CHRD1_HUMAN
ID CHRD1_HUMAN Reviewed; 332 AA.
AC Q9UHD1; B2R6P8; Q6IN49; Q8WVL9; Q9H3D6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cysteine and histidine-rich domain-containing protein 1;
DE AltName: Full=CHORD domain-containing protein 1;
DE Short=CHORD-containing protein 1;
DE Short=CHP-1;
DE AltName: Full=Protein morgana;
GN Name=CHORDC1; Synonyms=CHP1;
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-329.
RX PubMed=10571178; DOI=10.1016/s0092-8674(00)81522-6;
RA Shirasu K., Lahaye T., Tan M.-W., Zhou F., Azevedo C., Schulze-Lefert P.;
RT "A novel class of eukaryotic zinc-binding proteins is required for disease
RT resistance signaling in barley and development in C. elegans.";
RL Cell 99:355-366(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT ASP-329.
RC TISSUE=Heart;
RA Zhao Y., Cao H., Jiang Y., Meng X., Zhao X., Liu D., Ding J.;
RT "Isolation and characterization the chymotrypsin-like protein gene from
RT human heart cDNA library.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-329.
RC TISSUE=Thalamus;
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 GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASP-329.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Uterus;
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 [7]
RP PROTEIN SEQUENCE OF 2-8; 47-61; 108-121; 249-256; 282-289; 291-299 AND
RP 306-321, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Bilsland A.E., Keith W.N.;
RL Submitted (JAN-2010) to UniProtKB.
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47 AND SER-51, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP FUNCTION, INTERACTION WITH ROCK1 AND ROCK2, AND TISSUE SPECIFICITY.
RX PubMed=20230755; DOI=10.1016/j.devcel.2009.12.020;
RA Ferretti R., Palumbo V., Di Savino A., Velasco S., Sbroggio M.,
RA Sportoletti P., Micale L., Turco E., Silengo L., Palumbo G., Hirsch E.,
RA Teruya-Feldstein J., Bonaccorsi S., Pandolfi P.P., Gatti M., Tarone G.,
RA Brancaccio M.;
RT "Morgana/chp-1, a ROCK inhibitor involved in centrosome duplication and
RT tumorigenesis.";
RL Dev. Cell 18:486-495(2010).
RN [11]
RP INTERACTION WITH HSP90AA1.
RX PubMed=19875381; DOI=10.1074/mcp.m900261-mcp200;
RA Gano J.J., Simon J.A.;
RT "A proteomic investigation of ligand-dependent HSP90 complexes reveals
RT CHORDC1 as a novel ADP-dependent HSP90-interacting protein.";
RL Mol. Cell. Proteomics 9:255-270(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP IDENTIFICATION BY 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 [17]
RP FUNCTION.
RX PubMed=32053105; DOI=10.7554/elife.50986;
RA Haag A., Walser M., Henggeler A., Hajnal A.;
RT "The CHORD protein CHP-1 regulates EGF receptor trafficking and signaling
RT in C. elegans and in human cells.";
RL Elife 9:0-0(2020).
RN [18]
RP STRUCTURE BY NMR OF 1-68 IN COMPLEX WITH ZINC.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the CHORD domain of human CHORD-containing protein
RT 1.";
RL Submitted (APR-2008) to the PDB data bank.
CC -!- FUNCTION: Regulates centrosome duplication, probably by inhibiting the
CC kinase activity of ROCK2 (PubMed:20230755). Proposed to act as co-
CC chaperone for HSP90 (PubMed:20230755). May play a role in the
CC regulation of NOD1 via a HSP90 chaperone complex (PubMed:20230755). In
CC vitro, has intrinsic chaperone activity (PubMed:20230755). This
CC function may be achieved by inhibiting association of ROCK2 with NPM1
CC (PubMed:20230755). Plays a role in ensuring the localization of the
CC tyrosine kinase receptor EGFR to the plasma membrane, and thus ensures
CC the subsequent regulation of EGFR activity and EGF-induced actin
CC cytoskeleton remodeling (PubMed:32053105). Involved in stress response
CC (PubMed:20230755). Prevents tumorigenesis (PubMed:20230755).
CC {ECO:0000269|PubMed:20230755, ECO:0000269|PubMed:32053105}.
