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Pumilio homolog 3 (HBV X-transactivated gene 5 protein) (HBV XAg-transactivated protein 5) (Minor histocompatibility antigen HA-8) (HLA-HA8)

 PUM3_HUMAN              Reviewed;         648 AA.
Q15397; A8K804; Q547G7; Q5SZY9; Q6IB47; Q96B27; Q96L78; Q96L79;
Q96L80;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
08-NOV-2005, sequence version 3.
27-SEP-2017, entry version 156.
RecName: Full=Pumilio homolog 3 {ECO:0000305};
AltName: Full=HBV X-transactivated gene 5 protein;
AltName: Full=HBV XAg-transactivated protein 5;
AltName: Full=Minor histocompatibility antigen HA-8;
Short=HLA-HA8;
Name=PUM3 {ECO:0000312|HGNC:HGNC:29676};
Synonyms=cPERP-C {ECO:0000303|PubMed:20813266},
KIAA0020 {ECO:0000312|HGNC:HGNC:29676},
PUF-A {ECO:0000303|PubMed:21266351}, XTP5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Synovium;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE HA-8R).
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[3]
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE HA-8PL), AND VARIANT
ASN-13.
TISSUE=Uterus;
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 2-648 (ALLELE HA-8R), AND
TISSUE SPECIFICITY.
TISSUE=Bone marrow;
PubMed=7584026; DOI=10.1093/dnares/1.1.27;
Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y.,
Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.;
"Prediction of the coding sequences of unidentified human genes. I.
The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by
analysis of randomly sampled cDNA clones from human immature myeloid
cell line KG-1.";
DNA Res. 1:27-35(1994).
[6]
PROTEIN SEQUENCE OF 130-137; 294-301; 331-342; 345-352 AND 441-464,
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Cervix carcinoma;
Bienvenut W.V.;
Submitted (AUG-2005) to UniProtKB.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 141-648 (ALLELE HA-8R).
Liu Y., Cheng J., Lu Y., Wang G., Li K., Chen J., Li L.;
"Cloning and identification of human gene 5 transactivated by
hepatitis B virus X antigen.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 141-648 (ALLELE HA-8R).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 235-350 (ALLELES HA-8R; HA-8P AND
HA-8PL), IDENTIFICATION BY MASS SPECTROMETRY OF HA-8, AND
POLYMORPHISM.
TISSUE=B-cell;
PubMed=11148223; DOI=10.1084/jem.193.2.195;
Brickner A.G., Warren E.H., Caldwell J.A., Akatsuka Y., Golovina T.N.,
Zarling A.L., Shabanowitz J., Eisenlohr L.C., Hunt D.F.,
Engelhard V.H., Riddell S.R.;
"The immunogenicity of a new human minor histocompatibility antigen
results from differential antigen processing.";
J. Exp. Med. 193:195-206(2001).
[10]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=12429849; DOI=10.1091/mbc.E02-05-0271;
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
Greco A., Hochstrasser D.F., Diaz J.-J.;
"Functional proteomic analysis of human nucleolus.";
Mol. Biol. Cell 13:4100-4109(2002).
[11]
SUBCELLULAR LOCATION.
PubMed=20813266; DOI=10.1016/j.cell.2010.07.047;
Ohta S., Bukowski-Wills J.C., Sanchez-Pulido L., Alves Fde L.,
Wood L., Chen Z.A., Platani M., Fischer L., Hudson D.F., Ponting C.P.,
Fukagawa T., Earnshaw W.C., Rappsilber J.;
"The protein composition of mitotic chromosomes determined using
multiclassifier combinatorial proteomics.";
Cell 142:810-821(2010).
[12]
FUNCTION, INTERACTION WITH PARP1, SUBCELLULAR LOCATION, AND NUCLEAR
LOCALIZATION SIGNAL.
PubMed=21266351; DOI=10.1158/0008-5472.CAN-10-1831;
Chang H.Y., Fan C.C., Chu P.C., Hong B.E., Lee H.J., Chang M.S.;
"hPuf-A/KIAA0020 modulates PARP-1 cleavage upon genotoxic stress.";
Cancer Res. 71:1126-1134(2011).
[13]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 123-648 ALONE AND IN COMPLEX
WITH DOUBLE-STRANDED DNA, PUMILIO REPEATS, RNA-BINDING, AND
DNA-BINDING.
PubMed=25512524; DOI=10.1073/pnas.1407634112;
Qiu C., McCann K.L., Wine R.N., Baserga S.J., Hall T.M.;
"A divergent Pumilio repeat protein family for pre-rRNA processing and
mRNA localization.";
Proc. Natl. Acad. Sci. U.S.A. 111:18554-18559(2014).
