MCAT_HUMAN
ID MCAT_HUMAN Reviewed; 301 AA.
AC O43772; B2R7F4; Q9UIQ2;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Mitochondrial carnitine/acylcarnitine carrier protein {ECO:0000305};
DE AltName: Full=Carnitine/acylcarnitine translocase {ECO:0000303|PubMed:12892634};
DE Short=CAC {ECO:0000303|PubMed:18307102};
DE Short=CACT {ECO:0000303|PubMed:12892634};
DE AltName: Full=Solute carrier family 25 member 20;
GN Name=SLC25A20 {ECO:0000312|HGNC:HGNC:1421}; Synonyms=CAC, CACT;
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], AND DISEASE.
RC TISSUE=Liver;
RX PubMed=9399886; DOI=10.1086/301628;
RA Huizing M., Iacobazzi V., Ijlst L., Savelkoul P., Ruitenbeek W.,
RA van den Heuvel L., Indiveri C., Smeitink J., Trijbels F., Wanders R.,
RA Palmieri F.;
RT "Cloning of the human carnitine-acylcarnitine carrier cDNA and
RT identification of the molecular defect in a patient.";
RL Am. J. Hum. Genet. 61:1239-1245(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9837782; DOI=10.1006/bbrc.1998.9738;
RA Iacobazzi V., Naglieri M.A., Stanley C.A., Wanders R.J.A., Palmieri F.;
RT "The structure and organization of the human carnitine/acylcarnitine
RT translocase (CACT) gene.";
RL Biochem. Biophys. Res. Commun. 252:770-774(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 MRNA].
RC TISSUE=Skin;
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 TRANSPORT ACTIVITY.
RX PubMed=12892634; DOI=10.1016/s1087-1845(03)00049-5;
RA Perez P., Martinez O., Romero B., Olivas I., Pedregosa A.M., Palmieri F.,
RA Laborda F., Ramon De Lucas J.;
RT "Functional analysis of mutations in the human carnitine/acylcarnitine
RT translocase in Aspergillus nidulans.";
RL Fungal Genet. Biol. 39:211-220(2003).
RN [6]
RP FUNCTION, AND TRANSPORT ACTIVITY.
RX PubMed=18307102; DOI=10.1080/09687680701697476;
RA De Lucas J.R., Indiveri C., Tonazzi A., Perez P., Giangregorio N.,
RA Iacobazzi V., Palmieri F.;
RT "Functional characterization of residues within the carnitine/acylcarnitine
RT translocase RX2PANAAXF distinct motif.";
RL Mol. Membr. Biol. 25:152-163(2008).
RN [7]
RP FUNCTION, AND TRANSPORT ACTIVITY.
RX PubMed=20347717; DOI=10.1016/j.bbabio.2010.03.017;
RA Giangregorio N., Tonazzi A., Console L., Indiveri C., Palmieri F.;
RT "Site-directed mutagenesis of charged amino acids of the human
RT mitochondrial carnitine/acylcarnitine carrier: insight into the molecular
RT mechanism of transport.";
RL Biochim. Biophys. Acta 1797:839-845(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [11]
RP VARIANT CACTD ARG-238.
RX PubMed=12859414; DOI=10.1034/j.1399-0004.2003.00117.x;
RA Al-Aqeel A.I., Rashid M.S., Ruiter J.P., Ijlst L., Wanders R.J.A.;
RT "A novel molecular defect of the carnitine acylcarnitine translocase gene
RT in a Saudi patient.";
RL Clin. Genet. 64:163-165(2003).
RN [12]
RP VARIANT CACTD ARG-238.
RX PubMed=15057979; DOI=10.1002/ajmg.a.20573;
RA Iacobazzi V., Pasquali M., Singh R., Matern D., Rinaldo P.,
RA Amat di San Filippo C., Palmieri F., Longo N.;
RT "Response to therapy in carnitine/acylcarnitine translocase (CACT)
RT deficiency due to a novel missense mutation.";
RL Am. J. Med. Genet. A 126:150-155(2004).
RN [13]
RP VARIANTS CACTD TRP-133 AND HIS-231.
RX PubMed=15365988; DOI=10.1002/humu.20085;
RA Iacobazzi V., Invernizzi F., Baratta S., Pons R., Chung W., Garavaglia B.,
RA Dionisi-Vici C., Ribes A., Parini R., Huertas M.D., Roldan S., Lauria G.,
RA Palmieri F., Taroni F.;
RT "Molecular and functional analysis of SLC25A20 mutations causing carnitine-
RT acylcarnitine translocase deficiency.";
RL Hum. Mutat. 24:312-320(2004).
