CXXC5_HUMAN
ID CXXC5_HUMAN Reviewed; 322 AA.
AC Q7LFL8; B3KND0; C8CBA8; Q8TB79; Q9NV51; Q9P0S8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=CXXC-type zinc finger protein 5;
DE Short=CF5;
DE AltName: Full=Putative MAPK-activating protein PM08;
DE AltName: Full=Putative NF-kappa-B-activating protein 102;
DE AltName: Full=Retinoid-inducible nuclear factor;
DE Short=RINF;
GN Name=CXXC5; ORFNames=HSPC195, TCCCIA00297;
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, AND SUBCELLULAR LOCATION.
RX PubMed=19557330; DOI=10.1007/s11427-009-0083-7;
RA Zhang M., Wang R.-P., Wang Y.-Y., Diao F., Gao D., Chen D.-Y., Zhai Z.,
RA Shu H.-B.;
RT "The CXXC finger 5 protein is required for DNA damage-induced p53
RT activation.";
RL Sci. China, Ser. C, Life Sci. 52:528-538(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND POSSIBLE FUNCTION.
RC TISSUE=Lung;
RX PubMed=12761501; DOI=10.1038/sj.onc.1206406;
RA Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y.,
RA Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.;
RT "Large-scale identification and characterization of human genes that
RT activate NF-kappaB and MAPK signaling pathways.";
RL Oncogene 22:3307-3318(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Ovarian carcinoma, and Placenta;
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 2).
RC TISSUE=Leukemia;
RA Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A.,
RA Margolin J.F.;
RT "Pediatric leukemia cDNA sequencing project.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
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] (ISOFORM 1).
RC TISSUE=Eye, Lymph, Muscle, Placenta, and Skin;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-322 (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [9]
RP FUNCTION, INDUCTION BY RETINOIDS, AND SUBCELLULAR LOCATION.
RX PubMed=19182210; DOI=10.1182/blood-2008-07-170035;
RA Pendino F., Nguyen E., Jonassen I., Dysvik B., Azouz A., Lanotte M.,
RA Segal-Bendirdjian E., Lillehaug J.R.;
RT "Functional involvement of RINF, retinoid-inducible nuclear factor (CXXC5),
RT in normal and tumoral human myelopoiesis.";
RL Blood 113:3172-3181(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-53, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [11]
RP FUNCTION IN COX4I2 TRANSCRIPTION, AND INTERACTION WITH RBPJ.
RX PubMed=23303788; DOI=10.1093/nar/gks1454;
RA Aras S., Pak O., Sommer N., Finley R. Jr., Huttemann M., Weissmann N.,
RA Grossman L.I.;
RT "Oxygen-dependent expression of cytochrome c oxidase subunit 4-2 gene
RT expression is mediated by transcription factors RBPJ, CXXC5 and CHCHD2.";
RL Nucleic Acids Res. 41:2255-2266(2013).
RN [12] {ECO:0007744|PDB:5W9S}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 254-306 IN COMPLEX WITH CPG DNA,
RP FUNCTION, DOMAIN CXXC-TYPE ZINC-FINGER, AND ZINC-BINDING.
RX PubMed=29276034; DOI=10.1016/j.str.2017.11.022;
RA Xu C., Liu K., Lei M., Yang A., Li Y., Hughes T.R., Min J.;
RT "DNA Sequence Recognition of Human CXXC Domains and Their Structural
RT Determinants.";
RL Structure 26:85-95.e3(2018).
CC -!- FUNCTION: May indirectly participate in activation of the NF-kappa-B
CC and MAPK pathways. Acts as a mediator of BMP4-mediated modulation of
CC canonical Wnt signaling activity in neural stem cells (By similarity).
CC Required for DNA damage-induced ATM phosphorylation, p53 activation and
CC cell cycle arrest. Involved in myelopoiesis. Transcription factor.
CC Binds to the oxygen responsive element of COX4I2 and represses its
CC transcription under hypoxia conditions (4% oxygen), as well as normoxia
CC conditions (20% oxygen) (PubMed:23303788). May repress COX4I2
CC transactivation induced by CHCHD2 and RBPJ (PubMed:23303788). Binds
CC preferentially to DNA containing cytidine-phosphate-guanosine (CpG)
CC dinucleotides over CpH (H=A, T, and C), hemimethylated-CpG and
CC hemimethylated-hydroxymethyl-CpG (PubMed:29276034).
