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Peroxisomal N(1)-acetyl-spermine/spermidine oxidase (EC 1.5.3.13) (Polyamine oxidase)

 PAOX_HUMAN              Reviewed;         649 AA.
Q6QHF9; D3DXI6; Q5VWY0; Q6QHF5; Q6QHF6; Q6QHF7; Q6QHF8; Q6QHG0;
Q6QHG1; Q6QHG2; Q6QHG3; Q6QHG4; Q6QHG5; Q6QHG6; Q86WP9; Q8N555;
Q8NCX3;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 138.
RecName: Full=Peroxisomal N(1)-acetyl-spermine/spermidine oxidase;
EC=1.5.3.13;
AltName: Full=Polyamine oxidase;
Name=PAOX; Synonyms=PAO; ORFNames=UNQ1923/PRO4398;
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).
TISSUE=Liver;
PubMed=12660232; DOI=10.1074/jbc.M302149200;
Wu T., Yankovskaya V., McIntire W.S.;
"Cloning, sequencing, and heterologous expression of the murine
peroxisomal flavoprotein, N(1)-acetylated polyamine oxidase.";
J. Biol. Chem. 278:20514-20525(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5; 6; 8; 9; 10; 11; 12 AND
13).
Wang Y., Murray-Stewart T., Hacker A., Casero R.A. Jr.;
"Polyamine oxidase.";
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 364-649 (ISOFORM 9).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION, AND TISSUE
SPECIFICITY.
PubMed=12477380; DOI=10.1042/BJ20021779;
Vujcic S., Liang P., Diegelman P., Kramer D.L., Porter C.W.;
"Genomic identification and biochemical characterization of the
mammalian polyamine oxidase involved in polyamine back-conversion.";
Biochem. J. 370:19-28(2003).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: Flavoenzyme which catalyzes the oxidation of N(1)-
acetylspermine to spermidine and is thus involved in the polyamine
back-conversion. Can also oxidize N(1)-acetylspermidine to
putrescine. Substrate specificity: N(1)-acetylspermine = N(1)-
acetylspermidine > N(1),N(12)-diacylspermine >> spermine. Does not
oxidize spermidine. Plays an important role in the regulation of
polyamine intracellular concentration and has the potential to act
as a determinant of cellular sensitivity to the antitumor
polyamine analogs.
-!- CATALYTIC ACTIVITY: N(1)-acetylspermine + O(2) + H(2)O =
spermidine + 3-acetamidopropanal + H(2)O(2).
-!- CATALYTIC ACTIVITY: N(1)-acetylspermidine + O(2) + H(2)O =
putrescine + 3-acetamidopropanal + H(2)O(2).
-!- CATALYTIC ACTIVITY: N(1),N(12)-diacetylspermine + O(2) + H(2)O =
N(1)-acetylspermidine + 3-acetamidobutanal + H(2)O(2).
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
Note=Binds 1 FAD per subunit. {ECO:0000250};
-!- PATHWAY: Amine and polyamine metabolism; spermine metabolism.
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. Cytoplasm
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=11;
Name=9;
IsoId=Q6QHF9-1; Sequence=Displayed;
Name=1;
IsoId=Q6QHF9-2; Sequence=VSP_011249;
Name=3; Synonyms=7;
IsoId=Q6QHF9-6; Sequence=VSP_011250, VSP_011251;
Name=4; Synonyms=2;
IsoId=Q6QHF9-5; Sequence=VSP_011249, VSP_011255, VSP_011257;
Name=5;
IsoId=Q6QHF9-4; Sequence=VSP_011249, VSP_011258;
Note=Ref.2 (AAS64376) sequence is in conflict in position:
457:Q->E. {ECO:0000305};
Name=6;
IsoId=Q6QHF9-8; Sequence=VSP_011248, VSP_011256;
Note=Ref.2 (AAS64377) sequence differs from that shown due to a
frameshift in position 26. {ECO:0000305};
Name=8;
IsoId=Q6QHF9-3; Sequence=VSP_011249, VSP_011254;
Name=10;
IsoId=Q6QHF9-7; Sequence=VSP_011252;
Name=11;
IsoId=Q6QHF9-9; Sequence=VSP_011247, VSP_011253;
Name=12;
IsoId=Q6QHF9-10; Sequence=VSP_011259, VSP_011260;
Name=13;
IsoId=Q6QHF9-11; Sequence=VSP_011261, VSP_011262;
-!- TISSUE SPECIFICITY: Widely expressed. Not detected in spleen.
