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Calcium-activated chloride channel regulator 2 (EC 3.4.-.-) (Calcium-activated chloride channel family member 2) (hCLCA2) (Calcium-activated chloride channel protein 3) (CaCC-3) (hCaCC-3) [Cleaved into: Calcium-activated chloride channel regulator 2, 109 kDa form; Calcium-activated chloride channel regulator 2, 35 kDa form]

 CLCA2_HUMAN             Reviewed;         943 AA.
Q9UQC9; A8K2T3; Q9Y6N2;
20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
20-MAY-2008, sequence version 2.
18-JUL-2018, entry version 131.
RecName: Full=Calcium-activated chloride channel regulator 2;
EC=3.4.-.- {ECO:0000250|UniProtKB:A8K7I4};
AltName: Full=Calcium-activated chloride channel family member 2;
Short=hCLCA2;
AltName: Full=Calcium-activated chloride channel protein 3;
Short=CaCC-3;
Short=hCaCC-3;
Contains:
RecName: Full=Calcium-activated chloride channel regulator 2, 109 kDa form;
Contains:
RecName: Full=Calcium-activated chloride channel regulator 2, 35 kDa form;
Flags: Precursor;
Name=CLCA2; Synonyms=CACC3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
GLYCOSYLATION, AND MUTAGENESIS OF ASN-150; ASN-292; ASN-522; ASN-637;
ASN-822 AND ASN-938.
TISSUE=Lung;
PubMed=10362588;
Gruber A.D., Schreur K.D., Ji H.-L., Fuller C.M., Pauli B.U.;
"Molecular cloning and transmembrane structure of hCLCA2 from human
lung, trachea, and mammary gland.";
Am. J. Physiol. 276:C1261-C1270(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=10437792; DOI=10.1016/S0014-5793(99)00891-1;
Agnel M., Vermat T., Culouscou J.-M.;
"Identification of three novel members of the calcium-dependent
chloride channel (CaCC) family predominantly expressed in the
digestive tract and trachea.";
FEBS Lett. 455:295-301(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Corneal epithelium;
PubMed=11262615; DOI=10.1076/ceyr.21.6.918.6983;
Itoh R., Kawamoto S., Miyamoto Y., Kinoshita S., Okubo K.;
"Isolation and characterization of a Ca(2+)-activated chloride channel
from human corneal epithelium.";
Curr. Eye Res. 21:918-925(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INDUCTION, TISSUE SPECIFICITY, AND FUNCTION.
PubMed=10554024;
Gruber A.D., Pauli B.U.;
"Tumorigenicity of human breast cancer is associated with loss of the
Ca2+-activated chloride channel CLCA2.";
Cancer Res. 59:5488-5491(1999).
[8]
INDUCTION, AND FUNCTION.
PubMed=11445004; DOI=10.1089/10445490152122442;
Bustin S.A., Li S.-R., Dorudi S.;
"Expression of the Ca2+-activated chloride channel genes CLCA1 and
CLCA2 is downregulated in human colorectal cancer.";
DNA Cell Biol. 20:331-338(2001).
[9]
TISSUE SPECIFICITY, AND FUNCTION.
PubMed=11320086; DOI=10.1074/jbc.M100478200;
Abdel-Ghany M., Cheng H.-C., Elble R.C., Pauli B.U.;
"The breast cancer beta 4 integrin and endothelial human CLCA2 mediate
lung metastasis.";
J. Biol. Chem. 276:25438-25446(2001).
[10]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=14966209; DOI=10.1177/002215540405200313;
Connon C.J., Yamasaki K., Kawasaki S., Quantock A.J., Koizumi N.,
Kinoshita S.;
"Calcium-activated chloride channel-2 in human epithelia.";
J. Histochem. Cytochem. 52:415-418(2004).
[11]
SUBCELLULAR LOCATION, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15707651; DOI=10.1016/j.acthis.2004.08.003;
Connon C.J., Kawasaki S., Yamasaki K., Quantock A.J., Kinoshita S.;
"The quantification of hCLCA2 and colocalisation with integrin beta4
in stratified human epithelia.";
Acta Histochem. 106:421-425(2005).
[12]
TISSUE SPECIFICITY, AND FUNCTION.
