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Ubiquitin carboxyl-terminal hydrolase isozyme L5 (UCH-L5) (EC 3.4.19.12) (Ubiquitin C-terminal hydrolase UCH37) (Ubiquitin thioesterase L5)

 UCHL5_HUMAN             Reviewed;         329 AA.
Q9Y5K5; Q5LJA6; Q5LJA7; Q8TBS4; Q96BJ9; Q9H1W5; Q9P0I3; Q9UQN2;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
30-MAY-2006, sequence version 3.
22-NOV-2017, entry version 159.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase isozyme L5;
Short=UCH-L5;
EC=3.4.19.12;
AltName: Full=Ubiquitin C-terminal hydrolase UCH37;
AltName: Full=Ubiquitin thioesterase L5;
Name=UCHL5; Synonyms=UCH37; ORFNames=AD-019, CGI-70;
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 1), FUNCTION, ENZYME REGULATION,
MUTAGENESIS OF CYS-88, AND INTERACTION WITH ADRM1.
PubMed=16906146; DOI=10.1038/ncb1460;
Yao T., Song L., Xu W., DeMartino G.N., Florens L., Swanson S.K.,
Washburn M.P., Conaway R.C., Conaway J.W., Cohen R.E.;
"Proteasome recruitment and activation of the Uch37 deubiquitinating
enzyme by Adrm1.";
Nat. Cell Biol. 8:994-1002(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
PHE-197.
PubMed=10810093; DOI=10.1101/gr.10.5.703;
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
"Identification of novel human genes evolutionarily conserved in
Caenorhabditis elegans by comparative proteomics.";
Genome Res. 10:703-713(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
PHE-197.
TISSUE=Adrenal gland;
PubMed=10931946; DOI=10.1073/pnas.160270997;
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal
axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
TISSUE=Lung, and 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).
[7]
INTERACTION WITH ADRM1, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16990800; DOI=10.1038/sj.emboj.7601338;
Hamazaki J., Iemura S., Natsume T., Yashiroda H., Tanaka K.,
Murata S.;
"A novel proteasome-interacting protein recruits the deubiquitinating
enzyme UCH37 to 26S proteasomes.";
EMBO J. 25:4524-4536(2006).
[8]
INTERACTION WITH ADRM1, ENZYME REGULATION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=17139257; DOI=10.1038/sj.emboj.7601450;
Qiu X.-B., Ouyang S.-Y., Li C.-J., Miao S., Wang L., Goldberg A.L.;
"hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the
deubiquitinating enzyme, UCH37.";
EMBO J. 25:5742-5753(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17323924; DOI=10.1021/bi061994u;
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
"Mass spectrometric characterization of the affinity-purified human
26S proteasome complex.";
Biochemistry 46:3553-3565(2007).
[10]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION IN THE INO80
COMPLEX, INTERACTION WITH NFRKB AND ADRM1, AND ENZYME REGULATION.
PubMed=18922472; DOI=10.1016/j.molcel.2008.08.027;
Yao T., Song L., Jin J., Cai Y., Takahashi H., Swanson S.K.,
Washburn M.P., Florens L., Conaway R.C., Cohen R.E., Conaway J.W.;
"Distinct modes of regulation of the Uch37 deubiquitinating enzyme in
the proteasome and in the Ino80 chromatin-remodeling complex.";
Mol. Cell 31:909-917(2008).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-158, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[12]
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).
[13]
IDENTIFICATION IN THE INO80 COMPLEX.
PubMed=21303910; DOI=10.1074/jbc.M111.222505;
Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P.,
Conaway J.W., Conaway R.C.;
"Subunit organization of the human INO80 chromatin remodeling complex:
An evolutionarily conserved core complex catalyzes ATP-dependent
nucleosome remodeling.";
J. Biol. Chem. 286:11283-11289(2011).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-228.
PubMed=19836345; DOI=10.1016/j.bbrc.2009.10.062;
Nishio K., Kim S.W., Kawai K., Mizushima T., Yamane T., Hamazaki J.,
Murata S., Tanaka K., Morimoto Y.;
"Crystal structure of the de-ubiquitinating enzyme UCH37 (human UCH-
L5) catalytic domain.";
Biochem. Biophys. Res. Commun. 390:855-860(2009).
[16]
X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 2-328.
Center for eukaryotic structural genomics (CESG);
"Crystal structure of UCH37.";
Submitted (AUG-2009) to the PDB data bank.
