ANO7_HUMAN
ID ANO7_HUMAN Reviewed; 933 AA.
AC Q6IWH7; Q6IWH6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Anoctamin-7;
DE AltName: Full=Dresden transmembrane protein of the prostate;
DE Short=D-TMPP;
DE AltName: Full=IPCA-5;
DE AltName: Full=New gene expressed in prostate;
DE AltName: Full=Prostate cancer-associated protein 5;
DE AltName: Full=Transmembrane protein 16G;
GN Name=ANO7; Synonyms=NGEP, PCANAP5, TMEM16G;
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] (ISOFORMS 1 AND 2), VARIANT LYS-912, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=14981236; DOI=10.1073/pnas.0308746101;
RA Bera T.K., Das S., Maeda H., Beers R., Wolfgang C.D., Kumar V., Hahn Y.,
RA Lee B., Pastan I.;
RT "NGEP, a gene encoding a membrane protein detected only in prostate cancer
RT and normal prostate.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:3059-3064(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP IDENTIFICATION.
RX PubMed=10613842; DOI=10.1101/gr.9.12.1198;
RA Walker M.G., Volkmuth W., Sprinzak E., Hodgson D., Klingler T.;
RT "Prediction of gene function by genome-scale expression analysis: prostate
RT cancer-associated genes.";
RL Genome Res. 9:1198-1203(1999).
RN [4]
RP IDENTIFICATION.
RX PubMed=15375614;
RA Katoh M., Katoh M.;
RT "Characterization of human TMEM16G gene in silico.";
RL Int. J. Mol. Med. 14:759-764(2004).
RN [5]
RP ALTERNATIVE SPLICING (ISOFORM 3), TISSUE SPECIFICITY, AND INDUCTION BY
RP ANDROGEN.
RX PubMed=15761874; DOI=10.1002/pros.20250;
RA Kiessling A., Weigle B., Fuessel S., Ebner R., Meye A., Rieger M.A.,
RA Schmitz M., Temme A., Bachmann M., Wirth M.P., Rieber E.P.;
RT "D-TMPP: a novel androgen-regulated gene preferentially expressed in
RT prostate and prostate cancer that is the first characterized member of an
RT eukaryotic gene family.";
RL Prostate 64:387-400(2005).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17308099; DOI=10.1158/0008-5472.can-06-2673;
RA Das S., Hahn Y., Nagata S., Willingham M.C., Bera T.K., Lee B., Pastan I.;
RT "NGEP, a prostate-specific plasma membrane protein that promotes the
RT association of LNCaP cells.";
RL Cancer Res. 67:1594-1601(2007).
RN [7]
RP GLYCOSYLATION AT ASN-809 AND ASN-824, AND MEMBRANE TOPOLOGY.
RX PubMed=18676855; DOI=10.1158/0008-5472.can-08-0870;
RA Das S., Hahn Y., Walker D.A., Nagata S., Willingham M.C., Peehl D.M.,
RA Bera T.K., Lee B., Pastan I.;
RT "Topology of NGEP, a prostate-specific cell:cell junction protein widely
RT expressed in many cancers of different grade level.";
RL Cancer Res. 68:6306-6312(2008).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=20056604; DOI=10.1074/jbc.m109.065367;
RA Schreiber R., Uliyakina I., Kongsuphol P., Warth R., Mirza M.,
RA Martins J.R., Kunzelmann K.;
RT "Expression and function of epithelial anoctamins.";
RL J. Biol. Chem. 285:7838-7845(2010).
RN [9]
RP REVIEW.
RX PubMed=21642943; DOI=10.1038/aps.2011.48;
RA Duran C., Hartzell H.C.;
RT "Physiological roles and diseases of Tmem16/Anoctamin proteins: are they
RT all chloride channels?";
RL Acta Pharmacol. Sin. 32:685-692(2011).
RN [10]
RP REVIEW.
RX PubMed=21607626; DOI=10.1007/s00424-011-0975-9;
RA Kunzelmann K., Tian Y., Martins J.R., Faria D., Kongsuphol P.,
RA Ousingsawat J., Thevenod F., Roussa E., Rock J., Schreiber R.;
RT "Anoctamins.";
RL Pflugers Arch. 462:195-208(2011).
