CAH14_HUMAN
ID CAH14_HUMAN Reviewed; 337 AA.
AC Q9ULX7; Q5TB24; Q8NCF4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Carbonic anhydrase 14;
DE EC=4.2.1.1;
DE AltName: Full=Carbonate dehydratase XIV;
DE AltName: Full=Carbonic anhydrase XIV;
DE Short=CA-XIV;
DE Flags: Precursor;
GN Name=CA14; ORFNames=UNQ690/PRO1335;
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].
RX PubMed=10512682; DOI=10.1006/geno.1999.5938;
RA Fujikawa-Adachi K., Nishimori I., Taguchi T., Onishi S.;
RT "Human carbonic anhydrase XIV (CA14): cDNA cloning, mRNA expression, and
RT mapping to chromosome 1.";
RL Genomics 61:74-81(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lung, and 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 [7]
RP ACTIVITY REGULATION.
RX PubMed=16807956; DOI=10.1002/chem.200600159;
RA Temperini C., Scozzafava A., Vullo D., Supuran C.T.;
RT "Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII,
RT and XIV with l- and d-histidine and crystallographic analysis of their
RT adducts with isoform II: engineering proton-transfer processes within the
RT active site of an enzyme.";
RL Chemistry 12:7057-7066(2006).
RN [8]
RP ACTIVITY REGULATION.
RX PubMed=16686544; DOI=10.1021/jm0603320;
RA Temperini C., Scozzafava A., Vullo D., Supuran C.T.;
RT "Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII,
RT and XIV with L- and D-phenylalanine and crystallographic analysis of their
RT adducts with isozyme II: stereospecific recognition within the active site
RT of an enzyme and its consequences for the drug design.";
RL J. Med. Chem. 49:3019-3027(2006).
RN [9]
RP ACTIVITY REGULATION.
RX PubMed=17705204; DOI=10.1002/anie.200701189;
RA Koehler K., Hillebrecht A., Schulze Wischeler J., Innocenti A., Heine A.,
RA Supuran C.T., Klebe G.;
RT "Saccharin inhibits carbonic anhydrases: possible explanation for its
RT unpleasant metallic aftertaste.";
RL Angew. Chem. Int. Ed. Engl. 46:7697-7699(2007).
RN [10]
RP ACTIVITY REGULATION.
RX PubMed=17127057; DOI=10.1016/j.bmcl.2006.11.027;
RA Temperini C., Innocenti A., Scozzafava A., Mastrolorenzo A., Supuran C.T.;
RT "Carbonic anhydrase activators: L-Adrenaline plugs the active site entrance
RT of isozyme II, activating better isoforms I, IV, VA, VII, and XIV.";
RL Bioorg. Med. Chem. Lett. 17:628-635(2007).
RN [11]
RP ACTIVITY REGULATION.
RX PubMed=17314045; DOI=10.1016/j.bmcl.2007.01.113;
RA Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S.,
RA Supuran C.T.;
RT "Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray
RT crystal structure of the antiviral drug foscarnet complexed to human
RT carbonic anhydrase I.";
RL Bioorg. Med. Chem. Lett. 17:2210-2215(2007).
RN [12]
RP ACTIVITY REGULATION.
RX PubMed=19186056; DOI=10.1016/j.bmcl.2009.01.038;
RA Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A.,
RA Muehlschlegel F.A., Supuran C.T.;
RT "A thiabendazole sulfonamide shows potent inhibitory activity against
RT mammalian and nematode alpha-carbonic anhydrases.";
RL Bioorg. Med. Chem. Lett. 19:1371-1375(2009).
RN [13]
RP ACTIVITY REGULATION.
RX PubMed=19206230; DOI=10.1021/ja809683v;
RA Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A., Scozzafava A.,
RA Quinn R.J., Supuran C.T.;
RT "Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new
RT class of suicide inhibitors.";
RL J. Am. Chem. Soc. 131:3057-3062(2009).
RN [14]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=18618712; DOI=10.1002/prot.22144;
RA Di Fiore A., Monti S.M., Hilvo M., Parkkila S., Romano V., Scaloni A.,
RA Pedone C., Scozzafava A., Supuran C.T., De Simone G.;
RT "Crystal structure of human carbonic anhydrase XIII and its complex with
RT the inhibitor acetazolamide.";
RL Proteins 74:164-175(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, AND IDENTIFICATION BY
RP 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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 16-290, ZINC-BINDING SITES,
RP GLYCOSYLATION AT ASN-213, AND DISULFIDE BOND.