-!- FUNCTION: Inhibits the poly(ADP-ribosyl)ation activity of PARP1
and the degradation of PARP1 by CASP3 following genotoxic stress
(PubMed:21266351). Binds to double-stranded RNA or DNA without
sequence specificity (PubMed:25512524). Involved in development of
the eye and of primordial germ cells (By similarity).
{ECO:0000250|UniProtKB:X1WGX5, ECO:0000269|PubMed:21266351,
ECO:0000269|PubMed:25512524}.
-!- SUBUNIT: Interacts with PARP1 (via catalytic domain).
{ECO:0000269|PubMed:21266351}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:21266351,
ECO:0000269|Ref.6}. Nucleus, nucleoplasm
{ECO:0000269|PubMed:21266351}. Chromosome
{ECO:0000269|PubMed:20813266}. Note=Localizes predominantly in the
nucleolus with minor punctate signals in the nucleoplasm.
{ECO:0000269|PubMed:21266351}.
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:7584026}.
-!- DOMAIN: The HA-8 region can be cleaved and exposed at the cell
surface where it plays a role as a minor histocompatibility HLA-
A*0201-restricted antigen.
-!- DOMAIN: A 90 degree bend between Pumilio repeats 3 and 4 gives
rise to a L-shaped protein. {ECO:0000269|PubMed:25512524}.
-!- POLYMORPHISM: The following alleles of HA-8 are known: HA-8R, HA-
8P, HA-8PL, of which only HA-8R leads to specific cytotoxic T
lymphocyte (CTL) recognition. The lack of CTL recognition of cells
expressing HA-8P may be due to impaired transport associated with
antigen processing. The sequence shown is that of HA-8R.
{ECO:0000269|PubMed:11148223}.
-!- SEQUENCE CAUTION:
Sequence=BAA02808.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAI12924.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI15123.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AK292169; BAF84858.1; -; mRNA.
EMBL; AL354723; CAI15123.2; ALT_SEQ; Genomic_DNA.
EMBL; AL589675; CAI15123.2; JOINED; Genomic_DNA.
EMBL; AL589675; CAI12924.2; ALT_SEQ; Genomic_DNA.
EMBL; AL354723; CAI12924.2; JOINED; Genomic_DNA.
EMBL; CH471071; EAW58802.1; -; Genomic_DNA.
EMBL; BC016137; AAH16137.2; -; mRNA.
EMBL; D13645; BAA02808.1; ALT_INIT; mRNA.
EMBL; AF490254; AAO85462.1; -; mRNA.
EMBL; CR456957; CAG33238.1; -; mRNA.
EMBL; AY047588; AAL06072.1; -; mRNA.
EMBL; AY047589; AAL06073.1; -; mRNA.
EMBL; AY047590; AAL06074.1; -; mRNA.
CCDS; CCDS6448.2; -.
RefSeq; NP_055693.4; NM_014878.4.
UniGene; Hs.493309; -.
PDB; 4WZR; X-ray; 2.15 A; A/B=123-648.
PDB; 4WZW; X-ray; 2.95 A; A=129-648.
PDBsum; 4WZR; -.
PDBsum; 4WZW; -.
ProteinModelPortal; Q15397; -.
SMR; Q15397; -.
BioGrid; 115259; 133.
IntAct; Q15397; 13.
MINT; MINT-1404790; -.
STRING; 9606.ENSP00000380982; -.
iPTMnet; Q15397; -.
PhosphoSitePlus; Q15397; -.
SwissPalm; Q15397; -.
BioMuta; KIAA0020; -.
DMDM; 81175177; -.
SWISS-2DPAGE; Q15397; -.
EPD; Q15397; -.
MaxQB; Q15397; -.
PaxDb; Q15397; -.
PeptideAtlas; Q15397; -.
PRIDE; Q15397; -.
DNASU; 9933; -.
Ensembl; ENST00000397885; ENSP00000380982; ENSG00000080608.
GeneID; 9933; -.
KEGG; hsa:9933; -.
UCSC; uc003zhp.2; human.
CTD; 9933; -.
DisGeNET; 9933; -.
EuPathDB; HostDB:ENSG00000080608.9; -.
GeneCards; PUM3; -.
HGNC; HGNC:29676; PUM3.
HPA; HPA002353; -.
MIM; 609960; gene.
neXtProt; NX_Q15397; -.
OpenTargets; ENSG00000080608; -.
PharmGKB; PA134895115; -.
eggNOG; KOG2050; Eukaryota.
eggNOG; ENOG410XSHY; LUCA.
GeneTree; ENSGT00390000015757; -.
HOVERGEN; HBG052166; -.