PubMed=16158324; DOI=10.1007/s00441-005-0059-2;
Connon C.J., Kawasaki S., Liles M., Koizumi N., Yamasaki K.,
Nakamura T., Quantock A.J., Kinoshita S.;
"Gene expression and immunolocalisation of a calcium-activated
chloride channel during the stratification of cultivated and
developing corneal epithelium.";
Cell Tissue Res. 323:177-182(2006).
[13]
SUBCELLULAR LOCATION, SHEDDING, GLYCOSYLATION, AND TOPOLOGY.
PubMed=16873362; DOI=10.1074/jbc.M605919200;
Elble R.C., Walia V., Cheng H.-C., Connon C.J., Mundhenk L.,
Gruber A.D., Pauli B.U.;
"The putative chloride channel hCLCA2 has a single C-terminal
transmembrane segment.";
J. Biol. Chem. 281:29448-29454(2006).
[14]
VARIANT [LARGE SCALE ANALYSIS] GLU-754.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Plays a role in modulating chloride current across the
plasma membrane in a calcium-dependent manner, and cell adhesion.
Involved in basal cell adhesion and/or stratification of squamous
epithelia. May act as a tumor suppressor in breast and colorectal
cancer. Plays a key role for cell adhesion in the beginning stages
of lung metastasis via the binding to ITGB4.
{ECO:0000269|PubMed:10554024, ECO:0000269|PubMed:11320086,
ECO:0000269|PubMed:11445004, ECO:0000269|PubMed:15707651,
ECO:0000269|PubMed:16158324}.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Basal cell membrane; Single-pass type I membrane protein.
Cell junction.
-!- SUBCELLULAR LOCATION: Calcium-activated chloride channel regulator
2, 109 kDa form: Secreted. Note=Remains associated to the 35 kDa
form until an unidentified event triggers the release.
-!- TISSUE SPECIFICITY: Expressed in cornea, skin, vagina, esophagus,
and larynx (at protein level). Expressed in trachea and mammary
gland. Weakly expressed in testis and kidney. Highly expressed in
corneal epithelium, colon and trachea. Moderately expressed in
brain, urogenital organs, bladder, uterus and prostate. Highly
expressed in tissues containing stratified epithelium including
cornea, esophagus, larynx, skin and vagina than those tissues
which contain only epithelial monolayers. Expressed in normal
breast epithelium but not in breast cancer. Highly expressed
during epithelial stratification. Expressed in endothelial cells
of lung. Expressed selectively in endothelia of small pulmonary
arteries, arterioles, and subpleural and interlobular venules.
{ECO:0000269|PubMed:10362588, ECO:0000269|PubMed:10437792,
ECO:0000269|PubMed:10554024, ECO:0000269|PubMed:11262615,
ECO:0000269|PubMed:11320086, ECO:0000269|PubMed:14966209,
ECO:0000269|PubMed:15707651, ECO:0000269|PubMed:16158324}.
-!- INDUCTION: Significantly down-regulated in breast and colorectal
cancer. {ECO:0000269|PubMed:10554024,
ECO:0000269|PubMed:11445004}.
-!- DOMAIN: The metalloprotease region is responsible for
autoproteolytic processing. It can also cross-cleave other CLCA
substrates. {ECO:0000250|UniProtKB:A8K7I4}.
-!- PTM: The 141 kDa mature form is autoproteolytically cleaved by the
metalloprotease domain, producing a 109 kDa form and a 35 kDa
form. The cleavage is necessary for calcium-activated chloride
channel (CaCC) activation activity.
{ECO:0000250|UniProtKB:A8K7I4}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:10362588,
ECO:0000269|PubMed:16873362}.
-!- SIMILARITY: Belongs to the CLCR family. {ECO:0000305}.
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EMBL; AF043977; AAD40367.1; -; mRNA.
EMBL; AF127980; AAD48397.1; -; mRNA.
EMBL; AB026833; BAA77810.1; -; mRNA.
EMBL; AK290348; BAF83037.1; -; mRNA.
EMBL; CH471097; EAW73187.1; -; Genomic_DNA.
EMBL; BC041096; AAH41096.1; -; mRNA.
CCDS; CCDS708.1; -.
RefSeq; NP_006527.1; NM_006536.6.
