ZN692_HUMAN
ID ZN692_HUMAN Reviewed; 519 AA.
AC Q9BU19; B4DXZ0; Q5SRA5; Q5SRA6; Q9HBC9; Q9NW93; Q9NWY6; Q9UF97;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Zinc finger protein 692 {ECO:0000305};
DE AltName: Full=AICAR responsive element binding protein {ECO:0000303|PubMed:17097062};
GN Name=ZNF692;
GN Synonyms=AREBP {ECO:0000303|PubMed:17097062},
GN ZFP692 {ECO:0000250|UniProtKB:Q3U381};
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], TISSUE SPECIFICITY, MUTAGENESIS OF THR-62;
RP SER-63; THR-386; SER-402; THR-442 AND SER-470, PHOSPHORYLATION AT SER-470,
RP AND FUNCTION.
RX PubMed=17097062; DOI=10.1016/j.bbrc.2006.10.124;
RA Inoue E., Yamauchi J.;
RT "AMP-activated protein kinase regulates PEPCK gene expression by direct
RT phosphorylation of a novel zinc finger transcription factor.";
RL Biochem. Biophys. Res. Commun. 351:793-799(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 5), AND VARIANT
RP ARG-230.
RC TISSUE=Carcinoma, Embryo, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Testis;
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 221-519.
RC TISSUE=Parathyroid adenoma;
RA Pryor J.S., Sullivan L., Dial M., May K., Morgan M., Smith C., Buford D.,
RA Kirklin S., Williams D., Pugh M.;
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION.
RX PubMed=21910974; DOI=10.1016/j.bbrc.2011.08.120;
RA Shirai T., Inoue E., Ishimi Y., Yamauchi J.;
RT "AICAR response element binding protein (AREBP), a key modulator of hepatic
RT glucose production regulated by AMPK in vivo.";
RL Biochem. Biophys. Res. Commun. 414:287-291(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 AND SER-231, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP STRUCTURE BY NMR OF 328-481.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of ZF-C2H2 domains of zinc finger protein 692.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: May act as an transcriptional repressor for PCK1 gene
CC expression, in turn may participate in the hepatic gluconeogenesis
CC regulation through the activated AMPK signaling pathway.
CC {ECO:0000269|PubMed:17097062, ECO:0000269|PubMed:21910974}.
CC -!- INTERACTION:
CC Q9BU19; Q92993: KAT5; NbExp=3; IntAct=EBI-12076976, EBI-399080;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9BU19-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BU19-2; Sequence=VSP_018188;
CC Name=3;
CC IsoId=Q9BU19-3; Sequence=VSP_018186;
CC Name=4;
CC IsoId=Q9BU19-4; Sequence=VSP_018185, VSP_018187;
CC Name=5;
CC IsoId=Q9BU19-5; Sequence=VSP_043025;
CC -!- TISSUE SPECIFICITY: Ubiquitous (PubMed:17097062). Highly expressed in
CC brain, thymus and spleen (PubMed:17097062).
CC {ECO:0000269|PubMed:17097062}.
CC -!- PTM: Phosphorylation at Ser-470 results in loss of DNA-binding
CC activity. {ECO:0000269|PubMed:17097062}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK000538; BAA91239.1; -; mRNA.
DR EMBL; AK001070; BAA91490.1; -; mRNA.
DR EMBL; AK302187; BAG63552.1; -; mRNA.
DR EMBL; AL133100; CAB61410.2; -; mRNA.
DR EMBL; AL672291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002948; AAH02948.1; -; mRNA.
DR EMBL; AF256175; AAG15327.1; -; Transcribed_RNA.
DR CCDS; CCDS31127.1; -. [Q9BU19-1]
DR CCDS; CCDS44348.1; -. [Q9BU19-5]
DR CCDS; CCDS53487.1; -. [Q9BU19-2]
DR PIR; T42682; T42682.
DR RefSeq; NP_001129508.1; NM_001136036.2. [Q9BU19-5]
DR RefSeq; NP_001180257.1; NM_001193328.1. [Q9BU19-2]
DR RefSeq; NP_060335.2; NM_017865.3. [Q9BU19-1]
DR RefSeq; XP_011542524.1; XM_011544222.1. [Q9BU19-1]
DR PDB; 2D9H; NMR; -; A=417-481.
