ZUP1_HUMAN
ID ZUP1_HUMAN Reviewed; 578 AA.
AC Q96AP4; Q5TD92; Q6PJH7; Q96NV6;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Zinc finger-containing ubiquitin peptidase 1 {ECO:0000305};
DE EC=3.4.19.12 {ECO:0000269|PubMed:29476094};
DE AltName: Full=Lys-63-specific deubiquitinase ZUFSP;
DE Short=DUB;
DE AltName: Full=Zinc finger with UFM1-specific peptidase domain protein;
GN Name=ZUP1 {ECO:0000312|HGNC:HGNC:21224};
GN Synonyms=C6orf113, ZUFSP {ECO:0000312|HGNC:HGNC:21224};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-379.
RC TISSUE=Neuroblastoma;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Heart;
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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX 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., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., 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., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Duodenum, and Uterus;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-262, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [6]
RP FUNCTION, MUTAGENESIS OF CYS-360 AND HIS-491, AND INTERACTION WITH RPA1 AND
RP RPA2.
RX PubMed=29563501; DOI=10.1038/s41467-018-03511-6;
RA Hewings D.S., Heideker J., Ma T.P., AhYoung A.P., El Oualid F., Amore A.,
RA Costakes G.T., Kirchhofer D., Brasher B., Pillow T., Popovych N.,
RA Maurer T., Schwerdtfeger C., Forrest W.F., Yu K., Flygare J., Bogyo M.,
RA Wertz I.E.;
RT "Reactive-site-centric chemoproteomics identifies a distinct class of
RT deubiquitinase enzymes.";
RL Nat. Commun. 9:1162-1162(2018).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 231-578, FUNCTION, AND
RP MUTAGENESIS OF CYS-360; GLN-487; HIS-491 AND ASP-512.
RX PubMed=29576527; DOI=10.1016/j.molcel.2018.02.023;
RA Kwasna D., Abdul Rehman S.A., Natarajan J., Matthews S., Madden R.,
RA De Cesare V., Weidlich S., Virdee S., Ahel I., Gibbs-Seymour I.,
RA Kulathu Y.;
RT "Discovery and characterization of ZUFSP/ZUP1, a distinct deubiquitinase
RT class important for genome stability.";
RL Mol. Cell 70:150-164(2018).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP CYS-360, DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=29576528; DOI=10.1016/j.molcel.2018.02.024;
RA Haahr P., Borgermann N., Guo X., Typas D., Achuthankutty D., Hoffmann S.,
RA Shearer R., Sixma T.K., Mailand N.;
RT "ZUFSP deubiquitylates K63-linked polyubiquitin chains to promote genome
RT stability.";
RL Mol. Cell 70:165-174(2018).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 232-578, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, ACTIVE SITE, MUTAGENESIS
RP OF SER-351; CYS-360; ASP-406; GLU-428 AND HIS-491, AND SUBCELLULAR
RP LOCATION.
RX PubMed=29476094; DOI=10.1038/s41467-018-03148-5;
RA Hermanns T., Pichlo C., Woiwode I., Klopffleisch K., Witting K.F., Ovaa H.,
RA Baumann U., Hofmann K.;
RT "A family of unconventional deubiquitinases with modular chain specificity
RT determinants.";
RL Nat. Commun. 9:799-799(2018).