CC -!- SUBUNIT: Interacts with HSP90AA1, ROCK1 and ROCK2. Interacts with
CC HSP90AB1 and PPP5C (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9UHD1; P07900: HSP90AA1; NbExp=8; IntAct=EBI-2550959, EBI-296047;
CC Q9UHD1; P08238: HSP90AB1; NbExp=6; IntAct=EBI-2550959, EBI-352572;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UHD1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UHD1-2; Sequence=VSP_031150;
CC -!- TISSUE SPECIFICITY: Underexpressed in many breast and lung cancers.
CC {ECO:0000269|PubMed:20230755}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17789.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF192466; AAF18437.1; -; mRNA.
DR EMBL; AF123249; AAG43237.1; -; mRNA.
DR EMBL; AK290231; BAF82920.1; -; mRNA.
DR EMBL; AK312663; BAG35545.1; -; mRNA.
DR EMBL; AP002364; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471065; EAW66868.1; -; Genomic_DNA.
DR EMBL; CH471065; EAW66870.1; -; Genomic_DNA.
DR EMBL; BC017789; AAH17789.1; ALT_INIT; mRNA.
DR EMBL; BC072461; AAH72461.1; -; mRNA.
DR CCDS; CCDS44705.1; -. [Q9UHD1-2]
DR CCDS; CCDS8289.1; -. [Q9UHD1-1]
DR RefSeq; NP_001137545.1; NM_001144073.1. [Q9UHD1-2]
DR RefSeq; NP_036256.2; NM_012124.2. [Q9UHD1-1]
DR PDB; 2YRT; NMR; -; A=1-68.
DR PDBsum; 2YRT; -.
DR AlphaFoldDB; Q9UHD1; -.
DR SMR; Q9UHD1; -.
DR BioGRID; 117929; 95.
DR IntAct; Q9UHD1; 51.
DR MINT; Q9UHD1; -.
DR STRING; 9606.ENSP00000319255; -.
DR GlyGen; Q9UHD1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UHD1; -.
DR MetOSite; Q9UHD1; -.
DR PhosphoSitePlus; Q9UHD1; -.
DR SwissPalm; Q9UHD1; -.
DR BioMuta; CHORDC1; -.
DR DMDM; 167008724; -.
DR EPD; Q9UHD1; -.
DR jPOST; Q9UHD1; -.
DR MassIVE; Q9UHD1; -.
DR MaxQB; Q9UHD1; -.
DR PaxDb; Q9UHD1; -.
DR PeptideAtlas; Q9UHD1; -.
DR PRIDE; Q9UHD1; -.
DR ProteomicsDB; 84321; -. [Q9UHD1-1]
DR ProteomicsDB; 84322; -. [Q9UHD1-2]
DR Antibodypedia; 31553; 209 antibodies from 28 providers.
DR DNASU; 26973; -.
DR Ensembl; ENST00000320585.11; ENSP00000319255.6; ENSG00000110172.12. [Q9UHD1-1]
DR Ensembl; ENST00000457199.6; ENSP00000401080.2; ENSG00000110172.12. [Q9UHD1-2]
DR Ensembl; ENST00000646618.2; ENSP00000496744.1; ENSG00000285023.2. [Q9UHD1-1]
DR Ensembl; ENST00000647220.1; ENSP00000494044.1; ENSG00000285023.2. [Q9UHD1-2]
DR GeneID; 26973; -.
DR KEGG; hsa:26973; -.
DR MANE-Select; ENST00000320585.11; ENSP00000319255.6; NM_012124.3; NP_036256.2.
DR UCSC; uc001pdg.4; human. [Q9UHD1-1]
DR CTD; 26973; -.
DR DisGeNET; 26973; -.
DR GeneCards; CHORDC1; -.
DR HGNC; HGNC:14525; CHORDC1.
DR HPA; ENSG00000110172; Tissue enhanced (brain).
DR MIM; 604353; gene.
DR neXtProt; NX_Q9UHD1; -.
DR OpenTargets; ENSG00000110172; -.
DR PharmGKB; PA26476; -.
DR VEuPathDB; HostDB:ENSG00000110172; -.
DR eggNOG; KOG1667; Eukaryota.
DR GeneTree; ENSGT00940000154174; -.
DR HOGENOM; CLU_040079_0_0_1; -.