RX PubMed=24374484; DOI=10.1002/bip.22456;
RA Alterio V., Pan P., Parkkila S., Buonanno M., Supuran C.T., Monti S.M.,
RA De Simone G.;
RT "The structural comparison between membrane-associated human carbonic
RT anhydrases provides insights into drug design of selective inhibitors.";
RL Biopolymers 101:769-778(2014).
CC -!- FUNCTION: Reversible hydration of carbon dioxide.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17544; EC=4.2.1.1;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:24374484};
CC -!- ACTIVITY REGULATION: Activated by histamine, L-adrenaline, L- and D-
CC histidine, and L- and D-phenylalanine. Inhibited by coumarins,
CC saccharin, sulfonamide derivatives such as acetazolamide (AZA) and
CC Foscarnet (phosphonoformate trisodium salt).
CC {ECO:0000269|PubMed:16686544, ECO:0000269|PubMed:16807956,
CC ECO:0000269|PubMed:17127057, ECO:0000269|PubMed:17314045,
CC ECO:0000269|PubMed:17705204, ECO:0000269|PubMed:18618712,
CC ECO:0000269|PubMed:19186056, ECO:0000269|PubMed:19206230}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.9 mM for CO(2) {ECO:0000269|PubMed:18618712};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: High expression in all parts of the central nervous
CC system and lower expression in adult liver, heart, small intestine,
CC colon, kidney, urinary bladder and skeletal muscle.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; AB025904; BAA85002.1; -; mRNA.
DR EMBL; AY358689; AAQ89052.1; -; mRNA.
DR EMBL; AK074765; BAC11191.1; -; mRNA.
DR EMBL; BT020054; AAV38857.1; -; mRNA.
DR EMBL; AL138795; CAI22810.1; -; Genomic_DNA.
DR EMBL; BC034412; AAH34412.1; -; mRNA.
DR CCDS; CCDS947.1; -.
DR RefSeq; NP_036245.1; NM_012113.2.
DR PDB; 4LU3; X-ray; 2.00 A; A=16-290.
DR PDB; 5CJF; X-ray; 1.83 A; A=16-291.
DR PDBsum; 4LU3; -.
DR PDBsum; 5CJF; -.
DR AlphaFoldDB; Q9ULX7; -.
DR SMR; Q9ULX7; -.
DR BioGRID; 117162; 77.
DR IntAct; Q9ULX7; 32.
DR STRING; 9606.ENSP00000358107; -.
DR BindingDB; Q9ULX7; -.
DR ChEMBL; CHEMBL3510; -.
DR DrugBank; DB00819; Acetazolamide.
DR DrugBank; DB00562; Benzthiazide.
DR DrugBank; DB00606; Cyclothiazide.
DR DrugBank; DB08846; Ellagic acid.
DR DrugBank; DB00909; Zonisamide.
DR DrugCentral; Q9ULX7; -.
DR GuidetoPHARMACOLOGY; 2598; -.
DR GlyGen; Q9ULX7; 1 site.
DR iPTMnet; Q9ULX7; -.
DR PhosphoSitePlus; Q9ULX7; -.
DR BioMuta; CA14; -.
DR DMDM; 8928036; -.
DR EPD; Q9ULX7; -.
DR jPOST; Q9ULX7; -.
DR MassIVE; Q9ULX7; -.
DR PaxDb; Q9ULX7; -.
DR PeptideAtlas; Q9ULX7; -.
DR PRIDE; Q9ULX7; -.
DR ProteomicsDB; 85149; -.
DR Antibodypedia; 2374; 211 antibodies from 29 providers.
DR DNASU; 23632; -.
DR Ensembl; ENST00000369111.9; ENSP00000358107.3; ENSG00000118298.12.
DR Ensembl; ENST00000647854.1; ENSP00000498013.1; ENSG00000118298.12.
DR GeneID; 23632; -.
DR KEGG; hsa:23632; -.
DR MANE-Select; ENST00000369111.9; ENSP00000358107.3; NM_012113.3; NP_036245.1.
DR UCSC; uc001etx.5; human.
DR CTD; 23632; -.
