ID   ANO9_HUMAN              Reviewed;         782 AA.
AC   A1A5B4; B3KUC4; B4E134; Q8TEN4;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2015, sequence version 3.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=Anoctamin-9;
DE   AltName: Full=Transmembrane protein 16J;
DE   AltName: Full=Tumor protein p53-inducible protein 5;
DE   AltName: Full=p53-induced gene 5 protein;
GN   Name=ANO9; Synonyms=PIG5, TMEM16J, TP53I5;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS VAL-391
RP   AND ARG-399.
RC   TISSUE=Spleen;
RX   PubMed=12693554; DOI=10.1093/dnares/10.1.49;
RA   Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
RA   Ohara O.;
RT   "Characterization of long cDNA clones from human adult spleen. II. The
RT   complete sequences of 81 cDNA clones.";
RL   DNA Res. 10:49-57(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANTS
RP   VAL-391 AND ARG-399.
RC   TISSUE=Salivary gland, and Thymus;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS VAL-391
RP   AND ARG-399.
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   [5]
RP   FUNCTION, AND 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   [6]
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   [7]
RP   ABSENCE OF CALCIUM-ACTIVATED CHLORIDE CHANNEL ACTIVITY.
RX   PubMed=22178883; DOI=10.1159/000335765;
RA   Ousingsawat J., Kongsuphol P., Schreiber R., Kunzelmann K.;
RT   "CFTR and TMEM16A are separate but functionally related Cl-channels.";
RL   Cell. Physiol. Biochem. 28:715-724(2011).
RN   [8]
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   [9]
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   [10]
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   [11]
RP   FUNCTION, AND 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:22178883). Can inhibit the
CC       activity of ANO1 (PubMed:20056604, PubMed:22946059).
CC       {ECO:0000250|UniProtKB:P86044, ECO:0000269|PubMed:20056604,
CC       ECO:0000269|PubMed:22178883, ECO:0000269|PubMed:22946059}.
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:P86044};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38664;
CC         Evidence={ECO:0000250|UniProtKB:P86044};
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:P86044};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38900;
CC         Evidence={ECO:0000250|UniProtKB:P86044};
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:P86044};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38573;
CC         Evidence={ECO:0000250|UniProtKB:P86044};
CC   -!- INTERACTION:
CC       A1A5B4; Q12959: DLG1; NbExp=2; IntAct=EBI-3843564, EBI-357481;
CC       A1A5B4; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-3843564, EBI-742388;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20056604,
CC       ECO:0000269|PubMed:22946059}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22946059}. Note=Shows
CC       predominantly an intracellular localization with a weak expression in
CC       the cell membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=A1A5B4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A1A5B4-2; Sequence=VSP_036489, VSP_036492;
CC       Name=3;
CC         IsoId=A1A5B4-3; Sequence=VSP_036490, VSP_036491;
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAB84914.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; AK074088; BAB84914.1; ALT_SEQ; mRNA.
DR   EMBL; AK096874; BAG53386.1; -; mRNA.
DR   EMBL; AK303642; BAG64646.1; -; mRNA.
DR   EMBL; AC138230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC128557; AAI28558.1; -; mRNA.
DR   CCDS; CCDS31326.1; -. [A1A5B4-1]
DR   RefSeq; NP_001012302.2; NM_001012302.2. [A1A5B4-1]
DR   RefSeq; XP_011518355.1; XM_011520053.2.
DR   AlphaFoldDB; A1A5B4; -.
DR   SMR; A1A5B4; -.
DR   BioGRID; 130747; 5.
DR   IntAct; A1A5B4; 2.
DR   MINT; A1A5B4; -.
DR   STRING; 9606.ENSP00000332788; -.
DR   TCDB; 1.A.17.1.5; the calcium-dependent chloride channel (ca-clc) family.
DR   GlyCosmos; A1A5B4; 4 sites, No reported glycans.
DR   GlyGen; A1A5B4; 4 sites.
DR   iPTMnet; A1A5B4; -.
DR   PhosphoSitePlus; A1A5B4; -.
DR   BioMuta; ANO9; -.
DR   EPD; A1A5B4; -.
DR   jPOST; A1A5B4; -.
DR   MassIVE; A1A5B4; -.
DR   PaxDb; 9606-ENSP00000332788; -.
DR   PeptideAtlas; A1A5B4; -.
DR   ProteomicsDB; 110; -. [A1A5B4-1]
DR   ProteomicsDB; 111; -. [A1A5B4-2]
DR   ProteomicsDB; 112; -. [A1A5B4-3]
DR   Antibodypedia; 58906; 91 antibodies from 20 providers.
DR   DNASU; 338440; -.
DR   Ensembl; ENST00000332826.7; ENSP00000332788.6; ENSG00000185101.13. [A1A5B4-1]
DR   GeneID; 338440; -.
DR   KEGG; hsa:338440; -.
DR   MANE-Select; ENST00000332826.7; ENSP00000332788.6; NM_001012302.3; NP_001012302.2.
DR   UCSC; uc001lpi.3; human. [A1A5B4-1]
DR   AGR; HGNC:20679; -.
DR   CTD; 338440; -.
DR   DisGeNET; 338440; -.
DR   GeneCards; ANO9; -.
DR   HGNC; HGNC:20679; ANO9.
DR   HPA; ENSG00000185101; Tissue enhanced (intestine, skin).
DR   MIM; 619963; gene.
DR   neXtProt; NX_A1A5B4; -.
DR   OpenTargets; ENSG00000185101; -.
DR   PharmGKB; PA164715791; -.
DR   VEuPathDB; HostDB:ENSG00000185101; -.
