ID GATB_HUMAN Reviewed; 557 AA.
AC O75879; Q4W5M8; Q53GP4; Q9P0S6; Q9Y2B8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 27-MAR-2024, entry version 183.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03147};
DE Short=Glu-AdT subunit B {ECO:0000255|HAMAP-Rule:MF_03147};
DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_03147};
DE AltName: Full=Cytochrome c oxidase assembly factor PET112 homolog;
DE Flags: Precursor;
GN Name=GATB {ECO:0000255|HAMAP-Rule:MF_03147, ECO:0000312|HGNC:HGNC:8849};
GN Synonyms=PET112 {ECO:0000255|HAMAP-Rule:MF_03147},
GN PET112L {ECO:0000255|HAMAP-Rule:MF_03147}; ORFNames=HSPC199;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9878253; DOI=10.1006/geno.1998.5580;
RA Petruzzella V., Tiranti V., Fernandez P., Ianna P., Carrozzo R.,
RA Zeviani M.;
RT "Identification and characterization of human cDNAs specific to BCS1,
RT PET112, SCO1, COX15, and COX11, five genes involved in the formation and
RT function of the mitochondrial respiratory chain.";
RL Genomics 54:494-504(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
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=Kidney;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-557.
RC TISSUE=Periodontal ligament;
RA Yamamoto T., Takashiba S., Myokai F., Washio N., Nishimura F., Arai H.,
RA Murayama Y.;
RT "Unique genes expressed in fibroblasts of periodontal ligament.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION.
RX PubMed=19805282; DOI=10.1073/pnas.0907602106;
RA Nagao A., Suzuki T., Katoh T., Sakaguchi Y., Suzuki T.;
RT "Biogenesis of glutaminyl-mt tRNAGln in human mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16209-16214(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 INVOLVEMENT IN COXPD41, VARIANT COXPD41 LEU-136, AND CHARACTERIZATION OF
RP VARIANT COXPD41 LEU-136.
RX PubMed=30283131; DOI=10.1038/s41467-018-06250-w;
RA Friederich M.W., Timal S., Powell C.A., Dallabona C., Kurolap A.,
RA Palacios-Zambrano S., Bratkovic D., Derks T.G.J., Bick D., Bouman K.,
RA Chatfield K.C., Damouny-Naoum N., Dishop M.K., Falik-Zaccai T.C., Fares F.,
RA Fedida A., Ferrero I., Gallagher R.C., Garesse R., Gilberti M.,
RA Gonzalez C., Gowan K., Habib C., Halligan R.K., Kalfon L., Knight K.,
RA Lefeber D., Mamblona L., Mandel H., Mory A., Ottoson J., Paperna T.,
RA Pruijn G.J.M., Rebelo-Guiomar P.F., Saada A., Sainz B. Jr., Salvemini H.,
RA Schoots M.H., Smeitink J.A., Szukszto M.J., Ter Horst H.J.,
RA van den Brandt F., van Spronsen F.J., Veltman J.A., Wartchow E.,
RA Wintjes L.T., Zohar Y., Fernandez-Moreno M.A., Baris H.N., Donnini C.,
RA Minczuk M., Rodenburg R.J., Van Hove J.L.K.;
RT "Pathogenic variants in glutamyl-tRNAGln amidotransferase subunits cause a
RT lethal mitochondrial cardiomyopathy disorder.";
RL Nat. Commun. 9:4065-4065(2018).
CC -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC through the transamidation of misacylated Glu-tRNA(Gln) in the
CC mitochondria. The reaction takes place in the presence of glutamine and
CC ATP through an activated gamma-phospho-Glu-tRNA(Gln).
CC {ECO:0000255|HAMAP-Rule:MF_03147, ECO:0000269|PubMed:19805282}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) +
CC L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate;
CC Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03147};
CC -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT)
CC complex, composed of A (QRSL1), B (GATB) and C (GATC) subunits.
