;
FORGE Canada Consortium;
Dyment D.A., Sell E., Vanstone M.R., Smith A.C., Garandeau D.,
Garcia V., Carpentier S., Le Trionnaire E., Sabourdy F.,
Beaulieu C.L., Schwartzentruber J.A., McMillan H.J., Majewski J.,
Bulman D.E., Levade T., Boycott K.M.;
"Evidence for clinical, genetic and biochemical variability in spinal
muscular atrophy with progressive myoclonic epilepsy.";
Clin. Genet. 86:558-563(2014).
-!- FUNCTION: Hydrolyzes the sphingolipid ceramide into sphingosine
and free fatty acid. {ECO:0000269|PubMed:7744740}.
-!- CATALYTIC ACTIVITY: N-acylsphingosine + H(2)O = a carboxylate +
sphingosine. {ECO:0000269|PubMed:7744740}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=149 uM for N-lauroylsphingosine {ECO:0000269|PubMed:7744740};
Vmax=136 nmol/h/mg enzyme with N-lauroylsphingosine as substrate
{ECO:0000269|PubMed:7744740};
pH dependence:
Optimum pH is 3.8-4.3 with N-lauroylsphingosine as substrate.
{ECO:0000269|PubMed:7744740};
-!- SUBUNIT: Heterodimer of one alpha and one beta subunit.
{ECO:0000269|PubMed:7744740}.
-!- SUBCELLULAR LOCATION: Lysosome.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q13510-1; Sequence=Displayed;
Name=2;
IsoId=Q13510-2; Sequence=VSP_037504;
Note=Variant in position: 185:W->R (in FL). Variant in position:
382:K->Q (in FL). {ECO:0000269|PubMed:21982811};
Name=3;
IsoId=Q13510-3; Sequence=VSP_037504, VSP_046284, VSP_046285;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Broadly expressed with highest expression in
heart.
-!- DISEASE: Farber lipogranulomatosis (FRBRL) [MIM:228000]: An
autosomal recessive lysosomal storage disorder characterized by
subcutaneous lipid-loaded nodules, excruciating pain in the joints
and extremities, and marked accumulation of ceramide in lysosomes.
Disease severity is variable. The most severe disease subtype is a
rare neonatal form with death occurring before 1 year of age.
{ECO:0000269|PubMed:10610716, ECO:0000269|PubMed:10993717,
ECO:0000269|PubMed:11241842, ECO:0000269|PubMed:12638942,
ECO:0000269|PubMed:16951918, ECO:0000269|PubMed:20609603,
ECO:0000269|PubMed:21893389, ECO:0000269|PubMed:21982811,
ECO:0000269|PubMed:8955159}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Spinal muscular atrophy with progressive myoclonic
epilepsy (SMAPME) [MIM:159950]: An autosomal recessive
neuromuscular disorder characterized by childhood onset of motor
deficits and progressive myoclonic seizures, after normal
developmental milestones. Proximal muscle weakness and generalized
muscular atrophy are due to degeneration of spinal motor neurons.
Myoclonic epilepsy is generally resistant to conventional therapy.
The disease course is progressive and leads to respiratory muscle
involvement and severe handicap or early death from respiratory
insufficiency. {ECO:0000269|PubMed:22703880,
ECO:0000269|PubMed:24164096}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the acid ceramidase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC73009.1; Type=Frameshift; Positions=15, 21; Evidence={ECO:0000305};
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EMBL; U70063; AAC50907.1; -; mRNA.
EMBL; U47674; AAC73009.1; ALT_FRAME; mRNA.
EMBL; AY305384; AAQ75550.1; -; mRNA.
EMBL; AF220175; AAF91230.1; -; Genomic_DNA.
EMBL; AF220172; AAF91230.1; JOINED; Genomic_DNA.
EMBL; AF220173; AAF91230.1; JOINED; Genomic_DNA.
EMBL; AC124242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC016481; AAH16481.1; -; mRNA.
EMBL; BC016828; AAH16828.1; -; mRNA.
CCDS; CCDS47813.1; -. [Q13510-3]
CCDS; CCDS6005.1; -. [Q13510-2]
CCDS; CCDS6006.1; -. [Q13510-1]
RefSeq; NP_001120977.1; NM_001127505.2. [Q13510-3]
RefSeq; NP_004306.3; NM_004315.5. [Q13510-2]
RefSeq; NP_808592.2; NM_177924.4. [Q13510-1]
UniGene; Hs.527412; -.
UniGene; Hs.633993; -.
ProteinModelPortal; Q13510; -.
SMR; Q13510; -.
BioGrid; 106920; 36.
IntAct; Q13510; 8.
MINT; Q13510; -.
STRING; 9606.ENSP00000371152; -.
BindingDB; Q13510; -.
ChEMBL; CHEMBL5463; -.
SwissLipids; SLP:000000162; -.
