ID   RNLS_HUMAN              Reviewed;         342 AA.
AC   Q5VYX0; Q9BS33; Q9NUP8;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   24-JAN-2024, entry version 157.
DE   RecName: Full=Renalase {ECO:0000303|PubMed:15841207};
DE            EC=1.6.3.5 {ECO:0000269|PubMed:23964689, ECO:0000269|PubMed:25531177};
DE   AltName: Full=Monoamine oxidase-C;
DE            Short=MAO-C;
DE   Flags: Precursor;
GN   Name=RNLS; Synonyms=C10orf59;
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 2).
RC   TISSUE=Placenta;
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 GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-37.
RC   TISSUE=Kidney;
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   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15841207; DOI=10.1172/jci24066;
RA   Xu J., Li G., Wang P., Velazquez H., Yao X., Li Y., Wu Y., Peixoto A.,
RA   Crowley S., Desir G.V.;
RT   "Renalase is a novel, soluble monoamine oxidase that regulates cardiac
RT   function and blood pressure.";
RL   J. Clin. Invest. 115:1275-1280(2005).
RN   [5]
RP   FUNCTION.
RX   PubMed=17385068; DOI=10.1007/s00702-007-0672-1;
RA   Boomsma F., Tipton K.F.;
RT   "Renalase, a catecholamine-metabolising enzyme?";
RL   J. Neural Transm. 114:775-776(2007).
RN   [6]
RP   CATALYTIC ACTIVITY (ISOFORM 1).
RX   PubMed=23964689; DOI=10.1021/ja407384h;
RA   Beaupre B.A., Carmichael B.R., Hoag M.R., Shah D.D., Moran G.R.;
RT   "Renalase is an alpha-NAD(P)H oxidase/anomerase.";
RL   J. Am. Chem. Soc. 135:13980-13987(2013).
RN   [7]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=25531177; DOI=10.1021/bi5013436;
RA   Beaupre B.A., Hoag M.R., Roman J., Foersterling F.H., Moran G.R.;
RT   "Metabolic function for human renalase: oxidation of isomeric forms of
RT   beta-NAD(P)H that are inhibitory to primary metabolism.";
RL   Biochemistry 54:795-806(2015).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), COFACTOR, AND FAD-BINDING SITES.
RX   PubMed=21699903; DOI=10.1016/j.jmb.2011.06.010;
RA   Milani M., Ciriello F., Baroni S., Pandini V., Canevari G., Bolognesi M.,
RA   Aliverti A.;
RT   "FAD-binding site and NADP reactivity in human renalase: a new enzyme
RT   involved in blood pressure regulation.";
RL   J. Mol. Biol. 411:463-473(2011).
CC   -!- FUNCTION: Catalyzes the oxidation of the less abundant 1,2-dihydro-
CC       beta-NAD(P) and 1,6-dihydro-beta-NAD(P) to form beta-NAD(P)(+). The
CC       enzyme hormone is secreted by the kidney, and circulates in blood and
CC       modulates cardiac function and systemic blood pressure. Lowers blood
CC       pressure in vivo by decreasing cardiac contractility and heart rate and
CC       preventing a compensatory increase in peripheral vascular tone,
CC       suggesting a causal link to the increased plasma catecholamine and
CC       heightened cardiovascular risk. High concentrations of catecholamines
CC       activate plasma renalase and promotes its secretion and synthesis.
CC       {ECO:0000269|PubMed:15841207, ECO:0000269|PubMed:17385068,
CC       ECO:0000269|PubMed:25531177}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dihydro-beta-NAD + H(+) + O2 = H2O2 + NAD(+);
CC         Xref=Rhea:RHEA:40395, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:57540, ChEBI:CHEBI:88138; EC=1.6.3.5;
CC         Evidence={ECO:0000269|PubMed:23964689, ECO:0000269|PubMed:25531177};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dihydro-beta-NADP + H(+) + O2 = H2O2 + NADP(+);
CC         Xref=Rhea:RHEA:40399, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:58349, ChEBI:CHEBI:88137; EC=1.6.3.5;
CC         Evidence={ECO:0000269|PubMed:23964689, ECO:0000269|PubMed:25531177};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,6-dihydro-beta-NADP + H(+) + O2 = H2O2 + NADP(+);
CC         Xref=Rhea:RHEA:48000, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:58349, ChEBI:CHEBI:88139; EC=1.6.3.5;
CC         Evidence={ECO:0000269|PubMed:23964689, ECO:0000269|PubMed:25531177};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,6-dihydro-beta-NAD + H(+) + O2 = H2O2 + NAD(+);
CC         Xref=Rhea:RHEA:47996, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:57540, ChEBI:CHEBI:88140; EC=1.6.3.5;
CC         Evidence={ECO:0000269|PubMed:23964689, ECO:0000269|PubMed:25531177};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:21699903};
CC   -!- INTERACTION:
CC       Q5VYX0; P23634: ATP2B4; NbExp=3; IntAct=EBI-3386081, EBI-1174388;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15841207}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5VYX0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5VYX0-2; Sequence=VSP_015211, VSP_015212;
CC   -!- TISSUE SPECIFICITY: Secreted into the blood by the kidney. Highly
CC       expressed in the kidney, expressed at lower level in heart, skeletal
CC       muscle and small intestine. Its plasma concentration is markedly
CC       reduced in patients with end-stage renal disease, as compared with
CC       healthy subjects. {ECO:0000269|PubMed:15841207}.
