ID   PACC1_HUMAN             Reviewed;         350 AA.
AC   Q9H813; B7Z4D6; Q6IA87; Q9NV85;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=Proton-activated chloride channel {ECO:0000303|PubMed:31023925};
DE            Short=PAC {ECO:0000303|PubMed:31023925};
DE            Short=hPAC {ECO:0000303|PubMed:31023925};
DE   AltName: Full=Acid-sensitive outwardly-rectifying anion channel {ECO:0000303|PubMed:31318332};
DE            Short=ASOR {ECO:0000303|PubMed:31318332};
DE   AltName: Full=Proton-activated outwardly rectifying anion channel {ECO:0000303|PubMed:31318332};
DE            Short=PAORAC {ECO:0000303|PubMed:31318332};
DE   AltName: Full=Transmembrane protein 206 {ECO:0000305};
DE            Short=hTMEM206 {ECO:0000303|PubMed:31318332};
GN   Name=PACC1 {ECO:0000312|HGNC:HGNC:25593};
GN   Synonyms=C1orf75 {ECO:0000312|HGNC:HGNC:25593}, TMEM206
GN   {ECO:0000312|HGNC:HGNC:25593};
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] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, Retinoblastoma, and Teratocarcinoma;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Muscle;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-155 AND ASN-162.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [9]
RP   FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY, AND
RP   GLYCOSYLATION.
RX   PubMed=31318332; DOI=10.7554/elife.49187;
RA   Ullrich F., Blin S., Lazarow K., Daubitz T., von Kries J.P., Jentsch T.J.;
RT   "Identification of TMEM206 proteins as pore of PAORAC/ASOR acid-sensitive
RT   chloride channels.";
RL   Elife 8:0-0(2019).
RN   [10]
RP   FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE
RP   SPECIFICITY, AND MUTAGENESIS OF ILE-307.
RX   PubMed=31023925; DOI=10.1126/science.aav9739;
RA   Yang J., Chen J., Del Carmen Vitery M., Osei-Owusu J., Chu J., Yu H.,
RA   Sun S., Qiu Z.;
RT   "PAC, an evolutionarily conserved membrane protein, is a proton-activated
RT   chloride channel.";
RL   Science 364:395-399(2019).
RN   [11]
RP   VARIANT [LARGE SCALE ANALYSIS] ASN-336.
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: Chloride channel gated by pH that facilitates the entry of
CC       chloride ions into cells upon exposure to extracellular acidic pH
CC       (PubMed:31023925, PubMed:31318332). Involved in acidosis-induced cell
CC       death by mediating chloride influx and subsequent cell swelling
CC       (PubMed:31023925, PubMed:31318332). {ECO:0000269|PubMed:31023925,
CC       ECO:0000269|PubMed:31318332}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823,
CC         ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:31023925,
CC         ECO:0000269|PubMed:31318332};
CC   -!- INTERACTION:
CC       Q9H813; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-4319734, EBI-12019274;
CC       Q9H813; Q9Y342: PLLP; NbExp=3; IntAct=EBI-4319734, EBI-3919291;
CC       Q9H813; Q04941: PLP2; NbExp=5; IntAct=EBI-4319734, EBI-608347;
CC       Q9H813; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-4319734, EBI-8652744;
CC       Q9H813; Q9BVK8: TMEM147; NbExp=4; IntAct=EBI-4319734, EBI-348587;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31023925,
CC       ECO:0000269|PubMed:31318332}; Multi-pass membrane protein
CC       {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9H813-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H813-2; Sequence=VSP_042887;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in brain.
CC       {ECO:0000269|PubMed:31023925}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:31318332}.
CC   -!- SIMILARITY: Belongs to the proton-activated chloride channel family.
CC       {ECO:0000305}.
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DR   EMBL; AK001736; BAA91870.1; -; mRNA.
DR   EMBL; AK024066; BAB14810.1; -; mRNA.
DR   EMBL; AK297200; BAH12522.1; -; mRNA.
DR   EMBL; CR457268; CAG33549.1; -; mRNA.
DR   EMBL; AC092803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL360091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC006320; AAH06320.1; -; mRNA.
DR   CCDS; CCDS1504.1; -. [Q9H813-1]
DR   CCDS; CCDS55687.1; -. [Q9H813-2]
DR   RefSeq; NP_001185791.1; NM_001198862.1. [Q9H813-2]
DR   RefSeq; NP_060722.2; NM_018252.2. [Q9H813-1]
DR   PDB; 7JNA; EM; 3.60 A; A/B/C=1-350.
DR   PDB; 7JNC; EM; 3.73 A; A/B/C=1-350.
DR   PDB; 7SQF; EM; 3.10 A; A/B/C=1-350.