RN [11]
RP ABSENCE OF CALCIUM-ACTIVATED CHLORIDE CHANNEL ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=22075693; DOI=10.1152/ajpcell.00140.2011;
RA Duran C., Qu Z., Osunkoya A.O., Cui Y., Hartzell H.C.;
RT "ANOs 3-7 in the anoctamin/Tmem16 Cl- channel family are intracellular
RT proteins.";
RL Am. J. Physiol. 302:C482-C493(2012).
RN [12]
RP REVIEW.
RX PubMed=22302790; DOI=10.1113/expphysiol.2011.058214;
RA Winpenny J.P., Gray M.A.;
RT "The anoctamin (TMEM16) gene family: calcium-activated chloride channels
RT come of age.";
RL Exp. Physiol. 97:175-176(2012).
RN [13]
RP REVIEW, AND ABSENCE OF CALCIUM-ACTIVATED CHLORIDE CHANNEL ACTIVITY.
RX PubMed=21984732; DOI=10.1113/expphysiol.2011.058198;
RA Scudieri P., Sondo E., Ferrera L., Galietta L.J.;
RT "The anoctamin family: TMEM16A and TMEM16B as calcium-activated chloride
RT channels.";
RL Exp. Physiol. 97:177-183(2012).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=22946059; DOI=10.1242/jcs.109553;
RA Tian Y., Schreiber R., Kunzelmann K.;
RT "Anoctamins are a family of Ca2+ activated Cl- channels.";
RL J. Cell Sci. 125:4991-4998(2012).
CC -!- FUNCTION: Has calcium-dependent phospholipid scramblase activity;
CC scrambles phosphatidylserine, phosphatidylcholine and
CC galactosylceramide (By similarity). Does not exhibit calcium-activated
CC chloride channel (CaCC) activity (PubMed:22075693). May play a role in
CC cell-cell interactions (PubMed:17308099).
CC {ECO:0000250|UniProtKB:Q14AT5, ECO:0000269|PubMed:17308099,
CC ECO:0000269|PubMed:22075693}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-
CC sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663,
CC ChEBI:CHEBI:57262; Evidence={ECO:0000250|UniProtKB:Q14AT5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38664;
CC Evidence={ECO:0000250|UniProtKB:Q14AT5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine(out) = a
CC beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine(in);
CC Xref=Rhea:RHEA:38899, ChEBI:CHEBI:18390;
CC Evidence={ECO:0000250|UniProtKB:Q14AT5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38900;
CC Evidence={ECO:0000250|UniProtKB:Q14AT5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-
CC sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571,
CC ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:Q14AT5};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38573;
CC Evidence={ECO:0000250|UniProtKB:Q14AT5};
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:14981236, ECO:0000269|PubMed:17308099,
CC ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22946059}; Multi-pass
CC membrane protein {ECO:0000255}. Cell junction
CC {ECO:0000269|PubMed:17308099}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:22075693}. Note=Concentrates at sites of cell-cell
CC contact (PubMed:17308099). Shows an intracellular localization
CC according to PubMed:22075693 and PubMed:20056604.
CC {ECO:0000269|PubMed:17308099, ECO:0000269|PubMed:20056604,
CC ECO:0000269|PubMed:22075693}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol
CC {ECO:0000269|PubMed:14981236}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=NGEP-L;
CC IsoId=Q6IWH7-1; Sequence=Displayed;
CC Name=2; Synonyms=NGEP-S;
CC IsoId=Q6IWH7-2; Sequence=VSP_026004, VSP_026005, VSP_026006;
CC Name=3; Synonyms=D-TMPP;
CC IsoId=Q6IWH7-3; Sequence=VSP_026004, VSP_026007, VSP_026008;
CC -!- TISSUE SPECIFICITY: Specifically expressed in epithelial cells of the
CC prostate (at protein level). {ECO:0000269|PubMed:14981236,
CC ECO:0000269|PubMed:15761874, ECO:0000269|PubMed:17308099}.
