| IED ID | IndEnz0002002669 |
| Enzyme Type ID | protease002669 |
| Protein Name |
Cadherin-related hmr-1 Protein Hammerhead |
| Gene Name | hmr-1 W02B9.1 |
| Organism | Caenorhabditis elegans |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
| Enzyme Sequence | MSWNILLILLISNLDEVLAKTLLKLPSNAPPGWLISDLQFQNLIGDSEIATLQPSIFSTNFEVEDGYRIITNTTVTQFHGELFELFLNVKEQNFQRLVTLHVYVDPRGTSQQPATFLSTVYHATVYTSQQPGSTVVFSKPITVRNRKNFVISPISKIDKISKYSSPFSVMTRGKSVDIVMMKQKLEEDDITRHVIFLGAFTEKTGEMIAQTKVIIDVIDSGDVHFLLKSKKSIAKFASAIPANSTVFDVEKRNLSEPLLFHLEEPSRFFKIDQFSGRVSTVLPVGYGTYHIHVVARNQKKQRSDAWLEISVKKEQKLEPMTSSRSRRHLDDIVFRIPENTTMEDIEKKDMKIPLFAGETIGEINVAKEWLKIDDDGKIHLLKPLNYEKTSSIIATVPINGLQSTRTQTIRIHVADIDEPPSFVNSPLPMLAVVPLNPTIGRIVYQFVARDEHGDGDSNVLYKTIDVIPAGSFIVDPKSGVVRTGWSKYERGDTYRISAQAMDLSPSDNTTSQLSEVAILEILADERPPQFAKQEYEVTVSEDNLVDYSVVDVKAQSFRSFEDGRSKGPITYSLEGDTPEDETKWFRIDPSTGIIHLTRLLDFDDPALPKLHKLKVTAREDNRESHVDLTIRIDDVNDNVPTFTRPLYTAQVREDIPLNQTILKVTAVDKDTGDNSRITYSVDNHNFSINSNGEISAKVRLDADQLNERHFVYRFNVTARDHGEPVSLSSSAMIHIRTENTNDESAVFLPTSQYTAFVAEDAQGGTPVIQIQARDADRDEVTYSFMDKNGRSTQKMNLFSIDEHTGLVKLRHGVSAADLAEAENPINLTVIVQDDGSCCVYPSKTHTSYATLLIGIEDVNNNKPEFPDCAKYSDIAKIMEGTYKTDPPTIVKVEATDDDSSANGDIVYSLYYTQSESRKAFVIDRQTGVLTPSPHVVFDRETRPREDVTVKATDRGDRPLIGFCQFSVEVVDINDNSPQFERPSYETSVSRFEAVGTSVITVFAFDNDAAHNAEITYSLEIDTTAGEEHQNDLDFFELVNRRSGEITLIKPIPMKTQKFIFNVIADDNGIPEALQSSAQVTLNVLDKQQKAPKWQTSPDCKPGITVDENVELNKVILRCRAVSSGDSRNSDVIYKLTASGGPGNKAESKFRQFNKFENGNEWVEVVIMEGLDYEQVNNYTLTLTATDMTSRVASTKTFVVEVRDVNDVVPQFTVDLFTGTIDEEMTPNEHLEKTNGKPIVTVKAIDTDSDGPQNEVHYRIVGEANGEETKHFRIDELTGEIFPNEKFDREKIDMYILTVEASDRSVSALPGANGPNKDNVKVQIVINDVNDNAPSFEEQKYIGRVKESEGEGHDVITIKAHDLDKHSNLRYHLIGAGGGRIPFGVRTDSGTIFVKEPLDFEASDQYHLVLIASDGRHNATTNVYIHIEDVNDNAPQFEQQKYATTVIEEDVDIPKVLFNVHATDADQDEKSSRIVYRLEGQGADEVFRIGKYSGTIELVKALDRDPPAGVPSWNFVVQAIDDDGNGLVGYADVQVNVRDINDNSPIFPERLFGYIEENREPIHSDGVYFMDVQARDFDDPTTENANIEYGIVRNKLINGESVFRIDQNTGKIFAMRSLDREISSEREFIIEVRANDRGVPSREGFANVTIKVTDMNDNAPFFEKTRYEGSVEETAPIGAAVMSFSAFDADEEAKDNVFTYQLSEESDYFYVTTDKDSKQSSVGVLRVKQPLDYEDVTQRDGFHLGIRVSDGRHDAEAAVHVALVDRNDHAPHIHGATEHRVREDVPRGTSIGRYTATDRDAGDTARFRINRQSDPKRQFTIDQDGTLRVAHTLDREDIAVYNLIIEAYDNSNNIGRQMVAVYLQDVNDNGPEPYTVPRPCIFRENTPVNQLGTCEIRATDRDTAEFGPPFTMEVSPSFKYSQYLNVIFNANGDGGNGSMTITPLQEFDREAPVPGKILEIPLILADRAGRRNEASVHVIIGDLNDNTMHDGRMTIHVNSYLGRLKETVIGRVYVDDADDWDLGDKTFSWKDSRPGFELSDKGSITMAGEMAAGTYTMSANVHDNARDEDAVGYVTVIVNAVPQIAFDNQGSVQLLIAEETPLQLPDDFIRADSNGQSLMDTFKQEMTAYMGGDVTVDVFSVQVGIATLQTRDVPVLNVRFNARGSTYRDTAQLNGLIAAHRADLQRKLNVEIVGVGIDMCKFTQCDAGCQTLNSADYDGIVVSANSTVIVGVNATSRDDCTCPVWRAPPACQHSLCHNDGVCHNTNPGFFCECRNDGLKGARCQGTTRSFGGNGFAWYKPMPACTSLNISFSFMTTQSDALLFYNGPLETLRNDTHIEYSDYIFIQLRGGRISLEVSMNGQSRSSLEVASTALNDGTWHDISVNQEGKRVELVVDNCRFLGAGADDSSCRAELYTPDDDERLNIVTPVQIGGLAPLSGQDYPQTIPRAGLNGCVRNLNVNGDQYDLATPAFEQNSEKGCRLWGATCDSNSVDSLNHCIHGDCFADVQGSGAMVAKCVCDPGWGGARCERRMEWIQFAQGAFIEYSPRIAFPEQVSDIELLFISGKVNGAPAELSFGTDSQQSYVSTNLESGQNGVTAAGKFDIGTGGRRARQELRVSEVLLKENASYWLQFTRNPTRASLSIDNAYTVSTQLDKGEPFSLQVNQITLGTQGQNKGFQGCIGTYRWSKQNLPLKRGGAMDENEESIVSISNMAGVQDGCDLRITCADLPAGYCGGSFVCVDFWKGPFCTCNDGANAILGDDGQVVGCGETLAVSKLGISSPAIILILVSLALLILLVMMMVVYTRRSPGAFENVRPEEMNRDNLRQYGVEGGGEADNDQYSMAGLRKPVMPLDTGMGPAIGGHPPHYPPRGMAPPKDDHELNSKIKDLETDQNAAPYDELRIYDDERDNISVVTLESIESAQ |
| Enzyme Length | 2920 |
