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Mitochondrial ribonuclease P catalytic subunit (EC 3.1.26.5) (Mitochondrial ribonuclease P protein 3) (Mitochondrial RNase P protein 3)

 MRPP3_HUMAN             Reviewed;         583 AA.
O15091; B4DXD9; B4E0S8; B4E211; C4AM93; D3DS99; D3DSA1; Q86SZ4;
Q86YB5; Q8N5L5;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
20-JAN-2009, sequence version 2.
10-OCT-2018, entry version 137.
RecName: Full=Mitochondrial ribonuclease P catalytic subunit;
EC=3.1.26.5 {ECO:0000269|PubMed:25953853};
AltName: Full=Mitochondrial ribonuclease P protein 3 {ECO:0000303|PubMed:18984158};
Short=Mitochondrial RNase P protein 3 {ECO:0000303|PubMed:18984158};
Flags: Precursor;
Name=KIAA0391 {ECO:0000312|HGNC:HGNC:19958};
Synonyms=MRPP3 {ECO:0000303|PubMed:18984158};
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] (ISOFORM 2).
TISSUE=Brain;
PubMed=9205841; DOI=10.1093/dnares/4.2.141;
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VII.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 4:141-150(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Neuroblastoma, and T-cell;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4), AND
VARIANT SER-437.
TISSUE=Testis, Thymus, and Trachea;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
SER-437.
TISSUE=Lung, 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]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION,
AND INTERACTION WITH HSD17B10 AND TRMT10C.
PubMed=18984158; DOI=10.1016/j.cell.2008.09.013;
Holzmann J., Frank P., Loeffler E., Bennett K.L., Gerner C.,
Rossmanith W.;
"RNase P without RNA: identification and functional reconstitution of
the human mitochondrial tRNA processing enzyme.";
Cell 135:462-474(2008).
[8]
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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[11]
PROTEOLYTIC PROCESSING, AND INDUCTION.
PubMed=27350246; DOI=10.1038/nature18302;
Muench C., Harper J.W.;
"Mitochondrial unfolded protein response controls matrix pre-RNA
processing and translation.";
Nature 534:710-713(2016).
[12] {ECO:0000244|PDB:4XGL, ECO:0000244|PDB:4XGM}
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 207-583 IN COMPLEX WITH
ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DOMAIN, AND MUTAGENESIS
OF ASP-409; ASP-478; ASP-479; PRO-480; ARG-498; ASP-499 AND SER-569.
PubMed=25953853; DOI=10.1093/nar/gkv481;
Reinhard L., Sridhara S., Hallberg B.M.;
"Structure of the nuclease subunit of human mitochondrial RNase P.";
Nucleic Acids Res. 43:5664-5672(2015).
-!- FUNCTION: Catalytic ribonuclease component of mitochondrial
ribonuclease P, a complex composed of TRMT10C/MRPP1,
HSD17B10/MRPP2 and MRPP3, which cleaves tRNA molecules in their
5'-ends (PubMed:18984158, PubMed:25953853). The presence of
TRMT10C/MRPP1, HSD17B10/MRPP2 is required to catalyze tRNA
molecules in their 5'-ends (PubMed:25953853).
{ECO:0000269|PubMed:18984158, ECO:0000269|PubMed:25953853}.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of RNA, removing 5'-
extranucleotides from tRNA precursor.
{ECO:0000269|PubMed:25953853}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000305|PubMed:25953853};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000305|PubMed:25953853};
Note=Binds 2 Mg(2+) or Mg(2+) ions per subunit.
{ECO:0000305|PubMed:25953853};
-!- SUBUNIT: Catalytic component of mitochondrial ribonuclease P, a
complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and MRPP31
(PubMed:18984158). {ECO:0000269|PubMed:18984158}.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18984158}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=O15091-1; Sequence=Displayed;
Name=2;
IsoId=O15091-2; Sequence=VSP_036203;
Name=3;
IsoId=O15091-3; Sequence=VSP_036201;
Name=4;
IsoId=O15091-4; Sequence=VSP_036202;
Note=No experimental confirmation available.;
-!- INDUCTION: Down-regulated following mitochondrial unfolded protein
response. {ECO:0000269|PubMed:27350246}.
-!- DOMAIN: Displays a distorted and non-productive active site that
probably switches to a fully productive state only upon
association with TRMT10C/MRPP1, HSD17B10/MRPP2 and pre-tRNA
substrate. {ECO:0000305|PubMed:25953853}.
