GZF1_HUMAN
ID GZF1_HUMAN Reviewed; 711 AA.
AC Q9H116; A8K199; B2RBC3; B3KPL4; B4DF58; D3DW39; Q54A22; Q96N08; Q9BQK9;
AC Q9H117; Q9H6W6;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=GDNF-inducible zinc finger protein 1;
DE AltName: Full=Zinc finger and BTB domain-containing protein 23;
DE AltName: Full=Zinc finger protein 336;
GN Name=GZF1 {ECO:0000312|HGNC:HGNC:15808}; Synonyms=ZBTB23, ZNF336;
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), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, INDUCTION, AND MUTAGENESIS OF ASP-32 AND LYS-50.
RC TISSUE=Neuroblastoma;
RX PubMed=14522971; DOI=10.1074/jbc.m309629200;
RA Fukuda N., Ichihara M., Morinaga T., Kawai K., Hayashi H., Murakumo Y.,
RA Matsuo S., Takahashi M.;
RT "Identification of a novel glial cell line-derived neurotrophic factor-
RT inducible gene required for renal branching morphogenesis.";
RL J. Biol. Chem. 278:50386-50392(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP PRO-275.
RC TISSUE=Brain, Cerebellum, Hepatoma, Teratocarcinoma, and Trachea;
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=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=16049025; DOI=10.1093/nar/gki734;
RA Morinaga T., Enomoto A., Shimono Y., Hirose F., Fukuda N., Dambara A.,
RA Jijiwa M., Kawai K., Hashimoto K., Ichihara M., Asai N., Murakumo Y.,
RA Matsuo S., Takahashi M.;
RT "GDNF-inducible zinc finger protein 1 is a sequence-specific
RT transcriptional repressor that binds to the HOXA10 gene regulatory
RT region.";
RL Nucleic Acids Res. 33:4191-4201(2005).
RN [6]
RP INTERACTION WITH NCL, AND SUBCELLULAR LOCATION.
RX PubMed=17674968; DOI=10.1016/j.yexcr.2007.07.003;
RA Dambara A., Morinaga T., Fukuda N., Yamakawa Y., Kato T., Enomoto A.,
RA Asai N., Murakumo Y., Matsuo S., Takahashi M.;
RT "Nucleolin modulates the subcellular localization of GDNF-inducible zinc
RT finger protein 1 and its roles in transcription and cell proliferation.";
RL Exp. Cell Res. 313:3755-3766(2007).
RN [7]
RP VARIANT VAL-97.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
RN [8]
RP INVOLVEMENT IN JLSM, AND VARIANT JLSM 289-GLU--GLU-711 DEL.
RX PubMed=28475863; DOI=10.1016/j.ajhg.2017.04.008;
RA Patel N., Shamseldin H.E., Sakati N., Khan A.O., Softa A., Al-Fadhli F.M.,
RA Hashem M., Abdulwahab F.M., Alshidi T., Alomar R., Alobeid E., Wakil S.M.,
RA Colak D., Alkuraya F.S.;
RT "GZF1 Mutations Expand the Genetic Heterogeneity of Larsen Syndrome.";
RL Am. J. Hum. Genet. 100:831-836(2017).
CC -!- FUNCTION: Transcriptional repressor that binds the GZF1 responsive
CC element (GRE) (consensus: 5'-TGCGCN[TG][CA]TATA-3'). May be regulating
CC VSX2/HOX10 expression. {ECO:0000269|PubMed:14522971,
CC ECO:0000269|PubMed:16049025}.
CC -!- SUBUNIT: Interacts with NCL. {ECO:0000269|PubMed:17674968}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14522971}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:14522971, ECO:0000269|PubMed:17674968}.
CC Nucleus, nucleolus {ECO:0000269|PubMed:17674968}. Note=Nuclear
CC localization depends upon NCL. {ECO:0000269|PubMed:17674968}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H116-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H116-4; Sequence=VSP_055933;
CC -!- TISSUE SPECIFICITY: Expressed in adult brain, heart, skeletal muscle,
CC kidney and liver. Also detected in fetal brain and kidney, and at lower
CC levels in fetal lung and liver. {ECO:0000269|PubMed:14522971}.
