ID   CLCA2_HUMAN             Reviewed;         943 AA.
AC   Q9UQC9; A8K2T3; Q9Y6N2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Calcium-activated chloride channel regulator 2;
DE            EC=3.4.-.- {ECO:0000250|UniProtKB:A8K7I4};
DE   AltName: Full=Calcium-activated chloride channel family member 2;
DE            Short=hCLCA2;
DE   AltName: Full=Calcium-activated chloride channel protein 3;
DE            Short=CaCC-3;
DE            Short=hCaCC-3;
DE   Contains:
DE     RecName: Full=Calcium-activated chloride channel regulator 2, 109 kDa form;
DE   Contains:
DE     RecName: Full=Calcium-activated chloride channel regulator 2, 35 kDa form;
DE   Flags: Precursor;
GN   Name=CLCA2; Synonyms=CACC3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   GLYCOSYLATION, AND MUTAGENESIS OF ASN-150; ASN-292; ASN-522; ASN-637;
RP   ASN-822 AND ASN-938.
RC   TISSUE=Lung;
RX   PubMed=10362588; DOI=10.1152/ajpcell.1999.276.6.c1261;
RA   Gruber A.D., Schreur K.D., Ji H.-L., Fuller C.M., Pauli B.U.;
RT   "Molecular cloning and transmembrane structure of hCLCA2 from human lung,
RT   trachea, and mammary gland.";
RL   Am. J. Physiol. 276:C1261-C1270(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=10437792; DOI=10.1016/s0014-5793(99)00891-1;
RA   Agnel M., Vermat T., Culouscou J.-M.;
RT   "Identification of three novel members of the calcium-dependent chloride
RT   channel (CaCC) family predominantly expressed in the digestive tract and
RT   trachea.";
RL   FEBS Lett. 455:295-301(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Corneal epithelium;
RX   PubMed=11262615; DOI=10.1076/ceyr.21.6.918.6983;
RA   Itoh R., Kawamoto S., Miyamoto Y., Kinoshita S., Okubo K.;
RT   "Isolation and characterization of a Ca(2+)-activated chloride channel from
RT   human corneal epithelium.";
RL   Curr. Eye Res. 21:918-925(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tongue;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   INDUCTION, TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=10554024;
RA   Gruber A.D., Pauli B.U.;
RT   "Tumorigenicity of human breast cancer is associated with loss of the Ca2+-
RT   activated chloride channel CLCA2.";
RL   Cancer Res. 59:5488-5491(1999).
RN   [8]
RP   INDUCTION, AND FUNCTION.
RX   PubMed=11445004; DOI=10.1089/10445490152122442;
RA   Bustin S.A., Li S.-R., Dorudi S.;
RT   "Expression of the Ca2+-activated chloride channel genes CLCA1 and CLCA2 is
RT   downregulated in human colorectal cancer.";
RL   DNA Cell Biol. 20:331-338(2001).
RN   [9]
RP   TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=11320086; DOI=10.1074/jbc.m100478200;
RA   Abdel-Ghany M., Cheng H.-C., Elble R.C., Pauli B.U.;
RT   "The breast cancer beta 4 integrin and endothelial human CLCA2 mediate lung
RT   metastasis.";
RL   J. Biol. Chem. 276:25438-25446(2001).
RN   [10]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=14966209; DOI=10.1177/002215540405200313;
RA   Connon C.J., Yamasaki K., Kawasaki S., Quantock A.J., Koizumi N.,
RA   Kinoshita S.;
RT   "Calcium-activated chloride channel-2 in human epithelia.";
RL   J. Histochem. Cytochem. 52:415-418(2004).
RN   [11]
RP   SUBCELLULAR LOCATION, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=15707651; DOI=10.1016/j.acthis.2004.08.003;
RA   Connon C.J., Kawasaki S., Yamasaki K., Quantock A.J., Kinoshita S.;
RT   "The quantification of hCLCA2 and colocalisation with integrin beta4 in
RT   stratified human epithelia.";
RL   Acta Histochem. 106:421-425(2005).