CC -!- INDUCTION: Up-regulated by androgen. {ECO:0000269|PubMed:15761874}.
CC -!- MISCELLANEOUS: The term 'anoctamin' was coined because these channels
CC are anion selective and have eight (OCT) transmembrane segments. There
CC is some dissatisfaction in the field with the Ano nomenclature because
CC it is not certain that all the members of this family are anion
CC channels or have the 8-transmembrane topology.
CC -!- SIMILARITY: Belongs to the anoctamin family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-55 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AY617079; AAT40139.1; -; mRNA.
DR EMBL; AY617080; AAT40140.1; -; mRNA.
DR EMBL; AC005237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC111201; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001001666.1; NM_001001666.3.
DR RefSeq; NP_001001891.2; NM_001001891.3.
DR AlphaFoldDB; Q6IWH7; -.
DR SMR; Q6IWH7; -.
DR BioGRID; 119107; 67.
DR IntAct; Q6IWH7; 1.
DR STRING; 9606.ENSP00000274979; -.
DR TCDB; 1.A.17.1.27; the calcium-dependent chloride channel (ca-clc) family.
DR GlyGen; Q6IWH7; 2 sites.
DR iPTMnet; Q6IWH7; -.
DR PhosphoSitePlus; Q6IWH7; -.
DR BioMuta; ANO7; -.
DR DMDM; 334302764; -.
DR jPOST; Q6IWH7; -.
DR MassIVE; Q6IWH7; -.
DR PaxDb; Q6IWH7; -.
DR PeptideAtlas; Q6IWH7; -.
DR PRIDE; Q6IWH7; -.
DR ProteomicsDB; 66501; -. [Q6IWH7-1]
DR ProteomicsDB; 66502; -. [Q6IWH7-2]
DR ProteomicsDB; 66503; -. [Q6IWH7-3]
DR Antibodypedia; 47723; 121 antibodies from 26 providers.
DR DNASU; 50636; -.
DR Ensembl; ENST00000274979.12; ENSP00000274979.8; ENSG00000146205.15. [Q6IWH7-1]
DR GeneID; 50636; -.
DR KEGG; hsa:50636; -.
DR UCSC; uc002waw.4; human. [Q6IWH7-1]
DR CTD; 50636; -.
DR DisGeNET; 50636; -.
DR GeneCards; ANO7; -.
DR HGNC; HGNC:31677; ANO7.
DR HPA; ENSG00000146205; Tissue enhanced (intestine, prostate, stomach).
DR MIM; 605096; gene.
DR neXtProt; NX_Q6IWH7; -.
DR OpenTargets; ENSG00000146205; -.
DR PharmGKB; PA32980; -.
DR VEuPathDB; HostDB:ENSG00000146205; -.
DR eggNOG; KOG2514; Eukaryota.
DR GeneTree; ENSGT00940000158551; -.
DR HOGENOM; CLU_1502990_0_0_1; -.
DR InParanoid; Q6IWH7; -.
DR OMA; RWAMTSE; -.
DR OrthoDB; 1263362at2759; -.
DR PhylomeDB; Q6IWH7; -.
DR TreeFam; TF314265; -.
DR PathwayCommons; Q6IWH7; -.
DR Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 50636; 5 hits in 1072 CRISPR screens.
DR ChiTaRS; ANO7; human.
DR GenomeRNAi; 50636; -.
DR Pharos; Q6IWH7; Tbio.
DR PRO; PR:Q6IWH7; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q6IWH7; protein.
DR Bgee; ENSG00000146205; Expressed in mucosa of transverse colon and 107 other tissues.
DR ExpressionAtlas; Q6IWH7; baseline and differential.
DR Genevisible; Q6IWH7; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005254; F:chloride channel activity; IBA:GO_Central.
DR GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IDA:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0061588; P:calcium activated phospholipid scrambling; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0006821; P:chloride transport; IDA:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR InterPro; IPR032394; Anoct_dimer.
DR InterPro; IPR007632; Anoctamin.
DR InterPro; IPR031296; Anoctamin-7.
DR PANTHER; PTHR12308; PTHR12308; 1.
DR PANTHER; PTHR12308:SF22; PTHR12308:SF22; 1.
DR Pfam; PF16178; Anoct_dimer; 1.
DR Pfam; PF04547; Anoctamin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Cytoplasm;
KW Endoplasmic reticulum; Glycoprotein; Lipid transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..933
FT /note="Anoctamin-7"
FT /id="PRO_0000289326"
FT TOPO_DOM 1..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..420
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 442..499
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 521..550
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 551..571
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 572..588
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 589..609
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 610..714
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 715..735
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 736..763
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 764..784
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 785..843
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 844..864
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 865..933
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 43..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 809
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18676855"
FT CARBOHYD 824
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18676855"
FT VAR_SEQ 110
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14981236"
FT /id="VSP_026004"
FT VAR_SEQ 158..180
FT /note="QDVQDGNTTVHYALLSASWAVLC -> VRGGCHGQGPRPCIHSVTHDLAA
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14981236"
FT /id="VSP_026005"
FT VAR_SEQ 181..933
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14981236"
FT /id="VSP_026006"
FT VAR_SEQ 859
FT /note="H -> VAEAPAGSPIHGMRPRPCALPNSSTW (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_026007"
FT VAR_SEQ 860..933
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_026008"
FT VARIANT 67
FT /note="V -> I (in dbSNP:rs2302054)"
FT /id="VAR_032616"
FT VARIANT 912
FT /note="E -> K (in dbSNP:rs7590653)"
FT /evidence="ECO:0000269|PubMed:14981236"
FT /id="VAR_065166"
SQ SEQUENCE 933 AA; 105532 MW; D6FD42578A4BD773 CRC64;
MRMAATAWAG LQGPPLPTLC PAVRTGLYCR DQAHAERWAM TSETSSGSHC ARSRMLRRRA
QEEDSTVLID VSPPEAEKRG SYGSTAHASE PGGQQAAACR AGSPAKPRIA DFVLVWEEDL
KLDRQQDSAA RDRTDMHRTW RETFLDNLRA AGLCVDQQDV QDGNTTVHYA LLSASWAVLC
YYAEDLRLKL PLQELPNQAS NWSAGLLAWL GIPNVLLEVV PDVPPEYYSC RFRVNKLPRF
LGSDNQDTFF TSTKRHQILF EILAKTPYGH EKKNLLGIHQ LLAEGVLSAA FPLHDGPFKT
PPEGPQAPRL NQRQVLFQHW ARWGKWNKYQ PLDHVRRYFG EKVALYFAWL GFYTGWLLPA
AVVGTLVFLV GCFLVFSDIP TQELCGSKDS FEMCPLCLDC PFWLLSSACA LAQAGRLFDH
GGTVFFSLFM ALWAVLLLEY WKRKSATLAY RWDCSDYEDT EERPRPQFAA SAPMTAPNPI
TGEDEPYFPE RSRARRMLAG SVVIVVMVAV VVMCLVSIIL YRAIMAIVVS RSGNTLLAAW
ASRIASLTGS VVNLVFILIL SKIYVSLAHV LTRWEMHRTQ TKFEDAFTLK VFIFQFVNFY
SSPVYIAFFK GRFVGYPGNY HTLFGVRNEE CAAGGCLIEL AQELLVIMVG KQVINNMQEV
LIPKLKGWWQ KFRLRSKKRK AGASAGASQG PWEDDYELVP CEGLFDEYLE MVLQFGFVTI
FVAACPLAPL FALLNNWVEI RLDARKFVCE YRRPVAERAQ DIGIWFHILA GLTHLAVISN
AFLLAFSSDF LPRAYYRWTR AHDLRGFLNF TLARAPSSFA AAHNRTCRYR AFRDDDGHYS
QTYWNLLAIR LAFVIVFEHV VFSVGRLLDL LVPDIPESVE IKVKREYYLA KQALAENEVL
FGTNGTKDEQ PEGSELSSHW TPFTVPKASQ LQQ
