ID   CUL9_HUMAN              Reviewed;        2517 AA.
AC   Q8IWT3; O75188; Q5TCY3; Q68CP2; Q68D92; Q8N3W9; Q9BU56;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   05-OCT-2010, entry version 86.
DE   RecName: Full=Cullin-9;
DE            Short=CUL-9;
DE   AltName: Full=UbcH7-associated protein 1;
DE   AltName: Full=p53-associated parkin-like cytoplasmic protein;
GN   Name=CUL9; Synonyms=H7AP1, KIAA0708, PARC;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 786-791;
RP   2419-2431 AND 2432-2445, AND INTERACTION WITH TP53.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=12526791; DOI=10.1016/S0092-8674(02)01255-2;
RA   Nikolaev A.Y., Li M., Puskas N., Qin J., Gu W.;
RT   "Parc: a cytoplasmic anchor for p53.";
RL   Cell 112:29-40(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RA   Rose S.A., Ardley H.C., Tan N.G., Scott G.B., Markham A.F.,
RA   Robinson P.A.;
RT   "UbcH7 associated protein, H7AP1. A new member of the Parkin/Ariadne
RT   E3 ubiquitin Ligase (PAUL) family.";
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Amygdala, and Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22935763; PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-662 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 528-662 (ISOFORMS 1/2).
RC   TISSUE=Chondrocyte, and Thymus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 765-2517 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=98403880; PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA   Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA   Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. X.
RT   The complete sequences of 100 new cDNA clones from brain which can
RT   code for large proteins in vitro.";
RL   DNA Res. 5:169-176(1998).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1554-2517 (ISOFORM 1).
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   INTERACTION WITH UBCH7 AND UBCH8.
RX   MEDLINE=99452997; PubMed=10521492; DOI=10.1074/jbc.274.43.30963;
RA   Moynihan T.P., Ardley H.C., Nuber U., Rose S.A., Jones P.F.,
RA   Markham A.F., Scheffner M., Robinson P.A.;
RT   "The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with RING
RT   finger/IBR motif-containing domains of HHARI and H7-AP1.";
RL   J. Biol. Chem. 274:30963-30968(1999).
RN   [10]
RP   FUNCTION, INTERACTION WITH CUL7; RBX1 AND TP53, AND NEDDYLATION.
RX   PubMed=17332328; DOI=10.1158/0008-5472.CAN-06-3241;
RA   Skaar J.R., Florens L., Tsutsumi T., Arai T., Tron A., Swanson S.K.,
RA   Washburn M.P., DeCaprio J.A.;
RT   "PARC and CUL7 form atypical cullin RING ligase complexes.";
RL   Cancer Res. 67:2006-2014(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-947, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
CC   -!- FUNCTION: Cytoplasmic anchor protein in p53-associated protein
CC       complex. Regulates the subcellular localization of p53 and
CC       subsequent function. Seems to be part of an atypical cullin-RING-
CC       based E3 ubiquitin-protein ligase complex. In vitro, complexes of
CC       CUL9/PARC with either CUL7 or TP53 contain E3 ubiquitin-protein
CC       ligase activity.
CC   -!- SUBUNIT: Forms a complex with TP53/p53 in the cytoplasm of
CC       unstressed cells. Interacts with UBCH7 and UBCH8. Interacts with
CC       CUL7 and RBX1. The CUL7-CUL9 heterodimer seems to interact
CC       specifically with TP53.
CC   -!- INTERACTION:
CC       P12931:SRC; NbExp=1; IntAct=EBI-311123, EBI-621482;
CC       P04637:TP53; NbExp=1; IntAct=EBI-311123, EBI-366083;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8IWT3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8IWT3-3; Sequence=VSP_009573;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues with
CC       highest expression in testis brain and kidney.
CC   -!- DOMAIN: The IBR domain is required for interaction with UBCH7 and
CC       UBCH8.
CC   -!- PTM: In vitro, self-ubiquitination in the presence of E1, E2 and
CC       ubiquitin.
CC   -!- PTM: Neddylated.
CC   -!- SIMILARITY: Belongs to the cullin family.
CC   -!- SIMILARITY: Contains 1 DOC domain.
