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A disintegrin and metalloproteinase with thrombospondin motifs 9 (ADAM-TS 9) (ADAM-TS9) (ADAMTS-9) (EC 3.4.24.-)

 ATS9_HUMAN              Reviewed;        1935 AA.
Q9P2N4; A1L4L0; B7ZVX9; B9ZVN0; Q9NR29;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
04-NOV-2008, sequence version 4.
28-MAR-2018, entry version 170.
RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 9;
Short=ADAM-TS 9;
Short=ADAM-TS9;
Short=ADAMTS-9;
EC=3.4.24.- {ECO:0000269|PubMed:12514189};
Flags: Precursor;
Name=ADAMTS9; Synonyms=KIAA1312;
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 3).
TISSUE=Fetus;
PubMed=10936055; DOI=10.1006/geno.2000.6246;
Clark M.E., Kelner G.S., Turbeville L.A., Boyer A., Arden K.A.,
Maki R.A.;
"ADAMTS 9, a novel member of the ADAM-TS/Metallospondin gene family.";
Genomics 67:343-350(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PROTEOLYTIC CLEAVAGE,
GLYCOSYLATION, MUTAGENESIS OF ARG-33; ARG-74; ARG-280 AND ARG-287, AND
VARIANTS PRO-96 AND GLU-1674.
PubMed=12514189; DOI=10.1074/jbc.M211009200;
Somerville R.P., Longpre J.-M., Jungers K.A., Engle J.M., Ross M.,
Evanko S., Wight T.N., Leduc R., Apte S.S.;
"Characterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS
subfamily related to Caenorhabditis elegans GON-1.";
J. Biol. Chem. 278:9503-9513(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 159-1935 (ISOFORM 2).
TISSUE=Brain;
PubMed=10718198; DOI=10.1093/dnares/7.1.65;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVI.
The complete sequences of 150 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:65-73(2000).
[6]
FUNCTION IN TRANSPORT, AND SUBCELLULAR LOCATION.
PubMed=22419820; DOI=10.1091/mbc.E11-10-0857;
Yoshina S., Sakaki K., Yonezumi-Hayashi A., Gengyo-Ando K., Inoue H.,
Iino Y., Mitani S.;
"Identification of a novel ADAMTS9/GON-1 function for protein
transport from the ER to the Golgi.";
Mol. Biol. Cell 23:1728-1741(2012).
-!- FUNCTION: Cleaves the large aggregating proteoglycans, aggrecan
(at the '1838-Glu-|-Ala-1839' site) and versican (at the '1428-
Glu-|-Ala-1429' site). Has a protease-independent function in
promoting the transport from the endoplasmic reticulum to the
Golgi apparatus of a variety of secretory cargos.
{ECO:0000269|PubMed:12514189, ECO:0000269|PubMed:22419820}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:Q9UHI8};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9UHI8};
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000269|PubMed:12514189}. Endoplasmic reticulum
{ECO:0000269|PubMed:22419820}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=ADAMTS-9B;
IsoId=Q9P2N4-3; Sequence=Displayed;
Name=2; Synonyms=Long;
IsoId=Q9P2N4-1; Sequence=VSP_007548, VSP_007549;
Note=May result from the retention of an intron in the cDNA
leading to a prematurate stop codon.;
Name=3; Synonyms=Short;
IsoId=Q9P2N4-2; Sequence=VSP_005499, VSP_005500;
Name=4;
IsoId=Q9P2N4-4; Sequence=VSP_053399;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in all fetal tissues.
Expressed in a number of adult tissues with highest expression in
heart, placenta and skeletal muscle.
{ECO:0000269|PubMed:12514189}.
-!- DOMAIN: The spacer domain and the TSP type-1 domains are important
for a tight interaction with the extracellular matrix.
{ECO:0000250}.
-!- DOMAIN: The ancillary domains, including the TSRs domain, are
required for specific extracellular localization and for its
versicanase and aggrecanase activities.
-!- DOMAIN: The conserved cysteine present in the cysteine-switch
motif binds the catalytic zinc ion, thus inhibiting the enzyme.
The dissociation of the cysteine from the zinc ion upon the
activation-peptide release activates the enzyme.