MEROPS; C89.001; -.
iPTMnet; Q13510; -.
PhosphoSitePlus; Q13510; -.
SwissPalm; Q13510; -.
BioMuta; ASAH1; -.
DMDM; 239938949; -.
EPD; Q13510; -.
MaxQB; Q13510; -.
PaxDb; Q13510; -.
PeptideAtlas; Q13510; -.
PRIDE; Q13510; -.
ProteomicsDB; 59511; -.
ProteomicsDB; 59512; -. [Q13510-2]
TopDownProteomics; Q13510-1; -. [Q13510-1]
DNASU; 427; -.
Ensembl; ENST00000262097; ENSP00000262097; ENSG00000104763. [Q13510-1]
Ensembl; ENST00000314146; ENSP00000326970; ENSG00000104763. [Q13510-3]
Ensembl; ENST00000381733; ENSP00000371152; ENSG00000104763. [Q13510-2]
Ensembl; ENST00000635998; ENSP00000490506; ENSG00000104763. [Q13510-1]
Ensembl; ENST00000637790; ENSP00000490272; ENSG00000104763. [Q13510-1]
GeneID; 427; -.
KEGG; hsa:427; -.
UCSC; uc003wyl.3; human. [Q13510-1]
CTD; 427; -.
DisGeNET; 427; -.
EuPathDB; HostDB:ENSG00000104763.17; -.
GeneCards; ASAH1; -.
HGNC; HGNC:735; ASAH1.
HPA; HPA005468; -.
MalaCards; ASAH1; -.
MIM; 159950; phenotype.
MIM; 228000; phenotype.
MIM; 613468; gene.
neXtProt; NX_Q13510; -.
OpenTargets; ENSG00000104763; -.
Orphanet; 333; Farber lipogranulomatosis.
Orphanet; 2590; Hereditary myoclonus - progressive distal muscular atrophy.
PharmGKB; PA35025; -.
eggNOG; ENOG410IFSS; Eukaryota.
eggNOG; ENOG410XQ6Y; LUCA.
GeneTree; ENSGT00530000063548; -.
HOGENOM; HOG000007253; -.
HOVERGEN; HBG050586; -.
InParanoid; Q13510; -.
KO; K12348; -.
OMA; DAMWIGF; -.
OrthoDB; EOG091G08N9; -.
PhylomeDB; Q13510; -.
TreeFam; TF313219; -.
BRENDA; 3.5.1.23; 2681.
Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SABIO-RK; Q13510; -.
ChiTaRS; ASAH1; human.
GeneWiki; ASAH1; -.
GenomeRNAi; 427; -.
PRO; PR:Q13510; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000104763; -.
CleanEx; HS_ASAH1; -.
ExpressionAtlas; Q13510; baseline and differential.
Genevisible; Q13510; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
GO; GO:0003824; F:catalytic activity; TAS:ProtInc.
GO; GO:0102121; F:ceramidase activity; IEA:UniProtKB-EC.
GO; GO:0017040; F:N-acylsphingosine amidohydrolase activity; TAS:Reactome.
GO; GO:0006672; P:ceramide metabolic process; TAS:ProtInc.
GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:Reactome.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
InterPro; IPR016699; Acid_ceramidase-like.
InterPro; IPR029130; Acid_ceramidase_N.
InterPro; IPR029132; CBAH/NAAA_C.
Pfam; PF02275; CBAH; 1.
Pfam; PF15508; NAAA-beta; 1.
PIRSF; PIRSF017632; Acid_ceramidase-like; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Direct protein sequencing;
Disease mutation; Epilepsy; Glycoprotein; Hydrolase; Lysosome;
Neurodegeneration; Polymorphism; Reference proteome; Signal.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 142 Acid ceramidase subunit alpha.
/FTId=PRO_0000002312.
CHAIN 143 395 Acid ceramidase subunit beta.
/FTId=PRO_0000002313.
CARBOHYD 173 173 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 195 195 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 259 259 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 286 286 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19159218}.
CARBOHYD 342 342 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 348 348 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 26 MPGRSCVALVLLAAAVSCAVAQHAPP -> MNCCIGLGEKA
RGSHRASYPSLSALFTEASILGFGSFAVKAQ (in
isoform 2 and isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4}.
/FTId=VSP_037504.
VAR_SEQ 42 42 T -> TVFPAVIR (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_046284.
VAR_SEQ 73 101 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_046285.
VARIANT 22 22 Q -> H (in FRBRL).
{ECO:0000269|PubMed:10993717}.
/FTId=VAR_038166.
VARIANT 23 23 H -> D (in FRBRL).
{ECO:0000269|PubMed:10993717}.
/FTId=VAR_038167.
VARIANT 36 36 Y -> C (in FRBRL; dbSNP:rs137853595).
{ECO:0000269|PubMed:11241842}.
/FTId=VAR_021579.