Expressed at lower level in neoplastic tissues.
{ECO:0000269|PubMed:12477380}.
-!- INDUCTION: By polyamine analogs.
-!- MISCELLANEOUS: Oxidizes N(1)-acetylated polyamines on the exo-side
of their N(4)-amino groups. Plant PAO oxidizes spermine on the
endo-side of the N(4)-nitrogen (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
{ECO:0000305}.
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EMBL; AF226657; AAN40706.1; -; mRNA.
EMBL; AF312698; AAO63265.1; -; mRNA.
EMBL; AY541513; AAS64373.1; -; mRNA.
EMBL; AY541514; AAS64374.1; -; mRNA.
EMBL; AY541515; AAS64375.1; -; mRNA.
EMBL; AY541516; AAS64376.1; -; mRNA.
EMBL; AY541517; AAS64377.1; ALT_FRAME; mRNA.
EMBL; AY541518; AAS64378.1; -; mRNA.
EMBL; AY541519; AAS64379.1; -; mRNA.
EMBL; AY541520; AAS64380.1; -; mRNA.
EMBL; AY541521; AAS64381.1; -; mRNA.
EMBL; AY541522; AAS64382.1; -; mRNA.
EMBL; AY541523; AAS64383.1; -; mRNA.
EMBL; AY541524; AAS64384.1; -; mRNA.
EMBL; AY358418; AAQ88784.1; -; mRNA.
EMBL; AL360181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471211; EAW61340.1; -; Genomic_DNA.
EMBL; CH471211; EAW61341.1; -; Genomic_DNA.
EMBL; CH471211; EAW61344.1; -; Genomic_DNA.
EMBL; BC032778; AAH32778.1; -; mRNA.
EMBL; AL834535; CAD39191.1; -; mRNA.
CCDS; CCDS7682.1; -. [Q6QHF9-4]
CCDS; CCDS7683.1; -. [Q6QHF9-2]
CCDS; CCDS7684.1; -. [Q6QHF9-5]
RefSeq; NP_690875.1; NM_152911.3. [Q6QHF9-2]
RefSeq; NP_997010.1; NM_207127.2. [Q6QHF9-5]
RefSeq; NP_997011.1; NM_207128.2. [Q6QHF9-4]
UniGene; Hs.501578; -.
ProteinModelPortal; Q6QHF9; -.
SMR; Q6QHF9; -.
BioGrid; 128224; 1.
STRING; 9606.ENSP00000278060; -.
BindingDB; Q6QHF9; -.
ChEMBL; CHEMBL2105; -.
iPTMnet; Q6QHF9; -.
PhosphoSitePlus; Q6QHF9; -.
DMDM; 51316248; -.
EPD; Q6QHF9; -.
MaxQB; Q6QHF9; -.
PaxDb; Q6QHF9; -.
PeptideAtlas; Q6QHF9; -.
PRIDE; Q6QHF9; -.
ProteomicsDB; 67289; -.
ProteomicsDB; 67290; -. [Q6QHF9-10]
ProteomicsDB; 67291; -. [Q6QHF9-11]
ProteomicsDB; 67292; -. [Q6QHF9-2]
ProteomicsDB; 67293; -. [Q6QHF9-3]
ProteomicsDB; 67294; -. [Q6QHF9-4]
ProteomicsDB; 67295; -. [Q6QHF9-5]
ProteomicsDB; 67296; -. [Q6QHF9-6]
ProteomicsDB; 67297; -. [Q6QHF9-7]
ProteomicsDB; 67298; -. [Q6QHF9-8]
ProteomicsDB; 67299; -. [Q6QHF9-9]
DNASU; 196743; -.