InParanoid; Q15397; -.
KO; K14844; -.
OMA; REWYGPE; -.
OrthoDB; EOG091G06QP; -.
PhylomeDB; Q15397; -.
TreeFam; TF312954; -.
ChiTaRS; KIAA0020; human.
GeneWiki; KIAA0020; -.
GenomeRNAi; 9933; -.
PRO; PR:Q15397; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000080608; -.
CleanEx; HS_KIAA0020; -.
ExpressionAtlas; Q15397; baseline and differential.
Genevisible; Q15397; HS.
GO; GO:0005694; C:chromosome; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0010835; P:regulation of protein ADP-ribosylation; IMP:UniProtKB.
GO; GO:0006417; P:regulation of translation; IBA:GO_Central.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR012959; CPL_dom.
InterPro; IPR033133; PUM-HD.
InterPro; IPR001313; Pumilio_RNA-bd_rpt.
Pfam; PF08144; CPL; 1.
SMART; SM00025; Pumilio; 6.
SUPFAM; SSF48371; SSF48371; 2.
PROSITE; PS50302; PUM; 5.
PROSITE; PS50303; PUM_HD; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chromosome; Complete proteome;
Direct protein sequencing; DNA-binding; Nucleus; Polymorphism;
Reference proteome; Repeat; RNA-binding.
CHAIN 1 648 Pumilio homolog 3.
/FTId=PRO_0000075929.
DOMAIN 143 510 PUM-HD. {ECO:0000255|PROSITE-
ProRule:PRU00318}.
REPEAT 177 212 Pumilio 1. {ECO:0000269|PubMed:25512524}.
REPEAT 213 248 Pumilio 2. {ECO:0000269|PubMed:25512524}.
REPEAT 249 277 Pumilio 3. {ECO:0000269|PubMed:25512524}.
REPEAT 289 325 Pumilio 4. {ECO:0000269|PubMed:25512524}.
REPEAT 326 361 Pumilio 5. {ECO:0000269|PubMed:25512524}.
REPEAT 362 397 Pumilio 6. {ECO:0000269|PubMed:25512524}.
REPEAT 398 435 Pumilio 7. {ECO:0000269|PubMed:25512524}.
REPEAT 436 504 Pumilio 8. {ECO:0000269|PubMed:25512524}.
REPEAT 505 551 Pumilio 9. {ECO:0000269|PubMed:25512524}.
REPEAT 552 596 Pumilio 10.
{ECO:0000269|PubMed:25512524}.
REPEAT 597 636 Pumilio 11.
{ECO:0000269|PubMed:25512524}.
REGION 289 297 HA-8.
MOTIF 106 118 Nuclear localization signal.
{ECO:0000269|PubMed:21266351}.
MOD_RES 33 33 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8BKS9}.
VARIANT 13 13 S -> N (in dbSNP:rs10968457).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_051613.
VARIANT 264 264 I -> V (in dbSNP:rs35869387).
/FTId=VAR_051614.
VARIANT 289 289 R -> P (in allele HA-8P and allele HA-
8PL; dbSNP:rs2173904).
{ECO:0000269|PubMed:11148223,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_023772.
VARIANT 297 297 V -> L (in allele HA-8PL;
dbSNP:rs2270891).
{ECO:0000269|PubMed:11148223,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_023773.
VARIANT 414 414 T -> S (in dbSNP:rs3736390).
/FTId=VAR_051615.
VARIANT 480 480 R -> Q (in dbSNP:rs2270889).
/FTId=VAR_051616.
CONFLICT 625 625 L -> S (in Ref. 8; CAG33238).
{ECO:0000305}.
HELIX 132 145 {ECO:0000244|PDB:4WZR}.
STRAND 147 149 {ECO:0000244|PDB:4WZR}.
HELIX 152 166 {ECO:0000244|PDB:4WZR}.
TURN 167 169 {ECO:0000244|PDB:4WZR}.
HELIX 170 175 {ECO:0000244|PDB:4WZR}.
TURN 177 179 {ECO:0000244|PDB:4WZR}.
HELIX 180 189 {ECO:0000244|PDB:4WZR}.
HELIX 192 202 {ECO:0000244|PDB:4WZR}.
HELIX 203 205 {ECO:0000244|PDB:4WZR}.
HELIX 206 210 {ECO:0000244|PDB:4WZR}.
HELIX 213 225 {ECO:0000244|PDB:4WZR}.
HELIX 228 238 {ECO:0000244|PDB:4WZR}.
TURN 239 241 {ECO:0000244|PDB:4WZR}.
HELIX 242 245 {ECO:0000244|PDB:4WZR}.