CC   -!- SIMILARITY: Belongs to the renalase family. {ECO:0000305}.
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DR   EMBL; AK002080; BAA92073.1; -; mRNA.
DR   EMBL; AL353149; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL365185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL139406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC005364; AAH05364.1; -; mRNA.
DR   CCDS; CCDS31239.1; -. [Q5VYX0-1]
DR   CCDS; CCDS7388.1; -. [Q5VYX0-2]
DR   RefSeq; NP_001026879.2; NM_001031709.2. [Q5VYX0-1]
DR   RefSeq; NP_060833.1; NM_018363.3. [Q5VYX0-2]
DR   RefSeq; XP_011538226.1; XM_011539924.2. [Q5VYX0-2]
DR   RefSeq; XP_016871869.1; XM_017016380.1. [Q5VYX0-2]
DR   PDB; 3QJ4; X-ray; 2.50 A; A/B=1-342.
DR   PDBsum; 3QJ4; -.
DR   AlphaFoldDB; Q5VYX0; -.
DR   SMR; Q5VYX0; -.
DR   BioGRID; 120609; 2.
DR   IntAct; Q5VYX0; 36.
DR   STRING; 9606.ENSP00000332530; -.
DR   iPTMnet; Q5VYX0; -.
DR   PhosphoSitePlus; Q5VYX0; -.
DR   BioMuta; RNLS; -.
DR   DMDM; 73914006; -.
DR   MassIVE; Q5VYX0; -.
DR   PaxDb; 9606-ENSP00000332530; -.
DR   PeptideAtlas; Q5VYX0; -.
DR   ProteomicsDB; 65655; -. [Q5VYX0-1]
DR   ProteomicsDB; 65656; -. [Q5VYX0-2]
DR   Pumba; Q5VYX0; -.
DR   Antibodypedia; 30183; 320 antibodies from 32 providers.
DR   DNASU; 55328; -.
DR   Ensembl; ENST00000331772.9; ENSP00000332530.4; ENSG00000184719.13. [Q5VYX0-1]
DR   Ensembl; ENST00000371947.7; ENSP00000361015.3; ENSG00000184719.13. [Q5VYX0-2]
DR   GeneID; 55328; -.
DR   KEGG; hsa:55328; -.
DR   MANE-Select; ENST00000331772.9; ENSP00000332530.4; NM_001031709.3; NP_001026879.2.
DR   UCSC; uc001kfd.3; human. [Q5VYX0-1]
DR   AGR; HGNC:25641; -.
DR   CTD; 55328; -.
DR   DisGeNET; 55328; -.
DR   GeneCards; RNLS; -.
DR   HGNC; HGNC:25641; RNLS.
DR   HPA; ENSG00000184719; Low tissue specificity.
DR   MIM; 609360; gene.
DR   neXtProt; NX_Q5VYX0; -.
DR   OpenTargets; ENSG00000184719; -.
DR   PharmGKB; PA165549084; -.
DR   VEuPathDB; HostDB:ENSG00000184719; -.
DR   eggNOG; ENOG502QUZR; Eukaryota.
DR   GeneTree; ENSGT00390000016052; -.
DR   HOGENOM; CLU_036034_1_0_1; -.
DR   InParanoid; Q5VYX0; -.
DR   OMA; ICGGDAF; -.
DR   OrthoDB; 5394503at2759; -.
DR   PhylomeDB; Q5VYX0; -.