CC -!- FUNCTION: Deubiquitinase with endodeubiquitinase activity that
CC specifically interacts with and cleaves 'Lys-63'-linked long
CC polyubiquitin chains. Shows only weak activity against 'Lys-11' and
CC 'Lys-48'-linked chains (PubMed:29576528, PubMed:29563501,
CC PubMed:29476094). Plays an important role in genome stability pathways,
CC functioning to prevent spontaneous DNA damage and also promote cellular
CC survival in response to exogenous DNA damage (PubMed:29576528,
CC PubMed:29576527). Modulates the ubiquitination status of replication
CC protein A (RPA) complex proteins in response to replication stress
CC (PubMed:29563501). {ECO:0000269|PubMed:29476094,
CC ECO:0000269|PubMed:29563501, ECO:0000269|PubMed:29576527,
CC ECO:0000269|PubMed:29576528}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:29476094,
CC ECO:0000269|PubMed:29576528};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50.4 uM for Arg-Leu-Arg-Gly-Gly-AMC {ECO:0000269|PubMed:29476094};
CC KM=4.9 uM for Ub-Rhodamine {ECO:0000269|PubMed:29576528};
CC Note=kcat is 4.9 sec(-1) with Arg-Leu-Arg-Gly-Gly-AMC as substrate
CC (PubMed:29476094). kcat is 0.084 sec(-1) with Ub-Rhodamine as
CC substrate (PubMed:29576528). {ECO:0000269|PubMed:29476094,
CC ECO:0000269|PubMed:29576528};
CC -!- SUBUNIT: Interacts with RPA1 and RPA2. {ECO:0000269|PubMed:29563501}.
CC -!- INTERACTION:
CC Q96AP4; Q92619: ARHGAP45; NbExp=3; IntAct=EBI-744706, EBI-2825900;
CC Q96AP4; P50281: MMP14; NbExp=3; IntAct=EBI-744706, EBI-992788;
CC Q96AP4; Q8WVC2: RPS21; NbExp=3; IntAct=EBI-744706, EBI-10276945;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29476094}. Nucleus
CC {ECO:0000269|PubMed:29476094, ECO:0000269|PubMed:29576527,
CC ECO:0000269|PubMed:29576528}. Note=Mostly present in the nuclear
CC fraction. Localizes to DNA lesions. {ECO:0000269|PubMed:29576527,
CC ECO:0000269|PubMed:29576528}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96AP4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96AP4-2; Sequence=VSP_019533;
CC -!- DOMAIN: The motif interacting with ubiquitin (MIU) and ZUFSP ubiquitin-
CC binding domain (zUBD, also called ZUFSP helical arm ZHA) are
CC responsible for binding the distal (outgoing) ubiquitin units S1 and S2
CC respectively. {ECO:0000269|PubMed:29576528,
CC ECO:0000305|PubMed:29476094, ECO:0000305|PubMed:29576527}.
CC -!- DOMAIN: C2H2-type zinc finger 4 is a ubiquitin-binding zinc finger
CC (UBZ) and required for polyubiquitin binding, possibly binding the
CC proximal ubiqutin, and for catalytic activity (PubMed:29576528)
CC (Probable). C2H2-type zinc fingers 1-3 are required for localization to
CC sites of DNA damage (PubMed:29576528). {ECO:0000269|PubMed:29576528,
CC ECO:0000305|PubMed:29576527}.
CC -!- SIMILARITY: Belongs to the peptidase C78 family. ZUFSP subfamily.
CC {ECO:0000305}.
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DR EMBL; AK054582; BAB70765.1; -; mRNA.
DR EMBL; BX537872; CAD97873.1; -; mRNA.
DR EMBL; AL132795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015420; AAH15420.1; -; mRNA.
DR EMBL; BC016879; AAH16879.1; -; mRNA.
DR CCDS; CCDS5110.1; -. [Q96AP4-1]
DR RefSeq; NP_659499.2; NM_145062.2. [Q96AP4-1]
DR RefSeq; XP_011533867.1; XM_011535565.2.
DR PDB; 6EI1; X-ray; 1.73 A; A=232-578.
DR PDB; 6FGE; X-ray; 1.74 A; A=231-578.
DR PDBsum; 6EI1; -.
DR PDBsum; 6FGE; -.
DR AlphaFoldDB; Q96AP4; -.
DR SMR; Q96AP4; -.
DR BioGRID; 128708; 171.
DR IntAct; Q96AP4; 8.
DR MINT; Q96AP4; -.
DR STRING; 9606.ENSP00000357565; -.
DR MEROPS; C78.003; -.
DR iPTMnet; Q96AP4; -.
DR PhosphoSitePlus; Q96AP4; -.
DR BioMuta; ZUFSP; -.
DR DMDM; 74762646; -.
DR EPD; Q96AP4; -.