RN   [12]
RP   TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=16158324; DOI=10.1007/s00441-005-0059-2;
RA   Connon C.J., Kawasaki S., Liles M., Koizumi N., Yamasaki K., Nakamura T.,
RA   Quantock A.J., Kinoshita S.;
RT   "Gene expression and immunolocalisation of a calcium-activated chloride
RT   channel during the stratification of cultivated and developing corneal
RT   epithelium.";
RL   Cell Tissue Res. 323:177-182(2006).
RN   [13]
RP   SUBCELLULAR LOCATION, SHEDDING, GLYCOSYLATION, AND TOPOLOGY.
RX   PubMed=16873362; DOI=10.1074/jbc.m605919200;
RA   Elble R.C., Walia V., Cheng H.-C., Connon C.J., Mundhenk L., Gruber A.D.,
RA   Pauli B.U.;
RT   "The putative chloride channel hCLCA2 has a single C-terminal transmembrane
RT   segment.";
RL   J. Biol. Chem. 281:29448-29454(2006).
RN   [14]
RP   VARIANT [LARGE SCALE ANALYSIS] GLU-754.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Plays a role in modulating chloride current across the plasma
CC       membrane in a calcium-dependent manner, and cell adhesion. Involved in
CC       basal cell adhesion and/or stratification of squamous epithelia. May
CC       act as a tumor suppressor in breast and colorectal cancer. Plays a key
CC       role for cell adhesion in the beginning stages of lung metastasis via
CC       the binding to ITGB4. {ECO:0000269|PubMed:10554024,
CC       ECO:0000269|PubMed:11320086, ECO:0000269|PubMed:11445004,
CC       ECO:0000269|PubMed:15707651, ECO:0000269|PubMed:16158324}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Basal cell membrane; Single-pass type I membrane protein. Cell
CC       junction.
CC   -!- SUBCELLULAR LOCATION: [Calcium-activated chloride channel regulator 2,
CC       109 kDa form]: Secreted. Note=Remains associated to the 35 kDa form
CC       until an unidentified event triggers the release.
CC   -!- TISSUE SPECIFICITY: Expressed in cornea, skin, vagina, esophagus, and
CC       larynx (at protein level). Expressed in trachea and mammary gland.
CC       Weakly expressed in testis and kidney. Highly expressed in corneal
CC       epithelium, colon and trachea. Moderately expressed in brain,
CC       urogenital organs, bladder, uterus and prostate. Highly expressed in
CC       tissues containing stratified epithelium including cornea, esophagus,
CC       larynx, skin and vagina than those tissues which contain only
CC       epithelial monolayers. Expressed in normal breast epithelium but not in
CC       breast cancer. Highly expressed during epithelial stratification.
CC       Expressed in endothelial cells of lung. Expressed selectively in
CC       endothelia of small pulmonary arteries, arterioles, and subpleural and
CC       interlobular venules. {ECO:0000269|PubMed:10362588,
CC       ECO:0000269|PubMed:10437792, ECO:0000269|PubMed:10554024,
CC       ECO:0000269|PubMed:11262615, ECO:0000269|PubMed:11320086,
CC       ECO:0000269|PubMed:14966209, ECO:0000269|PubMed:15707651,
CC       ECO:0000269|PubMed:16158324}.
CC   -!- INDUCTION: Significantly down-regulated in breast and colorectal
CC       cancer. {ECO:0000269|PubMed:10554024, ECO:0000269|PubMed:11445004}.
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: The 141 kDa mature form is autoproteolytically cleaved by the
CC       metalloprotease domain, producing a 109 kDa form and a 35 kDa form. The
CC       cleavage is necessary for calcium-activated chloride channel (CaCC)
CC       activation activity. {ECO:0000250|UniProtKB:A8K7I4}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10362588,
CC       ECO:0000269|PubMed:16873362}.
