CLCA2_HUMAN
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 03-AUG-2022, entry version 154.
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}.
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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 GlyConnect; 1057; 13 N-Linked glycans (3 sites).
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; Q9UQC9; -.
DR PeptideAtlas; Q9UQC9; -.
DR PRIDE; Q9UQC9; -.
DR ProteomicsDB; 85543; -.
DR Antibodypedia; 33584; 91 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 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; TREIFTF; -.
DR OrthoDB; 685640at2759; -.
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 1077 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 113 other tissues.
DR Genevisible; Q9UQC9; HS.
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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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 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:ion transmembrane transport; TAS:Reactome.
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 SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR TIGRFAMs; TIGR00868; hCaCC; 1.
DR PROSITE; PS50234; VWFA; 1.
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