DR InParanoid; Q9UHD1; -.
DR OMA; MKQWSCC; -.
DR OrthoDB; 1163528at2759; -.
DR PhylomeDB; Q9UHD1; -.
DR TreeFam; TF105394; -.
DR PathwayCommons; Q9UHD1; -.
DR SignaLink; Q9UHD1; -.
DR BioGRID-ORCS; 26973; 522 hits in 1088 CRISPR screens.
DR ChiTaRS; CHORDC1; human.
DR EvolutionaryTrace; Q9UHD1; -.
DR GenomeRNAi; 26973; -.
DR Pharos; Q9UHD1; Tbio.
DR PRO; PR:Q9UHD1; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9UHD1; protein.
DR Bgee; ENSG00000110172; Expressed in corpus callosum and 103 other tissues.
DR ExpressionAtlas; Q9UHD1; baseline and differential.
DR Genevisible; Q9UHD1; HS.
DR GO; GO:0043531; F:ADP binding; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR GO; GO:0051879; F:Hsp90 protein binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0051298; P:centrosome duplication; IBA:GO_Central.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
DR GO; GO:2000299; P:negative regulation of Rho-dependent protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:1900034; P:regulation of cellular response to heat; ISS:UniProtKB.
DR GO; GO:0010824; P:regulation of centrosome duplication; IEA:Ensembl.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007051; CHORD_dom.
DR InterPro; IPR039790; CHORD_protein.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR PANTHER; PTHR12621; PTHR12621; 1.
DR Pfam; PF04968; CHORD; 2.
DR Pfam; PF04969; CS; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51401; CHORD; 2.
DR PROSITE; PS51203; CS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chaperone;
KW Direct protein sequencing; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Stress response; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:22814378"
FT CHAIN 2..332
FT /note="Cysteine and histidine-rich domain-containing
FT protein 1"
FT /id="PRO_0000317770"
FT DOMAIN 5..64
FT /note="CHORD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT DOMAIN 157..216
FT /note="CHORD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT DOMAIN 227..316
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT REGION 2..77
FT /note="Interaction with PPP5C"
FT /evidence="ECO:0000250"
FT REGION 65..316
FT /note="Interaction with HSP90AA1 and HSP90AB1"
FT /evidence="ECO:0000250"
FT BINDING 5
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.18, ECO:0007744|PDB:2YRT"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.18, ECO:0007744|PDB:2YRT"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.18, ECO:0007744|PDB:2YRT"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.18, ECO:0007744|PDB:2YRT"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.18, ECO:0007744|PDB:2YRT"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.18, ECO:0007744|PDB:2YRT"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|Ref.18, ECO:0007744|PDB:2YRT"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|Ref.18, ECO:0007744|PDB:2YRT"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:22814378"
FT MOD_RES 47
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 39..57
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_031150"
FT VARIANT 329
FT /note="A -> D (in dbSNP:rs1045861)"
FT /evidence="ECO:0000269|PubMed:10571178,
FT ECO:0000269|PubMed:14702039, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.5"
FT /id="VAR_038676"
FT CONFLICT 234
FT /note="W -> L (in Ref. 1; AAF18437)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="H -> I (in Ref. 1; AAF18437)"
FT /evidence="ECO:0000305"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:2YRT"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:2YRT"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:2YRT"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:2YRT"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:2YRT"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:2YRT"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:2YRT"
SQ SEQUENCE 332 AA; 37490 MW; 3142D8EC8A879155 CRC64;
MALLCYNRGC GQRFDPETNS DDACTYHPGV PVFHDALKGW SCCKRRTTDF SDFLSIVGCT
KGRHNSEKPP EPVKPEVKTT EKKELCELKP KFQEHIIQAP KPVEAIKRPS PDEPMTNLEL
KISASLKQAL DKLKLSSGNE ENKKEEDNDE IKIGTSCKNG GCSKTYQGLE SLEEVCVYHS
GVPIFHEGMK YWSCCRRKTS DFNTFLAQEG CTKGKHMWTK KDAGKKVVPC RHDWHQTGGE
VTISVYAKNS LPELSRVEAN STLLNVHIVF EGEKEFDQNV KLWGVIDVKR SYVTMTATKI
EITMRKAEPM QWASLELPAA KKQEKQKDAT TD