-!- DOMAIN: The GON domain mediates protease-independent function in
ER to Golgi transport.
-!- PTM: The precursor is cleaved by a furin endopeptidase.
{ECO:0000269|PubMed:12514189}.
-!- PTM: N-glycosylated (PubMed:12514189). Can be O-fucosylated by
POFUT2 on a serine or a threonine residue found within the
consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat
domains where C1 and C2 are the first and second cysteine residue
of the repeat, respectively. Fucosylated repeats can then be
further glycosylated by the addition of a beta-1,3-glucose residue
by the glucosyltransferase, B3GALTL. Fucosylation mediates the
efficient secretion of ADAMTS family members. Also can be C-
glycosylated with one or two mannose molecules on tryptophan
residues within the consensus sequence W-X-X-W of the TPRs, and N-
glycosylated. These other glycosylations can also facilitate
secretion (By similarity). {ECO:0000250|UniProtKB:Q76LX8,
ECO:0000269|PubMed:12514189}.
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EMBL; AF261918; AAF89106.1; -; mRNA.
EMBL; AF488803; AAO15765.1; -; mRNA.
EMBL; AC096888; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC122178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC130578; AAI30579.1; -; mRNA.
EMBL; BC171764; AAI71764.1; -; mRNA.
EMBL; AB037733; BAA92550.1; -; mRNA.
CCDS; CCDS2903.1; -. [Q9P2N4-3]
CCDS; CCDS82801.1; -. [Q9P2N4-4]
RefSeq; NP_001305710.1; NM_001318781.1. [Q9P2N4-4]
RefSeq; NP_891550.1; NM_182920.1. [Q9P2N4-3]
UniGene; Hs.656071; -.
ProteinModelPortal; Q9P2N4; -.
SMR; Q9P2N4; -.
IntAct; Q9P2N4; 1.
STRING; 9606.ENSP00000418735; -.
MEROPS; M12.021; -.
iPTMnet; Q9P2N4; -.
PhosphoSitePlus; Q9P2N4; -.
BioMuta; ADAMTS9; -.
DMDM; 212276516; -.
PaxDb; Q9P2N4; -.
PeptideAtlas; Q9P2N4; -.
PRIDE; Q9P2N4; -.
Ensembl; ENST00000295903; ENSP00000295903; ENSG00000163638. [Q9P2N4-4]
Ensembl; ENST00000498707; ENSP00000418735; ENSG00000163638. [Q9P2N4-3]
GeneID; 56999; -.
KEGG; hsa:56999; -.
UCSC; uc003dmg.4; human. [Q9P2N4-3]
CTD; 56999; -.
DisGeNET; 56999; -.
EuPathDB; HostDB:ENSG00000163638.13; -.
GeneCards; ADAMTS9; -.
HGNC; HGNC:13202; ADAMTS9.
HPA; HPA028567; -.
HPA; HPA028577; -.
HPA; HPA028601; -.
MIM; 605421; gene.
neXtProt; NX_Q9P2N4; -.
OpenTargets; ENSG00000163638; -.
PharmGKB; PA24553; -.
eggNOG; KOG3538; Eukaryota.
eggNOG; ENOG410XPKZ; LUCA.
GeneTree; ENSGT00900000140774; -.
HOGENOM; HOG000004798; -.
HOVERGEN; HBG037334; -.
InParanoid; Q9P2N4; -.
KO; K08624; -.
OMA; GTFNTVH; -.
OrthoDB; EOG091G00AX; -.
PhylomeDB; Q9P2N4; -.
TreeFam; TF331949; -.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-5083635; Defective B3GALTL causes Peters-plus syndrome (PpS).
Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
ChiTaRS; ADAMTS9; human.
GeneWiki; ADAMTS9; -.
GenomeRNAi; 56999; -.
PMAP-CutDB; Q9P2N4; -.
PRO; PR:Q9P2N4; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000163638; -.
CleanEx; HS_ADAMTS9; -.
ExpressionAtlas; Q9P2N4; baseline and differential.
Genevisible; Q9P2N4; HS.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:MGI.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0008237; F:metallopeptidase activity; IDA:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0035909; P:aorta morphogenesis; ISS:BHF-UCL.
