IED Industry Enzyme Database

Detail Information for IndEnz0016000142
IED ID IndEnz0016000142
Enzyme Type ID tyrosinase000142
Protein Name Hemocyanin 2
Keyhole limpet hemocyanin B
KLH-B
Gene Name KLH2
Organism Megathura crenulata (Giant keyhole limpet)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Spiralia Lophotrochozoa Mollusca Gastropoda Vetigastropoda Lepetellida Fissurelloidea Fissurellidae Megathura Megathura crenulata (Giant keyhole limpet)
Enzyme Sequence MWTILALLTATLLFEGAFSVDTVVRKNVDSLSSDEVLALEKALDDLQQDDSNQGYQAIAGYHGVPTMCVDKHEKNVACCLHGMPSFPLWHRLYVVQLERALIRKKATISIPYWDWTSELTHLPELVSHPLFVGTEGGKAHDNSWYRADITFLNKKTSRAVDDRLFEKVQPGHHTRLMEGILDALEQDEFCKFEIQFELAHNAIHYLVGGRHTYSMSHLEYTSYDPLFFLHHSNTDRIFAIWQRLQQLRGKDPNSADCAHNLIHTPMEPFDRDTNPLDLTREHAKPADSFDYGRLGYQYDDLSLNGMSPEELNVYLGERAAKERTFASFILSGFGGSANVVVYVCRPAHDEISDDQCIKAGDFFLLGGPTEMKWGFYRAYHFDVTDSVASIDDDGHGHYYVKSELFSVNGSALSNDILRQPTLVHRPAKGHFDKPPVPVAQANLAVRKNINDLTAEETYSLRKAMERFQNDKSVDGYQATVEFHALPARCPRPDAKDRFACCVHGMATFPHWHRLFVTQVEDALLRRGSTIGLPNWDWTMPMDHLPELATSETYLDPVTGETKNNPFHHAQVAFENGVTSRNPDAKLFMKPTYGDHTYLFDSMIYAFEQEDFCDFEVQYELTHNAIHAWVGGSEKYSMSSLHYTAFDPIFYLHHSNVDRLWAIWQALQIRRGKSYKAHCASSQEREPLKPFAFSSPLNNNEKTYHNSVPTNVYDYVGVLHYRYDDLQFGGMTMSELEEYIHKQTQHDRTFAGFFLSYIGTSASVDIFINREGHDKYKVGSFVVLGGSKEMKWGFDRMYKYEITEALKTLNVAVDDGFSITVEITDVDGSPPSADLIPPPAIIFERADAKDFGHSRKIRKAVDSLTVEEQTSLRRAMADLQDDKTSGGFQQIAAFHGEPKWCPSPEAEKKFACCVHGMAVFPHWHRLLTVQGENALRKHGFTGGLPYWDWTRSMSALPHFVADPTYNDAISSQEEDNPWHHGHIDSVGHDTTRDVRDDLYQSPGFGHYTDIAKQVLLAFEQDDFCDFEVQFEIAHNFIHALVGGNEPYSMSSLRYTTYDPIFFLHRSNTDRLWAIWQALQKYRGKPYNTANCAIASMRKPLQPFGLDSVINPDDETREHSVPFRVFDYKNNFDYEYESLAFNGLSIAQLDRELQRRKSHDRVFAGFLLHEIGQSALVKFYVCKHNVSDCDHYAGEFYILGDEAEMPWRYDRVYKYEITQQLHDLDLHVGDNFFLKYEAFDLNGGSLGGSIFSQPSVIFEPAAGSHQADEYREAVTSASHIRKNIRDLSEGEIESIRSAFLQIQKEGIYENIAKFHGKPGLCEHDGHPVACCVHGMPTFPHWHRLYVLQVENALLERGSAVAVPYWDWTEKADSLPSLINDATYFNSRSQTFDPNPFFRGHIAFENAVTSRDPQPELWDNKDFYENVMLALEQDNFCDFEIQLELIHNALHSRLGGRAKYSLSSLDYTAFDPVFFLHHANVDRIWAIWQDLQRYRKKPYNEADCAVNEMRKPLQPFNNPELNSDSMTLKHNLPQDSFDYQNRFRYQYDNLQFNHFSIQKLDQTIQARKQHDRVFAGFILHNIGTSAVVDIYICVEQGGEQNCKTKAGSFTILGGETEMPFHFDRLYKFDITSALHKLGVPLDGHGFDIKVDVRAVNGSHLDQHILNEPSLLFVPGERKNIYYDGLSQHNLVRKEVSSLTTLEKHFLRKALKNMQADDSPDGYQAIASFHALPPLCPSPSAAHRHACCLHGMATFPQWHRLYTVQFEDSLKRHGSIVGLPYWDWLKPQSALPDLVTQETYEHLFSHKTFPNPFLKANIEFEGEGVTTERDVDAEHLFAKGNLVYNNWFCNQALYALEQENYCDFEIQFEILHNGIHSWVGGSKTHSIGHLHYASYDPLFYIHHSQTDRIWAIWQALQEHRGLSGKEAHCALEQMKDPLKPFSFGSPYNLNKRTQEFSKPEDTFDYHRFGYEYDSLEFVGMSVSSLHNYIKQQQEADRVFAGFLLKGFGQSASVSFDICRPDQSCQEAGYFSVLGGSSEMPWQFDRLYKYDITKTLKDMKLRYDDTFTIKVHIKDIAGAELDSDLIPTPSVLLEEGKHGINVRHVGRNRIRMELSELTERDLASLKSAMRSLQADDGVNGYQAIASFHGLPASCHDDEGHEIACCIHGMPVFPHWHRLYTLQMDMALLSHGSAVAIPYWDWTKPISKLPDLFTSPEYYDPWRDAVVNNPFAKGYIKSEDAYTVRDPQDILYHLQDETGTSVLLDQTLLALEQTDFCDFEVQFEVVHNAIHYLVGGRQVYALSSQHYASYDPAFFIHHSFVDKIWAVWQALQKKRKRPYHKADCALNMMTKPMRPFAHDFNHNGFTKMHAVPNTLFDFQDLFYTYDNLEIAGMNVNQLEAEINRRKSQTRVFAGFLLHGIGRSADVRFWICKTADDCHASGMIFILGGSKEMHWAYDRNFKYDITQALKAQSIHPEDVFDTDAPFFIKVEVHGVNKTALPSSAIPAPTIIYSAGEGHTDDHGSDHIAGSGVRKDVTSLTASEIENLRHALQSVMDDDGPNGFQAIAAYHGSPPMCHMXDGRDVACCTHGMASFPHWHRLFVKQMEDALAAHGAHIGIPYWDWTSAFSHLPALVTDHEHNPFHHGHIAHRNVDTSRSPRDMLFNDPEHGSESFFYRQVLLALEQTDFCQFEVQFEITHNAIHSWTGGHTPYGMSSLEYTAYDPLFYLHHSNTDRIWAIWQALQKYRGFQYNAAHCDIQVLKQPLKPFSESRNPNPVTRANSRAVDSFDYERLNYQYDTLTFHGHSISELDAMLQERKKEERTFAAFLLHGFGASADVSFDVCTPDGHCAFAGTFAVLGGELEMPWSFERLFRYDITKVLKQMNLHYDSEFHFELKIVGTDGTELPSDRIKSPTIEHHGGDHHGGDTSGHDHSERHDGFFRKEVGSLSLDEANDLKNALYKLQNDQGPNGYESIAGYHGYPFLCPEHGEDQYACCVHGMPVFPHWHRLHTIQFERALKEHGSHLGIPYWDWTKSMIALPAFFADSSNSNPFYKYHIMKAGHDTARSPSDLLFNQPQLHGYDYLYYLALSTLEEDNYCDFEVHYEILHNAVHLWLGGTETYSMSSLAFSAYDPVFMILHSGLDRLWIIWQELQKLRKKPYNAAKCAGHMMDEPLHPFNYESANHDSFTRANAKPSTVFDSHKFNYHYDNPDVRGNSIQEISAIIHDLRNQPRVFAGFVLSGIYTSANVKIYLVREGHDDENVGSFVVLGGPKEMPWAYERIFKYDITEVANRLNMHHDDTFNFRLEVQSYTGEMVTHHLPEPLIIYRPAKQEYDVLVIPLGSGHKLPPKVIVKRGTRIMFHPVDDTVNRPVVDLGSHTALYNCVVPPFTYNGYELDHAYSLRDGHYYIAGPTKDLCTSGNVRIHIHIEDE
Enzyme Length 3421
Uniprot Accession Number Q10584
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods. {ECO:0000305|PubMed:8829804}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Compositional bias (2); Cross-link (8); Disulfide bond (23); Glycosylation (3); Metal binding (48); Region (10); Repeat (8); Signal peptide (1)