CC   -!- SIMILARITY: Contains 1 IBR-type zinc finger.
CC   -!- SIMILARITY: Contains 2 RING-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC85207.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC       Sequence=BAC86090.1; Type=Miscellaneous discrepancy; Note=Intron retention;
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DR   EMBL; AY145132; AAN61516.1; -; mRNA.
DR   EMBL; AJ318215; CAC85756.1; -; mRNA.
DR   EMBL; CR749511; CAH18328.1; -; mRNA.
DR   EMBL; CR749841; CAH18696.1; -; mRNA.
DR   EMBL; AL133375; CAI20204.1; -; Genomic_DNA.
DR   EMBL; CH471081; EAX04163.1; -; Genomic_DNA.
DR   EMBL; AK125228; BAC86090.1; ALT_SEQ; mRNA.
DR   EMBL; AK129649; BAC85207.1; ALT_SEQ; mRNA.
DR   EMBL; AB014608; BAA31683.3; -; mRNA.
DR   EMBL; BC002879; AAH02879.2; -; mRNA.
DR   IPI; IPI00402732; -.
DR   IPI; IPI00744001; -.
DR   PIR; T00350; T00350.
DR   RefSeq; NP_055904.1; -.
DR   UniGene; Hs.485434; -.
DR   PDB; 2JUF; NMR; -; A=366-466.
DR   PDBsum; 2JUF; -.
DR   ProteinModelPortal; Q8IWT3; -.
DR   SMR; Q8IWT3; 1302-1953, 2068-2153, 2134-2213, 2231-2281.
DR   IntAct; Q8IWT3; 4.
DR   MINT; MINT-6615845; -.
DR   STRING; Q8IWT3; -.
DR   PhosphoSite; Q8IWT3; -.
DR   PRIDE; Q8IWT3; -.
DR   Ensembl; ENST00000252050; ENSP00000252050; ENSG00000112659.
DR   GeneID; 23113; -.
DR   KEGG; hsa:23113; -.
DR   UCSC; uc003ouj.1; human.
DR   UCSC; uc003ouk.1; human.
DR   UCSC; uc003oum.1; human.
DR   CTD; 23113; -.
DR   GeneCards; GC06P043149; -.
DR   H-InvDB; HIX0005898; -.
DR   HGNC; HGNC:15982; CUL9.
DR   HPA; HPA016434; -.
DR   MIM; 607489; gene.
DR   eggNOG; prNOG05581; -.
DR   PhylomeDB; Q8IWT3; -.
DR   NextBio; 44317; -.
DR   ArrayExpress; Q8IWT3; -.
DR   Bgee; Q8IWT3; -.
DR   Genevestigator; Q8IWT3; -.
DR   GermOnline; ENSG00000112659; Homo sapiens.
DR   GO; GO:0005680; C:anaphase-promoting complex; IEA:InterPro.
DR   GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030071; P:regulation of mitotic metaphase/anaphase tr...; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR004939; Ananphase-promot_cplx_su10_DOC.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR021097; CPH_domain.
DR   InterPro; IPR016157; Cullin_CS.
DR   InterPro; IPR016158; Cullin_homology.
DR   InterPro; IPR001373; Cullin_N.
DR   InterPro; IPR019559; Cullin_neddylation_domain.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR002867; Znf_C6HC.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF03256; APC10; 1.
DR   Pfam; PF11515; Cul7; 1.
DR   Pfam; PF00888; Cullin; 1.
DR   Pfam; PF01485; IBR; 2.
DR   SMART; SM00884; Cullin_Nedd8; 1.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00184; RING; 2.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF75632; Cullin_homology; 1.
DR   SUPFAM; SSF49785; Gal_bind_like; 1.
DR   PROSITE; PS01256; CULLIN_1; 1.
DR   PROSITE; PS50069; CULLIN_2; 1.
DR   PROSITE; PS51284; DOC; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Coiled coil;
KW   Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism;
KW   Repeat; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1   2517       Cullin-9.
FT                                /FTId=PRO_0000119815.
FT   DOMAIN     1143   1322       DOC.
FT   NP_BIND    1363   1370       ATP (Potential).