DR PDB; 2DLK; NMR; -; A=328-393.
DR PDB; 6H0G; X-ray; 4.25 A; C/F=416-441.
DR PDBsum; 2D9H; -.
DR PDBsum; 2DLK; -.
DR PDBsum; 6H0G; -.
DR AlphaFoldDB; Q9BU19; -.
DR SMR; Q9BU19; -.
DR BioGRID; 120789; 39.
DR IntAct; Q9BU19; 29.
DR STRING; 9606.ENSP00000391200; -.
DR iPTMnet; Q9BU19; -.
DR PhosphoSitePlus; Q9BU19; -.
DR BioMuta; ZNF692; -.
DR DMDM; 74761262; -.
DR EPD; Q9BU19; -.
DR jPOST; Q9BU19; -.
DR MassIVE; Q9BU19; -.
DR MaxQB; Q9BU19; -.
DR PaxDb; Q9BU19; -.
DR PeptideAtlas; Q9BU19; -.
DR PRIDE; Q9BU19; -.
DR ProteomicsDB; 79040; -. [Q9BU19-1]
DR ProteomicsDB; 79041; -. [Q9BU19-2]
DR ProteomicsDB; 79042; -. [Q9BU19-3]
DR ProteomicsDB; 79044; -. [Q9BU19-5]
DR TopDownProteomics; Q9BU19-3; -. [Q9BU19-3]
DR Antibodypedia; 54395; 45 antibodies from 15 providers.
DR DNASU; 55657; -.
DR Ensembl; ENST00000306601.9; ENSP00000305483.5; ENSG00000171163.16. [Q9BU19-1]
DR Ensembl; ENST00000366471.7; ENSP00000355427.3; ENSG00000171163.16. [Q9BU19-2]
DR Ensembl; ENST00000451251.5; ENSP00000391200.1; ENSG00000171163.16. [Q9BU19-5]
DR Ensembl; ENST00000463519.5; ENSP00000436308.1; ENSG00000171163.16. [Q9BU19-4]
DR GeneID; 55657; -.
DR KEGG; hsa:55657; -.
DR MANE-Select; ENST00000306601.9; ENSP00000305483.5; NM_017865.4; NP_060335.2.
DR UCSC; uc001ifc.3; human. [Q9BU19-1]
DR CTD; 55657; -.
DR DisGeNET; 55657; -.
DR GeneCards; ZNF692; -.
DR HGNC; HGNC:26049; ZNF692.
DR HPA; ENSG00000171163; Low tissue specificity.
DR MIM; 617758; gene.
DR neXtProt; NX_Q9BU19; -.
DR OpenTargets; ENSG00000171163; -.
DR PharmGKB; PA142670491; -.
DR VEuPathDB; HostDB:ENSG00000171163; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161175; -.
DR HOGENOM; CLU_045687_1_0_1; -.
DR InParanoid; Q9BU19; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9BU19; -.
DR TreeFam; TF332664; -.
DR PathwayCommons; Q9BU19; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q9BU19; -.
DR SIGNOR; Q9BU19; -.
DR BioGRID-ORCS; 55657; 128 hits in 1102 CRISPR screens.
DR ChiTaRS; ZNF692; human.
DR EvolutionaryTrace; Q9BU19; -.
DR GenomeRNAi; 55657; -.
DR Pharos; Q9BU19; Tbio.
DR PRO; PR:Q9BU19; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BU19; protein.
DR Bgee; ENSG00000171163; Expressed in right hemisphere of cerebellum and 192 other tissues.
DR ExpressionAtlas; Q9BU19; baseline and differential.