Keywords Copper;Direct protein sequencing;Disulfide bond;Glycoprotein;Metal-binding;Oxygen transport;Repeat;Secreted;Signal;Thioether bond;Transport;WD repeat
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted, extracellular space.
Modified Residue
Post Translational Modification PTM: Probably N-glycosylated. Asn-2489 is buried deeply in the protein which make it inaccessible for sugar attachment. {ECO:0000250|UniProtKB:Q10583}.
Signal Peptide SIGNAL 1..19; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 391,513
Kinetics
Metal Binding METAL 62; /note="Copper 1; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 81; /note="Copper 1; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 90; /note="Copper 1; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 200; /note="Copper 2; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 204; /note="Copper 2; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 231; /note="Copper 2; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 483; /note="Copper 3; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 503; /note="Copper 3; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 512; /note="Copper 3; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 622; /note="Copper 4; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 626; /note="Copper 4; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 653; /note="Copper 4; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 894; /note="Copper 5; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 914; /note="Copper 5; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 923; /note="Copper 5; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 1033; /note="Copper 6; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 1037; /note="Copper 6; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 1063; /note="Copper 6; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583, ECO:0000305"; METAL 1313; /note="Copper 7; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 1331; /note="Copper 7; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 1340; /note="Copper 7; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 1444; /note="Copper 8; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 1448; /note="Copper 8; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 1475; /note="Copper 8; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 1726; /note="Copper 9; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 1746; /note="Copper 9; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 1755; /note="Copper 9; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 1868; /note="Copper 10; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 1872; /note="Copper 10; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 1899; /note="Copper 10; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 2143; /note="Copper 11; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 2162; /note="Copper 11; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 2171; /note="Copper 11; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 2281; /note="Copper 12; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 2285; /note="Copper 12; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 2312; /note="Copper 12; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 2563; /note="Copper 13; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 2582; /note="Copper 13; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 2591; /note="Copper 13; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 2691; /note="Copper 14; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 2695; /note="Copper 14; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 2722; /note="Copper 14; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 2970; /note="Copper 15; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 2989; /note="Copper 15; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 2998; /note="Copper 15; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 3099; /note="Copper 16; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 3103; /note="Copper 16; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"; METAL 3130; /note="Copper 16; via tele nitrogen"; /evidence="ECO:0000250|UniProtKB:Q10583"
Rhea ID
Cross Reference Brenda