PM34_HUMAN
ID PM34_HUMAN Reviewed; 307 AA.
AC O43808; A8KA59; Q5TFL0; Q9UGW8; Q9UGY7;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Peroxisomal membrane protein PMP34;
DE AltName: Full=34 kDa peroxisomal membrane protein;
DE AltName: Full=Solute carrier family 25 member 17;
GN Name=SLC25A17; Synonyms=PMP34;
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].
RC TISSUE=Liver;
RX PubMed=9874197; DOI=10.1046/j.1432-1327.1998.2580332.x;
RA Wylin T., Baes M., Brees C., Mannaerts G.P., Fransen M.,
RA Van Veldhoven P.P.;
RT "Identification and characterization of human PMP34, a protein closely
RT related to the peroxisomal integral membrane protein PMP47 of Candida
RT boidinii.";
RL Eur. J. Biochem. 258:332-338(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin, and Uterus;
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 [7]
RP INTERACTION WITH PEX19.
RX PubMed=10704444; DOI=10.1083/jcb.148.5.931;
RA Sacksteder K.A., Jones J.M., South S.T., Li X., Liu Y., Gould S.J.;
RT "PEX19 binds multiple peroxisomal membrane proteins, is predominantly
RT cytoplasmic, and is required for peroxisome membrane synthesis.";
RL J. Cell Biol. 148:931-944(2000).
RN [8]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF 190-LYS--LYS-199.
RX PubMed=11121399; DOI=10.1074/jbc.m003304200;
RA Honsho M., Fujiki Y.;
RT "Topogenesis of peroxisomal membrane protein requires a short, positively
RT charged intervening-loop sequence and flanking hydrophobic segments: study
RT using human membrane protein PMP34.";
RL J. Biol. Chem. 276:9375-9382(2001).
RN [9]
RP INTERACTION WITH PEX19, TOPOLOGY, SUBCELLULAR LOCATION, AND PEROXISOMAL
RP TARGETING.
RX PubMed=11402059; DOI=10.1083/jcb.153.6.1141;
RA Jones J.M., Morrell J.C., Gould S.J.;
RT "Multiple distinct targeting signals in integral peroxisomal membrane
RT proteins.";
RL J. Cell Biol. 153:1141-1150(2001).
RN [10]
RP FUNCTION.
RX PubMed=12445829; DOI=10.1016/s0006-291x(02)02663-3;
RA Visser W.F., van Roermund C.W., Waterham H.R., Wanders R.J.;
RT "Identification of human PMP34 as a peroxisomal ATP transporter.";
RL Biochem. Biophys. Res. Commun. 299:494-497(2002).
RN [11]
RP INTERACTION WITH PEX19, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 283-LEU--PHE-285; 289-GLU-LYS-290 AND 302-LYS-GLU-303.
RX PubMed=14709540; DOI=10.1083/jcb.200304111;
RA Jones J.M., Morrell J.C., Gould S.J.;
RT "PEX19 is a predominantly cytosolic chaperone and import receptor for class
RT 1 peroxisomal membrane proteins.";
RL J. Cell Biol. 164:57-67(2004).
RN [12]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22185573; DOI=10.1042/bj20111420;
RA Agrimi G., Russo A., Scarcia P., Palmieri F.;
RT "The human gene SLC25A17 encodes a peroxisomal transporter of coenzyme A,
RT FAD and NAD+.";
RL Biochem. J. 443:241-247(2012).
CC -!- FUNCTION: Peroxisomal transporter for multiple cofactors like coenzyme
CC A (CoA), flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN)
CC and nucleotide adenosine monophosphate (AMP), and to a lesser extent
CC for nicotinamide adenine dinucleotide (NAD(+)), adenosine diphosphate
CC (ADP) and adenosine 3',5'-diphosphate (PAP). May catalyze the transport
CC of free CoA, FAD and NAD(+) from the cytosol into the peroxisomal
CC matrix by a counter-exchange mechanism. Inhibited by pyridoxal 5'-
CC phosphate and bathophenanthroline in vitro.
