UCK2_HUMAN
ID UCK2_HUMAN Reviewed; 261 AA.
AC Q9BZX2; Q5VV91; Q7KZV3; Q92528; Q96KG5; Q9BU42;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Uridine-cytidine kinase 2;
DE Short=UCK 2;
DE EC=2.7.1.48 {ECO:0000269|PubMed:11306702, ECO:0000269|PubMed:11494055};
DE AltName: Full=Cytidine monophosphokinase 2;
DE AltName: Full=Testis-specific protein TSA903;
DE AltName: Full=Uridine monophosphokinase 2;
GN Name=UCK2; Synonyms=UMPK;
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 [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=8812458; DOI=10.1006/geno.1996.0467;
RA Ozaki K., Kuroki T., Hayashi S., Nakamura Y.;
RT "Isolation of three testis-specific genes (TSA303, TSA806, TSA903) by a
RT differential mRNA display method.";
RL Genomics 36:316-319(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=11306702; DOI=10.1124/mol.59.5.1181;
RA Van Rompay A.R., Norda A., Linden K., Johansson M., Karlsson A.;
RT "Phosphorylation of uridine and cytidine nucleoside analogs by two human
RT uridine-cytidine kinases.";
RL Mol. Pharmacol. 59:1181-1186(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-261 (ISOFORM 1), FUNCTION, CATALYTIC
RP ACTIVITY, AND PATHWAY.
RC TISSUE=Fibrosarcoma;
RX PubMed=11494055;
RA Koizumi K., Shimamoto Y., Azuma A., Wataya Y., Matsuda A., Sasaki T.,
RA Fukushima M.;
RT "Cloning and expression of uridine/cytidine kinase cDNA from human
RT fibrosarcoma cells.";
RL Int. J. Mol. Med. 8:273-278(2001).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-250 IN COMPLEXES WITH ADP;
RP CYTIDINE; CMP; CTP AND UTP, AND SUBUNIT.
RX PubMed=15130468; DOI=10.1016/j.str.2004.02.038;
RA Suzuki N.N., Koizumi K., Fukushima M., Matsuda A., Inagaki F.;
RT "Structural basis for the specificity, catalysis, and regulation of human
RT uridine-cytidine kinase.";
RL Structure 12:751-764(2004).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ADP AND CMP, AND
RP SUBUNIT.
RX PubMed=15735337; DOI=10.1107/s0907444904032937;
RA Appleby T.C., Larson G., Cheney I.W., Walker H., Wu J.Z., Zhong W.,
RA Hong Z., Yao N.;
RT "Structure of human uridine-cytidine kinase 2 determined by SIRAS using a
RT rotating-anode X-ray generator and a single samarium derivative.";
RL Acta Crystallogr. D 61:278-284(2005).
CC -!- FUNCTION: Phosphorylates uridine and cytidine to uridine monophosphate
CC and cytidine monophosphate (PubMed:11306702, PubMed:11494055). Does not
CC phosphorylate deoxyribonucleosides or purine ribonucleosides
CC (PubMed:11306702). Can use ATP or GTP as a phosphate donor
CC (PubMed:11306702). Can also phosphorylate cytidine and uridine
CC nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4-
CC thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)-benzoylcytidine,
CC 5-fluorocytidine, 2-thiocytidine, 5-methylcytidine, and N(4)-
CC anisoylcytidine (PubMed:11306702). {ECO:0000269|PubMed:11306702,
CC ECO:0000269|PubMed:11494055}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + uridine = ADP + H(+) + UMP; Xref=Rhea:RHEA:16825,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16704, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57865, ChEBI:CHEBI:456216; EC=2.7.1.48;
CC Evidence={ECO:0000269|PubMed:11306702, ECO:0000269|PubMed:11494055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cytidine = ADP + CMP + H(+); Xref=Rhea:RHEA:24674,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17562, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.1.48;
CC Evidence={ECO:0000269|PubMed:11306702, ECO:0000269|PubMed:11494055};
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC CTP from cytidine: step 1/3. {ECO:0000269|PubMed:11306702,
CC ECO:0000269|PubMed:11494055}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uridine: step 1/1. {ECO:0000269|PubMed:11306702,
CC ECO:0000269|PubMed:11494055}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15130468,
CC ECO:0000269|PubMed:15735337}.
CC -!- INTERACTION:
CC Q9BZX2; Q9BZX2: UCK2; NbExp=3; IntAct=EBI-1053938, EBI-1053938;
CC Q9BZX2-1; Q9BZX2-1: UCK2; NbExp=2; IntAct=EBI-21013535, EBI-21013535;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BZX2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BZX2-2; Sequence=VSP_014262;
CC -!- TISSUE SPECIFICITY: According to PubMed:8812458; testis-specific.