-!- FUNCTION: Protease that specifically cleaves 'Lys-48'-linked
polyubiquitin chains. Deubiquitinating enzyme associated with the
19S regulatory subunit of the 26S proteasome. Putative regulatory
component of the INO80 complex; however is inactive in the INO80
complex and is activated by a transient interaction of the INO80
complex with the proteasome via ADRM1.
{ECO:0000269|PubMed:16906146, ECO:0000269|PubMed:18922472}.
-!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
thioester, amide, peptide and isopeptide bonds formed by the C-
terminal Gly of ubiquitin (a 76-residue protein attached to
proteins as an intracellular targeting signal).
-!- ENZYME REGULATION: Activated by ADRM1. Inhibited by interaction
with NFRKB. {ECO:0000269|PubMed:16906146,
ECO:0000269|PubMed:17139257, ECO:0000269|PubMed:18922472}.
-!- SUBUNIT: Component of the 19S (PA700) regulatory complex of the
26S proteasome. Interacts with ADRM1 and NFRKB; in vitro ADRM1 and
NFRKB compete for interaction with UCHL5. Component of the INO80
complex; specifically part of a complex module associated with N-
terminus of INO80. {ECO:0000269|PubMed:16906146,
ECO:0000269|PubMed:16990800, ECO:0000269|PubMed:17139257,
ECO:0000269|PubMed:18922472, ECO:0000269|PubMed:21303910}.
-!- INTERACTION:
Q9H981:ACTR8; NbExp=3; IntAct=EBI-1051183, EBI-769597;
Q16186:ADRM1; NbExp=20; IntAct=EBI-1051183, EBI-954387;
Q8NBZ0:INO80E; NbExp=7; IntAct=EBI-1051183, EBI-769401;
Q6P4R8:NFRKB; NbExp=12; IntAct=EBI-1051183, EBI-2511210;
P60900:PSMA6; NbExp=4; IntAct=EBI-1051183, EBI-357793;
Q13200:PSMD2; NbExp=5; IntAct=EBI-1051183, EBI-357648;
P55036:PSMD4; NbExp=5; IntAct=EBI-1051183, EBI-359318;
P0C1Z6:TFPT; NbExp=3; IntAct=EBI-1051183, EBI-1245626;
O96006:ZBED1; NbExp=3; IntAct=EBI-1051183, EBI-740037;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18922472}.
Nucleus {ECO:0000269|PubMed:18922472}. Note=Associates with the
proteasome 19S subunit in the cytoplasm. Associates with the INO80
complex in the nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Experimental confirmation may be lacking for some
isoforms.;
Name=1;
IsoId=Q9Y5K5-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y5K5-2; Sequence=VSP_005253, VSP_005254;
Name=3;
IsoId=Q9Y5K5-3; Sequence=VSP_005253;
Name=4;
IsoId=Q9Y5K5-4; Sequence=VSP_005253, VSP_017062;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the peptidase C12 family. {ECO:0000305}.
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EMBL; AF147717; AAD31528.1; -; mRNA.
EMBL; AF151828; AAD34065.1; -; mRNA.
EMBL; AF157320; AAF67486.1; -; mRNA.
EMBL; BT006790; AAP35436.1; -; mRNA.
EMBL; AL136370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC015521; AAH15521.1; -; mRNA.
EMBL; BC025369; AAH25369.1; -; mRNA.
CCDS; CCDS1378.1; -. [Q9Y5K5-1]
CCDS; CCDS55668.1; -. [Q9Y5K5-3]
CCDS; CCDS55669.1; -. [Q9Y5K5-2]
CCDS; CCDS55670.1; -. [Q9Y5K5-4]
RefSeq; NP_001186190.1; NM_001199261.1. [Q9Y5K5-3]
RefSeq; NP_001186191.1; NM_001199262.1. [Q9Y5K5-4]
RefSeq; NP_001186192.1; NM_001199263.1. [Q9Y5K5-2]
RefSeq; NP_057068.1; NM_015984.3. [Q9Y5K5-1]
UniGene; Hs.145469; -.
PDB; 3A7S; X-ray; 2.20 A; A=1-228.
PDB; 3IHR; X-ray; 2.95 A; A=1-329.
PDB; 3RII; X-ray; 2.00 A; A/B=1-228.
PDB; 3RIS; X-ray; 2.40 A; A/B/C/D=1-240.
PDB; 3TB3; X-ray; 2.30 A; A/B=1-227.
PDB; 4UEL; X-ray; 2.30 A; A=1-329.
PDB; 4UEM; X-ray; 2.82 A; A=1-329.
