ZN207_HUMAN
ID ZN207_HUMAN Reviewed; 478 AA.
AC O43670; A8K6Y6; E1P660; E1P661; E1P662; Q53XS9; Q96HW5; Q9BUQ7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=BUB3-interacting and GLEBS motif-containing protein ZNF207 {ECO:0000303|PubMed:24462186, ECO:0000303|PubMed:24462187};
DE Short=BuGZ {ECO:0000303|PubMed:24462186, ECO:0000303|PubMed:24462187};
DE Short=hBuGZ {ECO:0000303|PubMed:26388440};
DE AltName: Full=Zinc finger protein 207;
GN Name=ZNF207 {ECO:0000312|HGNC:HGNC:12998};
GN Synonyms=BUGZ {ECO:0000303|PubMed:24462186, ECO:0000303|PubMed:24462187};
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 TISSUE SPECIFICITY.
RX PubMed=9799612; DOI=10.1006/geno.1998.5442;
RA Pahl P.M.B., Hodges Y.K., Meltesen L., Perryman M.B., Horwitz K.B.,
RA Horwitz L.D.;
RT "ZNF207, a ubiquitously expressed zinc finger gene on chromosome 6p21.3.";
RL Genomics 53:410-412(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Prostate;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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 [8]
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BUB3, MUTAGENESIS OF
RP 373-GLU-GLU-374, AND MICROTUBULE-BINDING.
RX PubMed=24462186; DOI=10.1016/j.devcel.2013.12.013;
RA Jiang H., He X., Wang S., Jia J., Wan Y., Wang Y., Zeng R., Yates J. III,
RA Zhu X., Zheng Y.;
RT "A microtubule-associated zinc finger protein, BuGZ, regulates mitotic
RT chromosome alignment by ensuring Bub3 stability and kinetochore
RT targeting.";
RL Dev. Cell 28:268-281(2014).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BUB3, AND MUTAGENESIS OF
RP 373-GLU-GLU-374.
RX PubMed=24462187; DOI=10.1016/j.devcel.2013.12.014;
RA Toledo C.M., Herman J.A., Olsen J.B., Ding Y., Corrin P., Girard E.J.,
RA Olson J.M., Emili A., Deluca J.G., Paddison P.J.;
RT "BuGZ is required for Bub3 stability, Bub1 kinetochore function, and
RT chromosome alignment.";
RL Dev. Cell 28:282-294(2014).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26388440; DOI=10.1016/j.cell.2015.08.010;
RA Jiang H., Wang S., Huang Y., He X., Cui H., Zhu X., Zheng Y.;
RT "Phase transition of spindle-associated protein regulate spindle apparatus
RT assembly.";
RL Cell 163:108-122(2015).
CC -!- FUNCTION: Kinetochore- and microtubule-binding protein that plays a key
CC role in spindle assembly (PubMed:24462186, PubMed:24462187,
CC PubMed:26388440). ZNF207/BuGZ is mainly composed of disordered low-
CC complexity regions and undergoes phase transition or coacervation to
CC form temperature-dependent liquid droplets. Coacervation promotes
CC microtubule bundling and concentrates tubulin, promoting microtubule
CC polymerization and assembly of spindle and spindle matrix by
CC concentrating its building blocks (PubMed:26388440). Also acts as a
CC regulator of mitotic chromosome alignment by mediating the stability
CC and kinetochore loading of BUB3 (PubMed:24462186, PubMed:24462187).
CC Mechanisms by which BUB3 is protected are unclear: according to a first
CC report, ZNF207/BuGZ may act by blocking ubiquitination and proteasomal
CC degradation of BUB3 (PubMed:24462186). According to another report, the
CC stabilization is independent of the proteasome (PubMed:24462187).
CC {ECO:0000269|PubMed:24462186, ECO:0000269|PubMed:24462187,
CC ECO:0000269|PubMed:26388440}.
CC -!- SUBUNIT: Interacts (via GLEBS region) with BUB3.
CC {ECO:0000269|PubMed:24462186, ECO:0000269|PubMed:24462187}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24462186,
CC ECO:0000269|PubMed:24462187}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:24462186, ECO:0000269|PubMed:24462187}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:26388440}. Note=Localizes
CC primarily to the nucleus in interphase, concentrates at kinetochores
CC prior to nuclear envelope breakdown and during early prometaphase, and
CC disappears from kinetochores upon microtubule-binding.
