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Sterile alpha motif domain-containing protein 9 (SAM domain-containing protein 9)

 SAMD9_HUMAN             Reviewed;        1589 AA.
Q5K651; A2RU68; Q5K649; Q6P080; Q75N21; Q8IVG6; Q9NXS8;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
15-FEB-2005, sequence version 1.
22-NOV-2017, entry version 121.
RecName: Full=Sterile alpha motif domain-containing protein 9;
Short=SAM domain-containing protein 9;
Name=SAMD9; Synonyms=C7orf5, DRIF1, KIAA2004, OEF1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=17407603; DOI=10.1186/1471-2164-8-92;
Li C.F., MacDonald J.R., Wei R.Y., Ray J., Lau K., Kandel C.,
Koffman R., Bell S., Scherer S.W., Alman B.A.;
"Human sterile alpha motif domain 9, a novel gene identified as down-
regulated in aggressive fibromatosis, is absent in the mouse.";
BMC Genomics 8:92-92(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Aortic endothelium;
Nagase T., Kikuno R., Ohara O.;
"The nucleotide sequence of a long cDNA clone isolated from human.";
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum, and Testis;
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 955-1589.
TISSUE=Colon;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
FUNCTION, INDUCTION, AND VARIANT NFTC GLU-1495.
PubMed=18094730; DOI=10.1038/sj.jid.5701203;
Chefetz I., Ben Amitai D., Browning S., Skorecki K., Adir N.,
Thomas M.G., Kogleck L., Topaz O., Indelman M., Uitto J., Richard G.,
Bradman N., Sprecher E.;
"Normophosphatemic familial tumoral calcinosis is caused by
deleterious mutations in SAMD9, encoding a TNF-alpha responsive
protein.";
J. Invest. Dermatol. 128:1423-1429(2008).
[9]
FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT NFTC
GLU-1495, AND CHARACTERIZATION OF VARIANT NFTC GLU-1495.
PubMed=16960814; DOI=10.1086/508069;
Topaz O., Indelman M., Chefetz I., Geiger D., Metzker A.,
Altschuler Y., Choder M., Bercovich D., Uitto J., Bergman R.,
Richard G., Sprecher E.;
"A deleterious mutation in SAMD9 causes normophosphatemic familial
tumoral calcinosis.";
Am. J. Hum. Genet. 79:759-764(2006).
[10]
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).
[11]
FUNCTION, INDUCTION BY IFNG, AND INTERACTION WITH RGL2.
PubMed=21160498; DOI=10.1038/jid.2010.387;
Hershkovitz D., Gross Y., Nahum S., Yehezkel S., Sarig O., Uitto J.,
Sprecher E.;
"Functional characterization of SAMD9, a protein deficient in
normophosphatemic familial tumoral calcinosis.";
J. Invest. Dermatol. 131:662-669(2011).
[12]
FUNCTION IN ENDOSOME FUSION, AND INTERACTION WITH EEA1.
PubMed=24029230; DOI=10.1016/j.ccr.2013.08.011;
Nagamachi A., Matsui H., Asou H., Ozaki Y., Aki D., Kanai A.,
Takubo K., Suda T., Nakamura T., Wolff L., Honda H., Inaba T.;
"Haploinsufficiency of SAMD9L, an endosome fusion facilitator, causes
myeloid malignancies in mice mimicking human diseases with monosomy
7.";
Cancer Cell 24:305-317(2013).
[13]
INVOLVEMENT IN MIRAGE, VARIANTS MIRAGE GLN-459; ASN-769; TYR-834;
LYS-974; VAL-1195; LEU-1280; LYS-1286 AND TRP-1293, AND
CHARACTERIZATION OF VARIANTS MIRAGE GLN-459; ASN-769; TYR-834;
LYS-974; VAL-1195; LEU-1280; LYS-1286 AND TRP-1293.
PubMed=27182967; DOI=10.1038/ng.3569;
Narumi S., Amano N., Ishii T., Katsumata N., Muroya K., Adachi M.,
Toyoshima K., Tanaka Y., Fukuzawa R., Miyako K., Kinjo S., Ohga S.,
Ihara K., Inoue H., Kinjo T., Hara T., Kohno M., Yamada S., Urano H.,
Kitagawa Y., Tsugawa K., Higa A., Miyawaki M., Okutani T., Kizaki Z.,
Hamada H., Kihara M., Shiga K., Yamaguchi T., Kenmochi M.,
Kitajima H., Fukami M., Shimizu A., Kudoh J., Shibata S., Okano H.,
Miyake N., Matsumoto N., Hasegawa T.;
"SAMD9 mutations cause a novel multisystem disorder, MIRAGE syndrome,
and are associated with loss of chromosome 7.";
Nat. Genet. 48:792-797(2016).