-!- PTM: Degraded by LONP1 following mitochondrial unfolded protein
response, probably leading to inhibit translation in
mitochondrion. {ECO:0000269|PubMed:27350246}.
-!- SIMILARITY: Belongs to the PPR family. P subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA20845.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AB002389; BAA20845.2; ALT_INIT; mRNA.
EMBL; BX161394; CAD61881.1; -; mRNA.
EMBL; BX161487; CAD61937.1; -; mRNA.
EMBL; AK301931; BAG63351.1; -; mRNA.
EMBL; AK303508; BAG64540.1; -; mRNA.
EMBL; AK304066; BAG64973.1; -; mRNA.
EMBL; AL121594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471078; EAW65878.1; -; Genomic_DNA.
EMBL; CH471078; EAW65882.1; -; Genomic_DNA.
EMBL; CH471078; EAW65879.1; -; Genomic_DNA.
EMBL; CH471078; EAW65880.1; -; Genomic_DNA.
EMBL; CH471078; EAW65881.1; -; Genomic_DNA.
EMBL; CH471078; EAW65883.1; -; Genomic_DNA.
EMBL; CH471078; EAW65884.1; -; Genomic_DNA.
EMBL; BC032221; AAH32221.1; -; mRNA.
EMBL; BC044580; AAH44580.1; -; mRNA.
CCDS; CCDS32063.1; -. [O15091-1]
CCDS; CCDS58312.1; -. [O15091-2]
CCDS; CCDS58313.1; -. [O15091-4]
CCDS; CCDS58314.1; -. [O15091-3]
RefSeq; NP_001243607.1; NM_001256678.1. [O15091-2]
RefSeq; NP_001243608.1; NM_001256679.1. [O15091-4]
RefSeq; NP_001243609.1; NM_001256680.1. [O15091-3]
RefSeq; NP_001243610.1; NM_001256681.1. [O15091-3]
RefSeq; NP_055487.2; NM_014672.3. [O15091-1]
RefSeq; XP_005268294.1; XM_005268237.3. [O15091-1]
RefSeq; XP_011535711.1; XM_011537409.2.
RefSeq; XP_011535712.1; XM_011537410.2. [O15091-1]
RefSeq; XP_016877324.1; XM_017021835.1.
RefSeq; XP_016877325.1; XM_017021836.1. [O15091-2]
RefSeq; XP_016877326.1; XM_017021837.1.
UniGene; Hs.458487; -.
UniGene; Hs.739309; -.
PDB; 4ROU; X-ray; 2.71 A; A/B=274-583.
PDB; 4XGL; X-ray; 1.80 A; A=207-583.
PDB; 4XGM; X-ray; 1.98 A; A=207-583.
PDBsum; 4ROU; -.
PDBsum; 4XGL; -.
PDBsum; 4XGM; -.
ProteinModelPortal; O15091; -.
SMR; O15091; -.
BioGrid; 115044; 31.
IntAct; O15091; 6.
MINT; O15091; -.
STRING; 9606.ENSP00000454657; -.
iPTMnet; O15091; -.
PhosphoSitePlus; O15091; -.
BioMuta; KIAA0391; -.
EPD; O15091; -.
MaxQB; O15091; -.
PaxDb; O15091; -.
PeptideAtlas; O15091; -.
PRIDE; O15091; -.
ProteomicsDB; 48444; -.
ProteomicsDB; 48445; -. [O15091-2]
ProteomicsDB; 48446; -. [O15091-3]
ProteomicsDB; 48447; -. [O15091-4]
Ensembl; ENST00000250377; ENSP00000250377; ENSG00000100890. [O15091-2]
Ensembl; ENST00000321130; ENSP00000324697; ENSG00000100890. [O15091-3]
Ensembl; ENST00000534898; ENSP00000440915; ENSG00000100890. [O15091-1]
Ensembl; ENST00000603544; ENSP00000473856; ENSG00000100890. [O15091-2]
Ensembl; ENST00000604948; ENSP00000474620; ENSG00000100890. [O15091-4]
Ensembl; ENST00000605870; ENSP00000474299; ENSG00000100890. [O15091-3]
GeneID; 9692; -.
KEGG; hsa:9692; -.
UCSC; uc001wsy.3; human. [O15091-1]
CTD; 9692; -.