Ensembl; ENST00000278060; ENSP00000278060; ENSG00000148832. [Q6QHF9-2]
Ensembl; ENST00000356306; ENSP00000348654; ENSG00000148832. [Q6QHF9-5]
Ensembl; ENST00000357296; ENSP00000349847; ENSG00000148832. [Q6QHF9-4]
Ensembl; ENST00000476834; ENSP00000432737; ENSG00000148832. [Q6QHF9-6]
Ensembl; ENST00000480071; ENSP00000435514; ENSG00000148832. [Q6QHF9-5]
Ensembl; ENST00000483211; ENSP00000434550; ENSG00000148832. [Q6QHF9-6]
Ensembl; ENST00000529585; ENSP00000432517; ENSG00000148832. [Q6QHF9-6]
GeneID; 196743; -.
KEGG; hsa:196743; -.
UCSC; uc001lmv.5; human. [Q6QHF9-1]
CTD; 196743; -.
DisGeNET; 196743; -.
EuPathDB; HostDB:ENSG00000148832.14; -.
GeneCards; PAOX; -.
HGNC; HGNC:20837; PAOX.
HPA; HPA047782; -.
MIM; 615853; gene.
neXtProt; NX_Q6QHF9; -.
OpenTargets; ENSG00000148832; -.
PharmGKB; PA134907695; -.
eggNOG; KOG0685; Eukaryota.
eggNOG; ENOG410XQW0; LUCA.
GeneTree; ENSGT00530000062888; -.
HOVERGEN; HBG053499; -.
InParanoid; Q6QHF9; -.
KO; K00308; -.
OMA; ELGAHWI; -.
OrthoDB; EOG091G06OV; -.
PhylomeDB; Q6QHF9; -.
TreeFam; TF318348; -.
BRENDA; 1.5.3.13; 2681.
Reactome; R-HSA-141334; PAOs oxidise polyamines to amines.
Reactome; R-HSA-351200; Interconversion of polyamines.
Reactome; R-HSA-9033241; Peroxisomal protein import.
SABIO-RK; Q6QHF9; -.
UniPathway; UPA00826; -.
ChiTaRS; PAOX; human.
GeneWiki; PAOX; -.
GenomeRNAi; 196743; -.
PRO; PR:Q6QHF9; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000148832; Expressed in 159 organ(s), highest expression level in left testis.
CleanEx; HS_PAOX; -.
Genevisible; Q6QHF9; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
GO; GO:0052899; F:N(1),N(12)-diacetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity; IEA:UniProtKB-EC.
GO; GO:0052904; F:N1-acetylspermidine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity; TAS:Reactome.
GO; GO:0052903; F:N1-acetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity; IEA:UniProtKB-EC.
GO; GO:0046592; F:polyamine oxidase activity; IDA:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
GO; GO:0052902; F:spermidine:oxygen oxidoreductase (3-aminopropanal-forming) activity; IEA:UniProtKB-EC.
GO; GO:0052901; F:spermine:oxygen oxidoreductase (spermidine-forming) activity; IEA:UniProtKB-EC.
GO; GO:0006596; P:polyamine biosynthetic process; TAS:Reactome.
GO; GO:0006598; P:polyamine catabolic process; IDA:UniProtKB.
GO; GO:1901307; P:positive regulation of spermidine biosynthetic process; IDA:UniProtKB.
GO; GO:0006625; P:protein targeting to peroxisome; TAS:Reactome.
GO; GO:0009446; P:putrescine biosynthetic process; IDA:UniProtKB.