DR jPOST; Q96AP4; -.
DR MassIVE; Q96AP4; -.
DR MaxQB; Q96AP4; -.
DR PaxDb; Q96AP4; -.
DR PeptideAtlas; Q96AP4; -.
DR PRIDE; Q96AP4; -.
DR ProteomicsDB; 75981; -. [Q96AP4-1]
DR ProteomicsDB; 75982; -. [Q96AP4-2]
DR Antibodypedia; 32518; 110 antibodies from 17 providers.
DR DNASU; 221302; -.
DR Ensembl; ENST00000368576.8; ENSP00000357565.3; ENSG00000153975.10. [Q96AP4-1]
DR GeneID; 221302; -.
DR KEGG; hsa:221302; -.
DR MANE-Select; ENST00000368576.8; ENSP00000357565.3; NM_145062.3; NP_659499.2.
DR UCSC; uc003pxf.3; human. [Q96AP4-1]
DR CTD; 221302; -.
DR DisGeNET; 221302; -.
DR GeneCards; ZUP1; -.
DR HGNC; HGNC:21224; ZUP1.
DR HPA; ENSG00000153975; Low tissue specificity.
DR neXtProt; NX_Q96AP4; -.
DR OpenTargets; ENSG00000153975; -.
DR PharmGKB; PA162411072; -.
DR VEuPathDB; HostDB:ENSG00000153975; -.
DR eggNOG; KOG4696; Eukaryota.
DR GeneTree; ENSGT00390000008232; -.
DR HOGENOM; CLU_017060_1_1_1; -.
DR InParanoid; Q96AP4; -.
DR OMA; EEPRIHT; -.
DR PhylomeDB; Q96AP4; -.
DR TreeFam; TF323699; -.
DR PathwayCommons; Q96AP4; -.
DR SignaLink; Q96AP4; -.
DR BioGRID-ORCS; 221302; 10 hits in 1088 CRISPR screens.
DR GenomeRNAi; 221302; -.
DR Pharos; Q96AP4; Tbio.
DR PRO; PR:Q96AP4; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q96AP4; protein.
DR Bgee; ENSG00000153975; Expressed in secondary oocyte and 165 other tissues.
DR ExpressionAtlas; Q96AP4; baseline and differential.
DR Genevisible; Q96AP4; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR InterPro; IPR012462; Peptidase_C78_UfSP1/2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF07910; Peptidase_C78; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Hydrolase;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..578
FT /note="Zinc finger-containing ubiquitin peptidase 1"
FT /id="PRO_0000244336"
FT ZN_FING 2..24
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 29..52
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000305|PubMed:29476094"
FT ZN_FING 154..177
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 193..215
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 226..248
FT /note="MIU"
FT /evidence="ECO:0000305|PubMed:29476094,
FT ECO:0000305|PubMed:29576527"
FT REGION 249..274
FT /note="zUBD/ZHA"
FT /evidence="ECO:0000305|PubMed:29476094,
FT ECO:0000305|PubMed:29576527"
FT ACT_SITE 360
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:29476094"
FT ACT_SITE 491
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:29476094"
FT ACT_SITE 512
FT /evidence="ECO:0000250|UniProtKB:Q99K23"
FT SITE 487
FT /note="Involved in the stabilization of negative charge on
FT the oxyanion by the formation of the oxyanion hole"
FT /evidence="ECO:0000305|PubMed:29576527"
FT MOD_RES 262
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..519
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019533"
FT VARIANT 379
FT /note="N -> D (in dbSNP:rs4946188)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_026889"
FT MUTAGEN 351
FT /note="S->A,Q,Y: No effect."
