SCLY_HUMAN
ID SCLY_HUMAN Reviewed; 445 AA.
AC Q96I15; B9A068; J3KN06; Q53SN1; Q53SN8; Q7L670; Q9NVT7; Q9NZR7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 4.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Selenocysteine lyase {ECO:0000303|PubMed:10692412};
DE Short=hSCL {ECO:0000303|PubMed:10692412};
DE EC=4.4.1.16 {ECO:0000250|UniProtKB:Q68FT9};
GN Name=SCLY; Synonyms=SCL;
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).
RC TISSUE=Brain;
RX PubMed=10692412; DOI=10.1074/jbc.275.9.6195;
RA Mihara H., Kurihara T., Watanabe T., Yoshimura T., Esaki N.;
RT "cDNA cloning, purification, and characterization of mouse liver
RT selenocysteine lyase. Candidate for selenium delivery protein in
RT selenoprotein synthesis.";
RL J. Biol. Chem. 275:6195-6200(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-175.
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 189-445.
RC TISSUE=Teratocarcinoma;
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 [6]
RP INDUCTION BY JUN.
RX PubMed=16874457; DOI=10.2478/s11658-006-0035-1;
RA Jafari C., Panzer U., Steinmetz O.M., Zahner G., Stahl R.A., Harendza S.;
RT "Enhanced expression of selenocysteine lyase in acute glomerulonephritis
RT and its regulation by AP-1.";
RL Cell. Mol. Biol. Lett. 11:424-437(2006).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 8-445 IN COMPLEX WITH PYRIDOXAL
RP PHOSPHATE, AND COFACTOR.
RG Structural genomics consortium (SGC);
RT "Structure of human selenocysteine lyase.";
RL Submitted (JUL-2006) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the decomposition of L-selenocysteine to L-alanine
CC and elemental selenium. {ECO:0000250|UniProtKB:Q68FT9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + L-selenocysteine = A + H(+) + hydrogenselenide + L-
CC alanine; Xref=Rhea:RHEA:11632, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:29317, ChEBI:CHEBI:57843,
CC ChEBI:CHEBI:57972; EC=4.4.1.16;
CC Evidence={ECO:0000250|UniProtKB:Q68FT9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11633;
CC Evidence={ECO:0000250|UniProtKB:Q68FT9};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|Ref.12};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q68FT9}.
CC -!- INTERACTION:
CC Q96I15; Q8N448: LNX2; NbExp=3; IntAct=EBI-2823066, EBI-2340947;
CC Q96I15; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-2823066, EBI-750109;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9JLI6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96I15-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96I15-2; Sequence=VSP_030854;
CC -!- INDUCTION: Up-regulated in acute glomerulonephritis. Regulated by
CC JUN/AP-1. {ECO:0000269|PubMed:16874457}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91659.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF175767; AAF36816.1; -; mRNA.
DR EMBL; AC016757; AAY24333.1; -; Genomic_DNA.
DR EMBL; AC016776; AAY24221.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW71139.1; -; Genomic_DNA.
DR EMBL; BC000586; AAH00586.2; -; mRNA.
DR EMBL; BC007891; AAH07891.1; -; mRNA.
DR EMBL; AK001377; BAA91659.1; ALT_INIT; mRNA.
DR CCDS; CCDS2524.2; -. [Q96I15-1]
DR RefSeq; NP_057594.4; NM_016510.5. [Q96I15-1]
DR PDB; 3GZC; X-ray; 2.10 A; A/B=8-445.
DR PDB; 3GZD; X-ray; 1.80 A; A/B/C/D=8-445.
DR PDBsum; 3GZC; -.
DR PDBsum; 3GZD; -.
DR AlphaFoldDB; Q96I15; -.
DR SMR; Q96I15; -.
DR BioGRID; 119599; 39.
DR IntAct; Q96I15; 10.
DR MINT; Q96I15; -.
DR STRING; 9606.ENSP00000254663; -.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR DrugBank; DB11135; Selenium.
DR GlyGen; Q96I15; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96I15; -.
DR PhosphoSitePlus; Q96I15; -.
DR BioMuta; SCLY; -.
DR DMDM; 527504087; -.
DR EPD; Q96I15; -.
DR jPOST; Q96I15; -.
DR MassIVE; Q96I15; -.
DR MaxQB; Q96I15; -.
DR PaxDb; Q96I15; -.
DR PeptideAtlas; Q96I15; -.
DR PRIDE; Q96I15; -.
DR ProteomicsDB; 76802; -. [Q96I15-1]
DR ProteomicsDB; 76803; -. [Q96I15-2]
DR Antibodypedia; 34490; 138 antibodies from 22 providers.
DR DNASU; 51540; -.
DR Ensembl; ENST00000254663.12; ENSP00000254663.7; ENSG00000132330.18. [Q96I15-1]
DR Ensembl; ENST00000409736.6; ENSP00000387162.2; ENSG00000132330.18. [Q96I15-2]
DR GeneID; 51540; -.
DR KEGG; hsa:51540; -.
DR MANE-Select; ENST00000254663.12; ENSP00000254663.7; NM_016510.7; NP_057594.5.
DR UCSC; uc061uct.1; human. [Q96I15-1]
DR CTD; 51540; -.
DR DisGeNET; 51540; -.
DR GeneCards; SCLY; -.
DR HGNC; HGNC:18161; SCLY.
DR HPA; ENSG00000132330; Tissue enhanced (liver).
DR MIM; 611056; gene.
DR neXtProt; NX_Q96I15; -.
DR OpenTargets; ENSG00000132330; -.
