CYAC3_HUMAN
ID CYAC3_HUMAN Reviewed; 242 AA.
AC Q8NBI2; B3KPU2; B4DLN9; J3KQH4; Q6PK96;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Lysosomal membrane ascorbate-dependent ferrireductase CYB561A3 {ECO:0000305};
DE EC=7.2.1.3 {ECO:0000250|UniProtKB:Q6P1H1};
DE AltName: Full=Cytochrome b ascorbate-dependent protein 3 {ECO:0000312|HGNC:HGNC:23014};
DE AltName: Full=Cytochrome b561 family member A3 {ECO:0000312|HGNC:HGNC:23014};
DE AltName: Full=Lysosomal cytochrome b {ECO:0000250|UniProtKB:Q6P1H1};
DE Short=LCytb {ECO:0000250|UniProtKB:Q6P1H1};
GN Name=CYB561A3 {ECO:0000312|HGNC:HGNC:23014};
GN Synonyms=CYBASC3 {ECO:0000312|HGNC:HGNC:23014}; ORFNames=PSEC0259;
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=Blood, and 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 MRNA] (ISOFORM 1).
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Lymph, and Pancreas;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Placenta;
RX PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H.,
RA Elsaesser H.-P., Mann M., Hasilik A.;
RT "Integral and associated lysosomal membrane proteins.";
RL Traffic 8:1676-1686(2007).
CC -!- FUNCTION: Transmembrane reductase that uses ascorbate as an electron
CC donor in the cytoplasm and transfers electrons across membranes to
CC reduce iron cations Fe(3+) into Fe(2+) in the lumen of the late
CC endosome and lysosome. Reduced iron can then be extruded from the late
CC endosome and lysosome to the cytoplasm by divalent metal-specific
CC transporters. It is therefore most probably involved in endosomal and
CC lysosomal cellular iron homeostasis. {ECO:0000250|UniProtKB:Q6P1H1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fe(3+)(out) + L-ascorbate(in) = Fe(2+)(out) + H(+) +
CC monodehydro-L-ascorbate radical(in); Xref=Rhea:RHEA:30403,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:59513; EC=7.2.1.3;
CC Evidence={ECO:0000250|UniProtKB:Q6P1H1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30404;
CC Evidence={ECO:0000250|UniProtKB:Q6P1H1};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:Q53TN4};
CC Note=Binds 2 heme b groups non-covalently.
CC {ECO:0000250|UniProtKB:Q53TN4};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q53TN4}.
CC -!- INTERACTION:
CC Q8NBI2; Q9NUQ2: AGPAT5; NbExp=3; IntAct=EBI-10269179, EBI-6916385;
CC Q8NBI2; Q13520: AQP6; NbExp=3; IntAct=EBI-10269179, EBI-13059134;
CC Q8NBI2; P25942: CD40; NbExp=3; IntAct=EBI-10269179, EBI-525714;
CC Q8NBI2; P11912: CD79A; NbExp=3; IntAct=EBI-10269179, EBI-7797864;
CC Q8NBI2; O00501: CLDN5; NbExp=3; IntAct=EBI-10269179, EBI-18400628;
CC Q8NBI2; O95471: CLDN7; NbExp=3; IntAct=EBI-10269179, EBI-740744;
CC Q8NBI2; Q68CJ9: CREB3L3; NbExp=3; IntAct=EBI-10269179, EBI-852194;
CC Q8NBI2; Q08426: EHHADH; NbExp=3; IntAct=EBI-10269179, EBI-2339219;
CC Q8NBI2; O15552: FFAR2; NbExp=3; IntAct=EBI-10269179, EBI-2833872;
CC Q8NBI2; Q96P66: GPR101; NbExp=3; IntAct=EBI-10269179, EBI-17935713;
CC Q8NBI2; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-10269179, EBI-13345167;
CC Q8NBI2; O60883: GPR37L1; NbExp=3; IntAct=EBI-10269179, EBI-2927498;
CC Q8NBI2; Q8TED1: GPX8; NbExp=3; IntAct=EBI-10269179, EBI-11721746;
CC Q8NBI2; Q9BSE4: HERPUD2; NbExp=3; IntAct=EBI-10269179, EBI-2868124;
CC Q8NBI2; P26715: KLRC1; NbExp=3; IntAct=EBI-10269179, EBI-9018187;
CC Q8NBI2; Q86VI4: LAPTM4B; NbExp=3; IntAct=EBI-10269179, EBI-3267258;
CC Q8NBI2; P15151: PVR; NbExp=3; IntAct=EBI-10269179, EBI-3919694;
CC Q8NBI2; Q96GF1: RNF185; NbExp=3; IntAct=EBI-10269179, EBI-2340249;
CC Q8NBI2; Q99942: RNF5; NbExp=6; IntAct=EBI-10269179, EBI-348482;
CC Q8NBI2; Q3SXP7: SHISAL1; NbExp=3; IntAct=EBI-10269179, EBI-18037857;
CC Q8NBI2; Q96CE8: TM4SF18; NbExp=3; IntAct=EBI-10269179, EBI-13351685;
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000250|UniProtKB:Q6P1H1}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q53TN4}. Lysosome membrane
CC {ECO:0000269|PubMed:17897319}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q53TN4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NBI2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NBI2-2; Sequence=VSP_047358;
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6P1H1}.
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DR EMBL; AK056751; BAG51804.1; -; mRNA.
DR EMBL; AK075559; BAC11698.1; -; mRNA.
DR EMBL; AK297084; BAG59601.1; -; mRNA.
DR EMBL; AP003108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW73941.1; -; Genomic_DNA.
