ZN347_HUMAN
ID ZN347_HUMAN Reviewed; 839 AA.
AC Q96SE7; B3KU77; B9EG59; G5E9N4; Q8TCN1;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Zinc finger protein 347;
DE AltName: Full=Zinc finger protein 1111;
GN Name=ZNF347; Synonyms=ZNF1111;
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 1), AND VARIANT ASP-264.
RA Aitken C.J., Nicholson G.C.;
RT "RANKL regulated zinc finger protein in osteoclastogenesis.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ASP-264.
RC TISSUE=Brain;
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 GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-264.
RC TISSUE=Testis;
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 [LARGE SCALE MRNA] OF 305-839 (ISOFORMS 1/2).
RC TISSUE=Brain;
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 [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-827, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [8]
RP STRUCTURE BY NMR OF 282-792.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the C2H2 type zinc finger region of human zinc
RT finger protein 347.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96SE7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96SE7-2; Sequence=VSP_046841;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AY029765; AAK37403.1; -; mRNA.
DR EMBL; AK096623; BAG53339.1; -; mRNA.
DR EMBL; AC010328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471135; EAW72119.1; -; Genomic_DNA.
DR EMBL; BC136255; AAI36256.1; -; mRNA.
DR EMBL; AL713691; CAD28491.1; -; mRNA.
DR CCDS; CCDS33097.1; -. [Q96SE7-1]
DR CCDS; CCDS54314.1; -. [Q96SE7-2]
DR RefSeq; NP_001166145.1; NM_001172674.1. [Q96SE7-2]
DR RefSeq; NP_001166146.1; NM_001172675.1. [Q96SE7-2]
DR RefSeq; NP_115973.2; NM_032584.2. [Q96SE7-1]
DR RefSeq; XP_005259392.1; XM_005259335.4.
DR RefSeq; XP_016882873.1; XM_017027384.1.
DR PDB; 2EMA; NMR; -; A=312-344.
DR PDB; 2EMP; NMR; -; A=536-568.
DR PDB; 2EN4; NMR; -; A=284-316.
DR PDB; 2ENE; NMR; -; A=592-624.
DR PDB; 2ENF; NMR; -; A=340-372.
DR PDB; 2EOE; NMR; -; A=508-540.
DR PDB; 2EOW; NMR; -; A=368-400.
DR PDB; 2EQ0; NMR; -; A=452-484.
DR PDB; 2EQ1; NMR; -; A=480-512.
DR PDB; 2EQ2; NMR; -; A=676-708.
DR PDB; 2EQ3; NMR; -; A=704-736.
DR PDB; 2YTI; NMR; -; A=564-596.
DR PDB; 2YTK; NMR; -; A=396-428.
DR PDB; 2YTN; NMR; -; A=732-764.
DR PDB; 2YTR; NMR; -; A=760-792.
DR PDB; 2YU8; NMR; -; A=648-680.
DR PDBsum; 2EMA; -.
DR PDBsum; 2EMP; -.
DR PDBsum; 2EN4; -.
DR PDBsum; 2ENE; -.
DR PDBsum; 2ENF; -.
DR PDBsum; 2EOE; -.
DR PDBsum; 2EOW; -.
DR PDBsum; 2EQ0; -.
DR PDBsum; 2EQ1; -.
DR PDBsum; 2EQ2; -.
DR PDBsum; 2EQ3; -.
DR PDBsum; 2YTI; -.
DR PDBsum; 2YTK; -.
DR PDBsum; 2YTN; -.
DR PDBsum; 2YTR; -.
DR PDBsum; 2YU8; -.
DR AlphaFoldDB; Q96SE7; -.
DR SMR; Q96SE7; -.
DR IntAct; Q96SE7; 1.
DR STRING; 9606.ENSP00000405218; -.
DR iPTMnet; Q96SE7; -.
DR PhosphoSitePlus; Q96SE7; -.
DR BioMuta; ZNF347; -.
DR DMDM; 296453051; -.
DR jPOST; Q96SE7; -.
DR MassIVE; Q96SE7; -.
DR MaxQB; Q96SE7; -.
DR PaxDb; Q96SE7; -.
DR PeptideAtlas; Q96SE7; -.
DR PRIDE; Q96SE7; -.
DR ProteomicsDB; 33993; -.
DR ProteomicsDB; 78108; -. [Q96SE7-1]
DR Antibodypedia; 19156; 14 antibodies from 8 providers.
DR DNASU; 84671; -.