DR   PDB; 7SQG; EM; 2.60 A; A/B/C=1-350.
DR   PDB; 7SQH; EM; 2.50 A; A/B/C=1-350.
DR   PDB; 8EQ4; EM; 2.71 A; A/B/C=1-350.
DR   PDB; 8FBL; EM; 2.70 A; A/B/C=57-339.
DR   PDBsum; 7JNA; -.
DR   PDBsum; 7JNC; -.
DR   PDBsum; 7SQF; -.
DR   PDBsum; 7SQG; -.
DR   PDBsum; 7SQH; -.
DR   PDBsum; 8EQ4; -.
DR   PDBsum; 8FBL; -.
DR   AlphaFoldDB; Q9H813; -.
DR   EMDB; EMD-22403; -.
DR   EMDB; EMD-22404; -.
DR   EMDB; EMD-25383; -.
DR   EMDB; EMD-25384; -.
DR   EMDB; EMD-25385; -.
DR   EMDB; EMD-28535; -.
DR   EMDB; EMD-28964; -.
DR   SMR; Q9H813; -.
DR   BioGRID; 120539; 122.
DR   IntAct; Q9H813; 94.
DR   STRING; 9606.ENSP00000438863; -.
DR   TCDB; 1.A.114.1.1; the proton-activated chloride channel (pacc) family.
DR   GlyCosmos; Q9H813; 2 sites, No reported glycans.
DR   GlyGen; Q9H813; 3 sites.
DR   iPTMnet; Q9H813; -.
DR   PhosphoSitePlus; Q9H813; -.
DR   SwissPalm; Q9H813; -.
DR   BioMuta; TMEM206; -.
DR   DMDM; 74752717; -.
DR   EPD; Q9H813; -.
DR   jPOST; Q9H813; -.
DR   MassIVE; Q9H813; -.
DR   MaxQB; Q9H813; -.
DR   PaxDb; 9606-ENSP00000438863; -.
DR   PeptideAtlas; Q9H813; -.
DR   ProteomicsDB; 81166; -. [Q9H813-1]
DR   ProteomicsDB; 81167; -. [Q9H813-2]
DR   Pumba; Q9H813; -.
DR   Antibodypedia; 47113; 34 antibodies from 12 providers.
DR   DNASU; 55248; -.
DR   Ensembl; ENST00000261455.9; ENSP00000261455.4; ENSG00000065600.13. [Q9H813-1]
DR   Ensembl; ENST00000535273.2; ENSP00000438863.1; ENSG00000065600.13. [Q9H813-2]
DR   GeneID; 55248; -.
DR   KEGG; hsa:55248; -.
DR   MANE-Select; ENST00000261455.9; ENSP00000261455.4; NM_018252.3; NP_060722.2.
DR   UCSC; uc001hjc.5; human. [Q9H813-1]
DR   AGR; HGNC:25593; -.
DR   CTD; 55248; -.
DR   DisGeNET; 55248; -.
DR   GeneCards; PACC1; -.
DR   HGNC; HGNC:25593; PACC1.
DR   HPA; ENSG00000065600; Tissue enriched (brain).
DR   MIM; 618427; gene.
DR   neXtProt; NX_Q9H813; -.
DR   OpenTargets; ENSG00000065600; -.
DR   PharmGKB; PA162406386; -.
DR   VEuPathDB; HostDB:ENSG00000065600; -.
DR   eggNOG; ENOG502QS5H; Eukaryota.
DR   GeneTree; ENSGT00390000017528; -.
DR   HOGENOM; CLU_068069_0_0_1; -.
DR   InParanoid; Q9H813; -.
DR   OMA; ELIFMQF; -.
DR   OrthoDB; 4313692at2759; -.
DR   PhylomeDB; Q9H813; -.
DR   TreeFam; TF333307; -.
DR   PathwayCommons; Q9H813; -.
DR   SignaLink; Q9H813; -.
DR   BioGRID-ORCS; 55248; 11 hits in 1158 CRISPR screens.
DR   ChiTaRS; TMEM206; human.
DR   GenomeRNAi; 55248; -.
DR   Pharos; Q9H813; Tdark.
DR   PRO; PR:Q9H813; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9H813; Protein.
DR   Bgee; ENSG00000065600; Expressed in C1 segment of cervical spinal cord and 157 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; HDA:UniProtKB.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0061797; F:pH-gated chloride channel activity; IDA:UniProtKB.
DR   GO; GO:0006821; P:chloride transport; IDA:UniProtKB.
DR   InterPro; IPR029366; TMEM206.
DR   PANTHER; PTHR16087:SF0; PROTON-ACTIVATED CHLORIDE CHANNEL; 1.