-!- FUNCTION: May play a role in the inflammatory response to tissue
injury and the control of extra-osseous calcification, acting as a
downstream target of TNF-alpha signaling. Involved in the
regulation of EGR1, in coordination with RGL2. May be involved in
endosome fusion. {ECO:0000269|PubMed:16960814,
ECO:0000269|PubMed:18094730, ECO:0000269|PubMed:21160498,
ECO:0000269|PubMed:24029230}.
-!- SUBUNIT: Interacts with RGL2 (PubMed:21160498). Interacts with
EEA1 (PubMed:24029230). {ECO:0000269|PubMed:21160498,
ECO:0000269|PubMed:24029230}.
-!- INTERACTION:
Q15075:EEA1; NbExp=2; IntAct=EBI-2814750, EBI-298113;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16960814,
ECO:0000269|PubMed:17407603}.
-!- TISSUE SPECIFICITY: Widely expressed. Very low levels are detected
in skeletal muscle. Not detected in brain. Down-regulated in
aggressive fibromatosis, as well as in breast and colon cancers.
Up-regulated in fibroblasts from patients with normophosphatemic
tumoral calcinosis (NFTC). {ECO:0000269|PubMed:16960814,
ECO:0000269|PubMed:17407603}.
-!- INDUCTION: Up-regulated by TNF-alpha through p38 MAPKs and NF-
kappa-B. Up-regulated by osmotic shock. Induced by IFNG.
{ECO:0000269|PubMed:18094730, ECO:0000269|PubMed:21160498}.
-!- DISEASE: Tumoral calcinosis, normophosphatemic, familial (NFTC)
[MIM:610455]: An uncommon, life-threatening disorder characterized
by progressive deposition of calcified masses in cutaneous and
subcutaneous tissues. Serum phosphate levels are normal. Clinical
features include painful calcified ulcerative lesions and massive
calcium deposition in the mid- and lower dermis, severe skin and
bone infections, erythematous papular skin eruption in infancy,
conjunctivitis, and gingivitis. NFTC shows a striking resemblance
to acquired dystrophic calcinosis, in which tissue calcification
occurs as a consequence of tissue injury/inflammation.
{ECO:0000269|PubMed:16960814, ECO:0000269|PubMed:18094730}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: MIRAGE syndrome (MIRAGE) [MIM:617053]: A form of
syndromic adrenal hypoplasia characterized by myelodysplasia,
infection, restriction of growth, adrenal hypoplasia, genital
phenotypes, and enteropathy. {ECO:0000269|PubMed:27182967}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAH65769.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAQ04689.3; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
Sequence=BAA90932.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC23101.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF445355; AAQ04637.1; -; mRNA.
EMBL; AF453311; AAQ04689.3; ALT_SEQ; mRNA.
EMBL; AB095925; BAC23101.1; ALT_INIT; mRNA.
EMBL; AC000119; AAQ96842.1; -; Genomic_DNA.
EMBL; CH236949; EAL24145.1; -; Genomic_DNA.
EMBL; CH471091; EAW76826.1; -; Genomic_DNA.
EMBL; BC065769; AAH65769.1; ALT_SEQ; mRNA.
EMBL; BC132773; AAI32774.1; -; mRNA.
EMBL; BC132775; AAI32776.1; -; mRNA.
EMBL; BC150249; AAI50250.1; -; mRNA.
EMBL; AK000080; BAA90932.1; ALT_INIT; mRNA.
CCDS; CCDS34680.1; -.
RefSeq; NP_001180236.1; NM_001193307.1.
RefSeq; NP_060124.2; NM_017654.3.
UniGene; Hs.65641; -.
ProteinModelPortal; Q5K651; -.
BioGrid; 120166; 12.
IntAct; Q5K651; 8.
STRING; 9606.ENSP00000369292; -.
iPTMnet; Q5K651; -.
PhosphoSitePlus; Q5K651; -.