UniGene; Hs.241551; -.
ProteinModelPortal; Q9UQC9; -.
BioGrid; 114994; 3.
IntAct; Q9UQC9; 1.
STRING; 9606.ENSP00000359596; -.
ChEMBL; CHEMBL2364708; -.
MEROPS; M87.003; -.
iPTMnet; Q9UQC9; -.
PhosphoSitePlus; Q9UQC9; -.
BioMuta; CLCA2; -.
DMDM; 189082520; -.
EPD; Q9UQC9; -.
PaxDb; Q9UQC9; -.
PeptideAtlas; Q9UQC9; -.
PRIDE; Q9UQC9; -.
ProteomicsDB; 85543; -.
Ensembl; ENST00000370565; ENSP00000359596; ENSG00000137975.
GeneID; 9635; -.
KEGG; hsa:9635; -.
UCSC; uc001dlr.5; human.
CTD; 9635; -.
DisGeNET; 9635; -.
EuPathDB; HostDB:ENSG00000137975.7; -.
GeneCards; CLCA2; -.
HGNC; HGNC:2016; CLCA2.
HPA; HPA047192; -.
MIM; 604003; gene.
neXtProt; NX_Q9UQC9; -.
OpenTargets; ENSG00000137975; -.
PharmGKB; PA26543; -.
eggNOG; ENOG410IEPS; Eukaryota.
eggNOG; ENOG410XPSZ; LUCA.
GeneTree; ENSGT00390000004810; -.
HOGENOM; HOG000015107; -.
HOVERGEN; HBG005560; -.
InParanoid; Q9UQC9; -.
KO; K05028; -.
OMA; NIQMNAP; -.
OrthoDB; EOG091G09E6; -.
PhylomeDB; Q9UQC9; -.
TreeFam; TF328396; -.
Reactome; R-HSA-2672351; Stimuli-sensing channels.
ChiTaRS; CLCA2; human.
GeneWiki; CLCA2; -.
GenomeRNAi; 9635; -.
PRO; PR:Q9UQC9; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000137975; -.
CleanEx; HS_CLCA2; -.
Genevisible; Q9UQC9; HS.
GO; GO:0009925; C:basal plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0005254; F:chloride channel activity; TAS:ProtInc.
GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IBA:GO_Central.
GO; GO:0015276; F:ligand-gated ion channel activity; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; TAS:Reactome.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR004727; CLCA_chordata.
InterPro; IPR013642; CLCA_N.
InterPro; IPR002035; VWF_A.
InterPro; IPR036465; vWFA_dom_sf.
Pfam; PF08434; CLCA; 1.
SMART; SM00327; VWA; 1.
SUPFAM; SSF53300; SSF53300; 1.
TIGRFAMs; TIGR00868; hCaCC; 1.
PROSITE; PS50234; VWFA; 1.
1: Evidence at protein level;
Autocatalytic cleavage; Calcium; Cell adhesion; Cell junction;
Cell membrane; Chloride; Complete proteome; Glycoprotein; Hydrolase;
Ion transport; Membrane; Metal-binding; Metalloprotease; Polymorphism;
Protease; Reference proteome; Secreted; Signal; Transmembrane;
Transmembrane helix; Transport; Zinc.
SIGNAL 1 31 {ECO:0000255}.
CHAIN 32 943 Calcium-activated chloride channel
regulator 2.
/FTId=PRO_0000333694.
CHAIN 33 ? Calcium-activated chloride channel
regulator 2, 109 kDa form.
/FTId=PRO_0000333695.
CHAIN ? 943 Calcium-activated chloride channel
regulator 2, 35 kDa form.
/FTId=PRO_0000344502.
TOPO_DOM 32 901 Extracellular. {ECO:0000255}.
TRANSMEM 902 922 Helical. {ECO:0000255}.
TOPO_DOM 923 943 Cytoplasmic. {ECO:0000255}.
DOMAIN 311 483 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
REGION 54 205 Metalloprotease domain.
{ECO:0000250|UniProtKB:A8K7I4}.
ACT_SITE 165 165 {ECO:0000250|UniProtKB:A8K7I4}.
METAL 164 164 Zinc; catalytic.
{ECO:0000250|UniProtKB:A8K7I4}.