GO; GO:0090673; P:endothelial cell-matrix adhesion; ISS:BHF-UCL.
GO; GO:0030198; P:extracellular matrix organization; ISS:BHF-UCL.
GO; GO:0006516; P:glycoprotein catabolic process; TAS:ProtInc.
GO; GO:0003179; P:heart valve morphogenesis; ISS:BHF-UCL.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:0010596; P:negative regulation of endothelial cell migration; ISS:BHF-UCL.
GO; GO:1903671; P:negative regulation of sprouting angiogenesis; ISS:BHF-UCL.
GO; GO:0045636; P:positive regulation of melanocyte differentiation; IEA:Ensembl.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0006508; P:proteolysis; IDA:MGI.
GO; GO:0003229; P:ventricular cardiac muscle tissue development; ISS:BHF-UCL.
GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
Gene3D; 2.20.100.10; -; 13.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR010294; ADAM_spacer1.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR012314; Pept_M12B_GON-ADAMTSs.
InterPro; IPR001590; Peptidase_M12B.
InterPro; IPR002870; Peptidase_M12B_N.
InterPro; IPR000884; TSP1_rpt.
InterPro; IPR036383; TSP1_rpt_sf.
Pfam; PF05986; ADAM_spacer1; 1.
Pfam; PF08685; GON; 1.
Pfam; PF01562; Pep_M12B_propep; 1.
Pfam; PF01421; Reprolysin; 1.
Pfam; PF00090; TSP_1; 13.
SMART; SM00209; TSP1; 15.
SUPFAM; SSF82895; SSF82895; 14.
PROSITE; PS50215; ADAM_MEPRO; 1.
PROSITE; PS51046; GON; 1.
PROSITE; PS50092; TSP1; 14.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
Alternative splicing; Cleavage on pair of basic residues;
Complete proteome; Disulfide bond; Endoplasmic reticulum;
ER-Golgi transport; Extracellular matrix; Glycoprotein; Hydrolase;
Metal-binding; Metalloprotease; Polymorphism; Protease;
Protein transport; Reference proteome; Repeat; Secreted; Signal;
Transport; Zinc; Zymogen.
SIGNAL 1 18 {ECO:0000255}.
PROPEP 19 287 {ECO:0000269|PubMed:12514189}.
/FTId=PRO_0000029182.
CHAIN 288 1935 A disintegrin and metalloproteinase with
thrombospondin motifs 9.
/FTId=PRO_0000029183.
DOMAIN 293 499 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 509 587 Disintegrin.
DOMAIN 588 643 TSP type-1 1. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 878 936 TSP type-1 2. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 939 997 TSP type-1 3. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 998 1049 TSP type-1 4. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1052 1109 TSP type-1 5. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1110 1166 TSP type-1 6. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1182 1240 TSP type-1 7. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1241 1296 TSP type-1 8. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1328 1379 TSP type-1 9. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1382 1440 TSP type-1 10. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1441 1494 TSP type-1 11. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1497 1555 TSP type-1 12. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1556 1611 TSP type-1 13. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1612 1676 TSP type-1 14. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1677 1734 TSP type-1 15. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1735 1935 GON. {ECO:0000255|PROSITE-
ProRule:PRU00383}.
REGION 753 877 Spacer.
MOTIF 221 228 Cysteine switch. {ECO:0000250}.
COMPBIAS 88 96 Poly-Ser.
COMPBIAS 644 752 Cys-rich.
ACT_SITE 435 435 {ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 223 223 Zinc; in inhibited form. {ECO:0000250}.
METAL 434 434 Zinc; catalytic. {ECO:0000250}.
METAL 438 438 Zinc; catalytic. {ECO:0000250}.
METAL 444 444 Zinc; catalytic. {ECO:0000250}.
SITE 287 288 Cleavage. {ECO:0000269|PubMed:12514189}.
CARBOHYD 112 112 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 135 135 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 271 271 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 749 749 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 840 840 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1213 1213 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1267 1267 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1788 1788 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1806 1806 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 368 418 {ECO:0000250}.
DISULFID 394 400 {ECO:0000250}.
DISULFID 412 494 {ECO:0000250}.