VARIANT 42 42 T -> M (in SMAPME; results in reduced
activity; dbSNP:rs145873635).
{ECO:0000269|PubMed:22703880}.
/FTId=VAR_068722.
VARIANT 70 70 A -> V (in dbSNP:rs10103355).
/FTId=VAR_057979.
VARIANT 72 72 V -> M (in dbSNP:rs1071645).
{ECO:0000269|PubMed:10993717,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8955159,
ECO:0000269|Ref.2}.
/FTId=VAR_008860.
VARIANT 88 88 V -> M (in dbSNP:rs1071645).
/FTId=VAR_057980.
VARIANT 93 93 I -> V (in dbSNP:rs1049874).
{ECO:0000269|PubMed:10993717,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8955159,
ECO:0000269|Ref.2}.
/FTId=VAR_008861.
VARIANT 96 96 Missing (in FRBRL).
{ECO:0000269|PubMed:12638942}.
/FTId=VAR_021580.
VARIANT 97 97 V -> E (in FRBRL).
{ECO:0000269|PubMed:12638942}.
/FTId=VAR_021581.
VARIANT 97 97 V -> G (in FRBRL).
{ECO:0000269|PubMed:21893389}.
/FTId=VAR_071994.
VARIANT 124 124 D -> E (in dbSNP:rs2472205).
/FTId=VAR_038168.
VARIANT 138 138 E -> V (in FRBRL; dbSNP:rs137853594).
{ECO:0000269|PubMed:10610716,
ECO:0000269|PubMed:10993717}.
/FTId=VAR_021582.
VARIANT 152 152 K -> N (in SMAPME; results in reduced
activity; dbSNP:rs200455852).
{ECO:0000269|PubMed:24164096}.
/FTId=VAR_072247.
VARIANT 168 168 G -> W (in FRBRL).
{ECO:0000269|PubMed:20609603}.
/FTId=VAR_071995.
VARIANT 182 182 L -> V (in FRBRL; dbSNP:rs137853597).
{ECO:0000269|PubMed:16951918}.
/FTId=VAR_038169.
VARIANT 222 222 T -> K (in FRBRL; dbSNP:rs137853593).
{ECO:0000269|PubMed:10993717,
ECO:0000269|PubMed:8955159}.
/FTId=VAR_008862.
VARIANT 235 235 G -> R (in FRBRL).
{ECO:0000269|PubMed:12638942}.
/FTId=VAR_021583.
VARIANT 246 246 V -> A (in dbSNP:rs10103355).
{ECO:0000269|PubMed:10993717,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8955159,
ECO:0000269|Ref.2}.
/FTId=VAR_038170.
VARIANT 254 254 R -> G (in FRBRL).
{ECO:0000269|PubMed:10610716}.
/FTId=VAR_021584.
VARIANT 320 320 N -> D (in FRBRL; dbSNP:rs137853596).
{ECO:0000269|PubMed:10993717,
ECO:0000269|PubMed:11241842}.
/FTId=VAR_021585.
VARIANT 362 362 P -> R (in FRBRL).
{ECO:0000269|PubMed:10610716}.
/FTId=VAR_021586.
VARIANT 369 369 V -> I (in dbSNP:rs17636067).
{ECO:0000269|PubMed:12638942}.
/FTId=VAR_021587.
CONFLICT 122 122 V -> A (in Ref. 4; AAQ75550).
{ECO:0000305}.
CONFLICT 142 142 I -> V (in Ref. 8; AAH16828).
{ECO:0000305}.
CONFLICT 155 155 L -> P (in Ref. 4; AAQ75550).
{ECO:0000305}.
CONFLICT 233 233 Y -> N (in Ref. 4; AAQ75550).
{ECO:0000305}.
CONFLICT 364 364 L -> P (in Ref. 4; AAQ75550).
{ECO:0000305}.
SEQUENCE 395 AA; 44660 MW; 83467DBE8917DB6D CRC64;
MPGRSCVALV LLAAAVSCAV AQHAPPWTED CRKSTYPPSG PTYRGAVPWY TINLDLPPYK
RWHELMLDKA PVLKVIVNSL KNMINTFVPS GKIMQVVDEK LPGLLGNFPG PFEEEMKGIA
AVTDIPLGEI ISFNIFYELF TICTSIVAED KKGHLIHGRN MDFGVFLGWN INNDTWVITE
QLKPLTVNLD FQRNNKTVFK ASSFAGYVGM LTGFKPGLFS LTLNERFSIN GGYLGILEWI
LGKKDVMWIG FLTRTVLENS TSYEEAKNLL TKTKILAPAY FILGGNQSGE GCVITRDRKE
SLDVYELDAK QGRWYVVQTN YDRWKHPFFL DDRRTPAKMC LNRTSQENIS FETMYDVLST
KPVLNKLTVY TTLIDVTKGQ FETYLRDCPD PCIGW


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