DR PharmGKB; PA134979359; -.
DR VEuPathDB; HostDB:ENSG00000132330; -.
DR eggNOG; KOG1549; Eukaryota.
DR GeneTree; ENSGT00940000157773; -.
DR HOGENOM; CLU_003433_10_0_1; -.
DR InParanoid; Q96I15; -.
DR OrthoDB; 697150at2759; -.
DR PhylomeDB; Q96I15; -.
DR TreeFam; TF313550; -.
DR BRENDA; 4.4.1.16; 2681.
DR PathwayCommons; Q96I15; -.
DR Reactome; R-HSA-2408508; Metabolism of ingested SeMet, Sec, MeSec into H2Se.
DR SignaLink; Q96I15; -.
DR BioGRID-ORCS; 51540; 15 hits in 1081 CRISPR screens.
DR ChiTaRS; SCLY; human.
DR EvolutionaryTrace; Q96I15; -.
DR GenomeRNAi; 51540; -.
DR Pharos; Q96I15; Tbio.
DR PRO; PR:Q96I15; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q96I15; protein.
DR Bgee; ENSG00000132330; Expressed in right lobe of liver and 105 other tissues.
DR ExpressionAtlas; Q96I15; baseline and differential.
DR Genevisible; Q96I15; HS.
DR GO; GO:1902494; C:catalytic complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016597; F:amino acid binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0009000; F:selenocysteine lyase activity; TAS:ProtInc.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0070279; F:vitamin B6 binding; IEA:Ensembl.
DR GO; GO:0006520; P:cellular amino acid metabolic process; TAS:ProtInc.
DR GO; GO:0016261; P:selenocysteine catabolic process; IEA:Ensembl.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR016454; Cysteine_dSase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Lyase;
KW Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..445
FT /note="Selenocysteine lyase"
FT /id="PRO_0000317012"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 388
FT /note="S-selanylcysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q68FT9"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 259
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|Ref.12"
FT VAR_SEQ 308..445
FT /note="AAELVTQNCEAYEAHMRDVRDYLEERLEAEFGQKRIHLNSQFPGTQRLPNTC
FT NFSIRGPRLQGHVVLAQCRVLMASVGAACHSDHGDQPSPVLLSYGVPFDVARNALRLSV
FT GRSTTRAEVDLVVQDLKQAVAQLEDQA -> VSPGELEEMS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10692412"
FT /id="VSP_030854"
FT VARIANT 52
FT /note="K -> E (in dbSNP:rs7597367)"
FT /id="VAR_038464"
FT VARIANT 175
FT /note="A -> T (in dbSNP:rs3210400)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038465"
FT VARIANT 276
FT /note="F -> S (in dbSNP:rs35637307)"
FT /id="VAR_038466"
FT CONFLICT 1
FT /note="M -> MPGSSGAGM (in Ref. 3; EAW71139)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="L -> V (in Ref. 1; AAF36816)"
FT /evidence="ECO:0000305"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:3GZD"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:3GZD"
FT HELIX 66..85
FT /evidence="ECO:0007829|PDB:3GZD"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:3GZD"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:3GZD"
FT HELIX 99..118
FT /evidence="ECO:0007829|PDB:3GZD"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:3GZD"
FT HELIX 146..157
FT /evidence="ECO:0007829|PDB:3GZD"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:3GZD"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:3GZD"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:3GZD"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:3GZD"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:3GZD"
FT HELIX 206..222
FT /evidence="ECO:0007829|PDB:3GZD"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:3GZD"
FT TURN 235..240
FT /evidence="ECO:0007829|PDB:3GZD"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:3GZD"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:3GZD"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3GZD"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:3GZD"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:3GZD"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:3GZD"
FT HELIX 299..338
FT /evidence="ECO:0007829|PDB:3GZD"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:3GZD"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:3GZD"
FT STRAND 358..363
FT /evidence="ECO:0007829|PDB:3GZD"
FT HELIX 370..376
FT /evidence="ECO:0007829|PDB:3GZD"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:3GZD"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:3GZD"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:3GZD"
FT HELIX 398..402
FT /evidence="ECO:0007829|PDB:3GZD"
FT HELIX 407..410
FT /evidence="ECO:0007829|PDB:3GZD"
FT STRAND 413..417
FT /evidence="ECO:0007829|PDB:3GZD"
FT HELIX 424..442
FT /evidence="ECO:0007829|PDB:3GZD"
SQ SEQUENCE 445 AA; 48149 MW; D26F3FCFB8B165D2 CRC64;
MEAAVAPGRD APAPAASQPS GCGKHNSPER KVYMDYNATT PLEPEVIQAM TKAMWEAWGN
PSSPYSAGRK AKDIINAARE SLAKMIGGKP QDIIFTSGGT ESNNLVIHSV VKHFHANQTS
KGHTGGHHSP VKGAKPHFIT SSVEHDSIRL PLEHLVEEQV AAVTFVPVSK VSGQAEVDDI
LAAVRPTTRL VTIMLANNET GIVMPVPEIS QRIKALNQER VAAGLPPILV HTDAAQALGK
QRVDVEDLGV DFLTIVGHKF YGPRIGALYI RGLGEFTPLY PMLFGGGQER NFRPGTENTP
MIAGLGKAAE LVTQNCEAYE AHMRDVRDYL EERLEAEFGQ KRIHLNSQFP GTQRLPNTCN
FSIRGPRLQG HVVLAQCRVL MASVGAACHS DHGDQPSPVL LSYGVPFDVA RNALRLSVGR
STTRAEVDLV VQDLKQAVAQ LEDQA