HELIX 249 261 {ECO:0000244|PDB:4WZR}.
HELIX 265 272 {ECO:0000244|PDB:4WZR}.
HELIX 273 276 {ECO:0000244|PDB:4WZR}.
HELIX 278 283 {ECO:0000244|PDB:4WZR}.
STRAND 286 288 {ECO:0000244|PDB:4WZR}.
HELIX 291 297 {ECO:0000244|PDB:4WZR}.
HELIX 299 301 {ECO:0000244|PDB:4WZR}.
HELIX 302 313 {ECO:0000244|PDB:4WZR}.
HELIX 314 318 {ECO:0000244|PDB:4WZR}.
HELIX 320 323 {ECO:0000244|PDB:4WZR}.
HELIX 326 338 {ECO:0000244|PDB:4WZR}.
HELIX 341 351 {ECO:0000244|PDB:4WZR}.
TURN 352 354 {ECO:0000244|PDB:4WZR}.
HELIX 355 358 {ECO:0000244|PDB:4WZR}.
HELIX 362 374 {ECO:0000244|PDB:4WZR}.
HELIX 377 386 {ECO:0000244|PDB:4WZR}.
TURN 387 390 {ECO:0000244|PDB:4WZR}.
HELIX 391 395 {ECO:0000244|PDB:4WZR}.
TURN 398 400 {ECO:0000244|PDB:4WZR}.
HELIX 401 410 {ECO:0000244|PDB:4WZR}.
HELIX 414 427 {ECO:0000244|PDB:4WZR}.
HELIX 429 433 {ECO:0000244|PDB:4WZR}.
HELIX 436 446 {ECO:0000244|PDB:4WZR}.
TURN 451 453 {ECO:0000244|PDB:4WZR}.
HELIX 456 463 {ECO:0000244|PDB:4WZR}.
TURN 464 467 {ECO:0000244|PDB:4WZR}.
HELIX 475 496 {ECO:0000244|PDB:4WZR}.
HELIX 498 502 {ECO:0000244|PDB:4WZR}.
HELIX 507 509 {ECO:0000244|PDB:4WZR}.
HELIX 510 517 {ECO:0000244|PDB:4WZR}.
HELIX 523 531 {ECO:0000244|PDB:4WZR}.
HELIX 548 550 {ECO:0000244|PDB:4WZR}.
HELIX 554 570 {ECO:0000244|PDB:4WZR}.
HELIX 577 585 {ECO:0000244|PDB:4WZR}.
HELIX 587 592 {ECO:0000244|PDB:4WZR}.
HELIX 593 595 {ECO:0000244|PDB:4WZR}.
HELIX 597 607 {ECO:0000244|PDB:4WZR}.
HELIX 612 622 {ECO:0000244|PDB:4WZR}.
HELIX 623 625 {ECO:0000244|PDB:4WZR}.
HELIX 626 629 {ECO:0000244|PDB:4WZR}.
HELIX 637 645 {ECO:0000244|PDB:4WZR}.
SEQUENCE 648 AA; 73584 MW; 449BFBF22F1BBA86 CRC64;
MEVKGKKQFT GKSTKTAQEK NRFHKNSDSG SSKTFPTRKV AKEGGPKVTS RNFEKSITKL
GKKGVKQFKN KQQGDKSPKN KFQPANKFNK KRKFQPDGRS DESAAKKPKW DDFKKKKKEL
KQSRQLSDKT NYDIVVRAKQ MWEILRRKDC DKEKRVKLMS DLQKLIQGKI KTIAFAHDST
RVIQCYIQYG NEEQRKQAFE ELRDDLVELS KAKYSRNIVK KFLMYGSKPQ IAEIIRSFKG
HVRKMLRHAE ASAIVEYAYN DKAILEQRNM LTEELYGNTF QLYKSADHRT LDKVLEVQPE
KLELIMDEMK QILTPMAQKE AVIKHSLVHK VFLDFFTYAP PKLRSEMIEA IREAVVYLAH
THDGARVAMH CLWHGTPKDR KVIVKTMKTY VEKVANGQYS HLVLLAAFDC IDDTKLVKQI
IISEIISSLP SIVNDKYGRK VLLYLLSPRD PAHTVREIIE VLQKGDGNAH SKKDTEVRRR
ELLESISPAL LSYLQEHAQE VVLDKSACVL VSDILGSATG DVQPTMNAIA SLAATGLHPG
GKDGELHIAE HPAGHLVLKW LIEQDKKMKE NGREGCFAKT LVEHVGMKNL KSWASVNRGA
IILSSLLQSC DLEVANKVKA ALKSLIPTLE KTKSTSKGIE ILLEKLST


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