DisGeNET; 9692; -.
EuPathDB; HostDB:ENSG00000100890.15; -.
GeneCards; KIAA0391; -.
H-InvDB; HIX0018405; -.
H-InvDB; HIX0079614; -.
HGNC; HGNC:19958; KIAA0391.
HPA; HPA020459; -.
MIM; 609947; gene.
neXtProt; NX_O15091; -.
OpenTargets; ENSG00000100890; -.
PharmGKB; PA134879499; -.
eggNOG; ENOG410IE4T; Eukaryota.
eggNOG; ENOG4111GT9; LUCA.
GeneTree; ENSGT00390000002201; -.
HOVERGEN; HBG099441; -.
InParanoid; O15091; -.
KO; K17655; -.
OMA; HDDPFLL; -.
OrthoDB; EOG091G0JTR; -.
PhylomeDB; O15091; -.
TreeFam; TF324726; -.
Reactome; R-HSA-6785470; tRNA processing in the mitochondrion.
Reactome; R-HSA-6787450; tRNA modification in the mitochondrion.
Reactome; R-HSA-8868766; rRNA processing in the mitochondrion.
ChiTaRS; KIAA0391; human.
GenomeRNAi; 9692; -.
PRO; PR:O15091; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100890; Expressed in 107 organ(s), highest expression level in leukocyte.
CleanEx; HS_KIAA0391; -.
ExpressionAtlas; O15091; baseline and differential.
Genevisible; O15091; HS.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0030678; C:mitochondrial ribonuclease P complex; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004526; F:ribonuclease P activity; IDA:UniProtKB.
GO; GO:0097745; P:mitochondrial tRNA 5'-end processing; IDA:UniProtKB.
GO; GO:0090646; P:mitochondrial tRNA processing; TAS:Reactome.
GO; GO:0001682; P:tRNA 5'-leader removal; IBA:GO_Central.
Gene3D; 1.25.40.10; -; 1.
InterPro; IPR033495; MRPP3.
InterPro; IPR031595; PRORP_C.
InterPro; IPR011990; TPR-like_helical_dom_sf.
PANTHER; PTHR13547:SF1; PTHR13547:SF1; 1.
Pfam; PF16953; PRORP; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Hydrolase;
Magnesium; Manganese; Metal-binding; Mitochondrion; Nuclease;
Phosphoprotein; Polymorphism; Reference proteome; Transit peptide;
tRNA processing.
TRANSIT 1 45 Mitochondrion. {ECO:0000255}.
CHAIN 46 583 Mitochondrial ribonuclease P catalytic
subunit.
/FTId=PRO_0000050749.
DOMAIN 342 578 PRORP.
METAL 348 348 Zinc. {ECO:0000244|PDB:4XGL,
ECO:0000244|PDB:4XGM,
ECO:0000269|PubMed:25953853}.
METAL 351 351 Zinc. {ECO:0000244|PDB:4XGL,
ECO:0000244|PDB:4XGM,
ECO:0000269|PubMed:25953853}.
METAL 409 409 Magnesium or manganese 1; catalytic.
{ECO:0000305|PubMed:25953853}.
METAL 478 478 Magnesium or manganese 1; catalytic.
{ECO:0000305|PubMed:25953853}.
METAL 479 479 Magnesium or manganese 2; catalytic.
{ECO:0000305|PubMed:25953853}.
METAL 499 499 Magnesium or manganese 2; catalytic.
{ECO:0000305|PubMed:25953853}.
METAL 557 557 Zinc; via tele nitrogen.
{ECO:0000244|PDB:4XGL,
ECO:0000244|PDB:4XGM,
ECO:0000269|PubMed:25953853}.
METAL 578 578 Zinc. {ECO:0000244|PDB:4XGL,
ECO:0000244|PDB:4XGM,
ECO:0000269|PubMed:25953853}.
MOD_RES 98 98 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 372 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.2}.
/FTId=VSP_036201.
VAR_SEQ 1 95 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036202.
VAR_SEQ 329 344 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:9205841}.
/FTId=VSP_036203.
VARIANT 437 437 N -> S (in dbSNP:rs11156878).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_054212.
MUTAGEN 409 409 D->N: Abolishes ribonuclease activity.
{ECO:0000269|PubMed:25953853}.
MUTAGEN 478 478 D->N: Abolishes ribonuclease activity.
{ECO:0000269|PubMed:25953853}.