DR Ensembl; ENST00000334197.12; ENSP00000334146.6; ENSG00000197937.13. [Q96SE7-1]
DR Ensembl; ENST00000452676.6; ENSP00000405218.2; ENSG00000197937.13. [Q96SE7-2]
DR Ensembl; ENST00000601469.2; ENSP00000471712.2; ENSG00000197937.13. [Q96SE7-2]
DR GeneID; 84671; -.
DR KEGG; hsa:84671; -.
DR MANE-Select; ENST00000334197.12; ENSP00000334146.6; NM_032584.3; NP_115973.2.
DR UCSC; uc002qbb.3; human. [Q96SE7-1]
DR CTD; 84671; -.
DR GeneCards; ZNF347; -.
DR HGNC; HGNC:16447; ZNF347.
DR HPA; ENSG00000197937; Low tissue specificity.
DR neXtProt; NX_Q96SE7; -.
DR OpenTargets; ENSG00000197937; -.
DR PharmGKB; PA38143; -.
DR VEuPathDB; HostDB:ENSG00000197937; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000164205; -.
DR HOGENOM; CLU_002678_17_0_1; -.
DR InParanoid; Q96SE7; -.
DR OMA; HATEEMC; -.
DR PhylomeDB; Q96SE7; -.
DR TreeFam; TF341892; -.
DR PathwayCommons; Q96SE7; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q96SE7; -.
DR BioGRID-ORCS; 84671; 7 hits in 1066 CRISPR screens.
DR ChiTaRS; ZNF347; human.
DR EvolutionaryTrace; Q96SE7; -.
DR GenomeRNAi; 84671; -.
DR Pharos; Q96SE7; Tdark.
DR PRO; PR:Q96SE7; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96SE7; protein.
DR Bgee; ENSG00000197937; Expressed in adrenal tissue and 113 other tissues.
DR ExpressionAtlas; Q96SE7; baseline and differential.
DR Genevisible; Q96SE7; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 18.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 19.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 12.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 17.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 20.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..839
FT /note="Zinc finger protein 347"
FT /id="PRO_0000047545"
FT DOMAIN 8..79
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 261..283
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 289..311
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 317..339
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 345..367
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 373..395
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 401..423
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 429..451
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 457..479
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 485..507
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 513..535
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 541..563
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 569..591
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 597..619
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 625..647
FT /note="C2H2-type 14; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 653..675
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 681..703
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 709..731
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 737..759
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 765..787
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 790..812
FT /note="C2H2-type 20; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 253
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN19"
FT CROSSLNK 827
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 47
FT /note="L -> LA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046841"
FT VARIANT 117
FT /note="M -> V (in dbSNP:rs34656962)"
FT /id="VAR_052815"
FT VARIANT 264
FT /note="N -> D (in dbSNP:rs2195310)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1"
FT /id="VAR_059913"
FT CONFLICT 215
FT /note="N -> D (in Ref. 2; BAG53339)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="K -> R (in Ref. 2; BAG53339)"
FT /evidence="ECO:0000305"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:2EN4"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:2EN4"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:2EN4"
FT HELIX 302..308