CC -!- INTERACTION:
CC O75879; Q9H0R6: QRSL1; NbExp=2; IntAct=EBI-6137441, EBI-2856796;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03147,
CC ECO:0000269|PubMed:9878253}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in tissues characterized by
CC high rates of oxidative phosphorylation (OxPhos), including muscle and
CC heart. {ECO:0000269|PubMed:9878253}.
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 41 (COXPD41)
CC [MIM:618838]: An autosomal recessive mitochondrial disorder
CC characterized by prenatal onset, fetal hydrops, intrauterine growth
CC retardation, hypertrophic cardiomyopathy, respiratory insufficiency,
CC lactic acidosis, and decreased activities of mitochondrial respiratory
CC complexes I, III, IV, and V. The disorder is lethal, with death
CC occurring in the perinatal period. {ECO:0000269|PubMed:30283131}.
CC Note=The disease may be caused by variants affecting the gene
CC represented in this entry.
CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03147}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF36119.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF026851; AAD08640.1; -; mRNA.
DR EMBL; AF151033; AAF36119.1; ALT_FRAME; mRNA.
DR EMBL; AK312957; BAG35796.1; -; mRNA.
DR EMBL; AK222887; BAD96607.1; -; mRNA.
DR EMBL; AC092611; AAY40897.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04981.1; -; Genomic_DNA.
DR EMBL; BC130348; AAI30349.1; -; mRNA.
DR EMBL; BC136547; AAI36548.1; -; mRNA.
DR EMBL; AB019410; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS3776.1; -.
DR RefSeq; NP_004555.1; NM_004564.2.
DR AlphaFoldDB; O75879; -.
DR SMR; O75879; -.
DR BioGRID; 111211; 140.
DR ComplexPortal; CPX-6174; Mitochondrial glutamyl-tRNA(Gln) amidotransferase complex.
DR CORUM; O75879; -.
DR DIP; DIP-48968N; -.
DR IntAct; O75879; 20.
DR MINT; O75879; -.
DR STRING; 9606.ENSP00000263985; -.
DR DrugBank; DB00130; L-Glutamine.
DR iPTMnet; O75879; -.
DR PhosphoSitePlus; O75879; -.
DR SwissPalm; O75879; -.
DR BioMuta; GATB; -.
DR EPD; O75879; -.
DR jPOST; O75879; -.
DR MassIVE; O75879; -.
DR PaxDb; 9606-ENSP00000263985; -.
DR PeptideAtlas; O75879; -.
DR ProteomicsDB; 50235; -.
DR Pumba; O75879; -.
DR Antibodypedia; 27767; 155 antibodies from 20 providers.
DR DNASU; 5188; -.
DR Ensembl; ENST00000263985.11; ENSP00000263985.6; ENSG00000059691.12.
DR GeneID; 5188; -.
DR KEGG; hsa:5188; -.
DR MANE-Select; ENST00000263985.11; ENSP00000263985.6; NM_004564.3; NP_004555.1.
DR UCSC; uc003iml.5; human.
DR AGR; HGNC:8849; -.
DR CTD; 5188; -.
DR DisGeNET; 5188; -.
DR GeneCards; GATB; -.
DR HGNC; HGNC:8849; GATB.
DR HPA; ENSG00000059691; Low tissue specificity.
DR MalaCards; GATB; -.
DR MIM; 603645; gene.
DR MIM; 618838; phenotype.
DR neXtProt; NX_O75879; -.
DR OpenTargets; ENSG00000059691; -.
DR PharmGKB; PA33191; -.
DR VEuPathDB; HostDB:ENSG00000059691; -.
DR eggNOG; KOG2438; Eukaryota.
DR GeneTree; ENSGT00390000016644; -.
DR HOGENOM; CLU_019240_0_1_1; -.
DR InParanoid; O75879; -.
DR OMA; ARKWWMG; -.
DR OrthoDB; 5474932at2759; -.
DR PhylomeDB; O75879; -.
DR TreeFam; TF314355; -.
DR BRENDA; 6.3.5.7; 2681.
DR PathwayCommons; O75879; -.
DR SignaLink; O75879; -.
DR BioGRID-ORCS; 5188; 220 hits in 1168 CRISPR screens.
DR ChiTaRS; GATB; human.