CC {ECO:0000269|PubMed:24462186, ECO:0000269|PubMed:24462187}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=O43670-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43670-2; Sequence=VSP_006904, VSP_006905;
CC Name=3;
CC IsoId=O43670-3; Sequence=VSP_006903, VSP_006904;
CC Name=4;
CC IsoId=O43670-4; Sequence=VSP_006904;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9799612}.
CC -!- DOMAIN: The GLEBS region mediates interaction with BUB3
CC (PubMed:24462186, PubMed:24462187). {ECO:0000269|PubMed:24462186,
CC ECO:0000269|PubMed:24462187}.
CC -!- DOMAIN: The microtubule-binding region is required for efficient
CC loading of BUB3 onto kinetochores and proper mitosis.
CC {ECO:0000269|PubMed:24462186}.
CC -!- DOMAIN: Mainly composed of disordered low-complexity regions outside of
CC the C2H2-type zinc fingers. Coacervation depends on hydrophobic and
CC aromatic Phe and Tyr in the disordered low-complexity region, that may
CC promote coacervation by forming intermolecular hydrophobic
CC interactions. {ECO:0000250|UniProtKB:Q9JMD0}.
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DR EMBL; AF046001; AAC78561.1; -; mRNA.
DR EMBL; BT007365; AAP36029.1; -; mRNA.
DR EMBL; AK291801; BAF84490.1; -; mRNA.
DR EMBL; AK226172; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC005899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471147; EAW80231.1; -; Genomic_DNA.
DR EMBL; CH471147; EAW80233.1; -; Genomic_DNA.
DR EMBL; CH471147; EAW80234.1; -; Genomic_DNA.
DR EMBL; CH471147; EAW80235.1; -; Genomic_DNA.
DR EMBL; CH471147; EAW80236.1; -; Genomic_DNA.
DR EMBL; CH471147; EAW80237.1; -; Genomic_DNA.
DR EMBL; BC002372; AAH02372.1; -; mRNA.
DR EMBL; BC008023; AAH08023.1; -; mRNA.
DR CCDS; CCDS11271.1; -. [O43670-1]
DR CCDS; CCDS32614.1; -. [O43670-2]
DR CCDS; CCDS42294.1; -. [O43670-4]
DR RefSeq; NP_001027464.1; NM_001032293.2. [O43670-2]
DR RefSeq; NP_001091977.1; NM_001098507.1. [O43670-4]
DR RefSeq; NP_003448.1; NM_003457.3. [O43670-1]
DR RefSeq; XP_016880508.1; XM_017025019.1.
DR AlphaFoldDB; O43670; -.
DR SMR; O43670; -.
DR BioGRID; 113540; 68.
DR CORUM; O43670; -.
DR IntAct; O43670; 31.
DR MINT; O43670; -.
DR STRING; 9606.ENSP00000378165; -.
DR GlyGen; O43670; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; O43670; -.
DR PhosphoSitePlus; O43670; -.
DR SwissPalm; O43670; -.
DR BioMuta; ZNF207; -.
DR EPD; O43670; -.
DR jPOST; O43670; -.
DR MassIVE; O43670; -.
DR MaxQB; O43670; -.
DR PaxDb; O43670; -.
DR PeptideAtlas; O43670; -.
DR PRIDE; O43670; -.
DR ProteomicsDB; 15215; -.
DR ProteomicsDB; 49099; -. [O43670-1]
DR ProteomicsDB; 49100; -. [O43670-2]
DR ProteomicsDB; 49101; -. [O43670-3]
DR Antibodypedia; 1741; 326 antibodies from 24 providers.
DR DNASU; 7756; -.
DR Ensembl; ENST00000321233.10; ENSP00000322777.6; ENSG00000010244.19. [O43670-1]
DR Ensembl; ENST00000394670.9; ENSP00000378165.4; ENSG00000010244.19. [O43670-4]
DR Ensembl; ENST00000394673.6; ENSP00000378168.2; ENSG00000010244.19. [O43670-2]
DR GeneID; 7756; -.
DR KEGG; hsa:7756; -.
DR MANE-Select; ENST00000394670.9; ENSP00000378165.4; NM_001098507.2; NP_001091977.1. [O43670-4]
DR UCSC; uc002hhh.5; human. [O43670-1]
DR CTD; 7756; -.
DR DisGeNET; 7756; -.