CC According to PubMed:11306702, placenta-specific.
CC {ECO:0000269|PubMed:8812458}.
CC -!- SIMILARITY: Belongs to the uridine kinase family. {ECO:0000305}.
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DR EMBL; D78335; BAA11349.1; -; mRNA.
DR EMBL; AF236637; AAK14053.1; -; mRNA.
DR EMBL; BT006860; AAP35506.1; -; mRNA.
DR EMBL; CR456857; CAG33138.1; -; mRNA.
DR EMBL; AL451074; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL358115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002906; AAH02906.2; -; mRNA.
DR EMBL; AB062451; BAB56162.1; -; mRNA.
DR CCDS; CCDS1252.1; -. [Q9BZX2-1]
DR RefSeq; NP_036606.2; NM_012474.4. [Q9BZX2-1]
DR PDB; 1UDW; X-ray; 2.60 A; A/B=1-250.
DR PDB; 1UEI; X-ray; 2.60 A; A/B=1-250.
DR PDB; 1UEJ; X-ray; 2.61 A; A/B=1-250.
DR PDB; 1UFQ; X-ray; 2.50 A; A/B/C/D=1-250.
DR PDB; 1UJ2; X-ray; 1.80 A; A/B=1-250.
DR PDB; 1XRJ; X-ray; 2.00 A; A/B=1-261.
DR PDB; 6N53; X-ray; 2.70 A; A/B=1-250.
DR PDB; 6N54; X-ray; 2.42 A; A/B=1-250.
DR PDB; 6N55; X-ray; 3.08 A; A/B/C/D/E/F/G/H=1-250.
DR PDB; 6PWZ; X-ray; 3.00 A; A/B/C/D/E/F/G/H=1-250.
DR PDBsum; 1UDW; -.
DR PDBsum; 1UEI; -.
DR PDBsum; 1UEJ; -.
DR PDBsum; 1UFQ; -.
DR PDBsum; 1UJ2; -.
DR PDBsum; 1XRJ; -.
DR PDBsum; 6N53; -.
DR PDBsum; 6N54; -.
DR PDBsum; 6N55; -.
DR PDBsum; 6PWZ; -.
DR AlphaFoldDB; Q9BZX2; -.
DR SMR; Q9BZX2; -.
DR BioGRID; 113217; 64.
DR IntAct; Q9BZX2; 10.
DR STRING; 9606.ENSP00000356853; -.
DR BindingDB; Q9BZX2; -.
DR ChEMBL; CHEMBL2469; -.
DR DrugBank; DB02097; Cytidine.
DR DrugBank; DB03403; Cytidine-5'-Monophosphate.
DR DrugBank; DB02431; Cytidine-5'-Triphosphate.
DR DrugBank; DB04005; Uridine 5'-triphosphate.
DR DrugCentral; Q9BZX2; -.
DR GlyGen; Q9BZX2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BZX2; -.
DR PhosphoSitePlus; Q9BZX2; -.
DR BioMuta; UCK2; -.
DR DMDM; 20455356; -.
DR EPD; Q9BZX2; -.
DR jPOST; Q9BZX2; -.
DR MassIVE; Q9BZX2; -.
DR MaxQB; Q9BZX2; -.
DR PaxDb; Q9BZX2; -.
DR PeptideAtlas; Q9BZX2; -.
DR PRIDE; Q9BZX2; -.
DR ProteomicsDB; 79917; -. [Q9BZX2-1]
DR ProteomicsDB; 79918; -. [Q9BZX2-2]
DR Antibodypedia; 34333; 200 antibodies from 27 providers.
DR DNASU; 7371; -.
DR Ensembl; ENST00000367879.9; ENSP00000356853.4; ENSG00000143179.16. [Q9BZX2-1]
DR Ensembl; ENST00000469256.6; ENSP00000476692.1; ENSG00000143179.16. [Q9BZX2-2]
DR Ensembl; ENST00000470820.1; ENSP00000476327.1; ENSG00000143179.16. [Q9BZX2-2]
DR GeneID; 7371; -.
DR KEGG; hsa:7371; -.
DR MANE-Select; ENST00000367879.9; ENSP00000356853.4; NM_012474.5; NP_036606.2.
DR UCSC; uc021pec.2; human. [Q9BZX2-1]
DR CTD; 7371; -.
DR DisGeNET; 7371; -.
DR GeneCards; UCK2; -.
DR HGNC; HGNC:12562; UCK2.
DR HPA; ENSG00000143179; Low tissue specificity.
DR MIM; 609329; gene.