CC   -!- SIMILARITY: Belongs to the CLCR family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF043977; AAD40367.1; -; mRNA.
DR   EMBL; AF127980; AAD48397.1; -; mRNA.
DR   EMBL; AB026833; BAA77810.1; -; mRNA.
DR   EMBL; AK290348; BAF83037.1; -; mRNA.
DR   EMBL; CH471097; EAW73187.1; -; Genomic_DNA.
DR   EMBL; BC041096; AAH41096.1; -; mRNA.
DR   CCDS; CCDS708.1; -.
DR   RefSeq; NP_006527.1; NM_006536.6.
DR   AlphaFoldDB; Q9UQC9; -.
DR   SMR; Q9UQC9; -.
DR   BioGRID; 114994; 5.
DR   IntAct; Q9UQC9; 3.
DR   STRING; 9606.ENSP00000359596; -.
DR   ChEMBL; CHEMBL2364708; -.
DR   MEROPS; M87.003; -.
DR   TCDB; 1.A.13.1.10; the epithelial chloride channel (e-clc) family.
DR   GlyConnect; 1057; 13 N-Linked glycans (3 sites).
DR   GlyCosmos; Q9UQC9; 8 sites, 13 glycans.
DR   GlyGen; Q9UQC9; 10 sites, 12 N-linked glycans (3 sites), 1 O-linked glycan (2 sites).
DR   iPTMnet; Q9UQC9; -.
DR   PhosphoSitePlus; Q9UQC9; -.
DR   BioMuta; CLCA2; -.
DR   DMDM; 189082520; -.
DR   EPD; Q9UQC9; -.
DR   jPOST; Q9UQC9; -.
DR   MassIVE; Q9UQC9; -.
DR   PaxDb; 9606-ENSP00000359596; -.
DR   PeptideAtlas; Q9UQC9; -.
DR   ProteomicsDB; 85543; -.
DR   Antibodypedia; 33584; 96 antibodies from 21 providers.
DR   DNASU; 9635; -.
DR   Ensembl; ENST00000370565.5; ENSP00000359596.4; ENSG00000137975.8.
DR   GeneID; 9635; -.
DR   KEGG; hsa:9635; -.
DR   MANE-Select; ENST00000370565.5; ENSP00000359596.4; NM_006536.7; NP_006527.1.
DR   UCSC; uc001dlr.5; human.
DR   AGR; HGNC:2016; -.
DR   CTD; 9635; -.
DR   DisGeNET; 9635; -.
DR   GeneCards; CLCA2; -.
DR   HGNC; HGNC:2016; CLCA2.
DR   HPA; ENSG00000137975; Tissue enhanced (esophagus, skin, vagina).
DR   MIM; 604003; gene.
DR   neXtProt; NX_Q9UQC9; -.
DR   OpenTargets; ENSG00000137975; -.
DR   PharmGKB; PA26543; -.
DR   VEuPathDB; HostDB:ENSG00000137975; -.
DR   eggNOG; ENOG502RIMV; Eukaryota.
DR   GeneTree; ENSGT00940000161548; -.
DR   HOGENOM; CLU_005812_0_1_1; -.
DR   InParanoid; Q9UQC9; -.
DR   OMA; GPICNLK; -.
DR   OrthoDB; 5479609at2759; -.
DR   PhylomeDB; Q9UQC9; -.
DR   TreeFam; TF328396; -.
DR   PathwayCommons; Q9UQC9; -.
DR   Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR   SignaLink; Q9UQC9; -.
DR   BioGRID-ORCS; 9635; 10 hits in 1159 CRISPR screens.
DR   ChiTaRS; CLCA2; human.
DR   GeneWiki; CLCA2; -.
DR   GenomeRNAi; 9635; -.
DR   Pharos; Q9UQC9; Tbio.
DR   PRO; PR:Q9UQC9; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9UQC9; Protein.
DR   Bgee; ENSG00000137975; Expressed in gingival epithelium and 115 other cell types or tissues.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0009925; C:basal plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030054; C:cell junction; IDA:HPA.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0005254; F:chloride channel activity; TAS:ProtInc.