CC -!- FUNCTION: Mediates the electroneutral exchange of acylcarnitines (O-
CC acyl-(R)-carnitine or L-acylcarnitine) of different acyl chain lengths
CC (ranging from O-acetyl-(R)-carnitine to long-chain O-acyl-(R)-
CC carnitines) with free carnitine ((R)-carnitine or L-carnitine) across
CC the mitochondrial inner membrane, via a ping-pong mechanism
CC (PubMed:12892634, PubMed:18307102) (Probable). Key player in the
CC mitochondrial oxidation pathway, it translocates the fatty acids in the
CC form of acylcarnitines into the mitochondrial matrix, where the
CC carnitine palmitoyltransferase 2 (CPT-2) activates them to undergo
CC fatty acid beta-oxidation (Probable). Catalyzes the unidirectional
CC transport (uniport) of carnitine at lower rates than the antiport
CC (exchange) (PubMed:18307102). {ECO:0000269|PubMed:12892634,
CC ECO:0000269|PubMed:18307102, ECO:0000305|PubMed:18307102,
CC ECO:0000305|PubMed:20347717}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine(out) + O-acetyl-(R)-carnitine(in) = (R)-
CC carnitine(in) + O-acetyl-(R)-carnitine(out); Xref=Rhea:RHEA:49908,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:57589;
CC Evidence={ECO:0000269|PubMed:12892634, ECO:0000269|PubMed:18307102};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine(out) + O-acyl-(R)-carnitine(in) = (R)-
CC carnitine(in) + O-acyl-(R)-carnitine(out); Xref=Rhea:RHEA:49924,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:75659;
CC Evidence={ECO:0000305|PubMed:12892634, ECO:0000305|PubMed:18307102,
CC ECO:0000305|PubMed:20347717};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine(out) + O-propanoyl-(R)-carnitine(in) = (R)-
CC carnitine(in) + O-propanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:49912,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:53210;
CC Evidence={ECO:0000250|UniProtKB:P97521};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine(out) + O-hexadecanoyl-(R)-carnitine(in) = (R)-
CC carnitine(in) + O-hexadecanoyl-(R)-carnitine(out);
CC Xref=Rhea:RHEA:49916, ChEBI:CHEBI:16347, ChEBI:CHEBI:17490;
CC Evidence={ECO:0000250|UniProtKB:P97521};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine(out) + O-octanoyl-(R)-carnitine(in) = (R)-
CC carnitine(in) + O-octanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:49920,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:18102;
CC Evidence={ECO:0000250|UniProtKB:P97521};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine(in) = (R)-carnitine(out); Xref=Rhea:RHEA:34959,
CC ChEBI:CHEBI:16347; Evidence={ECO:0000269|PubMed:18307102};
CC -!- INTERACTION:
CC O43772; P13473-2: LAMP2; NbExp=3; IntAct=EBI-727085, EBI-21591415;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein.
CC -!- DISEASE: Carnitine-acylcarnitine translocase deficiency (CACTD)
CC [MIM:212138]: A rare long-chain fatty acid oxidation disorder.
CC Metabolic consequences include hypoketotic hypoglycemia under fasting
CC conditions, hyperammonemia, elevated creatine kinase and transaminases,
CC dicarboxylic aciduria, very low free carnitine and abnormal
CC acylcarnitine profile with marked elevation of the long-chain
CC acylcarnitines. Clinical features include neurologic abnormalities,
CC cardiomyopathy, arrhythmias, skeletal muscle damage, liver dysfunction
CC and episodes of life-threatening coma, which eventually lead to death.
CC Most patients become symptomatic in the neonatal period with a rapidly
CC progressive deterioration and a high mortality rate.
CC {ECO:0000269|PubMed:12859414, ECO:0000269|PubMed:15057979,
CC ECO:0000269|PubMed:15365988}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; Y10319; CAA71367.1; -; mRNA.
DR EMBL; Y17775; CAB55356.1; -; Genomic_DNA.
DR EMBL; Y17776; CAB55356.1; JOINED; Genomic_DNA.
DR EMBL; Y17777; CAB55356.1; JOINED; Genomic_DNA.
DR EMBL; Y17778; CAB55356.1; JOINED; Genomic_DNA.
DR EMBL; Y17779; CAB55356.1; JOINED; Genomic_DNA.
DR EMBL; AK312962; BAG35801.1; -; mRNA.
DR EMBL; BC001689; AAH01689.1; -; mRNA.
DR CCDS; CCDS2779.1; -.
DR RefSeq; NP_000378.1; NM_000387.5.
DR AlphaFoldDB; O43772; -.
DR SMR; O43772; -.
DR BioGRID; 107241; 64.
DR IntAct; O43772; 16.
DR STRING; 9606.ENSP00000326305; -.
DR BindingDB; O43772; -.
DR ChEMBL; CHEMBL2216740; -.
DR DrugBank; DB00583; Levocarnitine.
DR TCDB; 2.A.29.8.3; the mitochondrial carrier (mc) family.
DR iPTMnet; O43772; -.
DR PhosphoSitePlus; O43772; -.
DR SwissPalm; O43772; -.
DR BioMuta; SLC25A20; -.
DR EPD; O43772; -.
DR jPOST; O43772; -.
DR MassIVE; O43772; -.
DR MaxQB; O43772; -.
DR PaxDb; O43772; -.
DR PeptideAtlas; O43772; -.