CC -!- INDUCTION: By GDNF. {ECO:0000269|PubMed:14522971}.
CC -!- DISEASE: Joint laxity, short stature, and myopia (JLSM) [MIM:617662]:
CC An autosomal recessive disease characterized by generalized joint
CC laxity, joint dislocation, pectus carinatum, short stature, and severe
CC myopia with retinal detachment. {ECO:0000269|PubMed:28475863}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15134.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB71107.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB100265; BAC98464.1; -; mRNA.
DR EMBL; AK025447; BAB15134.1; ALT_INIT; mRNA.
DR EMBL; AK056159; BAB71107.1; ALT_INIT; mRNA.
DR EMBL; AK056477; BAG51726.1; -; mRNA.
DR EMBL; AK289814; BAF82503.1; -; mRNA.
DR EMBL; AK293942; BAG57319.1; -; mRNA.
DR EMBL; AK314599; BAG37170.1; -; mRNA.
DR EMBL; AL096677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10159.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10160.1; -; Genomic_DNA.
DR CCDS; CCDS13151.1; -. [Q9H116-1]
DR RefSeq; NP_001303941.1; NM_001317012.1. [Q9H116-1]
DR RefSeq; NP_001303948.1; NM_001317019.1.
DR RefSeq; NP_071927.1; NM_022482.4. [Q9H116-1]
DR RefSeq; XP_011527623.1; XM_011529321.2. [Q9H116-1]
DR RefSeq; XP_011527624.1; XM_011529322.1. [Q9H116-1]
DR AlphaFoldDB; Q9H116; -.
DR SMR; Q9H116; -.
DR BioGRID; 122164; 75.
DR IntAct; Q9H116; 9.
DR STRING; 9606.ENSP00000338290; -.
DR iPTMnet; Q9H116; -.
DR PhosphoSitePlus; Q9H116; -.
DR BioMuta; GZF1; -.
DR DMDM; 23397004; -.
DR EPD; Q9H116; -.
DR jPOST; Q9H116; -.
DR MassIVE; Q9H116; -.
DR MaxQB; Q9H116; -.
DR PaxDb; Q9H116; -.
DR PeptideAtlas; Q9H116; -.
DR PRIDE; Q9H116; -.
DR ProteomicsDB; 4010; -.
DR ProteomicsDB; 80353; -. [Q9H116-1]
DR Antibodypedia; 9733; 59 antibodies from 20 providers.
DR DNASU; 64412; -.
DR Ensembl; ENST00000338121.10; ENSP00000338290.5; ENSG00000125812.16. [Q9H116-1]
DR Ensembl; ENST00000377051.2; ENSP00000366250.2; ENSG00000125812.16. [Q9H116-1]
DR GeneID; 64412; -.
DR KEGG; hsa:64412; -.
DR MANE-Select; ENST00000338121.10; ENSP00000338290.5; NM_022482.5; NP_071927.1.
DR UCSC; uc002wsy.4; human. [Q9H116-1]
DR CTD; 64412; -.
DR DisGeNET; 64412; -.
DR GeneCards; GZF1; -.
DR HGNC; HGNC:15808; GZF1.
DR HPA; ENSG00000125812; Low tissue specificity.
DR MalaCards; GZF1; -.
DR MIM; 613842; gene.
DR MIM; 617662; phenotype.
DR neXtProt; NX_Q9H116; -.
DR OpenTargets; ENSG00000125812; -.
DR Orphanet; 527450; Severe myopia-generalized joint laxity-short stature syndrome.
DR PharmGKB; PA162390561; -.
DR VEuPathDB; HostDB:ENSG00000125812; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00870000136554; -.
DR HOGENOM; CLU_018348_1_0_1; -.
DR InParanoid; Q9H116; -.
DR OMA; VVYRCET; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9H116; -.
DR TreeFam; TF350965; -.
DR PathwayCommons; Q9H116; -.
DR SignaLink; Q9H116; -.
DR BioGRID-ORCS; 64412; 24 hits in 1151 CRISPR screens.
DR ChiTaRS; GZF1; human.
DR GenomeRNAi; 64412; -.
DR Pharos; Q9H116; Tbio.