| Uniprot Accession Number | Q967F4 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Cadherins are calcium-dependent cell adhesion proteins (PubMed:25938815, PubMed:25850673). They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types (PubMed:25938815, PubMed:25850673). Required for adherens junction assembly and connecting adherens junctions to the cytoskeleton (PubMed:26412237). {ECO:0000269|PubMed:25850673, ECO:0000269|PubMed:25938815, ECO:0000269|PubMed:26412237}.; FUNCTION: Isoform a is required for cell migration during body enclosure and cell shape changes during body elongation (PubMed:9531567, PubMed:12847081). Required for proper localization of other junctional components, such as hmp-1, hmp-2, jac-1 and pac-1 (PubMed:9531567, PubMed:25938815). Recruitment of pac-1 is required to establish cell polarity, independent of its role in cell adhesion (PubMed:25938815). Required for primodial germ cell ingression and adherence to endodermal cells during gastrulation (PubMed:20515680, PubMed:22675206). {ECO:0000269|PubMed:12847081, ECO:0000269|PubMed:20515680, ECO:0000269|PubMed:22675206, ECO:0000269|PubMed:25938815, ECO:0000269|PubMed:9531567}.; FUNCTION: Isoform b is involved in axonal guidance in a subset of motor neurons. {ECO:0000269|PubMed:11790304}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (6); Beta strand (2); Chain (1); Compositional bias (1); Disulfide bond (6); Domain (17); Erroneous initiation (1); Glycosylation (18); Helix (2); Modified residue (5); Mutagenesis (6); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1) |
| Keywords | 3D-structure;Alternative splicing;Calcium;Cell adhesion;Cell junction;Cell membrane;Developmental protein;Differentiation;Disulfide bond;EGF-like domain;Glycoprotein;Membrane;Neurogenesis;Phosphoprotein;Reference proteome;Repeat;Signal;Transmembrane;Transmembrane helix;Ubl conjugation |
| Interact With | O44326; Q9U308 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12847081, ECO:0000269|PubMed:25938815, ECO:0000269|PubMed:9531567}; Single-pass type I membrane protein {ECO:0000269|PubMed:12847081, ECO:0000269|PubMed:9531567}. Cell junction, adherens junction {ECO:0000269|PubMed:12847081, ECO:0000269|PubMed:20515680, ECO:0000269|PubMed:25850673, ECO:0000269|PubMed:25938815, ECO:0000269|PubMed:26412237}. Cell junction {ECO:0000269|PubMed:20689042}. Note=The basal to apical translocation from the cell membrane to adherens junctions is determined by the coupled sumoylation and desumoylation state of hmr-1. {ECO:0000269|PubMed:26412237}.; SUBCELLULAR LOCATION: [Isoform a]: Cell junction, adherens junction {ECO:0000269|PubMed:12847081, ECO:0000269|PubMed:25850673}. |
| Modified Residue | MOD_RES 2839; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:25850673; MOD_RES 2909; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:25850673; MOD_RES 2912; /note=Phosphothreonine; /evidence=ECO:0000269|PubMed:25850673; MOD_RES 2915; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:25850673; MOD_RES 2918; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:25850673 |
| Post Translational Modification | PTM: Phosphorylation at T-2912 increases the binding affinity for hmp-2. {ECO:0000269|PubMed:25850673}.; PTM: Sumoylated. Sumoylation prevents accumulation at adherens junctions and decreases the binding affinity for hmp-2. {ECO:0000269|PubMed:26412237}. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 4R10; 4R11; |
| Mapped Pubmed ID | 10531027; 10778742; 11099033; 11231151; 11381264; 12023307; 12097347; 12819787; 14551910; 14961122; 15791247; 16117677; 17164286; 17276345; 17417969; 17601533; 17704769; 18718757; 19343510; 20439774; 20439776; 20610404; 21034729; 21085631; 21177967; 21367940; 21527776; 22267497; 22286215; 22347378; 22560298; 23800452; 24884423; 25487147; 25858456; 26443865; 26780296; 26923492; 27506200; 27989674; 28298447; 29045470; 29183946; 30389847; 6593563; |
| Motif | |
| Gene Encoded By | |
| Mass | 323,914 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |