CLCA4_HUMAN
ID CLCA4_HUMAN Reviewed; 919 AA.
AC Q14CN2; A8MQC9; B7Z1Q5; Q6UX81; Q9UNF7;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Calcium-activated chloride channel regulator 4;
DE EC=3.4.-.- {ECO:0000250|UniProtKB:A8K7I4};
DE AltName: Full=Calcium-activated chloride channel family member 4;
DE Short=hCLCA4;
DE AltName: Full=Calcium-activated chloride channel protein 2;
DE Short=CaCC-2;
DE Short=hCaCC-2;
DE AltName: Full=Chloride channel accessory 4;
DE Contains:
DE RecName: Full=Calcium-activated chloride channel regulator 4, 110 kDa form;
DE Contains:
DE RecName: Full=Calcium-activated chloride channel regulator 4, 30 kDa form;
DE Flags: Precursor;
GN Name=CLCA4; Synonyms=CaCC2; ORFNames=UNQ562/PRO1124;
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] (ISOFORM 1), VARIANT 877-PRO-THR-878 DEL, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Colon;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS LEU-810
RP AND 877-PRO-THR-878 DEL.
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=15490240; DOI=10.1007/s00439-004-1190-y;
RA Ritzka M., Stanke F., Jansen S., Gruber A.D., Pusch L., Woelfl S.,
RA Veeze H.J., Halley D.J., Tummler B.;
RT "The CLCA gene locus as a modulator of the gastrointestinal basic defect in
RT cystic fibrosis.";
RL Hum. Genet. 115:483-491(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=16012037; DOI=10.1080/00016480510028519;
RA Lee S.H., Park J.H., Jung H.H., Lee S.H., Oh J.W., Lee H.M., Jun H.S.,
RA Cho W.J., Lee J.Y.;
RT "Expression and distribution of ion transport mRNAs in human nasal mucosa
RT and nasal polyps.";
RL Acta Oto-Laryngol. 125:745-752(2005).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-811.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [9]
RP INDUCTION.
RX PubMed=18254958; DOI=10.1186/1471-2164-9-69;
RA Ye H., Yu T., Temam S., Ziober B.L., Wang J., Schwartz J.L., Mao L.,
RA Wong D.T., Zhou X.;
RT "Transcriptomic dissection of tongue squamous cell carcinoma.";
RL BMC Genomics 9:69-69(2008).
CC -!- FUNCTION: May be involved in mediating calcium-activated chloride
CC conductance.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}. Apical cell membrane {ECO:0000250}. Secreted
CC {ECO:0000250}. Note=The C-terminus 30 kDa form is anchored to the
CC membrane. The N-terminus 110 kDa form is released from the membrane
CC triggered by an unknown stimulus. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14CN2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14CN2-2; Sequence=VSP_056117, VSP_056118, VSP_056119;
CC -!- TISSUE SPECIFICITY: Primarily expressed in the digestive tract, mainly
CC in colon. Detected in smaller amounts in brain, urogenital organs,
CC testis, and salivary and mammary glands. Highly expressed in the
CC epithelial layer and submucosal gland of the inferior turbinate mucosa.
CC Lower levels in the epithelial layer of nasal polyp.
CC {ECO:0000269|PubMed:10437792, ECO:0000269|PubMed:15490240,
CC ECO:0000269|PubMed:16012037}.
CC -!- INDUCTION: Down-regulated in oral tongue squamous cell carcinomas.
CC {ECO:0000269|PubMed:18254958}.
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 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}.
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; AF127035; AAD48398.1; -; mRNA.
DR EMBL; AY358470; AAQ88834.1; -; mRNA.
DR EMBL; AK293766; BAH11591.1; -; mRNA.
DR EMBL; AL122002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC113687; AAI13688.1; -; mRNA.
DR EMBL; BC113689; AAI13690.1; -; mRNA.
DR CCDS; CCDS41355.1; -. [Q14CN2-1]
DR RefSeq; NP_036260.2; NM_012128.3. [Q14CN2-1]
DR AlphaFoldDB; Q14CN2; -.
DR SMR; Q14CN2; -.
DR BioGRID; 116482; 26.
DR IntAct; Q14CN2; 1.
DR MINT; Q14CN2; -.
DR STRING; 9606.ENSP00000359594; -.
DR ChEMBL; CHEMBL2364708; -.
DR MEROPS; M87.002; -.
DR TCDB; 1.A.13.1.2; the epithelial chloride channel (e-clc) family.
DR GlyGen; Q14CN2; 10 sites.
DR iPTMnet; Q14CN2; -.
DR PhosphoSitePlus; Q14CN2; -.
DR BioMuta; CLCA4; -.
DR DMDM; 205831469; -.
DR jPOST; Q14CN2; -.
DR MassIVE; Q14CN2; -.
DR PaxDb; Q14CN2; -.
DR PeptideAtlas; Q14CN2; -.
DR PRIDE; Q14CN2; -.
DR ProteomicsDB; 1948; -.
DR ProteomicsDB; 60328; -. [Q14CN2-1]
DR Antibodypedia; 2241; 71 antibodies from 14 providers.
DR DNASU; 22802; -.
DR Ensembl; ENST00000370563.3; ENSP00000359594.3; ENSG00000016602.9. [Q14CN2-1]
DR GeneID; 22802; -.
DR KEGG; hsa:22802; -.
DR MANE-Select; ENST00000370563.3; ENSP00000359594.3; NM_012128.4; NP_036260.2.
DR UCSC; uc009wcs.4; human. [Q14CN2-1]
DR CTD; 22802; -.
DR DisGeNET; 22802; -.
DR GeneCards; CLCA4; -.
DR HGNC; HGNC:2018; CLCA4.
DR HPA; ENSG00000016602; Tissue enhanced (esophagus, intestine).
DR MalaCards; CLCA4; -.
DR MIM; 616857; gene.
DR neXtProt; NX_Q14CN2; -.
DR OpenTargets; ENSG00000016602; -.
DR Orphanet; 586; Cystic fibrosis.
DR PharmGKB; PA26545; -.
DR VEuPathDB; HostDB:ENSG00000016602; -.
DR eggNOG; ENOG502QRRD; Eukaryota.
DR GeneTree; ENSGT00940000160416; -.
DR HOGENOM; CLU_005812_0_1_1; -.
DR InParanoid; Q14CN2; -.
DR OMA; TRTCRID; -.
DR OrthoDB; 685640at2759; -.
DR PhylomeDB; Q14CN2; -.
DR TreeFam; TF328396; -.
DR PathwayCommons; Q14CN2; -.
DR Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR SignaLink; Q14CN2; -.
DR BioGRID-ORCS; 22802; 9 hits in 1064 CRISPR screens.
DR ChiTaRS; CLCA4; human.
DR GeneWiki; CLCA4; -.
DR GenomeRNAi; 22802; -.
DR Pharos; Q14CN2; Tbio.
DR PRO; PR:Q14CN2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q14CN2; protein.
DR Bgee; ENSG00000016602; Expressed in lower esophagus mucosa and 141 other tissues.
DR Genevisible; Q14CN2; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
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:0005886; C:plasma membrane; TAS:Reactome.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; TAS:Reactome.
DR GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR004727; CLCA_chordata.
DR InterPro; IPR013642; CLCA_N.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF08434; CLCA; 1.
DR Pfam; PF00092; VWA; 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 Alternative splicing; Autocatalytic cleavage; Cell membrane; Chloride;
KW Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Secreted; Signal; Transmembrane;
KW Transmembrane helix; Transport; Zinc.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..919
FT /note="Calcium-activated chloride channel regulator 4"
FT /id="PRO_0000345389"
FT CHAIN 22..?
FT /note="Calcium-activated chloride channel regulator 4, 110
FT kDa form"
FT /id="PRO_0000345390"
FT CHAIN ?..919
FT /note="Calcium-activated chloride channel regulator 4, 30
FT kDa form"
FT /id="PRO_0000345391"
FT TRANSMEM 895..915
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 306..476
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 45..199
FT /note="Metalloprotease domain"
FT /evidence="ECO:0000250|UniProtKB:A8K7I4"
FT REGION 870..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 156
FT /evidence="ECO:0000250|UniProtKB:A8K7I4"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:A8K7I4"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:A8K7I4"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:A8K7I4"
FT SITE 697..698
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:A8K7I4"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 811
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16740002"
FT CARBOHYD 832
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 837
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 852
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..287
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056117"
FT VAR_SEQ 490..524
FT /note="LESKGLTLNSNAWMNDTVIIDSTVGKDTFFLITWN -> VRVLIPWVFMFTF
FT ATRKNHLVVISFEFHIFLKVNF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056118"
FT VAR_SEQ 525..919
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056119"
FT VARIANT 43
FT /note="P -> S (in dbSNP:rs2231580)"
FT /id="VAR_045816"
FT VARIANT 443
FT /note="D -> V (in dbSNP:rs2839932)"
FT /id="VAR_045817"
FT VARIANT 449
FT /note="M -> L (in dbSNP:rs1011048)"
FT /id="VAR_045818"
FT VARIANT 810
FT /note="V -> L (in dbSNP:rs2231604)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_045819"
FT VARIANT 877..878
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:10437792,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_045820"
FT CONFLICT 303
FT /note="S -> R (in Ref. 1; AAD48398)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 919 AA; 101283 MW; 47C0DF125A319810 CRC64;
MGLFRGFVFL LVLCLLHQSN TSFIKLNNNG FEDIVIVIDP SVPEDEKIIE QIEDMVTTAS
TYLFEATEKR FFFKNVSILI PENWKENPQY KRPKHENHKH ADVIVAPPTL PGRDEPYTKQ
FTECGEKGEY IHFTPDLLLG KKQNEYGPPG KLFVHEWAHL RWGVFDEYNE DQPFYRAKSK
KIEATRCSAG ISGRNRVYKC QGGSCLSRAC RIDSTTKLYG KDCQFFPDKV QTEKASIMFM
QSIDSVVEFC NEKTHNQEAP SLQNIKCNFR STWEVISNSE DFKNTIPMVT PPPPPVFSLL
KISQRIVCLV LDKSGSMGGK DRLNRMNQAA KHFLLQTVEN GSWVGMVHFD STATIVNKLI
QIKSSDERNT LMAGLPTYPL GGTSICSGIK YAFQVIGELH SQLDGSEVLL LTDGEDNTAS
SCIDEVKQSG AIVHFIALGR AADEAVIEMS KITGGSHFYV SDEAQNNGLI DAFGALTSGN
TDLSQKSLQL ESKGLTLNSN AWMNDTVIID STVGKDTFFL ITWNSLPPSI SLWDPSGTIM
ENFTVDATSK MAYLSIPGTA KVGTWAYNLQ AKANPETLTI TVTSRAANSS VPPITVNAKM
NKDVNSFPSP MIVYAEILQG YVPVLGANVT AFIESQNGHT EVLELLDNGA GADSFKNDGV
YSRYFTAYTE NGRYSLKVRA HGGANTARLK LRPPLNRAAY IPGWVVNGEI EANPPRPEID
EDTQTTLEDF SRTASGGAFV VSQVPSLPLP DQYPPSQITD LDATVHEDKI ILTWTAPGDN
FDVGKVQRYI IRISASILDL RDSFDDALQV NTTDLSPKEA NSKESFAFKP ENISEENATH
IFIAIKSIDK SNLTSKVSNI AQVTLFIPQA NPDDIDPTPT PTPTPTPDKS HNSGVNISTL
VLSVIGSVVI VNFILSTTI