PDB; 4UF5; X-ray; 3.70 A; A=1-329.
PDB; 4UF6; X-ray; 3.69 A; A/D/G/J=1-329.
PDB; 4WLP; X-ray; 3.10 A; A=5-322.
PDBsum; 3A7S; -.
PDBsum; 3IHR; -.
PDBsum; 3RII; -.
PDBsum; 3RIS; -.
PDBsum; 3TB3; -.
PDBsum; 4UEL; -.
PDBsum; 4UEM; -.
PDBsum; 4UF5; -.
PDBsum; 4UF6; -.
PDBsum; 4WLP; -.
ProteinModelPortal; Q9Y5K5; -.
SMR; Q9Y5K5; -.
BioGrid; 119509; 222.
DIP; DIP-42671N; -.
IntAct; Q9Y5K5; 65.
MINT; MINT-2823912; -.
STRING; 9606.ENSP00000356425; -.
BindingDB; Q9Y5K5; -.
ChEMBL; CHEMBL3407316; -.
MEROPS; C12.005; -.
iPTMnet; Q9Y5K5; -.
PhosphoSitePlus; Q9Y5K5; -.
BioMuta; UCHL5; -.
DMDM; 108936023; -.
EPD; Q9Y5K5; -.
PaxDb; Q9Y5K5; -.
PeptideAtlas; Q9Y5K5; -.
PRIDE; Q9Y5K5; -.
DNASU; 51377; -.
Ensembl; ENST00000367448; ENSP00000356418; ENSG00000116750. [Q9Y5K5-4]
Ensembl; ENST00000367449; ENSP00000356419; ENSG00000116750. [Q9Y5K5-2]
Ensembl; ENST00000367454; ENSP00000356424; ENSG00000116750. [Q9Y5K5-3]
Ensembl; ENST00000367455; ENSP00000356425; ENSG00000116750. [Q9Y5K5-1]
GeneID; 51377; -.
KEGG; hsa:51377; -.
UCSC; uc001gsm.4; human. [Q9Y5K5-1]
CTD; 51377; -.
DisGeNET; 51377; -.
EuPathDB; HostDB:ENSG00000116750.13; -.
GeneCards; UCHL5; -.
HGNC; HGNC:19678; UCHL5.
HPA; HPA005908; -.
HPA; HPA006069; -.
HPA; HPA075383; -.
MIM; 610667; gene.
neXtProt; NX_Q9Y5K5; -.
OpenTargets; ENSG00000116750; -.
PharmGKB; PA134916228; -.
eggNOG; KOG2778; Eukaryota.
eggNOG; ENOG410XP0P; LUCA.
GeneTree; ENSGT00510000046560; -.
HOVERGEN; HBG056021; -.
InParanoid; Q9Y5K5; -.
KO; K05610; -.
PhylomeDB; Q9Y5K5; -.
TreeFam; TF313976; -.
BRENDA; 3.4.19.12; 2681.
Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-HSA-5689603; UCH proteinases.
SignaLink; Q9Y5K5; -.
SIGNOR; Q9Y5K5; -.
ChiTaRS; UCHL5; human.
EvolutionaryTrace; Q9Y5K5; -.
GeneWiki; Ubiquitin_carboxyl-terminal_hydrolase_L5; -.
GenomeRNAi; 51377; -.
PRO; PR:Q9Y5K5; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000116750; -.
CleanEx; HS_UCHL5; -.
ExpressionAtlas; Q9Y5K5; baseline and differential.
Genevisible; Q9Y5K5; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0031597; C:cytosolic proteasome complex; IEA:Ensembl.
GO; GO:0031011; C:Ino80 complex; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0004866; F:endopeptidase inhibitor activity; IMP:UniProtKB.
GO; GO:0070628; F:proteasome binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:UniProtKB.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0048853; P:forebrain morphogenesis; IEA:Ensembl.
GO; GO:0021670; P:lateral ventricle development; IEA:Ensembl.
GO; GO:0030901; P:midbrain development; IEA:Ensembl.
GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
CDD; cd02255; Peptidase_C12; 1.
Gene3D; 3.40.532.10; -; 1.
InterPro; IPR001578; Peptidase_C12_UCH.
InterPro; IPR036959; Peptidase_C12_UCH_sf.
InterPro; IPR017390; Ubiquitinyl_hydrolase_UCH37.
InterPro; IPR033837; UCH37.
PANTHER; PTHR10589; PTHR10589; 1.