FT /evidence="ECO:0007829|PDB:2EN4"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:2EN4"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:2EMA"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:2EMA"
FT HELIX 329..336
FT /evidence="ECO:0007829|PDB:2EMA"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:2EMA"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:2ENF"
FT HELIX 357..364
FT /evidence="ECO:0007829|PDB:2ENF"
FT TURN 365..369
FT /evidence="ECO:0007829|PDB:2ENF"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:2EOW"
FT HELIX 385..395
FT /evidence="ECO:0007829|PDB:2EOW"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:2YTK"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:2YTK"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:2YTK"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:2YTK"
FT HELIX 413..423
FT /evidence="ECO:0007829|PDB:2YTK"
FT STRAND 424..427
FT /evidence="ECO:0007829|PDB:2YTK"
FT TURN 460..462
FT /evidence="ECO:0007829|PDB:2EQ0"
FT STRAND 465..468
FT /evidence="ECO:0007829|PDB:2EQ0"
FT HELIX 469..476
FT /evidence="ECO:0007829|PDB:2EQ0"
FT TURN 477..479
FT /evidence="ECO:0007829|PDB:2EQ0"
FT TURN 488..491
FT /evidence="ECO:0007829|PDB:2EQ1"
FT HELIX 497..504
FT /evidence="ECO:0007829|PDB:2EQ1"
FT TURN 505..507
FT /evidence="ECO:0007829|PDB:2EQ1"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:2EOE"
FT TURN 516..518
FT /evidence="ECO:0007829|PDB:2EOE"
FT HELIX 525..532
FT /evidence="ECO:0007829|PDB:2EOE"
FT HELIX 533..535
FT /evidence="ECO:0007829|PDB:2EOE"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:2EMP"
FT STRAND 544..546
FT /evidence="ECO:0007829|PDB:2EMP"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:2EMP"
FT HELIX 553..564
FT /evidence="ECO:0007829|PDB:2EMP"
FT STRAND 572..574
FT /evidence="ECO:0007829|PDB:2YTI"
FT HELIX 581..588
FT /evidence="ECO:0007829|PDB:2YTI"
FT TURN 589..591
FT /evidence="ECO:0007829|PDB:2YTI"
FT STRAND 594..598
FT /evidence="ECO:0007829|PDB:2ENE"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:2ENE"
FT STRAND 605..608
FT /evidence="ECO:0007829|PDB:2ENE"
FT HELIX 609..616
FT /evidence="ECO:0007829|PDB:2ENE"
FT TURN 617..619
FT /evidence="ECO:0007829|PDB:2ENE"
FT STRAND 651..654
FT /evidence="ECO:0007829|PDB:2YU8"
FT STRAND 656..658
FT /evidence="ECO:0007829|PDB:2YU8"
FT STRAND 661..665
FT /evidence="ECO:0007829|PDB:2YU8"
FT HELIX 666..671
FT /evidence="ECO:0007829|PDB:2YU8"
FT STRAND 676..678
FT /evidence="ECO:0007829|PDB:2EQ2"
FT STRAND 680..682
FT /evidence="ECO:0007829|PDB:2EQ2"
FT HELIX 693..699
FT /evidence="ECO:0007829|PDB:2EQ2"
FT HELIX 700..703
FT /evidence="ECO:0007829|PDB:2EQ2"
FT STRAND 708..711
FT /evidence="ECO:0007829|PDB:2EQ3"
FT TURN 712..715
FT /evidence="ECO:0007829|PDB:2EQ3"
FT HELIX 721..728
FT /evidence="ECO:0007829|PDB:2EQ3"
FT TURN 740..742
FT /evidence="ECO:0007829|PDB:2YTN"
FT HELIX 749..755
FT /evidence="ECO:0007829|PDB:2YTN"
FT HELIX 756..758
FT /evidence="ECO:0007829|PDB:2YTN"
FT TURN 768..770
FT /evidence="ECO:0007829|PDB:2YTR"
FT HELIX 777..784
FT /evidence="ECO:0007829|PDB:2YTR"
FT TURN 785..789
FT /evidence="ECO:0007829|PDB:2YTR"
SQ SEQUENCE 839 AA; 95770 MW; C951647ECF4D644D CRC64;
MALTQGQVTF RDVAIEFSQE EWTCLDPAQR TLYRDVMLEN YRNLASLGIS CFDLSIISML
EQGKEPFTLE SQVQIAGNPD GWEWIKAVIT ALSSEFVMKD LLHKGKSNTG EVFQTVMLER
QESQDIEGCS FREVQKNTHG LEYQCRDAEG NYKGVLLTQE GNLTHGRDEH DKRDARNKLI
KNQLGLSLQS HLPELQLFQY EGKIYECNQV EKSFNNNSSV SPPQQMPYNV KTHISKKYLK
DFISSLLLTQ GQKANNWGSP YKSNGCGMVF PQNSHLASHQ RSHTKEKPYK CYECGKAFRT
RSNLTTHQVI HTGEKRYKCN ECGKVFSRNS QLSQHQKIHT GEKPYKCNEC GKVFTQNSHL
VRHRGIHTGE KPYKCNECGK AFRARSSLAI HQATHSGEKP YKCNECGKVF TQNSHLTNHW
RIHTGEKPYK CNECGKAFGV RSSLAIHLVI HTGEKPYKCH ECGKVFRRNS HLARHQLIHT
GEKPYKCNEC GKAFRAHSNL TTHQVIHTGE KPYKCNECGK VFTQNSHLAN HQRIHTGVKP
YMCNECGKAF SVYSSLTTHQ VIHTGEKPYK CNECGKVFTQ NSHLARHRGI HTGEKPYKCN
ECGKVFRHNS YLSRHQRIHT GEKPYKYNEY GKAFSEHSNL TTHQVIHTGE KPYKCNECGK
VFTQNSHLAR HRRVHTGGKP YQCNECGKAF SQTSKLARHQ RVHTGEKPYE CNQCGKAFSV
RSSLTTHQAI HTGKKPYKCN ECGKVFTQNS HLARHRGIHT GEKPYKCNEC GKAFSQTSKL
ARHQRIHTGE KPYECGKPFS ICSSLTTHQT IHTGGKPYKC NVWKVLKSEF KPCKPSQNS