DISULFID 450 478 {ECO:0000250}.
DISULFID 521 543 {ECO:0000250}.
DISULFID 532 553 {ECO:0000250}.
DISULFID 538 572 {ECO:0000250}.
DISULFID 566 577 {ECO:0000250}.
DISULFID 600 637 {ECO:0000250}.
DISULFID 604 642 {ECO:0000250}.
DISULFID 615 627 {ECO:0000250}.
DISULFID 890 931 {ECO:0000250}.
DISULFID 894 935 {ECO:0000250}.
DISULFID 904 918 {ECO:0000250}.
DISULFID 1250 1290 {ECO:0000250}.
DISULFID 1254 1295 {ECO:0000250}.
DISULFID 1265 1278 {ECO:0000250}.
DISULFID 1624 1670 {ECO:0000250}.
DISULFID 1628 1675 {ECO:0000250}.
DISULFID 1639 1659 {ECO:0000250}.
VAR_SEQ 324 351 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_053399.
VAR_SEQ 1064 1072 CLVTCGKGH -> VRWEGCYFP (in isoform 3).
{ECO:0000303|PubMed:10936055}.
/FTId=VSP_005499.
VAR_SEQ 1073 1935 Missing (in isoform 3).
{ECO:0000303|PubMed:10936055}.
/FTId=VSP_005500.
VAR_SEQ 1624 1629 CSVTCG -> VPSWEL (in isoform 2).
{ECO:0000303|PubMed:10718198}.
/FTId=VSP_007548.
VAR_SEQ 1630 1935 Missing (in isoform 2).
{ECO:0000303|PubMed:10718198}.
/FTId=VSP_007549.
VARIANT 96 96 S -> P (in dbSNP:rs36115950).
{ECO:0000269|PubMed:12514189}.
/FTId=VAR_047081.
VARIANT 96 96 S -> T (in dbSNP:rs36115950).
/FTId=VAR_051592.
VARIANT 1579 1579 K -> E (in dbSNP:rs17071010).
/FTId=VAR_047082.
VARIANT 1674 1674 D -> E (in dbSNP:rs6787633).
{ECO:0000269|PubMed:12514189}.
/FTId=VAR_047083.
VARIANT 1740 1740 K -> R (in dbSNP:rs17070967).
/FTId=VAR_047084.
VARIANT 1791 1791 E -> Q (in dbSNP:rs3796381).
/FTId=VAR_047085.
VARIANT 1921 1921 K -> E (in dbSNP:rs17070909).
/FTId=VAR_051593.
VARIANT 1933 1933 R -> Q (in dbSNP:rs17070905).
/FTId=VAR_047086.
MUTAGEN 33 33 R->A: No effect on mature form
production.
{ECO:0000269|PubMed:12514189}.
MUTAGEN 74 74 R->A: No effect on mature form
production.
{ECO:0000269|PubMed:12514189}.
MUTAGEN 280 280 R->A: No effect on mature form
production.
{ECO:0000269|PubMed:12514189}.
MUTAGEN 287 287 R->A: No mature form produced.
{ECO:0000269|PubMed:12514189}.
CONFLICT 46 46 S -> G (in Ref. 1; AAF89106).
{ECO:0000305}.
CONFLICT 182 182 D -> G (in Ref. 2; AAO15765).
{ECO:0000305}.
CONFLICT 367 367 F -> L (in Ref. 1; AAF89106).
{ECO:0000305}.
CONFLICT 1117 1117 G -> V (in Ref. 2; AAO15765).
{ECO:0000305}.
SEQUENCE 1935 AA; 216491 MW; 150B78D4C5CC2CCC CRC64;
MQFVSWATLL TLLVRDLAEM GSPDAAAAVR KDRLHPRQVK LLETLSEYEI VSPIRVNALG
EPFPTNVHFK RTRRSINSAT DPWPAFASSS SSSTSSQAHY RLSAFGQQFL FNLTANAGFI
APLFTVTLLG TPGVNQTKFY SEEEAELKHC FYKGYVNTNS EHTAVISLCS GMLGTFRSHD
GDYFIEPLQS MDEQEDEEEQ NKPHIIYRRS APQREPSTGR HACDTSEHKN RHSKDKKKTR
ARKWGERINL AGDVAALNSG LATEAFSAYG NKTDNTREKR THRRTKRFLS YPRFVEVLVV
ADNRMVSYHG ENLQHYILTL MSIVASIYKD PSIGNLINIV IVNLIVIHNE QDGPSISFNA
QTTLKNFCQW QHSKNSPGGI HHDTAVLLTR QDICRAHDKC DTLGLAELGT ICDPYRSCSI
SEDSGLSTAF TIAHELGHVF NMPHDDNNKC KEEGVKSPQH VMAPTLNFYT NPWMWSKCSR
KYITEFLDTG YGECLLNEPE SRPYPLPVQL PGILYNVNKQ CELIFGPGSQ VCPYMMQCRR
LWCNNVNGVH KGCRTQHTPW ADGTECEPGK HCKYGFCVPK EMDVPVTDGS WGSWSPFGTC
SRTCGGGIKT AIRECNRPEP KNGGKYCVGR RMKFKSCNTE PCLKQKRDFR DEQCAHFDGK
HFNINGLLPN VRWVPKYSGI LMKDRCKLFC RVAGNTAYYQ LRDRVIDGTP CGQDTNDICV
QGLCRQAGCD HVLNSKARRD KCGVCGGDNS SCKTVAGTFN TVHYGYNTVV RIPAGATNID
VRQHSFSGET DDDNYLALSS SKGEFLLNGN FVVTMAKREI RIGNAVVEYS GSETAVERIN
STDRIEQELL LQVLSVGKLY NPDVRYSFNI PIEDKPQQFY WNSHGPWQAC SKPCQGERKR
KLVCTRESDQ LTVSDQRCDR LPQPGHITEP CGTDCDLRWH VASRSECSAQ CGLGYRTLDI
YCAKYSRLDG KTEKVDDGFC SSHPKPSNRE KCSGECNTGG WRYSAWTECS KSCDGGTQRR
RAICVNTRND VLDDSKCTHQ EKVTIQRCSE FPCPQWKSGD WSECLVTCGK GHKHRQVWCQ
FGEDRLNDRM CDPETKPTSM QTCQQPECAS WQAGPWGQCS VTCGQGYQLR AVKCIIGTYM
SVVDDNDCNA ATRPTDTQDC ELPSCHPPPA APETRRSTYS APRTQWRFGS WTPCSATCGK
GTRMRYVSCR DENGSVADES ACATLPRPVA KEECSVTPCG QWKALDWSSC SVTCGQGRAT
RQVMCVNYSD HVIDRSECDQ DYIPETDQDC SMSPCPQRTP DSGLAQHPFQ NEDYRPRSAS
PSRTHVLGGN QWRTGPWGAC SSTCAGGSQR RVVVCQDENG YTANDCVERI KPDEQRACES
GPCPQWAYGN WGECTKLCGG GIRTRLVVCQ RSNGERFPDL SCEILDKPPD REQCNTHACP
HDAAWSTGPW SSCSVSCGRG HKQRNVYCMA KDGSHLESDY CKHLAKPHGH RKCRGGRCPK
WKAGAWSQCS VSCGRGVQQR HVGCQIGTHK IARETECNPY TRPESERDCQ GPRCPLYTWR
AEEWQECTKT CGEGSRYRKV VCVDDNKNEV HGARCDVSKR PVDRESCSLQ PCEYVWITGE
WSECSVTCGK GYKQRLVSCS EIYTGKENYE YSYQTTINCP GTQPPSVHPC YLRDCPVSAT
WRVGNWGSCS VSCGVGVMQR SVQCLTNEDQ PSHLCHTDLK PEERKTCRNV YNCELPQNCK
EVKRLKGASE DGEYFLMIRG KLLKIFCAGM HSDHPKEYVT LVHGDSENFS EVYGHRLHNP
TECPYNGSRR DDCQCRKDYT AAGFSSFQKI RIDLTSMQII TTDLQFARTS EGHPVPFATA
GDCYSAAKCP QGRFSINLYG TGLSLTESAR WISQGNYAVS DIKKSPDGTR VVGKCGGYCG
KCTPSSGTGL EVRVL


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