DR PRIDE; O43772; -.
DR ProteomicsDB; 49166; -.
DR TopDownProteomics; O43772; -.
DR Antibodypedia; 3111; 226 antibodies from 27 providers.
DR DNASU; 788; -.
DR Ensembl; ENST00000319017.5; ENSP00000326305.4; ENSG00000178537.10.
DR GeneID; 788; -.
DR KEGG; hsa:788; -.
DR MANE-Select; ENST00000319017.5; ENSP00000326305.4; NM_000387.6; NP_000378.1.
DR UCSC; uc003cva.5; human.
DR CTD; 788; -.
DR DisGeNET; 788; -.
DR GeneCards; SLC25A20; -.
DR HGNC; HGNC:1421; SLC25A20.
DR HPA; ENSG00000178537; Tissue enhanced (liver).
DR MalaCards; SLC25A20; -.
DR MIM; 212138; phenotype.
DR MIM; 613698; gene.
DR neXtProt; NX_O43772; -.
DR OpenTargets; ENSG00000178537; -.
DR Orphanet; 159; Carnitine-acylcarnitine translocase deficiency.
DR PharmGKB; PA35031; -.
DR VEuPathDB; HostDB:ENSG00000178537; -.
DR eggNOG; KOG0758; Eukaryota.
DR GeneTree; ENSGT00940000157863; -.
DR HOGENOM; CLU_015166_16_0_1; -.
DR InParanoid; O43772; -.
DR OMA; QYTIGQI; -.
DR OrthoDB; 1072378at2759; -.
DR PhylomeDB; O43772; -.
DR TreeFam; TF300894; -.
DR BioCyc; MetaCyc:ENSG00000178537-MON; -.
DR PathwayCommons; O43772; -.
DR Reactome; R-HSA-200425; Carnitine metabolism.
DR SignaLink; O43772; -.
DR SIGNOR; O43772; -.
DR BioGRID-ORCS; 788; 14 hits in 1080 CRISPR screens.
DR ChiTaRS; SLC25A20; human.
DR GenomeRNAi; 788; -.
DR Pharos; O43772; Tbio.
DR PRO; PR:O43772; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O43772; protein.
DR Bgee; ENSG00000178537; Expressed in right lobe of liver and 194 other tissues.
DR ExpressionAtlas; O43772; baseline and differential.
DR Genevisible; O43772; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005740; C:mitochondrial envelope; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0015227; F:acyl carnitine transmembrane transporter activity; EXP:Reactome.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006853; P:carnitine shuttle; TAS:Reactome.
DR GO; GO:1902603; P:carnitine transmembrane transport; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0006839; P:mitochondrial transport; IBA:GO_Central.
DR Gene3D; 1.50.40.10; -; 2.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Acetylation; Disease variant; Lipid transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..301
FT /note="Mitochondrial carnitine/acylcarnitine carrier
FT protein"
FT /id="PRO_0000090628"
FT TOPO_DOM 2..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..31
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..73
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..93
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..170
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..190
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..230
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..267
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..287
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 8..99
FT /note="Solcar 1"
FT REPEAT 108..196
FT /note="Solcar 2"
FT REPEAT 207..293
FT /note="Solcar 3"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:25944712"
FT MOD_RES 148
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2Z6"
FT MOD_RES 157
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2Z6"
FT MOD_RES 170
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2Z6"
FT MOD_RES 170
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2Z6"
FT VARIANT 133
FT /note="R -> W (in CACTD; dbSNP:rs748394731)"
FT /evidence="ECO:0000269|PubMed:15365988"
FT /id="VAR_021818"
FT VARIANT 231
FT /note="D -> H (in CACTD; dbSNP:rs577331691)"
FT /evidence="ECO:0000269|PubMed:15365988"
FT /id="VAR_021819"
FT VARIANT 238
FT /note="Q -> R (in CACTD; dbSNP:rs28934589)"
FT /evidence="ECO:0000269|PubMed:12859414,
FT ECO:0000269|PubMed:15057979"
FT /id="VAR_021820"
FT CONFLICT 203
FT /note="R -> S (in Ref. 2; CAB55356)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="A -> G (in Ref. 2; CAB55356)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 301 AA; 32944 MW; AEB34E4E335102B0 CRC64;
MADQPKPISP LKNLLAGGFG GVCLVFVGHP LDTVKVRLQT QPPSLPGQPP MYSGTFDCFR
KTLFREGITG LYRGMAAPII GVTPMFAVCF FGFGLGKKLQ QKHPEDVLSY PQLFAAGMLS
GVFTTGIMTP GERIKCLLQI QASSGESKYT GTLDCAKKLY QEFGIRGIYK GTVLTLMRDV
PASGMYFMTY EWLKNIFTPE GKRVSELSAP RILVAGGIAG IFNWAVAIPP DVLKSRFQTA
PPGKYPNGFR DVLRELIRDE GVTSLYKGFN AVMIRAFPAN AACFLGFEVA MKFLNWATPN
L