GO; GO:0009447; P:putrescine catabolic process; IDA:UniProtKB.
GO; GO:0046203; P:spermidine catabolic process; IDA:UniProtKB.
GO; GO:0046208; P:spermine catabolic process; IDA:UniProtKB.
Gene3D; 3.50.50.60; -; 4.
InterPro; IPR002937; Amino_oxidase.
InterPro; IPR036188; FAD/NAD-bd_sf.
Pfam; PF01593; Amino_oxidase; 2.
SUPFAM; SSF51905; SSF51905; 3.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm; FAD;
Flavoprotein; Oxidoreductase; Peroxisome; Reference proteome.
CHAIN 1 649 Peroxisomal N(1)-acetyl-
spermine/spermidine oxidase.
/FTId=PRO_0000099875.
MOTIF 647 649 Microbody targeting signal.
{ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
VAR_SEQ 1 267 Missing (in isoform 11).
{ECO:0000303|Ref.2}.
/FTId=VSP_011247.
VAR_SEQ 14 45 PRVLVVGGGIAGLGAAQRLCGHSAFPHLRVLE -> GHGPR
RGPHPLGALLRWRGGGGRALDPWALPG (in isoform
13). {ECO:0000303|Ref.2}.
/FTId=VSP_011261.
VAR_SEQ 23 83 IAGLGAAQRLCGHSAFPHLRVLEATARAGGRIRSERCFGGV
VEVGAHWIHGPSRGNPVFQL -> SSRSCLRGKPHIARFTP
RRTGLCCRDGWRPTASSVCGPRRCSSPGRGSSWAQPTLFHP
CRG (in isoform 12). {ECO:0000303|Ref.2}.
/FTId=VSP_011259.
VAR_SEQ 31 168 Missing (in isoform 1, isoform 5, isoform
4 and isoform 8).
{ECO:0000303|PubMed:12660232,
ECO:0000303|PubMed:12975309,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2}.
/FTId=VSP_011249.
VAR_SEQ 46 649 Missing (in isoform 13).
{ECO:0000303|Ref.2}.
/FTId=VSP_011262.
VAR_SEQ 61 80 GGVVEVGAHWIHGPSRGNPV -> RVSRTHKLHDGRPAGGH
CSF (in isoform 6). {ECO:0000303|Ref.2}.
/FTId=VSP_011248.
VAR_SEQ 62 69 GVVEVGAH -> AIKDSQTA (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_011250.
VAR_SEQ 70 649 Missing (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_011251.
VAR_SEQ 73 489 Missing (in isoform 10).
{ECO:0000303|Ref.2}.
/FTId=VSP_011252.
VAR_SEQ 81 649 Missing (in isoform 6).
{ECO:0000303|Ref.2}.
/FTId=VSP_011256.
VAR_SEQ 84 649 Missing (in isoform 12).
{ECO:0000303|Ref.2}.
/FTId=VSP_011260.
VAR_SEQ 338 649 MDLVALAPFGEYTVLPGLDCTFSKGYQGLTNCMMAALPEDT
VVFEKPVKTIHWNGSFQEAAFPGETFPVSVECEDGDRFPAH
HVIVTVPLGFLREHLDTFFDPPLPAEKAEAIRKIGFGTNNK
IFLEFEEPFWEPDCQLIQLVWEDTSPLEDAAPELQDAWFRK
LIGFVVLPAFASVHVLCGFIAGLESEFMETLSDEEVLLCLT
QVLRRVTGNPRLPAPKSVLRSRWHSAPYTRGSYSYVAVGST
GGDLDLLAQPLPADGAGAQLQILFAGEATHRTFYSTTHGAL
LSGWREADRLLSLWAPQVQQPRPRL -> TGLCCRDGGRPT
ASSVCGPRRCSSPGRGSSWAQPTLFHPCRG (in
isoform 11). {ECO:0000303|Ref.2}.
/FTId=VSP_011253.