METAL 168 168 Zinc; catalytic.
{ECO:0000250|UniProtKB:A8K7I4}.
METAL 175 175 Zinc; catalytic.
{ECO:0000250|UniProtKB:A8K7I4}.
SITE 708 709 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:A8K7I4}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 150 150 N-linked (GlcNAc...) asparagine.
CARBOHYD 231 231 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 522 522 N-linked (GlcNAc...) asparagine.
CARBOHYD 822 822 N-linked (GlcNAc...) asparagine.
VARIANT 80 80 V -> I (in dbSNP:rs11580625).
/FTId=VAR_054057.
VARIANT 306 306 Q -> E (in dbSNP:rs17409304).
/FTId=VAR_043148.
VARIANT 534 534 G -> D (in dbSNP:rs1413426).
/FTId=VAR_054058.
VARIANT 754 754 G -> E (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_043149.
MUTAGEN 150 150 N->Q: Reduction in size by around 2 kDa.
{ECO:0000269|PubMed:10362588}.
MUTAGEN 292 292 N->Q: No change in size.
{ECO:0000269|PubMed:10362588}.
MUTAGEN 522 522 N->Q: Reduction in size by around 2 kDa.
{ECO:0000269|PubMed:10362588}.
MUTAGEN 637 637 N->Q: No change in size.
{ECO:0000269|PubMed:10362588}.
MUTAGEN 822 822 N->Q: Reduction in size by around 2 kDa.
{ECO:0000269|PubMed:10362588}.
MUTAGEN 938 938 N->Q: No change in size.
{ECO:0000269|PubMed:10362588}.
CONFLICT 178 178 N -> I (in Ref. 3; BAA77810).
{ECO:0000305}.
CONFLICT 830 830 Q -> R (in Ref. 4; BAF83037).
{ECO:0000305}.
SEQUENCE 943 AA; 103941 MW; 0E09A09090D2529B CRC64;
MTQRSIAGPI CNLKFVTLLV ALSSELPFLG AGVQLQDNGY NGLLIAINPQ VPENQNLISN
IKEMITEASF YLFNATKRRV FFRNIKILIP ATWKANNNSK IKQESYEKAN VIVTDWYGAH
GDDPYTLQYR GCGKEGKYIH FTPNFLLNDN LTAGYGSRGR VFVHEWAHLR WGVFDEYNND
KPFYINGQNQ IKVTRCSSDI TGIFVCEKGP CPQENCIISK LFKEGCTFIY NSTQNATASI
MFMQSLSSVV EFCNASTHNQ EAPNLQNQMC SLRSAWDVIT DSADFHHSFP MNGTELPPPP
TFSLVQAGDK VVCLVLDVSS KMAEADRLLQ LQQAAEFYLM QIVEIHTFVG IASFDSKGEI
RAQLHQINSN DDRKLLVSYL PTTVSAKTDI SICSGLKKGF EVVEKLNGKA YGSVMILVTS
GDDKLLGNCL PTVLSSGSTI HSIALGSSAA PNLEELSRLT GGLKFFVPDI SNSNSMIDAF
SRISSGTGDI FQQHIQLEST GENVKPHHQL KNTVTVDNTV GNDTMFLVTW QASGPPEIIL
FDPDGRKYYT NNFITNLTFR TASLWIPGTA KPGHWTYTLN NTHHSLQALK VTVTSRASNS
AVPPATVEAF VERDSLHFPH PVMIYANVKQ GFYPILNATV TATVEPETGD PVTLRLLDDG
AGADVIKNDG IYSRYFFSFA ANGRYSLKVH VNHSPSISTP AHSIPGSHAM YVPGYTANGN
IQMNAPRKSV GRNEEERKWG FSRVSSGGSF SVLGVPAGPH PDVFPPCKII DLEAVKVEEE
LTLSWTAPGE DFDQGQATSY EIRMSKSLQN IQDDFNNAIL VNTSKRNPQQ AGIREIFTFS
PQISTNGPEH QPNGETHESH RIYVAIRAMD RNSLQSAVSN IAQAPLFIPP NSDPVPARDY
LILKGVLTAM GLIGIICLII VVTHHTLSRK KRADKKENGT KLL


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