FT /evidence="ECO:0000269|PubMed:29476094"
FT MUTAGEN 360
FT /note="C->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:29476094,
FT ECO:0000269|PubMed:29563501, ECO:0000269|PubMed:29576527,
FT ECO:0000269|PubMed:29576528"
FT MUTAGEN 406
FT /note="D->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:29476094"
FT MUTAGEN 428
FT /note="E->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:29476094"
FT MUTAGEN 487
FT /note="Q->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:29576527"
FT MUTAGEN 491
FT /note="H->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:29476094,
FT ECO:0000269|PubMed:29563501, ECO:0000269|PubMed:29576527"
FT MUTAGEN 512
FT /note="D->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:29576527"
FT HELIX 241..266
FT /evidence="ECO:0007829|PDB:6EI1"
FT HELIX 275..288
FT /evidence="ECO:0007829|PDB:6EI1"
FT HELIX 294..310
FT /evidence="ECO:0007829|PDB:6EI1"
FT HELIX 322..332
FT /evidence="ECO:0007829|PDB:6EI1"
FT STRAND 336..342
FT /evidence="ECO:0007829|PDB:6EI1"
FT TURN 353..358
FT /evidence="ECO:0007829|PDB:6EI1"
FT HELIX 360..373
FT /evidence="ECO:0007829|PDB:6EI1"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:6EI1"
FT HELIX 379..382
FT /evidence="ECO:0007829|PDB:6EI1"
FT HELIX 390..403
FT /evidence="ECO:0007829|PDB:6EI1"
FT HELIX 407..412
FT /evidence="ECO:0007829|PDB:6EI1"
FT TURN 413..415
FT /evidence="ECO:0007829|PDB:6EI1"
FT HELIX 426..435
FT /evidence="ECO:0007829|PDB:6EI1"
FT STRAND 438..445
FT /evidence="ECO:0007829|PDB:6EI1"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:6EI1"
FT HELIX 456..466
FT /evidence="ECO:0007829|PDB:6EI1"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:6EI1"
FT STRAND 484..488
FT /evidence="ECO:0007829|PDB:6EI1"
FT STRAND 491..501
FT /evidence="ECO:0007829|PDB:6EI1"
FT STRAND 506..511
FT /evidence="ECO:0007829|PDB:6EI1"
FT HELIX 517..520
FT /evidence="ECO:0007829|PDB:6EI1"
FT HELIX 521..524
FT /evidence="ECO:0007829|PDB:6EI1"
FT STRAND 525..527
FT /evidence="ECO:0007829|PDB:6EI1"
FT HELIX 530..533
FT /evidence="ECO:0007829|PDB:6EI1"
FT TURN 534..536
FT /evidence="ECO:0007829|PDB:6EI1"
FT HELIX 540..542
FT /evidence="ECO:0007829|PDB:6EI1"
FT STRAND 548..556
FT /evidence="ECO:0007829|PDB:6EI1"
FT HELIX 559..568
FT /evidence="ECO:0007829|PDB:6EI1"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:6EI1"
SQ SEQUENCE 578 AA; 65959 MW; 8590426B41F2C9A0 CRC64;
MLSCNICGET VTSEPDMKAH LIVHMESEII CPFCKLSGVN YDEMCFHIET AHFEQNTLER
NFERINTVQY GTSDNKKDNT LQCGMEVNSS ILSGCASNHP KNSAQNLTKD STLKHEGFYS
ENLTESRKFL KSREKQSSLT EIKGSVYETT YSPPECPFCG KIEEHSEDME THVKTKHANL
LDIPLEDCDQ PLYDCPMCGL ICTNYHILQE HVDLHLEENS FQQGMDRVQC SGDLQLAHQL
QQEEDRKRRS EESRQEIEEF QKLQRQYGLD NSGGYKQQQL RNMEIEVNRG RMPPSEFHRR
KADMMESLAL GFDDGKTKTS GIIEALHRYY QNAATDVRRV WLSSVVDHFH SSLGDKGWGC
GYRNFQMLLS SLLQNDAYND CLKGMLIPCI PKIQSMIEDA WKEGFDPQGA SQLNNRLQGT
KAWIGACEVY ILLTSLRVKC HIVDFHKSTG PLGTHPRLFE WILNYYSSEG EGSPKVVCTS
KPPIYLQHQG HSRTVIGIEE KKNRTLCLLI LDPGCPSREM QKLLKQDIEA SSLKQLRKSM
GNLKHKQYQI LAVEGALSLE EKLARRQASQ VFTAEKIP