DR Genevisible; Q9BU19; HS.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006111; P:regulation of gluconeogenesis; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..519
FT /note="Zinc finger protein 692"
FT /id="PRO_0000234014"
FT ZN_FING 328..353
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 359..383
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 389..411
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 417..439
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 448..471
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 123..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..207
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 470
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000269|PubMed:17097062"
FT VAR_SEQ 1
FT /note="M -> MPLVHM (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043025"
FT VAR_SEQ 61..96
FT /note="YTSSGCVLCAGPEPLPPKGLQYLVLLSHAHSRECSL -> ACPAALFHPQVS
FT HFTRTACVTCGLRGSCSPPHGLSE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_018185"
FT VAR_SEQ 88..259
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_018186"
FT VAR_SEQ 97..519
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_018187"
FT VAR_SEQ 175..220
FT /note="RRVGPPPETFPPPGEEEGEEEEDNDEDEEEMLSDASLWTYSSSPDD -> S
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_018188"
FT VARIANT 230
FT /note="P -> R (in dbSNP:rs13313088)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_033590"
FT MUTAGEN 62
FT /note="T->A: Does not affect phosphorylation by AMPK."
FT /evidence="ECO:0000269|PubMed:17097062"
FT MUTAGEN 63
FT /note="S->A: Does not affect phosphorylation by AMPK."
FT /evidence="ECO:0000269|PubMed:17097062"
FT MUTAGEN 386
FT /note="T->A: Does not affect phosphorylation by AMPK."
FT /evidence="ECO:0000269|PubMed:17097062"
FT MUTAGEN 402
FT /note="S->A: Does not affect phosphorylation by AMPK."
FT /evidence="ECO:0000269|PubMed:17097062"
FT MUTAGEN 442
FT /note="T->A: Does not affect phosphorylation by AMPK."
FT /evidence="ECO:0000269|PubMed:17097062"
FT MUTAGEN 470
FT /note="S->A: Reduces phosphorylation by AMPK. Does not
FT affect DNA binding. Does not repress transcription of
FT PCK1."
FT /evidence="ECO:0000269|PubMed:17097062"
FT CONFLICT 373
FT /note="K -> R (in Ref. 2; BAA91490)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="S -> G (in Ref. 2; BAA91239)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="H -> R (in Ref. 2; BAA91490)"
FT /evidence="ECO:0000305"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:2DLK"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:2DLK"
FT HELIX 342..351
FT /evidence="ECO:0007829|PDB:2DLK"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:2DLK"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:2DLK"
FT STRAND 369..372
FT /evidence="ECO:0007829|PDB:2DLK"
FT HELIX 373..384
FT /evidence="ECO:0007829|PDB:2DLK"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:2D9H"
FT STRAND 425..428
FT /evidence="ECO:0007829|PDB:2D9H"
FT HELIX 429..442
FT /evidence="ECO:0007829|PDB:2D9H"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:2D9H"
FT TURN 451..453
FT /evidence="ECO:0007829|PDB:2D9H"
FT STRAND 456..459
FT /evidence="ECO:0007829|PDB:2D9H"
FT HELIX 460..469
FT /evidence="ECO:0007829|PDB:2D9H"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:2D9H"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:2D9H"
SQ SEQUENCE 519 AA; 56968 MW; DEFAEF73C910619E CRC64;
MASSPAVDVS CRRREKRRQL DARRSKCRIR LGGHMEQWCL LKERLGFSLH SQLAKFLLDR
YTSSGCVLCA GPEPLPPKGL QYLVLLSHAH SRECSLVPGL RGPGGQDGGL VWECSAGHTF
SWGPSLSPTP SEAPKPASLP HTTRRSWCSE ATSGQELADL ESEHDERTQE ARLPRRVGPP
PETFPPPGEE EGEEEEDNDE DEEEMLSDAS LWTYSSSPDD SEPDAPRLLP SPVTCTPKEG
ETPPAPAALS SPLAVPALSA SSLSSRAPPP AEVRVQPQLS RTPQAAQQTE ALASTGSQAQ
SAPTPAWDED TAQIGPKRIR KAAKRELMPC DFPGCGRIFS NRQYLNHHKK YQHIHQKSFS
CPEPACGKSF NFKKHLKEHM KLHSDTRDYI CEFCARSFRT SSNLVIHRRI HTGEKPLQCE
ICGFTCRQKA SLNWHQRKHA ETVAALRFPC EFCGKRFEKP DSVAAHRSKS HPALLLAPQE
SPSGPLEPCP SISAPGPLGS SEGSRPSASP QAPTLLPQQ