FT   ZN_FING    2070   2120       RING-type 1.
FT   ZN_FING    2140   2203       IBR-type.
FT   ZN_FING    2236   2265       RING-type 2.
FT   COILED     1649   1691       Potential.
FT   COILED     2365   2385       Potential.
FT   COMPBIAS   1661   1689       Glu-rich.
FT   MOD_RES     947    947       Phosphoserine.
FT   VAR_SEQ     418    527       Missing (in isoform 2).
FT                                /FTId=VSP_009573.
FT   VARIANT    2058   2058       H -> P (in dbSNP:rs2273709).
FT                                /FTId=VAR_048844.
FT   VARIANT    2180   2180       T -> I (in dbSNP:rs11962520).
FT                                /FTId=VAR_048845.
FT   CONFLICT    527    527       E -> G (in Ref. 3; CAH18696).
FT   CONFLICT    663    663       E -> K (in Ref. 1; AAN61516).
FT   CONFLICT   1171   1171       E -> K (in Ref. 3; CAH18328).
FT   CONFLICT   1230   1230       M -> T (in Ref. 3; CAH18328).
FT   CONFLICT   1268   1268       N -> S (in Ref. 3; CAH18328).
FT   CONFLICT   1277   1277       R -> H (in Ref. 3; CAH18328).
FT   CONFLICT   1830   1857       Missing (in Ref. 3; CAH18696).
FT   CONFLICT   2049   2049       L -> P (in Ref. 3; CAH18696).
FT   CONFLICT   2058   2059       HQ -> PL (in Ref. 3; CAH18696).
FT   CONFLICT   2345   2345       V -> VV (in Ref. 4; CAI20204 and 5;
FT                                EAX04163).
FT   HELIX       378    382
FT   STRAND      390    393
FT   STRAND      406    408
FT   STRAND      416    419
FT   STRAND      426    429
FT   HELIX       431    433
SQ   SEQUENCE   2517 AA;  281229 MW;  42387A55DCC52EAF CRC64;
     MVGERHAGDL MVPLGPRLQA YPEELIRQRP GHDGHPEYLI RWSVLKCGEV GKVGVEEGKA
     EHILMWLSAP EVYANCPGLL GERALSKGLQ HEPAGVSGSF PRDPGGLDEV AMGEMEADVQ
     ALVRRAARQL AESGTPSLTA AVLHTIHVLS AYASIGPLTG VFRETGALDL LMHMLCNPEP
     QIRRSAGKML QALAAHDAGS RAHVLLSLSQ QDGIEQHMDF DSRYTLLELF AETTSSEEHC
     MAFEGIHLPQ IPGKLLFSLV KRYLCVTSLL DQLNSSPELG AGDQSSPCAT REKSRGQREL
     EFSMAVGNLI SELVRSMGWA RNLSEQGMSP PRPTRSIFQP YISGPSLLLP TIVTTPRRQG
     WVFRQRSEFS SRSGYGEYVQ QTLQPGMRVR MLDDYEEISA GDEGEFRQSN NGIPPVQVFW
     QSTGRTYWVH WHMLEILGPE EATEDKASAA VEKGAGATVL GTAFPSWDWN PMDGLYPLPY
     LQPEPQKNER VGYLTQAEWW ELLFFIKKLD LCEQQPIFQN LWKNLDETLG EKALGEISVS
     VEMAESLLQV LSSRFEGSTL NDLLNSQIYT KYGLLSNEPS SSSTSRNHSC TPDPEEESKS
