CLCA1_MACMU
ID CLCA1_MACMU Reviewed; 913 AA.
AC Q6PT52;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Calcium-activated chloride channel regulator 1;
DE EC=3.4.-.- {ECO:0000250|UniProtKB:A8K7I4};
DE AltName: Full=Calcium-activated chloride channel family member 1;
DE Flags: Precursor;
GN Name=CLCA1;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ileum;
RA Tam J., Vaillancourt J.P., Xanthoudakis S.;
RT "Rhesus monkey calcium-activated chloride channel sequence.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in mediating calcium-activated chloride
CC conductance. May play critical roles in goblet cell metaplasia, mucus
CC hypersecretion, cystic fibrosis and AHR. May be involved in the
CC regulation of mucus production and/or secretion by goblet cells.
CC Involved in the regulation of tissue inflammation in the innate immune
CC response. May play a role as a tumor suppressor. Induces MUC5AC (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC -!- DOMAIN: The metalloprotease region is responsible for autoproteolytic
CC processing. It can also cross-cleave other CLCA substrates.
CC {ECO:0000250|UniProtKB:A8K7I4}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- PTM: The translation product is autoproteolytically cleaved by the
CC metalloprotease domain in the endoplasmic reticulum into a N-terminal
CC and a C-terminal products that remain physically associated with each
CC other. The cleavage is necessary for calcium-activated chloride channel
CC (CaCC) activation activity. {ECO:0000250|UniProtKB:A8K7I4}.
CC -!- SIMILARITY: Belongs to the CLCR family. {ECO:0000305}.
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DR EMBL; AY581306; AAS90562.1; -; mRNA.
DR RefSeq; NP_001028084.1; NM_001032912.1.
DR AlphaFoldDB; Q6PT52; -.
DR SMR; Q6PT52; -.
DR STRING; 9544.ENSMMUP00000008987; -.
DR MEROPS; M87.001; -.
DR GeneID; 574295; -.
DR KEGG; mcc:574295; -.
DR CTD; 1179; -.
DR eggNOG; ENOG502QRRD; Eukaryota.
DR InParanoid; Q6PT52; -.
DR OrthoDB; 685640at2759; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006816; P:calcium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR004727; CLCA_chordata.
DR InterPro; IPR013642; CLCA_N.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF08434; CLCA; 1.
DR Pfam; PF13519; VWA_2; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR TIGRFAMs; TIGR00868; hCaCC; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 2: Evidence at transcript level;
KW Autocatalytic cleavage; Calcium; Calcium transport; Chloride; Glycoprotein;
KW Hydrolase; Ion transport; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal; Transport; Zinc.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..913
FT /note="Calcium-activated chloride channel regulator 1"
FT /id="PRO_0000333691"
FT DOMAIN 306..475
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 46..199
FT /note="Metalloprotease domain"
FT /evidence="ECO:0000250|UniProtKB:A8K7I4"
FT REGION 866..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 157
FT /evidence="ECO:0000250|UniProtKB:A8K7I4"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:A8K7I4"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:A8K7I4"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:A8K7I4"
FT SITE 694..695
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:A8K7I4"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 769
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 803
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 809
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 830
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 835
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 885
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 889
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 913 AA; 100361 MW; 833DDF47578E8CC5 CRC64;
MGPFKSSVFI LILHLLEGAL SDSLIQLNNN GYEGIVIAID PNVPEDETLI QQIKDMVTQA
SPYLFEATGK RFYFKNVAIL IPETWKTKAD YVRPKLETYK NADVLVAEST PSGGDEPYTE
HIGKCGDQGE RIHLTPHFLA GKQLKEYGPQ GRAFVHEWAH LRWGVFDEYN NDEKFYLSNG
RIQAVRCSVG ITGKIEVNKC QGGSCYTKRC TFNKATGLYE KGCEFIPHSQ QTEKASIMFA
QHVDSVVEFC TEQNHNKEAP NMQNTKCNLR STWEVIRDSE DFKKTTPTTT QPPNPTFSLL
QIGQRIVCLV LDKSGSMATG NRLNRLNQAG QLFLLQIIEL RSWVGMVTFD SAAHVQSELI
QINSGSDRDT LTKRLPTAAS GGTSICSGLR LAFTVIKKKY PTDGSEIVLL TDGEDNTISG
CFNEVKQSGA IIHTVALGPS AARELEELSK MTGGLQTYAS DQVQNNGLID AFGALSSGNG
VVSERSIQLE SKGSTLQNSQ WMNGTVIVDS TVGKDTLFLV TWTTQPPQIL LWDPSGQKQD
GFVVDKNTKM AFLQIPGIAK VGTWKYSLQA SSQTLTLTVT SRASSATLPP ITVTSKMNKD
TGKFPSPMIV YANIRQGASP ILRASVTALI ESENGKTVTL ELLDNGAGAD AAKDDGVYSR
YFTTYDTNGR YSVKVRALGG VNAVRRRAIP QQSGVMYIPG WIENDEIQWN PPRPEIEDDV
QRKQVCFSRT SSGGSFVASG VPNAPIPDLF PPCQITDLKA EIHGHSLINL TWTAPGDDYD
HGTAHKYIIR ISTSILDLRD KFNESLQVNT TALIPKEANS EEVFLFKPEN ITFENGTDLF
IAIQAVDKVD LKSEISNIAR VSLFIPPQTP PETPSPDETS APCPNISINS TIPGIHILKI
MWKWIGELQL SIG