CC {ECO:0000269|PubMed:12445829, ECO:0000269|PubMed:22185573}.
CC -!- SUBUNIT: Interacts (via N- and C-terminus peroxisomal targeting
CC regions) with PEX19; the interaction occurs with the newly synthesized
CC SLC25A17 in the cytosol. {ECO:0000269|PubMed:10704444,
CC ECO:0000269|PubMed:11402059, ECO:0000269|PubMed:14709540}.
CC -!- INTERACTION:
CC O43808; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-594912, EBI-16439278;
CC O43808; P40855: PEX19; NbExp=4; IntAct=EBI-594912, EBI-594747;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Peroxisome membrane; Multi-pass
CC membrane protein.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in liver.
CC {ECO:0000269|PubMed:22185573}.
CC -!- DOMAIN: The N- and C-terminal portions are exposed to the cytoplasm.
CC Lacks a typical peroxisomal sorting signal. A region between helical
CC transmembrane domains (TM) 4 and 5 and TM1-TM3 or TM4-TM6 are necessary
CC for the peroxisome-targeting activity.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC -!- CAUTION: Was first identified as a peroxisomal ATP transporter
CC (PubMed:12445829). However, later experiments showed that it acts as a
CC peroxisomal transporter for multiple cofactors (PubMed:22185573).
CC {ECO:0000305|PubMed:12445829, ECO:0000305|PubMed:22185573}.
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DR EMBL; Y12860; CAA73367.1; -; mRNA.
DR EMBL; CR456577; CAG30463.1; -; mRNA.
DR EMBL; AK292924; BAF85613.1; -; mRNA.
DR EMBL; AL049764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z98048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60390.1; -; Genomic_DNA.
DR EMBL; BC005957; AAH05957.1; -; mRNA.
DR EMBL; BC012998; AAH12998.1; -; mRNA.
DR CCDS; CCDS14005.1; -.
DR RefSeq; NP_001269656.1; NM_001282727.1.
DR RefSeq; NP_006349.1; NM_006358.3.
DR AlphaFoldDB; O43808; -.
DR SMR; O43808; -.
DR BioGRID; 115741; 66.
DR IntAct; O43808; 15.
DR STRING; 9606.ENSP00000390722; -.
DR TCDB; 2.A.29.20.1; the mitochondrial carrier (mc) family.
DR GlyGen; O43808; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43808; -.
DR PhosphoSitePlus; O43808; -.
DR BioMuta; SLC25A17; -.
DR EPD; O43808; -.
DR jPOST; O43808; -.
DR MassIVE; O43808; -.
DR MaxQB; O43808; -.
DR PaxDb; O43808; -.
DR PeptideAtlas; O43808; -.
DR PRIDE; O43808; -.
DR ProteomicsDB; 49175; -.
DR Antibodypedia; 26801; 105 antibodies from 23 providers.
DR DNASU; 10478; -.
DR Ensembl; ENST00000435456.7; ENSP00000390722.2; ENSG00000100372.15.
DR GeneID; 10478; -.
DR KEGG; hsa:10478; -.
DR MANE-Select; ENST00000435456.7; ENSP00000390722.2; NM_006358.4; NP_006349.1.
DR UCSC; uc003azc.5; human.
DR CTD; 10478; -.
DR DisGeNET; 10478; -.
DR GeneCards; SLC25A17; -.
DR HGNC; HGNC:10987; SLC25A17.
DR HPA; ENSG00000100372; Low tissue specificity.
DR MIM; 606795; gene.
DR neXtProt; NX_O43808; -.
DR OpenTargets; ENSG00000100372; -.
DR PharmGKB; PA35863; -.
DR VEuPathDB; HostDB:ENSG00000100372; -.
DR eggNOG; KOG0769; Eukaryota.
DR GeneTree; ENSGT00920000149129; -.
DR InParanoid; O43808; -.
DR OMA; YEWTRSF; -.
DR OrthoDB; 1186395at2759; -.
DR PhylomeDB; O43808; -.
DR TreeFam; TF324772; -.