DR   eggNOG; KOG2514; Eukaryota.
DR   GeneTree; ENSGT00940000158300; -.
DR   HOGENOM; CLU_006685_3_1_1; -.
DR   InParanoid; A1A5B4; -.
DR   OMA; KTWARWR; -.
DR   OrthoDB; 534027at2759; -.
DR   TreeFam; TF314265; -.
DR   PathwayCommons; A1A5B4; -.
DR   Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR   Reactome; R-HSA-9733458; Induction of Cell-Cell Fusion.
DR   SignaLink; A1A5B4; -.
DR   BioGRID-ORCS; 338440; 17 hits in 1164 CRISPR screens.
DR   ChiTaRS; ANO9; human.
DR   GenomeRNAi; 338440; -.
DR   Pharos; A1A5B4; Tbio.
DR   PRO; PR:A1A5B4; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; A1A5B4; Protein.
DR   Bgee; ENSG00000185101; Expressed in mucosa of transverse colon and 126 other cell types or tissues.
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; IMP:UniProtKB.
DR   GO; GO:0017128; F:phospholipid scramblase activity; IEA:Ensembl.
DR   GO; GO:0061591; P:calcium activated galactosylceramide scrambling; IEA:Ensembl.
DR   GO; GO:0061590; P:calcium activated phosphatidylcholine scrambling; IEA:Ensembl.
DR   GO; GO:0061589; P:calcium activated phosphatidylserine scrambling; IEA:Ensembl.
DR   GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006821; P:chloride transport; IMP:UniProtKB.
DR   GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0034220; P:monoatomic ion transmembrane transport; TAS:Reactome.
DR   GO; GO:1902939; P:negative regulation of intracellular calcium activated chloride channel activity; IDA:UniProtKB.
DR   InterPro; IPR007632; Anoctamin.
DR   InterPro; IPR049452; Anoctamin_TM.
DR   PANTHER; PTHR12308; ANOCTAMIN; 1.
DR   PANTHER; PTHR12308:SF37; ANOCTAMIN-9; 1.
DR   Pfam; PF04547; Anoctamin; 1.
DR   Genevisible; A1A5B4; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Glycoprotein; Lipid metabolism;
KW   Lipid transport; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..782
FT                   /note="Anoctamin-9"
FT                   /id="PRO_0000289329"
FT   TOPO_DOM        1..198
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        220..264
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        265..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        286..331
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        332..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        353..373
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        374..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        395..423
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        424..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        445..552
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        553..573
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        574..604
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        605..625
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        626..703
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        704..724
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        725..782
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          756..782
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        641
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        652
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        674
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        690
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..299
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_036489"
FT   VAR_SEQ         156..186
FT                   /note="GEGRLKKTWARWRHMFREQPVDEIRNYFGEK -> VRGGPAWRGPWGGTLGW
FT                   GLSLSVTRARGRDA (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_036490"
FT   VAR_SEQ         187..782
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_036491"
FT   VAR_SEQ         300..305
FT                   /note="VWDEEQ -> MPAVSE (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_036492"
FT   VARIANT         93
FT                   /note="L -> F (in dbSNP:rs7395065)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_054621"
FT   VARIANT         391
FT                   /note="I -> V (in dbSNP:rs10794324)"
FT                   /evidence="ECO:0000269|PubMed:12693554,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT                   /id="VAR_032617"
FT   VARIANT         399
FT                   /note="C -> R (in dbSNP:rs10794323)"
FT                   /evidence="ECO:0000269|PubMed:12693554,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT                   /id="VAR_032618"
SQ   SEQUENCE   782 AA;  90333 MW;  6A359B63DD92AFF7 CRC64;
     MQGEESLRIL VEPEGDSFPL MEISTCETEA SEQWDYVLVA QRHTQRDPRQ ARQQQFLEEL
     RRKGFHIKVI RDQKQVFFGI RADNSVFGLY RTLLLEPEGP APHAELAAPT TIPVTTSLRI
     RIVNFVVMNN KTSAGETFED LMKDGVFEAR FPLHKGEGRL KKTWARWRHM FREQPVDEIR
     NYFGEKVALY FVWLGWYTYM LVPAALTGLL VFLSGFSLFE ASQISKEICE AHDILMCPLG
     DHSRRYQRLS ETCTFAKLTH LFDNDGTVVF AIFMALWATV FLEIWKRQRA RVVLHWDLYV
     WDEEQEEMAL QLINCPDYKL RPYQHSYLRS TVILVLTLLM ICLMIGMAHV LVVYRVLASA
     LFSSSAVPFL EEQVTTAVVV TGALVHYVTI IIMTKINRCV ALKLCDFEMP RTFSERESRF
     TIRFFTLQFF THFSSLIYIA FILGRINGHP GKSTRLAGLW KLEECHASGC MMDLFVQMAI
     IMGLKQTLSN CVEYLVPWVT HKCRSLRASE SGHLPRDPEL RDWRRNYLLN PVNTFSLFDE
     FMEMMIQYGF TTIFVAAFPL APLLALFSNL VEIRLDAIKM VWLQRRLVPR KAKDIGTWLQ
     VLETIGVLAV IANGMVIAFT SEFIPRVVYK YRYSPCLKEG NSTVDCLKGY VNHSLSVFHT
     KDFQDPDGIE GSENVTLCRY RDYRNPPDYN FSEQFWFLLA IRLAFVILFE HVALCIKLIA
     AWFVPDIPQS VKNKVLEVKY QRLREKMWHG RQRLGGVGAG SRPPMPAHPT PASIFSARST
     DV
//