DR   PANTHER; PTHR16087; TRANSMEMBRANE PROTEIN 206; 1.
DR   Pfam; PF15122; TMEM206; 1.
DR   Genevisible; Q9H813; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Chloride;
KW   Chloride channel; Glycoprotein; Ion channel; Ion transport; Membrane;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..350
FT                   /note="Proton-activated chloride channel"
FT                   /id="PRO_0000279471"
FT   TOPO_DOM        1..64
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:31023925,
FT                   ECO:0000305|PubMed:31318332"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        86..301
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        302..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        319..350
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:31023925,
FT                   ECO:0000305|PubMed:31318332"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         10
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D771"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D771"
FT   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q66H28"
FT   CARBOHYD        155
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   VAR_SEQ         12
FT                   /note="E -> EAVRPALPSSKPCLLTSPAVLVKLLSSSASTSRPPNLGHLWQPSSSV
FT                   PLHRAASLAKVRQFQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_042887"
FT   VARIANT         336
FT                   /note="K -> N (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs1034429230)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035847"
FT   MUTAGEN         307
FT                   /note="I->A: Reduced I(-) permeability."
FT                   /evidence="ECO:0000269|PubMed:31023925"
FT   CONFLICT        11..12
FT                   /note="QE -> RV (in Ref. 2; CAG33549)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        23
FT                   /note="N -> S (in Ref. 1; BAA91870)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        47
FT                   /note="D -> G (in Ref. 2; CAG33549)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        227
FT                   /note="Y -> C (in Ref. 1; BAA91870)"
FT                   /evidence="ECO:0000305"
FT   HELIX           66..97
FT                   /evidence="ECO:0007829|PDB:7SQG"
FT   STRAND          100..107
FT                   /evidence="ECO:0007829|PDB:7SQG"
FT   STRAND          115..119
FT                   /evidence="ECO:0007829|PDB:7SQG"
FT   STRAND          124..134
FT                   /evidence="ECO:0007829|PDB:7SQG"
FT   STRAND          147..149
FT                   /evidence="ECO:0007829|PDB:7SQG"
FT   STRAND          151..157
FT                   /evidence="ECO:0007829|PDB:7SQG"
FT   TURN            159..161
FT                   /evidence="ECO:0007829|PDB:7SQG"
FT   STRAND          165..172
FT                   /evidence="ECO:0007829|PDB:7SQG"
FT   TURN            177..180
FT                   /evidence="ECO:0007829|PDB:7SQG"
FT   STRAND          181..189
FT                   /evidence="ECO:0007829|PDB:7SQG"
FT   STRAND          198..205
FT                   /evidence="ECO:0007829|PDB:7SQG"
FT   HELIX           207..211
FT                   /evidence="ECO:0007829|PDB:7SQG"
FT   HELIX           216..226
FT                   /evidence="ECO:0007829|PDB:7SQG"
FT   STRAND          229..233
FT                   /evidence="ECO:0007829|PDB:7SQG"
FT   STRAND          236..248
FT                   /evidence="ECO:0007829|PDB:7SQG"
FT   STRAND          250..252
FT                   /evidence="ECO:0007829|PDB:7SQG"
FT   STRAND          254..266
FT                   /evidence="ECO:0007829|PDB:7SQG"
FT   HELIX           273..277
FT                   /evidence="ECO:0007829|PDB:7SQG"
FT   STRAND          278..288
FT                   /evidence="ECO:0007829|PDB:7SQG"
FT   STRAND          290..298
FT                   /evidence="ECO:0007829|PDB:7SQG"
FT   HELIX           303..333
FT                   /evidence="ECO:0007829|PDB:7SQG"
SQ   SEQUENCE   350 AA;  40043 MW;  5F68ACA21DDD0674 CRC64;
     MIRQERSTSY QELSEELVQV VENSELADEQ DKETVRVQGP GILPGLDSES ASSSIRFSKA
     CLKNVFSVLL IFIYLLLMAV AVFLVYRTIT DFREKLKHPV MSVSYKEVDR YDAPGIALYP
     GQAQLLSCKH HYEVIPPLTS PGQPGDMNCT TQRINYTDPF SNQTVKSALI VQGPREVKKR
     ELVFLQFRLN KSSEDFSAID YLLFSSFQEF LQSPNRVGFM QACESAYSSW KFSGGFRTWV
     KMSLVKTKEE DGREAVEFRQ ETSVVNYIDQ RPAAKKSAQL FFVVFEWKDP FIQKVQDIVT
     ANPWNTIALL CGAFLALFKA AEFAKLSIKW MIKIRKRYLK RRGQATSHIS
//