DR   GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IBA:GO_Central.
DR   GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; TAS:Reactome.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0034220; P:monoatomic ion transmembrane transport; TAS:Reactome.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00198; vWFA; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR004727; CLCA_chordata.
DR   InterPro; IPR013642; CLCA_N.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   NCBIfam; NF041940; choice_anch_X; 1.
DR   NCBIfam; TIGR00868; hCaCC; 1.
DR   PANTHER; PTHR10579; CALCIUM-ACTIVATED CHLORIDE CHANNEL REGULATOR; 1.
DR   PANTHER; PTHR10579:SF66; CALCIUM-ACTIVATED CHLORIDE CHANNEL REGULATOR 2; 1.
DR   Pfam; PF08434; CLCA; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50234; VWFA; 1.
DR   Genevisible; Q9UQC9; HS.
PE   1: Evidence at protein level;
KW   Autocatalytic cleavage; Calcium; Cell adhesion; Cell junction;
KW   Cell membrane; Chloride; Glycoprotein; Hydrolase; Ion transport; Membrane;
KW   Metal-binding; Metalloprotease; Protease; Reference proteome; Secreted;
KW   Signal; Transmembrane; Transmembrane helix; Transport; Zinc.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..943
FT                   /note="Calcium-activated chloride channel regulator 2"
FT                   /id="PRO_0000333694"
FT   CHAIN           33..?
FT                   /note="Calcium-activated chloride channel regulator 2, 109
FT                   kDa form"
FT                   /id="PRO_0000333695"
FT   CHAIN           ?..943
FT                   /note="Calcium-activated chloride channel regulator 2, 35
FT                   kDa form"
FT                   /id="PRO_0000344502"
FT   TOPO_DOM        32..901
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        902..922
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        923..943
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          311..483
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   REGION          54..205
FT                   /note="Metalloprotease domain"
FT                   /evidence="ECO:0000250|UniProtKB:A8K7I4"
FT   ACT_SITE        165
FT                   /evidence="ECO:0000250|UniProtKB:A8K7I4"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:A8K7I4"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:A8K7I4"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:A8K7I4"
FT   SITE            708..709
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:A8K7I4"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        150
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        522
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        822
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   VARIANT         80
FT                   /note="V -> I (in dbSNP:rs11580625)"
FT                   /id="VAR_054057"
FT   VARIANT         306
FT                   /note="Q -> E (in dbSNP:rs17409304)"
FT                   /id="VAR_043148"
FT   VARIANT         534
FT                   /note="G -> D (in dbSNP:rs1413426)"
FT                   /id="VAR_054058"
FT   VARIANT         754
FT                   /note="G -> E (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_043149"
FT   MUTAGEN         150
FT                   /note="N->Q: Reduction in size by around 2 kDa."
FT                   /evidence="ECO:0000269|PubMed:10362588"
FT   MUTAGEN         292
FT                   /note="N->Q: No change in size."
FT                   /evidence="ECO:0000269|PubMed:10362588"
FT   MUTAGEN         522
FT                   /note="N->Q: Reduction in size by around 2 kDa."
FT                   /evidence="ECO:0000269|PubMed:10362588"
FT   MUTAGEN         637
FT                   /note="N->Q: No change in size."
FT                   /evidence="ECO:0000269|PubMed:10362588"
FT   MUTAGEN         822
FT                   /note="N->Q: Reduction in size by around 2 kDa."
FT                   /evidence="ECO:0000269|PubMed:10362588"
FT   MUTAGEN         938
FT                   /note="N->Q: No change in size."
FT                   /evidence="ECO:0000269|PubMed:10362588"
FT   CONFLICT        178
FT                   /note="N -> I (in Ref. 3; BAA77810)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        830
FT                   /note="Q -> R (in Ref. 4; BAF83037)"
FT                   /evidence="ECO:0000305"
SQ   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
//