ID   RF1ML_HUMAN             Reviewed;         380 AA.
AC   Q9UGC7; B3KTA0; Q3KR06; Q5TF44; Q5TF50; Q96CC5; Q96EX4; Q96K40;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Peptide chain release factor 1-like, mitochondrial {ECO:0000305};
DE   AltName: Full=Mitochondrial translational release factor 1-like;
DE   AltName: Full=mtRF1a {ECO:0000303|PubMed:20075246, ECO:0000303|PubMed:37141370};
DE   Flags: Precursor;
GN   Name=MTRF1L {ECO:0000312|HGNC:HGNC:21051};
GN   Synonyms=MTRF1A {ECO:0000303|PubMed:20075246,
GN   ECO:0000303|PubMed:37141370};
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; 2 AND 3).
RC   TISSUE=Tongue;
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=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS ALA-38 AND
RP   GLN-76.
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4), AND VARIANTS
RP   ALA-38 AND GLN-76.
RC   TISSUE=Eye, Muscle, and 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, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=17803939; DOI=10.1016/j.molcel.2007.06.031;
RA   Soleimanpour-Lichaei H.R., Kuehl I., Gaisne M., Passos J.F., Wydro M.,
RA   Rorbach J., Temperley R., Bonnefoy N., Tate W., Lightowlers R.,
RA   Chrzanowska-Lightowlers Z.;
RT   "mtRF1a is a human mitochondrial translation release factor decoding the
RT   major termination codons UAA and UAG.";
RL   Mol. Cell 27:745-757(2007).
RN   [6]
RP   METHYLATION AT GLN-252 BY HEMK1.
RX   PubMed=18541145; DOI=10.1016/j.bbrc.2008.05.176;
RA   Ishizawa T., Nozaki Y., Ueda T., Takeuchi N.;
RT   "The human mitochondrial translation release factor HMRF1L is methylated in
RT   the GGQ motif by the methyltransferase HMPrmC.";
RL   Biochem. Biophys. Res. Commun. 373:99-103(2008).
RN   [7]
RP   FUNCTION.
RX   PubMed=20075246; DOI=10.1126/science.1180674;
RA   Temperley R., Richter R., Dennerlein S., Lightowlers R.N.,
RA   Chrzanowska-Lightowlers Z.M.;
RT   "Hungry codons promote frameshifting in human mitochondrial ribosomes.";
RL   Science 327:301-301(2010).
RN   [8]
RP   METHYLATION AT GLN-252.
RX   PubMed=35260756; DOI=10.1038/s41598-022-08061-y;
RA   Fang Q., Kimura Y., Shimazu T., Suzuki T., Yamada A., Dohmae N.,
RA   Iwasaki S., Shinkai Y.;
RT   "Mammalian HEMK1 methylates glutamine residue of the GGQ motif of
RT   mitochondrial release factors.";
RL   Sci. Rep. 12:4104-4104(2022).
RN   [9]
RP   FUNCTION, AND MUTAGENESIS OF 250-GLY-GLY-251.
RX   PubMed=37141370; DOI=10.1126/science.adf9890;
RA   Saurer M., Leibundgut M., Nadimpalli H.P., Scaiola A., Schoenhut T.,
RA   Lee R.G., Siira S.J., Rackham O., Dreos R., Lenarcic T., Kummer E.,
RA   Gatfield D., Filipovska A., Ban N.;
RT   "Molecular basis of translation termination at noncanonical stop codons in
RT   human mitochondria.";
RL   Science 380:531-536(2023).
RN   [10] {ECO:0007744|PDB:7NQH}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 20-380 IN COMPLEX WITH
RP   MITOCHONDRIAL RIBOSOME, AND FUNCTION.
RX   PubMed=33878294; DOI=10.1016/j.molcel.2021.03.042;
RA   Kummer E., Schubert K.N., Schoenhut T., Scaiola A., Ban N.;
RT   "Structural basis of translation termination, rescue, and recycling in
RT   mammalian mitochondria.";
RL   Mol. Cell 81:2566-2582(2021).
CC   -!- FUNCTION: Mitochondrial peptide chain release factor that directs the
CC       termination of translation in response to the peptide chain termination
CC       codons UAA and UAG. {ECO:0000269|PubMed:17803939,
CC       ECO:0000269|PubMed:33878294, ECO:0000269|PubMed:37141370}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:17803939}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9UGC7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UGC7-2; Sequence=VSP_033141, VSP_033142;
CC       Name=3;
CC         IsoId=Q9UGC7-3; Sequence=VSP_033139;
CC       Name=4;
CC         IsoId=Q9UGC7-4; Sequence=VSP_033140, VSP_033141, VSP_033142;
CC   -!- TISSUE SPECIFICITY: Expressed in skeletal muscle (at protein level).
CC       {ECO:0000269|PubMed:17803939}.
CC   -!- DOMAIN: The GGQ domain interacts with the peptidyltransferase center
CC       (PTC) of the large ribosomal subunit to trigger nascent chain
CC       hydrolysis. {ECO:0000250|UniProtKB:Q9H3J6}.