DR neXtProt; NX_Q9BZX2; -.
DR OpenTargets; ENSG00000143179; -.
DR PharmGKB; PA362; -.
DR VEuPathDB; HostDB:ENSG00000143179; -.
DR eggNOG; KOG4203; Eukaryota.
DR GeneTree; ENSGT01020000230412; -.
DR HOGENOM; CLU_021278_1_1_1; -.
DR InParanoid; Q9BZX2; -.
DR OMA; WGEISNN; -.
DR PhylomeDB; Q9BZX2; -.
DR TreeFam; TF316686; -.
DR BioCyc; MetaCyc:HS07003-MON; -.
DR BRENDA; 2.7.1.48; 2681.
DR PathwayCommons; Q9BZX2; -.
DR Reactome; R-HSA-73614; Pyrimidine salvage.
DR SABIO-RK; Q9BZX2; -.
DR SignaLink; Q9BZX2; -.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR BioGRID-ORCS; 7371; 22 hits in 1083 CRISPR screens.
DR ChiTaRS; UCK2; human.
DR EvolutionaryTrace; Q9BZX2; -.
DR GeneWiki; UCK2; -.
DR GenomeRNAi; 7371; -.
DR Pharos; Q9BZX2; Tbio.
DR PRO; PR:Q9BZX2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BZX2; protein.
DR Bgee; ENSG00000143179; Expressed in mucosa of transverse colon and 155 other tissues.
DR ExpressionAtlas; Q9BZX2; baseline and differential.
DR Genevisible; Q9BZX2; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043771; F:cytidine kinase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004849; F:uridine kinase activity; IDA:UniProtKB.
DR GO; GO:0044211; P:CTP salvage; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0044206; P:UMP salvage; IDA:UniProtKB.
DR CDD; cd02023; UMPK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006083; PRK/URK.
DR InterPro; IPR029925; UCK-2.
DR InterPro; IPR000764; Uridine_kinase-like.
DR PANTHER; PTHR10285:SF131; PTHR10285:SF131; 1.
DR Pfam; PF00485; PRK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00235; udk; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..261
FT /note="Uridine-cytidine kinase 2"
FT /id="PRO_0000164455"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15130468,
FT ECO:0000269|PubMed:15735337"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15130468,
FT ECO:0000269|PubMed:15735337"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15130468,
FT ECO:0000269|PubMed:15735337"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15130468,
FT ECO:0000269|PubMed:15735337"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15130468,
FT ECO:0000269|PubMed:15735337"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15130468,
FT ECO:0000269|PubMed:15735337"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15130468,
FT ECO:0000269|PubMed:15735337"
FT BINDING 213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15130468,
FT ECO:0000269|PubMed:15735337"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1..150
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8812458, ECO:0000303|Ref.3,
FT ECO:0000303|Ref.4"
FT /id="VSP_014262"
FT CONFLICT 202
FT /note="K -> Q (in Ref. 1; BAA11349)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="V -> E (in Ref. 1; BAA11349)"
FT /evidence="ECO:0000305"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:1UJ2"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:1UJ2"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1UJ2"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:1UJ2"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:1UJ2"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:1UJ2"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:1UJ2"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1UJ2"
FT HELIX 91..102
FT /evidence="ECO:0007829|PDB:1UJ2"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:1UJ2"
FT TURN 114..117
FT /evidence="ECO:0007829|PDB:1UJ2"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:1UJ2"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:1UJ2"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:1UJ2"
FT HELIX 143..148
FT /evidence="ECO:0007829|PDB:1UJ2"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:1UJ2"
FT HELIX 159..173
FT /evidence="ECO:0007829|PDB:1UJ2"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:1UJ2"
FT HELIX 189..196
FT /evidence="ECO:0007829|PDB:1UJ2"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:1UJ2"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:1UJ2"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1UJ2"
FT HELIX 215..230
FT /evidence="ECO:0007829|PDB:1UJ2"
SQ SEQUENCE 261 AA; 29299 MW; 71791346F091EBFD CRC64;
MAGDSEQTLQ NHQQPNGGEP FLIGVSGGTA SGKSSVCAKI VQLLGQNEVD YRQKQVVILS
QDSFYRVLTS EQKAKALKGQ FNFDHPDAFD NELILKTLKE ITEGKTVQIP VYDFVSHSRK
EETVTVYPAD VVLFEGILAF YSQEVRDLFQ MKLFVDTDAD TRLSRRVLRD ISERGRDLEQ
ILSQYITFVK PAFEEFCLPT KKYADVIIPR GADNLVAINL IVQHIQDILN GGPSKRQTNG
CLNGYTPSRK RQASESSSRP H