DR GenomeRNAi; 5188; -.
DR Pharos; O75879; Tbio.
DR PRO; PR:O75879; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O75879; Protein.
DR Bgee; ENSG00000059691; Expressed in C1 segment of cervical spinal cord and 173 other cell types or tissues.
DR ExpressionAtlas; O75879; baseline and differential.
DR Genevisible; O75879; HS.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IDA:UniProtKB.
DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IDA:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; IMP:UniProtKB.
DR Gene3D; 1.10.10.410; -; 1.
DR HAMAP; MF_00121; GatB; 1.
DR InterPro; IPR017959; Asn/Gln-tRNA_amidoTrfase_suB/E.
DR InterPro; IPR006075; Asn/Gln-tRNA_Trfase_suB/E_cat.
DR InterPro; IPR018027; Asn/Gln_amidotransferase.
DR InterPro; IPR003789; Asn/Gln_tRNA_amidoTrase-B-like.
DR InterPro; IPR004413; GatB.
DR InterPro; IPR023168; GatB_Yqey_C_2.
DR InterPro; IPR017958; Gln-tRNA_amidoTrfase_suB_CS.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR NCBIfam; TIGR00133; gatB; 1.
DR PANTHER; PTHR11659; GLUTAMYL-TRNA GLN AMIDOTRANSFERASE SUBUNIT B MITOCHONDRIAL AND PROKARYOTIC PET112-RELATED; 1.
DR PANTHER; PTHR11659:SF0; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT B, MITOCHONDRIAL; 1.
DR Pfam; PF02934; GatB_N; 1.
DR Pfam; PF02637; GatB_Yqey; 1.
DR SMART; SM00845; GatB_Yqey; 1.
DR SUPFAM; SSF89095; GatB/YqeY motif; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR PROSITE; PS01234; GATB; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW Primary mitochondrial disease; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 42..557
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit B,
FT mitochondrial"
FT /id="PRO_0000010710"
FT REGION 26..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 529
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99JT1"
FT VARIANT 30
FT /note="A -> D (in dbSNP:rs11556167)"
FT /id="VAR_049128"
FT VARIANT 136
FT /note="F -> L (in COXPD41; uncertain significance;
FT dbSNP:rs376766195)"
FT /evidence="ECO:0000269|PubMed:30283131"
FT /id="VAR_083986"
FT CONFLICT 317
FT /note="H -> R (in Ref. 4; BAD96607)"
FT /evidence="ECO:0000305"
FT CONFLICT 418..419
FT /note="EP -> DK (in Ref. 2; AAF36119)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="N -> D (in Ref. 4; BAD96607)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 557 AA; 61864 MW; 449EB3EA2FD4769D CRC64;
MAAPMLRWGC RGRRWAFARV DGGSCHRRGA PTGSTSNQIR GESSVAQQPL HTAQKTRKGE
HKWAAVVGLE IHAQISSNSK LFSGSQVRFS APPNSLVSFF DASLPGTLPV LNRRCVEAAV
MTGLALNCHI NKKSLFDRKH YFYADLPAGY QITQQRLPIA VNGSLIYGVC AGKKQSQVIP
KTVRIKQIQL EQDSGKSLHD NLRSQTLIDL NRAGVGLLEV VLEPDMSCGE EAATAVRELQ
LILQALGTSQ ANMAEGQLRV DANISVHHPG EPLGVRTEVK NLNSIRFLAK AIDYEIQRQI
NELENGGEIL NETRSFHHKL GCTMSMRDKE GKQDYRFMPE PNLPPLVLYD ATSLPAGADP
QQVINIDQIR ETLPELPSVT REKLVQQYGM LLEHSFTLLN EVGLLEFFQN VIKETRAEPK
KVTSWVLNTF LGYLKQQNLA VSESPVTPSA LAELLDLLDS RTISSSAAKQ VFEELWKREG
KTPGQIVSEK QLELMQDQGA LEQLCHSVME AHPQVVMDVK NRNPRAINKL IGLVRKATQS
RADPVMIKEI LEKKLSL
//