DR GeneCards; ZNF207; -.
DR HGNC; HGNC:12998; ZNF207.
DR HPA; ENSG00000010244; Low tissue specificity.
DR MIM; 603428; gene.
DR neXtProt; NX_O43670; -.
DR OpenTargets; ENSG00000010244; -.
DR PharmGKB; PA37578; -.
DR VEuPathDB; HostDB:ENSG00000010244; -.
DR eggNOG; KOG2893; Eukaryota.
DR GeneTree; ENSGT00730000111057; -.
DR HOGENOM; CLU_037132_3_2_1; -.
DR InParanoid; O43670; -.
DR OMA; EPPKATF; -.
DR OrthoDB; 1453306at2759; -.
DR PhylomeDB; O43670; -.
DR TreeFam; TF313844; -.
DR PathwayCommons; O43670; -.
DR SignaLink; O43670; -.
DR BioGRID-ORCS; 7756; 647 hits in 1107 CRISPR screens.
DR ChiTaRS; ZNF207; human.
DR GenomeRNAi; 7756; -.
DR Pharos; O43670; Tbio.
DR PRO; PR:O43670; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O43670; protein.
DR Bgee; ENSG00000010244; Expressed in adrenal tissue and 208 other tissues.
DR ExpressionAtlas; O43670; baseline and differential.
DR Genevisible; O43670; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:1990047; C:spindle matrix; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IMP:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR GO; GO:0046785; P:microtubule polymerization; ISS:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; IDA:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:0051983; P:regulation of chromosome segregation; IMP:UniProtKB.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Cytoplasm; Cytoskeleton; DNA-binding; Kinetochore;
KW Metal-binding; Microtubule; Mitosis; Nucleus; Reference proteome; Repeat;
KW Zinc; Zinc-finger.
FT CHAIN 1..478
FT /note="BUB3-interacting and GLEBS motif-containing protein
FT ZNF207"
FT /id="PRO_0000047453"
FT ZN_FING 11..34
FT /note="C2H2-type 1"
FT ZN_FING 35..58
FT /note="C2H2-type 2"
FT REGION 1..92
FT /note="Microtubule-binding region"
FT /evidence="ECO:0000269|PubMed:24462186"
FT REGION 99..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..391
FT /note="GLEBS"
FT /evidence="ECO:0000269|PubMed:24462186,
FT ECO:0000269|PubMed:24462187"
FT REGION 384..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..157
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..253
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..420
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..468
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 48..146
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_006903"
FT VAR_SEQ 184
FT /note="G -> GLHHQRKYTQSFCGENI (in isoform 2, isoform 3 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2,
FT ECO:0000303|Ref.4"
FT /id="VSP_006904"
FT VAR_SEQ 261..291
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_006905"
FT VARIANT 224
FT /note="A -> S (in dbSNP:rs3795244)"
FT /id="VAR_019974"
FT MUTAGEN 373..374
FT /note="EE->AA: In BuGZAA: Abolishes interaction with BUB3."
FT /evidence="ECO:0000269|PubMed:24462186,
FT ECO:0000269|PubMed:24462187"
SQ SEQUENCE 478 AA; 50751 MW; 308B0303059052F7 CRC64;
MGRKKKKQLK PWCWYCNRDF DDEKILIQHQ KAKHFKCHIC HKKLYTGPGL AIHCMQVHKE
TIDAVPNAIP GRTDIELEIY GMEGIPEKDM DERRRLLEQK TQESQKKKQQ DDSDEYDDDD
SAASTSFQPQ PVQPQQGYIP PMAQPGLPPV PGAPGMPPGI PPLMPGVPPL MPGMPPVMPG
MPPGMMPMGG MMPPGPGIPP LMPGMPPGMP PPVPRPGIPP MTQAQAVSAP GILNRPPAPT
ATVPAPQPPV TKPLFPSAGQ MGTPVTSSST ASSNSESLSA SSKALFPSTA QAQAAVQGPV
GTDFKPLNST PATTTEPPKP TFPAYTQSTA STTSTTNSTA AKPAASITSK PATLTTTSAT
SKLIHPDEDI SLEERRAQLP KYQRNLPRPG QAPIGNPPVG PIGGMMPPQP GIPQQQGMRP
PMPPHGQYGG HHQGMPGYLP GAMPPYGQGP PMVPPYQGGP PRPPMGMRPP VMSQGGRY