DR DisGeNET; 23632; -.
DR GeneCards; CA14; -.
DR HGNC; HGNC:1372; CA14.
DR HPA; ENSG00000118298; Tissue enhanced (choroid plexus, retina, skeletal muscle, tongue).
DR MIM; 604832; gene.
DR neXtProt; NX_Q9ULX7; -.
DR OpenTargets; ENSG00000118298; -.
DR PharmGKB; PA25988; -.
DR VEuPathDB; HostDB:ENSG00000118298; -.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000156893; -.
DR HOGENOM; CLU_039326_1_2_1; -.
DR InParanoid; Q9ULX7; -.
DR OMA; HGQEHWP; -.
DR OrthoDB; 1377476at2759; -.
DR PhylomeDB; Q9ULX7; -.
DR TreeFam; TF316425; -.
DR BRENDA; 4.2.1.1; 2681.
DR PathwayCommons; Q9ULX7; -.
DR Reactome; R-HSA-1475029; Reversible hydration of carbon dioxide.
DR SABIO-RK; Q9ULX7; -.
DR SignaLink; Q9ULX7; -.
DR BioGRID-ORCS; 23632; 11 hits in 1075 CRISPR screens.
DR ChiTaRS; CA14; human.
DR GeneWiki; CA14; -.
DR GenomeRNAi; 23632; -.
DR Pharos; Q9ULX7; Tclin.
DR PRO; PR:Q9ULX7; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9ULX7; protein.
DR Bgee; ENSG00000118298; Expressed in pigmented layer of retina and 135 other tissues.
DR ExpressionAtlas; Q9ULX7; baseline and differential.
DR Genevisible; Q9ULX7; HS.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004089; F:carbonate dehydratase activity; IBA:GO_Central.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR Gene3D; 3.10.200.10; -; 1.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR InterPro; IPR018431; Carbonic_anhydrase_CA14.
DR PANTHER; PTHR18952; PTHR18952; 1.
DR PANTHER; PTHR18952:SF84; PTHR18952:SF84; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; SSF51069; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Lyase; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Zinc.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..337
FT /note="Carbonic anhydrase 14"
FT /id="PRO_0000004251"
FT TOPO_DOM 16..290
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..278
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT ACT_SITE 84
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:24374484"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:24374484"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:24374484"
FT BINDING 217..218
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24374484"
FT DISULFID 40..221
FT /evidence="ECO:0000269|PubMed:24374484"
FT CONFLICT 229
FT /note="V -> A (in Ref. 3; BAC11191)"
FT /evidence="ECO:0000305"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:5CJF"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:5CJF"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:5CJF"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:5CJF"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:5CJF"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:5CJF"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:5CJF"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:5CJF"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:5CJF"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:5CJF"
FT STRAND 103..112
FT /evidence="ECO:0007829|PDB:5CJF"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:5CJF"
FT STRAND 131..140
FT /evidence="ECO:0007829|PDB:5CJF"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:5CJF"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:5CJF"
FT STRAND 157..169
FT /evidence="ECO:0007829|PDB:5CJF"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:5CJF"
FT HELIX 179..183
FT /evidence="ECO:0007829|PDB:5CJF"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:5CJF"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:5CJF"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:5CJF"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:5CJF"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:5CJF"
FT HELIX 238..245
FT /evidence="ECO:0007829|PDB:5CJF"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:5CJF"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:5CJF"
SQ SEQUENCE 337 AA; 37668 MW; 6E101C44EA70A700 CRC64;
MLFSALLLEV IWILAADGGQ HWTYEGPHGQ DHWPASYPEC GNNAQSPIDI QTDSVTFDPD
LPALQPHGYD QPGTEPLDLH NNGHTVQLSL PSTLYLGGLP RKYVAAQLHL HWGQKGSPGG
SEHQINSEAT FAELHIVHYD SDSYDSLSEA AERPQGLAVL GILIEVGETK NIAYEHILSH
LHEVRHKDQK TSVPPFNLRE LLPKQLGQYF RYNGSLTTPP CYQSVLWTVF YRRSQISMEQ
LEKLQGTLFS TEEEPSKLLV QNYRALQPLN QRMVFASFIQ AGSSYTTGEM LSLGVGILVG
CLCLLLAVYF IARKIRKKRL ENRKSVVFTS AQATTEA