BioMuta; SAMD9; -.
DMDM; 71153739; -.
EPD; Q5K651; -.
MaxQB; Q5K651; -.
PaxDb; Q5K651; -.
PeptideAtlas; Q5K651; -.
PRIDE; Q5K651; -.
Ensembl; ENST00000379958; ENSP00000369292; ENSG00000205413.
Ensembl; ENST00000620985; ENSP00000484636; ENSG00000205413.
GeneID; 54809; -.
KEGG; hsa:54809; -.
UCSC; uc003umf.4; human.
CTD; 54809; -.
DisGeNET; 54809; -.
EuPathDB; HostDB:ENSG00000205413.7; -.
GeneCards; SAMD9; -.
HGNC; HGNC:1348; SAMD9.
HPA; HPA021318; -.
HPA; HPA021319; -.
MalaCards; SAMD9; -.
MIM; 610455; phenotype.
MIM; 610456; gene.
MIM; 617053; phenotype.
neXtProt; NX_Q5K651; -.
OpenTargets; ENSG00000205413; -.
Orphanet; 306658; Normocalcemic tumoral calcinosis.
PharmGKB; PA25948; -.
eggNOG; ENOG410IETT; Eukaryota.
eggNOG; ENOG41124X3; LUCA.
GeneTree; ENSGT00390000013973; -.
HOVERGEN; HBG080713; -.
InParanoid; Q5K651; -.
OMA; CAFYQDL; -.
OrthoDB; EOG091G00BC; -.
PhylomeDB; Q5K651; -.
TreeFam; TF331842; -.
ChiTaRS; SAMD9; human.
GeneWiki; SAMD9; -.
GenomeRNAi; 54809; -.
PRO; PR:Q5K651; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000205413; -.
CleanEx; HS_SAMD9; -.
ExpressionAtlas; Q5K651; baseline and differential.
Genevisible; Q5K651; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005769; C:early endosome; IBA:GO_Central.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0034058; P:endosomal vesicle fusion; IDA:UniProtKB.
Gene3D; 1.25.40.10; -; 1.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR011990; TPR-like_helical_dom_sf.
Pfam; PF07647; SAM_2; 1.
SMART; SM00454; SAM; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Disease mutation; Polymorphism;
Reference proteome.
CHAIN 1 1589 Sterile alpha motif domain-containing
protein 9.
/FTId=PRO_0000097573.
DOMAIN 14 78 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
VARIANT 143 143 I -> T (in dbSNP:rs6969691).
/FTId=VAR_031526.
VARIANT 449 449 N -> S (in dbSNP:rs10239435).
/FTId=VAR_031527.
VARIANT 459 459 R -> Q (in MIRAGE; decreased cell
proliferation; changed endosome
organization).
{ECO:0000269|PubMed:27182967}.
/FTId=VAR_077885.
VARIANT 549 549 V -> L (in dbSNP:rs10279499).
/FTId=VAR_031528.
VARIANT 769 769 D -> N (in MIRAGE; decreased cell
proliferation; changed endosome
organization).
{ECO:0000269|PubMed:27182967}.
/FTId=VAR_077886.
VARIANT 834 834 N -> Y (in MIRAGE; decreased cell
proliferation; changed endosome
organization).
{ECO:0000269|PubMed:27182967}.
/FTId=VAR_077887.
VARIANT 974 974 E -> K (in MIRAGE; decreased cell
proliferation; changed endosome
organization).
{ECO:0000269|PubMed:27182967}.
/FTId=VAR_077888.
VARIANT 1195 1195 A -> V (in MIRAGE; decreased cell
proliferation; changed endosome
organization).
{ECO:0000269|PubMed:27182967}.
/FTId=VAR_077889.
VARIANT 1280 1280 P -> L (in MIRAGE; decreased cell
proliferation; changed endosome
organization).
{ECO:0000269|PubMed:27182967}.
/FTId=VAR_077890.
VARIANT 1286 1286 Q -> K (in MIRAGE; decreased cell
proliferation; changed endosome
organization).
{ECO:0000269|PubMed:27182967}.
/FTId=VAR_077891.
VARIANT 1293 1293 R -> W (in MIRAGE; decreased cell
proliferation; changed endosome
organization).
{ECO:0000269|PubMed:27182967}.
/FTId=VAR_077813.