DR PRO; PR:Q9H116; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9H116; protein.
DR Bgee; ENSG00000125812; Expressed in sperm and 177 other tissues.
DR ExpressionAtlas; Q9H116; baseline and differential.
DR Genevisible; Q9H116; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; 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:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Disease variant; DNA-binding; Dwarfism;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..711
FT /note="GDNF-inducible zinc finger protein 1"
FT /id="PRO_0000047539"
FT DOMAIN 31..103
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 317..340
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 348..371
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 377..400
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 407..429
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 435..457
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 463..485
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 491..513
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 519..541
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 547..569
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 575..597
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 153..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4VBD9"
FT VAR_SEQ 1..491
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055933"
FT VARIANT 97
FT /note="A -> V (found in a renal cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064718"
FT VARIANT 190
FT /note="N -> S (in dbSNP:rs3810574)"
FT /id="VAR_052735"
FT VARIANT 275
FT /note="Q -> L (in dbSNP:rs6048760)"
FT /id="VAR_059890"
FT VARIANT 275
FT /note="Q -> P (in dbSNP:rs6048760)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_024212"
FT VARIANT 275
FT /note="Q -> R (in dbSNP:rs6048760)"
FT /id="VAR_059891"
FT VARIANT 289..711
FT /note="Missing (in JLSM)"
FT /evidence="ECO:0000269|PubMed:28475863"
FT /id="VAR_080250"
FT VARIANT 318
FT /note="K -> N (in dbSNP:rs6114068)"
FT /id="VAR_052736"
FT VARIANT 667
FT /note="D -> N (in dbSNP:rs6048766)"
FT /id="VAR_052737"
FT MUTAGEN 32
FT /note="D->N: Decreased repression activity."
FT /evidence="ECO:0000269|PubMed:14522971"
FT MUTAGEN 50
FT /note="K->D: Decreased repression activity."
FT /evidence="ECO:0000269|PubMed:14522971"
FT CONFLICT 520
FT /note="K -> R (in Ref. 2; BAG51726)"
FT /evidence="ECO:0000305"
FT CONFLICT 628
FT /note="E -> G (in Ref. 2; BAG51726)"
FT /evidence="ECO:0000305"
FT CONFLICT 632
FT /note="S -> P (in Ref. 2; BAB15134)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="T -> A (in Ref. 2; BAG51726)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 711 AA; 80492 MW; 9209B850193BCF1A CRC64;
MESGAVLLES KSSPFNLLHE MHELRLLGHL CDVTVSVEYQ GVRKDFMAHK AVLAATSKFF
KEVFLNEKSV DGTRTNVYLN EVQVADFASF LEFVYTAKVQ VEEDRVQRML EVAEKLKCLD
LSETCFQLKK QMLESVLLEL QNFSESQEVE VSSGSQVSAA PAPRASVATD GPHPSGLTDS
LDYPGERASN GMSSDLPPKK SKDKLDKKKE VVKPPYPKIR RASGRLAGRK VFVEIPKKKY
TRRLREQQKT AEGDVGDYRC PQDQSPDRVG TEMEQVSKNE GCQAGAELEE LSKKAGPEEE
EEEEEEDEEG EKKKSNFKCS ICEKAFLYEK SFLKHSKHRH GVATEVVYRC DTCGQTFANR
CNLKSHQRHV HSSERHFPCE LCGKKFKRKK DVKRHVLQVH EGGGERHRCG QCGKGLSSKT
ALRLHERTHT GDRPYGCTEC GARFSQPSAL KTHMRIHTGE KPFVCDECGA RFTQNHMLIY
HKRCHTGERP FMCETCGKSF ASKEYLKHHN RIHTGSKPFK CEVCFRTFAQ RNSLYQHIKV
HTGERPYCCD QCGKQFTQLN ALQRHRRIHT GERPFMCNAC GRTFTDKSTL RRHTSIHDKN
TPWKSFLVIV DGSPKNDDGH KTEQPDEEYV SSKLSDKLLS FAENGHFHNL AAVQDTVPTM
QENSSADTAC KADDSVVSQD TLLATTISEL SELTPQTDSM PTQLHSLSNM E