MUTAGEN 479 479 D->N: Abolishes ribonuclease activity.
{ECO:0000269|PubMed:25953853}.
MUTAGEN 480 480 P->G: Does not affect ribonuclease
activity. {ECO:0000269|PubMed:25953853}.
MUTAGEN 498 498 R->D,N: Does not affect ribonuclease
activity. {ECO:0000269|PubMed:25953853}.
MUTAGEN 499 499 D->N: Abolishes ribonuclease activity.
{ECO:0000269|PubMed:25953853}.
MUTAGEN 569 569 S->A: Does not affect ribonuclease
activity. {ECO:0000269|PubMed:25953853}.
CONFLICT 315 315 P -> L (in Ref. 3; BAG63351).
{ECO:0000305}.
CONFLICT 453 453 S -> F (in Ref. 3; BAG64540).
{ECO:0000305}.
HELIX 213 220 {ECO:0000244|PDB:4XGL}.
TURN 224 226 {ECO:0000244|PDB:4XGL}.
HELIX 227 237 {ECO:0000244|PDB:4XGL}.
HELIX 244 256 {ECO:0000244|PDB:4XGL}.
HELIX 260 272 {ECO:0000244|PDB:4XGL}.
HELIX 279 289 {ECO:0000244|PDB:4XGL}.
HELIX 295 310 {ECO:0000244|PDB:4XGL}.
HELIX 317 329 {ECO:0000244|PDB:4XGL}.
STRAND 335 340 {ECO:0000244|PDB:4XGL}.
STRAND 346 348 {ECO:0000244|PDB:4XGL}.
TURN 349 351 {ECO:0000244|PDB:4XGL}.
STRAND 357 359 {ECO:0000244|PDB:4XGL}.
HELIX 362 376 {ECO:0000244|PDB:4XGL}.
HELIX 388 399 {ECO:0000244|PDB:4XGL}.
STRAND 405 409 {ECO:0000244|PDB:4XGL}.
HELIX 410 413 {ECO:0000244|PDB:4XGL}.
HELIX 423 433 {ECO:0000244|PDB:4XGL}.
HELIX 434 436 {ECO:0000244|PDB:4XGL}.
STRAND 440 445 {ECO:0000244|PDB:4XGL}.
HELIX 446 449 {ECO:0000244|PDB:4XGL}.
HELIX 460 466 {ECO:0000244|PDB:4XGL}.
STRAND 467 472 {ECO:0000244|PDB:4XGL}.
HELIX 481 489 {ECO:0000244|PDB:4XGL}.
STRAND 494 498 {ECO:0000244|PDB:4XGL}.
HELIX 511 524 {ECO:0000244|PDB:4XGL}.
STRAND 553 561 {ECO:0000244|PDB:4XGL}.
STRAND 575 581 {ECO:0000244|PDB:4XGL}.
SEQUENCE 583 AA; 67315 MW; 6AB17E7E8820D818 CRC64;
MTFYLFGIRS FPKLWKSPYL GLGPGHSYVS LFLADRCGIR NQQRLFSLKT MSPQNTKATN
LIAKARYLRK DEGSNKQVYS VPHFFLAGAA KERSQMNSQT EDHALAPVRN TIQLPTQPLN
SEEWDKLKED LKENTGKTSF ESWIISQMAG CHSSIDVAKS LLAWVAAKNN GIVSYDLLVK
YLYLCVFHMQ TSEVIDVFEI MKARYKTLEP RGYSLLIRGL IHSDRWREAL LLLEDIKKVI
TPSKKNYNDC IQGALLHQDV NTAWNLYQEL LGHDIVPMLE TLKAFFDFGK DIKDDNYSNK
LLDILSYLRN NQLYPGESFA HSIKTWFESV PGKQWKGQFT TVRKSGQCSG CGKTIESIQL
SPEEYECLKG KIMRDVIDGG DQYRKTTPQE LKRFENFIKS RPPFDVVIDG LNVAKMFPKV
RESQLLLNVV SQLAKRNLRL LVLGRKHMLR RSSQWSRDEM EEVQKQASCF FADDISEDDP
FLLYATLHSG NHCRFITRDL MRDHKACLPD AKTQRLFFKW QQGHQLAIVN RFPGSKLTFQ
RILSYDTVVQ TTGDSWHIPY DEDLVERCSC EVPTKWLCLH QKT


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