DR   TreeFam; TF332799; -.
DR   BioCyc; MetaCyc:G66-32717-MONOMER; -.
DR   BRENDA; 1.6.3.5; 2681.
DR   PathwayCommons; Q5VYX0; -.
DR   Reactome; R-HSA-197264; Nicotinamide salvaging.
DR   SignaLink; Q5VYX0; -.
DR   BioGRID-ORCS; 55328; 11 hits in 1148 CRISPR screens.
DR   ChiTaRS; RNLS; human.
DR   GeneWiki; Renalase; -.
DR   GenomeRNAi; 55328; -.
DR   Pharos; Q5VYX0; Tbio.
DR   PRO; PR:Q5VYX0; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q5VYX0; Protein.
DR   Bgee; ENSG00000184719; Expressed in buccal mucosa cell and 155 other cell types or tissues.
DR   ExpressionAtlas; Q5VYX0; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0051379; F:epinephrine binding; IDA:UniProtKB.
DR   GO; GO:0097621; F:monoamine oxidase activity; IMP:UniProtKB.
DR   GO; GO:0070404; F:NADH binding; IDA:UniProtKB.
DR   GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IDA:UniProtKB.
DR   GO; GO:0045776; P:negative regulation of blood pressure; IDA:UniProtKB.
DR   GO; GO:0010459; P:negative regulation of heart rate; IDA:UniProtKB.
DR   GO; GO:0071871; P:response to epinephrine; IEA:Ensembl.
DR   GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
DR   GO; GO:1902074; P:response to salt; IEA:Ensembl.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR040174; RNLS.
DR   PANTHER; PTHR23357:SF1; RENALASE; 1.
DR   PANTHER; PTHR23357; UNCHARACTERIZED; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   Genevisible; Q5VYX0; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; FAD; Flavoprotein; NAD; NADP;
KW   Oxidoreductase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..342
FT                   /note="Renalase"
FT                   /id="PRO_0000019588"
FT   BINDING         12
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   BINDING         42
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   BINDING         61..62
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   VAR_SEQ         294..315
FT                   /note="TNAAANCPGQMTLHHKPFLACG -> PSAGVILGCAKSPWMMAIGFPI (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_015211"
FT   VAR_SEQ         316..342
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_015212"
FT   VARIANT         37
FT                   /note="E -> D (in dbSNP:rs2296545)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_023310"
FT   STRAND          2..7
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   HELIX           11..21
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   STRAND          28..33
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   STRAND          35..39
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   HELIX           41..43
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   STRAND          45..47
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   STRAND          55..59
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   STRAND          63..65
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   HELIX           69..72
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   HELIX           74..82
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   STRAND          103..106
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   HELIX           113..122
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   STRAND          125..129
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   STRAND          132..137
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   STRAND          139..149
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   STRAND          152..159
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   HELIX           163..166
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   HELIX           173..176
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   HELIX           179..186
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   STRAND          193..199
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   STRAND          211..214
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   STRAND          219..226
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   HELIX           227..230
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   STRAND          241..246
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   HELIX           248..253
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   TURN            254..256
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   HELIX           259..273
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   STRAND          281..288
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   STRAND          292..295
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   STRAND          298..300
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   STRAND          304..307
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   TURN            308..310
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   STRAND          311..314
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   HELIX           317..319
FT                   /evidence="ECO:0007829|PDB:3QJ4"
FT   HELIX           324..338
FT                   /evidence="ECO:0007829|PDB:3QJ4"
SQ   SEQUENCE   342 AA;  37847 MW;  952827FF7926AF48 CRC64;
     MAQVLIVGAG MTGSLCAALL RRQTSGPLYL AVWDKAEDSG GRMTTACSPH NPQCTADLGA
     QYITCTPHYA KKHQRFYDEL LAYGVLRPLS SPIEGMVMKE GDCNFVAPQG ISSIIKHYLK
     ESGAEVYFRH RVTQINLRDD KWEVSKQTGS PEQFDLIVLT MPVPEILQLQ GDITTLISEC
     QRQQLEAVSY SSRYALGLFY EAGTKIDVPW AGQYITSNPC IRFVSIDNKK RNIESSEIGP
     SLVIHTTVPF GVTYLEHSIE DVQELVFQQL ENILPGLPQP IATKCQKWRH SQVTNAAANC
     PGQMTLHHKP FLACGGDGFT QSNFDGCITS ALCVLEALKN YI
//