DR PathwayCommons; O43808; -.
DR Reactome; R-HSA-389599; Alpha-oxidation of phytanate.
DR Reactome; R-HSA-9603798; Class I peroxisomal membrane protein import.
DR SignaLink; O43808; -.
DR BioGRID-ORCS; 10478; 8 hits in 1077 CRISPR screens.
DR ChiTaRS; SLC25A17; human.
DR GeneWiki; SLC25A17; -.
DR GenomeRNAi; 10478; -.
DR Pharos; O43808; Tbio.
DR PRO; PR:O43808; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O43808; protein.
DR Bgee; ENSG00000100372; Expressed in left ovary and 184 other tissues.
DR ExpressionAtlas; O43808; baseline and differential.
DR Genevisible; O43808; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:BHF-UCL.
DR GO; GO:0000295; F:adenine nucleotide transmembrane transporter activity; TAS:Reactome.
DR GO; GO:0015217; F:ADP transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0080122; F:AMP transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005347; F:ATP transmembrane transporter activity; IGI:BHF-UCL.
DR GO; GO:0051087; F:chaperone binding; IPI:BHF-UCL.
DR GO; GO:0015228; F:coenzyme A transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015230; F:FAD transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0044610; F:FMN transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0051724; F:NAD transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015867; P:ATP transport; IGI:BHF-UCL.
DR GO; GO:0001561; P:fatty acid alpha-oxidation; TAS:Reactome.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IGI:BHF-UCL.
DR GO; GO:0015908; P:fatty acid transport; IGI:BHF-UCL.
DR Gene3D; 1.50.40.10; -; 2.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Cytoplasm; Membrane; Peroxisome; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..307
FT /note="Peroxisomal membrane protein PMP34"
FT /id="PRO_0000090705"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT TRANSMEM 10..30
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..66
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..160
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..280
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..307
FT /note="Cytoplasmic"
FT REPEAT 7..92
FT /note="Solcar 1"
FT REPEAT 99..192
FT /note="Solcar 2"
FT REPEAT 200..294
FT /note="Solcar 3"
FT REGION 1..147
FT /note="Necessary for targeting to peroxisomes and
FT interaction with PEX19"
FT REGION 244..307
FT /note="Necessary for targeting to peroxisomes and
FT interaction with PEX19"
FT MOTIF 190..199
FT /note="Peroxisome localization signal"
FT VARIANT 98
FT /note="H -> R (in dbSNP:rs12159334)"
FT /id="VAR_050139"
FT MUTAGEN 190..199
FT /note="KRQLLKKRMK->AAQLLAAAMA: Localizes in the cytoplasm."
FT /evidence="ECO:0000269|PubMed:11121399"
FT MUTAGEN 283..285
FT /note="LMF->KKK: Impairs interaction with PEX19."
FT /evidence="ECO:0000269|PubMed:14709540"
FT MUTAGEN 289..290
FT /note="EK->LL: Impairs interaction with PEX19."
FT /evidence="ECO:0000269|PubMed:14709540"
FT MUTAGEN 302..303
FT /note="KR->EE: No effect on interaction with PEX19."
FT /evidence="ECO:0000269|PubMed:14709540"
SQ SEQUENCE 307 AA; 34567 MW; B7043D82966D47A5 CRC64;
MASVLSYESL VHAVAGAVGS VTAMTVFFPL DTARLRLQVD EKRKSKTTHM VLLEIIKEEG
LLAPYRGWFP VISSLCCSNF VYFYTFNSLK ALWVKGQHST TGKDLVVGFV AGVVNVLLTT
PLWVVNTRLK LQGAKFRNED IVPTNYKGII DAFHQIIRDE GISALWNGTF PSLLLVFNPA
IQFMFYEGLK RQLLKKRMKL SSLDVFIIGA VAKAIATTVT YPLQTVQSIL RFGRHRLNPE
NRTLGSLRNI LYLLHQRVRR FGIMGLYKGL EAKLLQTVLT AALMFLVYEK LTAATFTVMG
LKRAHQH