     EASFSEEETE SLKAKAEAPK TEAEPTKTRT ETPMAQSDSQ LFNQLLVTEG MTLPTEMKEA
     ASEMARALRG PGPRSSLDQH VAAVVATVQI SSLDTNLQLS GLSALSQAVE EVTERDHPLV
     RPDRSLREKL VKMLVELLTN QVGEKMVVVQ ALRLLYLLMT KHEWRPLFAR EGGIYAVLVC
     MQEYKTSVLV QQAGLAALKM LAVASSSEIP TFVTGRDSIH SLFDAQMTRE IFASIDSATR
     PGSESLLLTV PAAVILMLNT EGCSSAARNG LLLLNLLLCN HHTLGDQIIT QELRDTLFRH
     SGIAPRTEPM PTTRTILMML LNRYSEPPGS PERAALETPI IQGQDGSPEL LIRSLVGGPS
     AELLLDLERV LCREGSPGGA VRPLLKRLQQ ETQPFLLLLR TLDAPGPNKT LLLSVLRVIT
     RLLDFPEAMV LPWHEVLEPC LNCLSGPSSD SEIVQELTCF LHRLASMHKD YAVVLCCLGA
     KEILSKVLDK HSAQLLLGCE LRDLVTECEK YAQLYSNLTS SILAGCIQMV LGQIEDHRRT
     HQPINIPFFD VFLRHLCQGS SVEVKEDKCW EKVEVSSNPH RASKLTDHNP KTYWESNGST
     GSHYITLHMH RGVLVRQLTL LVASEDSSYM PARVVVFGGD STSCIGTELN TVNVMPSASR
     VILLENLNRF WPIIQIRIKR CQQGGIDTRV RGVEVLGPKP TFWPLFREQL CRRTCLFYTI
     RAQAWSRDIA EDHRRLLQLC PRLNRVLRHE QNFADRFLPD DEAAQALGKT CWEALVSPLV
     QNITSPDAEG VSALGWLLDQ YLEQRETSRN PLSRAASFAS RVRRLCHLLV HVEPPPGPSP
     EPSTRPFSKN SKGRDRSPAP SPVLPSSSLR NITQCWLSVV QEQVSRFLAA AWRAPDFVPR
     YCKLYEHLQR AGSELFGPRA AFMLALRSGF SGALLQQSFL TAAHMSEQFA RYIDQQIQGG
     LIGGAPGVEM LGQLQRHLEP IMVLSGLELA TTFEHFYQHY MADRLLSFGS SWLEGAVLEQ
     IGLCFPNRLP QLMLQSLSTS EELQRQFHLF QLQRLDKLFL EQEDEEEKRL EEEEEEEEEE
     EAEKELFIED PSPAISILVL SPRCWPVSPL CYLYHPRKCL PTEFCDALDR FSSFYSQSQN
     HPVLDMGPHR RLQWTWLGRA ELQFGKQILH VSTVQMWLLL KFNQTEEVSV ETLLKDSDLS
     PELLLQALVP LTSGNGPLTL HEGQDFPHGG VLRLHEPGPQ RSGEALWLIP PQAYLNVEKD
     EGRTLEQKRN LLSCLLVRIL KAHGEKGLHI DQLVCLVLEA WQKGPNPPGT LGHTVAGGVA
     CTSTDVLSCI LHLLGQGYVK RRDDRPQILM YAAPEPMGPC RGQADVPFCG SQSETSKPSP
     EAVATLASLQ LPAGRTMSPQ EVEGLMKQTV RQVQETLNLE PDVAQHLLAH SHWGAEQLLQ
     SYSEDPEPLL LAAGLCVHQA QAVPVRPDHC PVCVSPLGCD DDLPSLCCMH YCCKSCWNEY
     LTTRIEQNLV LNCTCPIADC PAQPTGAFIR AIVSSPEVIS KYEKALLRGY VESCSNLTWC
     TNPQGCDRIL CRQGLGCGTT CSKCGWASCF NCSFPEAHYP ASCGHMSQWV DDGGYYDGMS
     VEAQSKHLAK LISKRCPSCQ APIEKNEGCL HMTCAKCNHG FCWRCLKSWK PNHKDYYNCS
     AMVSKAARQE KRFQDYNERC TFHHQAREFA VNLRNRVSAI HEVPPPRSFT FLNDACQGLE
     QARKVLAYAC VYSFYSQDAE YMDVVEQQTE NLELHTNALQ ILLEETLLRC RDLASSLRLL
     RADCLSTGME LLRRIQERLL AILQHSAQDF RVGLQSPSVE AWEAKGPNMP GSQPQASSGP
     EAEEEEEDDE DDVPEWQQDE FDEELDNDSF SYDESENLDQ ETFFFGDEEE DEDEAYD
//