CC {ECO:0000250|UniProtKB:Q5XIQ3, ECO:0000269|PubMed:19182210,
CC ECO:0000269|PubMed:19557330, ECO:0000269|PubMed:23303788,
CC ECO:0000269|PubMed:29276034}.
CC -!- SUBUNIT: Interacts with DVL1. Interacts with RBPJ (PubMed:23303788).
CC {ECO:0000250|UniProtKB:Q5XIQ3, ECO:0000269|PubMed:23303788}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19182210,
CC ECO:0000269|PubMed:19557330}. Cytoplasm {ECO:0000250|UniProtKB:Q5XIQ3}.
CC Note=Colocalizes with DVL1 in large bodies localized just outside the
CC nuclear membrane. {ECO:0000250|UniProtKB:Q5XIQ3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7LFL8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7LFL8-2; Sequence=VSP_031013;
CC -!- INDUCTION: By retinoic acid. {ECO:0000269|PubMed:19182210}.
CC -!- DOMAIN: The CXXC zinc finger mediates binding to CpG-DNA.
CC {ECO:0000269|PubMed:29276034}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF36115.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH02490.3; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH06428.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH17439.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH24040.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH41013.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; GQ379202; ACU80469.1; -; mRNA.
DR EMBL; AB097005; BAC77358.1; -; mRNA.
DR EMBL; AB097032; BAC77385.1; -; mRNA.
DR EMBL; AK001782; BAA91907.1; -; mRNA.
DR EMBL; AK024338; BAG51292.1; -; mRNA.
DR EMBL; AY007103; AAG01986.1; -; mRNA.
DR EMBL; AC113361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW62090.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62091.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62092.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62093.1; -; Genomic_DNA.
DR EMBL; BC002490; AAH02490.3; ALT_INIT; mRNA.
DR EMBL; BC006428; AAH06428.1; ALT_INIT; mRNA.
DR EMBL; BC017439; AAH17439.2; ALT_INIT; mRNA.
DR EMBL; BC024040; AAH24040.2; ALT_INIT; mRNA.
DR EMBL; BC041013; AAH41013.2; ALT_INIT; mRNA.
DR EMBL; AF151029; AAF36115.1; ALT_FRAME; mRNA.
DR CCDS; CCDS43370.1; -. [Q7LFL8-1]
DR RefSeq; NP_001304128.1; NM_001317199.1. [Q7LFL8-1]
DR RefSeq; NP_001304129.1; NM_001317200.1. [Q7LFL8-1]
DR RefSeq; NP_001304130.1; NM_001317201.1. [Q7LFL8-1]
DR RefSeq; NP_001304131.1; NM_001317202.1. [Q7LFL8-1]
DR RefSeq; NP_001304132.1; NM_001317203.1. [Q7LFL8-1]
DR RefSeq; NP_001304133.1; NM_001317204.1. [Q7LFL8-1]
DR RefSeq; NP_001304134.1; NM_001317205.1. [Q7LFL8-1]
DR RefSeq; NP_001304135.1; NM_001317206.1. [Q7LFL8-1]
DR RefSeq; NP_001304136.1; NM_001317207.1. [Q7LFL8-1]
DR RefSeq; NP_001304137.1; NM_001317208.1. [Q7LFL8-1]
DR RefSeq; NP_001304138.1; NM_001317209.1. [Q7LFL8-1]
DR RefSeq; NP_001304139.1; NM_001317210.1. [Q7LFL8-1]
DR RefSeq; NP_001304140.1; NM_001317211.1. [Q7LFL8-1]
DR RefSeq; NP_057547.5; NM_016463.8. [Q7LFL8-1]
DR RefSeq; XP_016865062.1; XM_017009573.1.
DR PDB; 5W9S; X-ray; 2.10 A; C=254-306.
DR PDBsum; 5W9S; -.
DR AlphaFoldDB; Q7LFL8; -.
DR SMR; Q7LFL8; -.
DR BioGRID; 119586; 11.
DR IntAct; Q7LFL8; 9.
DR MINT; Q7LFL8; -.
DR STRING; 9606.ENSP00000302543; -.
DR iPTMnet; Q7LFL8; -.
DR PhosphoSitePlus; Q7LFL8; -.
DR BioMuta; CXXC5; -.
DR DMDM; 167011303; -.
DR EPD; Q7LFL8; -.
DR jPOST; Q7LFL8; -.
DR MassIVE; Q7LFL8; -.
DR MaxQB; Q7LFL8; -.
DR PaxDb; Q7LFL8; -.
DR PeptideAtlas; Q7LFL8; -.