Pfam; PF01088; Peptidase_C12; 1.
PIRSF; PIRSF038120; Ubiquitinyl_hydrolase_UCH37; 1.
PRINTS; PR00707; UBCTHYDRLASE.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; DNA damage; DNA recombination; DNA repair; Hydrolase;
Nucleus; Polymorphism; Protease; Proteasome; Reference proteome;
Thiol protease; Transcription; Transcription regulation;
Ubl conjugation pathway.
CHAIN 1 329 Ubiquitin carboxyl-terminal hydrolase
isozyme L5.
/FTId=PRO_0000211066.
REGION 313 329 Interaction with ADRM1.
ACT_SITE 88 88 Nucleophile. {ECO:0000305}.
ACT_SITE 164 164 Proton donor. {ECO:0000250}.
SITE 179 179 Important for enzyme activity.
{ECO:0000250}.
MOD_RES 47 47 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9WUP7}.
MOD_RES 158 158 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 289 289 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9WUP7}.
VAR_SEQ 246 246 Missing (in isoform 2, isoform 3 and
isoform 4). {ECO:0000303|PubMed:10810093,
ECO:0000303|PubMed:10931946,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4}.
/FTId=VSP_005253.
VAR_SEQ 316 329 AKEKQNAKKAQETK -> GK (in isoform 2).
{ECO:0000303|PubMed:10810093,
ECO:0000303|PubMed:10931946}.
/FTId=VSP_005254.
VAR_SEQ 316 329 AKEKQNAKKAQETK -> FEKHFEKTLLGK (in
isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_017062.
VARIANT 197 197 I -> F. {ECO:0000269|PubMed:10810093,
ECO:0000269|PubMed:10931946}.
/FTId=VAR_011613.
MUTAGEN 88 88 C->A: Abolishes enzymatic activity.
{ECO:0000269|PubMed:16906146}.
CONFLICT 6 6 G -> V (in Ref. 2; AAD34065).
{ECO:0000305}.
HELIX 15 24 {ECO:0000244|PDB:3RII}.
STRAND 28 34 {ECO:0000244|PDB:3RII}.
TURN 40 46 {ECO:0000244|PDB:3RII}.
STRAND 48 56 {ECO:0000244|PDB:3RII}.
STRAND 65 68 {ECO:0000244|PDB:3RII}.
HELIX 72 75 {ECO:0000244|PDB:3RII}.
HELIX 85 87 {ECO:0000244|PDB:3RII}.
HELIX 88 98 {ECO:0000244|PDB:3RII}.
HELIX 109 118 {ECO:0000244|PDB:3RII}.
HELIX 123 131 {ECO:0000244|PDB:3RII}.
HELIX 134 142 {ECO:0000244|PDB:3RII}.
HELIX 159 162 {ECO:0000244|PDB:3RII}.
STRAND 163 171 {ECO:0000244|PDB:3RII}.
STRAND 174 178 {ECO:0000244|PDB:3RII}.
STRAND 182 184 {ECO:0000244|PDB:3RII}.
STRAND 186 190 {ECO:0000244|PDB:3RII}.
STRAND 193 195 {ECO:0000244|PDB:3RII}.
HELIX 197 213 {ECO:0000244|PDB:3RII}.
STRAND 218 225 {ECO:0000244|PDB:3RII}.
HELIX 227 244 {ECO:0000244|PDB:4UEL}.
HELIX 255 289 {ECO:0000244|PDB:4UEL}.
HELIX 293 305 {ECO:0000244|PDB:4UEL}.
HELIX 309 318 {ECO:0000244|PDB:4UEL}.
SEQUENCE 329 AA; 37607 MW; DF307347D48C9D0F CRC64;
MTGNAGEWCL MESDPGVFTE LIKGFGCRGA QVEEIWSLEP ENFEKLKPVH GLIFLFKWQP
GEEPAGSVVQ DSRLDTIFFA KQVINNACAT QAIVSVLLNC THQDVHLGET LSEFKEFSQS
FDAAMKGLAL SNSDVIRQVH NSFARQQMFE FDTKTSAKEE DAFHFVSYVP VNGRLYELDG
LREGPIDLGA CNQDDWISAV RPVIEKRIQK YSEGEIRFNL MAIVSDRKMI YEQKIAELQR
QLAEEEPMDT DQGNSMLSAI QSEVAKNQML IEEEVQKLKR YKIENIRRKH NYLPFIMELL
KTLAEHQQLI PLVEKAKEKQ NAKKAQETK


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