| IED ID | IndEnz0002018327 |
| Enzyme Type ID | protease018327 |
| Protein Name |
Calcium-activated chloride channel regulator 4 EC 3.4.-.- Calcium-activated chloride channel family member 4 hCLCA4 Calcium-activated chloride channel protein 2 CaCC-2 hCaCC-2 Chloride channel accessory 4 Cleaved into: Calcium-activated chloride channel regulator 4, 110 kDa form; Calcium-activated chloride channel regulator 4, 30 kDa form |
| Gene Name | CLCA4 CaCC2 UNQ562/PRO1124 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MGLFRGFVFLLVLCLLHQSNTSFIKLNNNGFEDIVIVIDPSVPEDEKIIEQIEDMVTTASTYLFEATEKRFFFKNVSILIPENWKENPQYKRPKHENHKHADVIVAPPTLPGRDEPYTKQFTECGEKGEYIHFTPDLLLGKKQNEYGPPGKLFVHEWAHLRWGVFDEYNEDQPFYRAKSKKIEATRCSAGISGRNRVYKCQGGSCLSRACRIDSTTKLYGKDCQFFPDKVQTEKASIMFMQSIDSVVEFCNEKTHNQEAPSLQNIKCNFRSTWEVISNSEDFKNTIPMVTPPPPPVFSLLKISQRIVCLVLDKSGSMGGKDRLNRMNQAAKHFLLQTVENGSWVGMVHFDSTATIVNKLIQIKSSDERNTLMAGLPTYPLGGTSICSGIKYAFQVIGELHSQLDGSEVLLLTDGEDNTASSCIDEVKQSGAIVHFIALGRAADEAVIEMSKITGGSHFYVSDEAQNNGLIDAFGALTSGNTDLSQKSLQLESKGLTLNSNAWMNDTVIIDSTVGKDTFFLITWNSLPPSISLWDPSGTIMENFTVDATSKMAYLSIPGTAKVGTWAYNLQAKANPETLTITVTSRAANSSVPPITVNAKMNKDVNSFPSPMIVYAEILQGYVPVLGANVTAFIESQNGHTEVLELLDNGAGADSFKNDGVYSRYFTAYTENGRYSLKVRAHGGANTARLKLRPPLNRAAYIPGWVVNGEIEANPPRPEIDEDTQTTLEDFSRTASGGAFVVSQVPSLPLPDQYPPSQITDLDATVHEDKIILTWTAPGDNFDVGKVQRYIIRISASILDLRDSFDDALQVNTTDLSPKEANSKESFAFKPENISEENATHIFIAIKSIDKSNLTSKVSNIAQVTLFIPQANPDDIDPTPTPTPTPTPDKSHNSGVNISTLVLSVIGSVVIVNFILSTTI |
| Enzyme Length | 919 |
| Uniprot Accession Number | Q14CN2 |
| Absorption | |
| Active Site | ACT_SITE 156; /evidence=ECO:0000250|UniProtKB:A8K7I4 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.-.- |
| Enzyme Function | FUNCTION: May be involved in mediating calcium-activated chloride conductance. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (3); Chain (3); Domain (1); Glycosylation (10); Metal binding (3); Natural variant (5); Region (2); Sequence conflict (1); Signal peptide (1); Site (1); Transmembrane (1) |
| Keywords | Alternative splicing;Autocatalytic cleavage;Cell membrane;Chloride;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Transmembrane;Transmembrane helix;Transport;Zinc |
| Interact With | |
| Induction | INDUCTION: Down-regulated in oral tongue squamous cell carcinomas. {ECO:0000269|PubMed:18254958}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Apical cell membrane {ECO:0000250}. Secreted {ECO:0000250}. Note=The C-terminus 30 kDa form is anchored to the membrane. The N-terminus 110 kDa form is released from the membrane triggered by an unknown stimulus. {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: The translation product is autoproteolytically cleaved by the metalloprotease domain in the endoplasmic reticulum into a N-terminal and a C-terminal products that remain physically associated with each other. The cleavage is necessary for calcium-activated chloride channel (CaCC) activation activity. {ECO:0000250|UniProtKB:A8K7I4}. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11842292; 11904445; 11956057; 12907679; 15010458; 15318163; 15919655; 16219661; 18724360; 19307298; 21984732; 22946059; 23073314; 23112050; 24386311; 30312171; 30887952; 31164625; 32773719; 32797167; 9662395; 9700209; |
| Motif | |
| Gene Encoded By | |
| Mass | 101,283 |
| Kinetics | |
| Metal Binding | METAL 155; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:A8K7I4; METAL 159; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:A8K7I4; METAL 166; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:A8K7I4 |
| Rhea ID | |
| Cross Reference Brenda |