VARIANT 1495 1495 K -> E (in NFTC; loss of cytoplasmic
expression; dbSNP:rs121918554).
{ECO:0000269|PubMed:16960814,
ECO:0000269|PubMed:18094730}.
/FTId=VAR_031529.
CONFLICT 1577 1577 S -> P (in Ref. 7; BAA90932).
{ECO:0000305}.
SEQUENCE 1589 AA; 184281 MW; CF3EF341ED092167 CRC64;
MAKQLNLPEN TDDWTKEDVN QWLESHKIDQ KHREILTEQD VNGAVLKWLK KEHLVDMGIT
HGPAIQIEEL FKELRKTAIE DSIQTSKMGK PSKNAPKDQT VSQKERRETS KQKQKGKENP
DMANPSAMST TAKGSKSLKV ELIEDKIDYT KERQPSIDLT CVSYPFDEFS NPYRYKLDFS
LQPETGPGNL IDPIHEFKAF TNTATATEED VKMKFSNEVF RFASACMNSR TNGTIHFGVK
DKPHGKIVGI KVTNDTKEAL INHFNLMINK YFEDHQVQQA KKCIREPRFV EVLLPNSTLS
DRFVIEVDII PQFSECQYDY FQIKMQNYNN KIWEQSKKFS LFVRDGTSSK DITKNKVDFR
AFKADFKTLA ESRKAAEEKF RAKTNKKERE GPKLVKLLTG NQDLLDNSYY EQYILVTNKC
HPDQTKHLDF LKEIKWFAVL EFDPESNING VVKAYKESRV ANLHFPSVYV EQKTTPNETI
STLNLYHQPS WIFCNGRLDL DSEKYKPFDP SSWQRERASD VRKLISFLTH EDIMPRGKFL
VVFLLLSSVD DPRDPLIETF CAFYQDLKGM ENILCICVHP HIFQGWKDLL EARLIKHQDE
ISSQCISALS LEEINGTILK LKSVTQSSKR LLPSIGLSTV LLKKEEDIMT ALEIICENEC
EGTLLEKDKN KFLEFKASKE EDFYRGGKVS WWNFYFSSES YSSPFVKRDK YERLEAMIQN
CADSSKPTST KIIHLYHHPG CGGTTLAMHI LWELRKKFRC AVLKNKTVDF SEIGEQVTSL
ITYGAMNRQE YVPVLLLVDD FEEQDNVYLL QYSIQTAIAK KYIRYEKPLV IILNCMRSQN
PEKSARIPDS IAVIQQLSPK EQRAFELKLK EIKEQHKNFE DFYSFMIMKT NFNKEYIENV
VRNILKGQNI FTKEAKLFSF LALLNSYVPD TTISLSQCEK FLGIGNKKAF WGTEKFEDKM
GTYSTILIKT EVIECGNYCG VRIIHSLIAE FSLEELKKSY HLNKSQIMLD MLTENLFFDT
GMGKSKFLQD MHTLLLTRHR DEHEGETGNW FSPFIEALHK DEGNEAVEAV LLESIHRFNP
NAFICQALAR HFYIKKKDFG NALNWAKQAK IIEPDNSYIS DTLGQVYKSK IRWWIEENGG
NGNISVDDLI ALLDLAEHAS SAFKESQQQS EDREYEVKER LYPKSKRRYD TYNIAGYQGE
IEVGLYTIQI LQLIPFFDNK NELSKRYMVN FVSGSSDIPG DPNNEYKLAL KNYIPYLTKL
KFSLKKSFDF FDEYFVLLKP RNNIKQNEEA KTRRKVAGYF KKYVDIFCLL EESQNNTGLG
SKFSEPLQVE RCRRNLVALK ADKFSGLLEY LIKSQEDAIS TMKCIVNEYT FLLEQCTVKI
QSKEKLNFIL ANIILSCIQP TSRLVKPVEK LKDQLREVLQ PIGLTYQFSE PYFLASLLFW
PENQQLDQHS EQMKEYAQAL KNSFKGQYKH MHRTKQPIAY FFLGKGKRLE RLVHKGKIDQ
CFKKTPDINS LWQSGDVWKE EKVQELLLRL QGRAENNCLY IEYGINEKIT IPITPAFLGQ
LRSGRSIEKV SFYLGFSIGG PLAYDIEIV


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