DR PRIDE; Q7LFL8; -.
DR ProteomicsDB; 68856; -. [Q7LFL8-1]
DR ProteomicsDB; 68857; -. [Q7LFL8-2]
DR Antibodypedia; 49849; 154 antibodies from 30 providers.
DR DNASU; 51523; -.
DR Ensembl; ENST00000302517.8; ENSP00000302543.3; ENSG00000171604.12. [Q7LFL8-1]
DR Ensembl; ENST00000511048.1; ENSP00000427379.1; ENSG00000171604.12. [Q7LFL8-1]
DR GeneID; 51523; -.
DR KEGG; hsa:51523; -.
DR MANE-Select; ENST00000302517.8; ENSP00000302543.3; NM_016463.9; NP_057547.5.
DR UCSC; uc003let.3; human. [Q7LFL8-1]
DR CTD; 51523; -.
DR DisGeNET; 51523; -.
DR GeneCards; CXXC5; -.
DR HGNC; HGNC:26943; CXXC5.
DR HPA; ENSG00000171604; Low tissue specificity.
DR MIM; 612752; gene.
DR neXtProt; NX_Q7LFL8; -.
DR OpenTargets; ENSG00000171604; -.
DR PharmGKB; PA128394661; -.
DR VEuPathDB; HostDB:ENSG00000171604; -.
DR eggNOG; ENOG502QT2M; Eukaryota.
DR GeneTree; ENSGT00940000154108; -.
DR HOGENOM; CLU_074593_0_0_1; -.
DR InParanoid; Q7LFL8; -.
DR OMA; ANGHDPP; -.
DR OrthoDB; 946583at2759; -.
DR PhylomeDB; Q7LFL8; -.
DR TreeFam; TF326617; -.
DR PathwayCommons; Q7LFL8; -.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR SignaLink; Q7LFL8; -.
DR BioGRID-ORCS; 51523; 16 hits in 1085 CRISPR screens.
DR ChiTaRS; CXXC5; human.
DR GeneWiki; CXXC5; -.
DR GenomeRNAi; 51523; -.
DR Pharos; Q7LFL8; Tbio.
DR PRO; PR:Q7LFL8; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q7LFL8; protein.
DR Bgee; ENSG00000171604; Expressed in kidney epithelium and 188 other tissues.
DR ExpressionAtlas; Q7LFL8; baseline and differential.
DR Genevisible; Q7LFL8; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IDA:UniProtKB.
DR GO; GO:0008327; F:methyl-CpG binding; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
DR InterPro; IPR040388; CXXC4/CXXC5.
DR InterPro; IPR002857; Znf_CXXC.
DR PANTHER; PTHR13419; PTHR13419; 1.
DR Pfam; PF02008; zf-CXXC; 1.
DR PROSITE; PS51058; ZF_CXXC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; DNA-binding; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Zinc; Zinc-finger.
FT CHAIN 1..322
FT /note="CXXC-type zinc finger protein 5"
FT /id="PRO_0000317548"
FT ZN_FING 256..297
FT /note="CXXC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 257..262
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:5W9S"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:5W9S"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:5W9S"
FT BINDING 275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:5W9S"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:5W9S"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:5W9S"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:5W9S"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509,
FT ECO:0000269|PubMed:29276034, ECO:0007744|PDB:5W9S"
FT MOD_RES 53
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..95
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.4"
FT /id="VSP_031013"
FT CONFLICT 111..112
FT /note="AA -> WP (in Ref. 8; AAF36115)"
FT /evidence="ECO:0000305"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:5W9S"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:5W9S"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:5W9S"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:5W9S"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:5W9S"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:5W9S"
SQ SEQUENCE 322 AA; 32977 MW; ECC19B4DE9872BC5 CRC64;
MSSLGGGSQD AGGSSSSSTN GSGGSGSSGP KAGAADKSAV VAAAAPASVA DDTPPPERRN
KSGIISEPLN KSLRRSRPLS HYSSFGSSGG SGGGSMMGGE SADKATAAAA AASLLANGHD
LAAAMAVDKS NPTSKHKSGA VASLLSKAER ATELAAEGQL TLQQFAQSTE MLKRVVQEHL
PLMSEAGAGL PDMEAVAGAE ALNGQSDFPY LGAFPINPGL FIMTPAGVFL AESALHMAGL
AEYPMQGELA SAISSGKKKR KRCGMCAPCR RRINCEQCSS CRNRKTGHQI CKFRKCEELK
KKPSAALEKV MLPTGAAFRW FQ