VAR_SEQ 429 463 FLREHLDTFFDPPLPAEKAEAIRKIGFGTNNKIFL -> LS
TFSVGSLPDLSLSSWRLCRMKKYFCVSPKCSGE (in
isoform 4). {ECO:0000303|Ref.2}.
/FTId=VSP_011255.
VAR_SEQ 435 482 Missing (in isoform 8).
{ECO:0000303|Ref.2}.
/FTId=VSP_011254.
VAR_SEQ 464 649 Missing (in isoform 4).
{ECO:0000303|Ref.2}.
/FTId=VSP_011257.
VAR_SEQ 550 649 GNPRLPAPKSVLRSRWHSAPYTRGSYSYVAVGSTGGDLDLL
AQPLPADGAGAQLQILFAGEATHRTFYSTTHGALLSGWREA
DRLLSLWAPQVQQPRPRL -> APDPVCGGSHTSHVLLHDA
RGSAVGMEGGRPPPQSVGPAGAAAQAQALAGPSLLCSTRVG
GRLGPSFLLTDFSLA (in isoform 5).
{ECO:0000303|Ref.2}.
/FTId=VSP_011258.
CONFLICT 23 23 I -> M (in Ref. 2; AAS64378).
{ECO:0000305}.
CONFLICT 40 40 H -> Q (in Ref. 2; AAS64378).
{ECO:0000305}.
CONFLICT 186 186 A -> T (in Ref. 2; AAS64379).
{ECO:0000305}.
CONFLICT 214 214 R -> Q (in Ref. 1; AAN40706).
{ECO:0000305}.
CONFLICT 223 223 A -> V (in Ref. 1; AAN40706).
{ECO:0000305}.
CONFLICT 376 376 E -> G (in Ref. 2; AAS64376).
{ECO:0000305}.
CONFLICT 396 396 E -> K (in Ref. 2; AAS64373).
{ECO:0000305}.
CONFLICT 502 502 L -> F (in Ref. 2; AAS64381).
{ECO:0000305}.
CONFLICT 506 506 V -> G (in Ref. 1; AAN40706).
{ECO:0000305}.
CONFLICT 551 551 N -> S (in Ref. 2; AAS64379).
{ECO:0000305}.
SEQUENCE 649 AA; 70290 MW; D332E2AA7242F609 CRC64;
MESTGSVGEA PGGPRVLVVG GGIAGLGAAQ RLCGHSAFPH LRVLEATARA GGRIRSERCF
GGVVEVGAHW IHGPSRGNPV FQLAAEYGLL GEKELSQENQ LVETGGHVGL PSVSYASSGT
SVSLQLVAEM ATLFYGLIDQ TREFLHAAET PVPSVGEYLK KEIGQHVARL CGHSAFPHLR
VLEATARAGG RIRSERCFGG VVEVGAHWIH GPSRGNPVFQ LAAEYGLLGE KELSQENQLV
ETGGHVGLPS VSYASSGASV SLQLVAEMAT LFYGLIDQTR EFLHAAETPV PSVGEYLKKE
IGQHVAGWTE DEETRKLKLA VLNSFFNLEC CVSGTHSMDL VALAPFGEYT VLPGLDCTFS
KGYQGLTNCM MAALPEDTVV FEKPVKTIHW NGSFQEAAFP GETFPVSVEC EDGDRFPAHH
VIVTVPLGFL REHLDTFFDP PLPAEKAEAI RKIGFGTNNK IFLEFEEPFW EPDCQLIQLV
WEDTSPLEDA APELQDAWFR KLIGFVVLPA FASVHVLCGF IAGLESEFME TLSDEEVLLC
LTQVLRRVTG NPRLPAPKSV LRSRWHSAPY TRGSYSYVAV GSTGGDLDLL AQPLPADGAG
AQLQILFAGE ATHRTFYSTT HGALLSGWRE ADRLLSLWAP QVQQPRPRL


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