DR EMBL; CH471076; EAW73942.1; -; Genomic_DNA.
DR EMBL; BC004391; AAH04391.1; -; mRNA.
DR EMBL; BC014045; AAH14045.2; -; mRNA.
DR EMBL; BC047710; AAH47710.1; -; mRNA.
DR CCDS; CCDS53639.1; -. [Q8NBI2-2]
DR CCDS; CCDS8004.1; -. [Q8NBI2-1]
DR RefSeq; NP_001154924.1; NM_001161452.1. [Q8NBI2-1]
DR RefSeq; NP_001154926.1; NM_001161454.1. [Q8NBI2-2]
DR RefSeq; NP_001287692.1; NM_001300763.1.
DR RefSeq; NP_705839.3; NM_153611.4. [Q8NBI2-1]
DR AlphaFoldDB; Q8NBI2; -.
DR SMR; Q8NBI2; -.
DR BioGRID; 128617; 24.
DR IntAct; Q8NBI2; 21.
DR STRING; 9606.ENSP00000389745; -.
DR GlyGen; Q8NBI2; 1 site.
DR BioMuta; CYB561A3; -.
DR DMDM; 74730147; -.
DR jPOST; Q8NBI2; -.
DR MassIVE; Q8NBI2; -.
DR MaxQB; Q8NBI2; -.
DR PaxDb; Q8NBI2; -.
DR PeptideAtlas; Q8NBI2; -.
DR PRIDE; Q8NBI2; -.
DR ProteomicsDB; 72770; -. [Q8NBI2-1]
DR Antibodypedia; 52925; 7 antibodies from 6 providers.
DR DNASU; 220002; -.
DR Ensembl; ENST00000294072.9; ENSP00000294072.4; ENSG00000162144.10. [Q8NBI2-1]
DR Ensembl; ENST00000426130.6; ENSP00000398979.2; ENSG00000162144.10. [Q8NBI2-2]
DR Ensembl; ENST00000536915.5; ENSP00000437390.1; ENSG00000162144.10. [Q8NBI2-1]
DR GeneID; 220002; -.
DR KEGG; hsa:220002; -.
DR MANE-Select; ENST00000294072.9; ENSP00000294072.4; NM_153611.6; NP_705839.3.
DR UCSC; uc001nrg.4; human. [Q8NBI2-1]
DR CTD; 220002; -.
DR GeneCards; CYB561A3; -.
DR HGNC; HGNC:23014; CYB561A3.
DR HPA; ENSG00000162144; Tissue enhanced (adrenal).
DR MIM; 618757; gene.
DR neXtProt; NX_Q8NBI2; -.
DR OpenTargets; ENSG00000162144; -.
DR PharmGKB; PA134880796; -.
DR VEuPathDB; HostDB:ENSG00000162144; -.
DR eggNOG; KOG1619; Eukaryota.
DR GeneTree; ENSGT00950000183197; -.
DR InParanoid; Q8NBI2; -.
DR OMA; FAWDGSI; -.
DR OrthoDB; 1503869at2759; -.
DR PhylomeDB; Q8NBI2; -.
DR TreeFam; TF314222; -.
DR PathwayCommons; Q8NBI2; -.
DR SignaLink; Q8NBI2; -.
DR BioGRID-ORCS; 220002; 21 hits in 1079 CRISPR screens.
DR ChiTaRS; CYB561A3; human.
DR GenomeRNAi; 220002; -.
DR Pharos; Q8NBI2; Tdark.
DR PRO; PR:Q8NBI2; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8NBI2; protein.
DR Bgee; ENSG00000162144; Expressed in right adrenal gland and 174 other tissues.
DR ExpressionAtlas; Q8NBI2; baseline and differential.
DR Genevisible; Q8NBI2; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0140571; F:transmembrane ascorbate ferrireductase activity; ISS:UniProtKB.
DR GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR InterPro; IPR043205; CYB561/CYBRD1-like.
DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR PANTHER; PTHR10106; PTHR10106; 1.
DR Pfam; PF03188; Cytochrom_B561; 1.
DR SMART; SM00665; B561; 1.
DR PROSITE; PS50939; CYTOCHROME_B561; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Electron transport; Endosome; Glycoprotein; Heme;
KW Iron; Lysosome; Membrane; Metal-binding; Oxidoreductase;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..242
FT /note="Lysosomal membrane ascorbate-dependent
FT ferrireductase CYB561A3"
FT /id="PRO_0000314838"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..45
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..119
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..202
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT DOMAIN 12..219
FT /note="Cytochrome b561"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT BINDING 47
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 67
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 76
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 80
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 83
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 112..115
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 117
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 149
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 156
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 177
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 224
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1
FT /note="M -> MGKNFSDSFLSRECVIRM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047358"
FT CONFLICT 122
FT /note="I -> T (in Ref. 5; AAH04391)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="I -> N (in Ref. 1; BAG59601)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 242 AA; 27214 MW; 1D0C4904CEAED747 CRC64;
MVSGRFYLSC LLLGSLGSMC ILFTIYWMQY WRGGFAWNGS IYMFNWHPVL MVAGMVVFYG
GASLVYRLPQ SWVGPKLPWK LLHAALHLMA FVLTVVGLVA VFTFHNHGRT ANLYSLHSWL
GITTVFLFAC QWFLGFAVFL LPWASMWLRS LLKPIHVFFG AAILSLSIAS VISGINEKLF
FSLKNTTRPY HSLPSEAVFA NSTGMLVVAF GLLVLYILLA SSWKRPEPGI LTDRQPLLHD
GE