CC   -!- PTM: Methylation of glutamine in the GGQ triplet by HEMK1 is conserved
CC       from bacteria to mammals. {ECO:0000269|PubMed:18541145,
CC       ECO:0000269|PubMed:35260756}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000305}.
CC   -!- CAUTION: Was initially thought to promote the termination of non-
CC       canonical termination stop codons AGG and AGA in addition to canonical
CC       termination codons UAA and UAG (PubMed:20075246). However, it was later
CC       shown that termination of non-canonical termination stop codons AGG and
CC       AGA is mediated by MTRF1 (PubMed:37141370).
CC       {ECO:0000269|PubMed:20075246, ECO:0000269|PubMed:37141370}.
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DR   EMBL; AK027684; BAB55295.1; -; mRNA.
DR   EMBL; AK095240; BAG53012.1; -; mRNA.
DR   EMBL; AK290662; BAF83351.1; -; mRNA.
DR   EMBL; AL080276; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471051; EAW47712.1; -; Genomic_DNA.
DR   EMBL; BC011873; AAH11873.1; -; mRNA.
DR   EMBL; BC014428; AAH14428.1; -; mRNA.
DR   EMBL; BC105973; AAI05974.1; -; mRNA.
DR   CCDS; CCDS47502.1; -. [Q9UGC7-2]
DR   CCDS; CCDS5243.1; -. [Q9UGC7-1]
DR   CCDS; CCDS75540.1; -. [Q9UGC7-4]
DR   RefSeq; NP_001107656.1; NM_001114184.2. [Q9UGC7-2]
DR   RefSeq; NP_001287976.1; NM_001301047.2. [Q9UGC7-4]
DR   RefSeq; NP_001288799.1; NM_001301870.1.
DR   RefSeq; NP_001288800.1; NM_001301871.1. [Q9UGC7-3]
DR   RefSeq; NP_061914.3; NM_019041.6. [Q9UGC7-1]
DR   RefSeq; XP_016866448.1; XM_017010959.1.
DR   RefSeq; XP_016866449.1; XM_017010960.1.
DR   PDB; 7NQH; EM; 3.50 A; BL=20-380.
DR   PDBsum; 7NQH; -.
DR   AlphaFoldDB; Q9UGC7; -.
DR   EMDB; EMD-12527; -.
DR   SMR; Q9UGC7; -.
DR   BioGRID; 120010; 242.
DR   IntAct; Q9UGC7; 8.
DR   STRING; 9606.ENSP00000356202; -.
DR   iPTMnet; Q9UGC7; -.
DR   PhosphoSitePlus; Q9UGC7; -.
DR   BioMuta; MTRF1L; -.
DR   DMDM; 74753314; -.
DR   EPD; Q9UGC7; -.
DR   jPOST; Q9UGC7; -.
DR   MassIVE; Q9UGC7; -.
DR   MaxQB; Q9UGC7; -.
DR   PaxDb; 9606-ENSP00000356202; -.
DR   PeptideAtlas; Q9UGC7; -.
DR   ProteomicsDB; 84207; -. [Q9UGC7-1]
DR   ProteomicsDB; 84208; -. [Q9UGC7-2]
DR   ProteomicsDB; 84209; -. [Q9UGC7-3]
DR   ProteomicsDB; 84210; -. [Q9UGC7-4]
DR   Pumba; Q9UGC7; -.
DR   Antibodypedia; 33386; 280 antibodies from 15 providers.
DR   DNASU; 54516; -.
DR   Ensembl; ENST00000367230.5; ENSP00000356199.1; ENSG00000112031.16. [Q9UGC7-4]
DR   Ensembl; ENST00000367231.9; ENSP00000356200.5; ENSG00000112031.16. [Q9UGC7-2]
DR   Ensembl; ENST00000367233.10; ENSP00000356202.5; ENSG00000112031.16. [Q9UGC7-1]
DR   GeneID; 54516; -.
DR   KEGG; hsa:54516; -.
DR   MANE-Select; ENST00000367233.10; ENSP00000356202.5; NM_019041.7; NP_061914.3.
DR   UCSC; uc003qpi.5; human. [Q9UGC7-1]
DR   AGR; HGNC:21051; -.
DR   CTD; 54516; -.
DR   DisGeNET; 54516; -.
DR   GeneCards; MTRF1L; -.
DR   HGNC; HGNC:21051; MTRF1L.
DR   HPA; ENSG00000112031; Low tissue specificity.
DR   MIM; 613542; gene.
DR   neXtProt; NX_Q9UGC7; -.
DR   OpenTargets; ENSG00000112031; -.
DR   PharmGKB; PA134870441; -.
DR   VEuPathDB; HostDB:ENSG00000112031; -.
DR   eggNOG; KOG2726; Eukaryota.
DR   GeneTree; ENSGT00940000155683; -.
DR   HOGENOM; CLU_036856_0_3_1; -.
DR   InParanoid; Q9UGC7; -.
DR   OMA; DHRVGFK; -.
DR   OrthoDB; 131884at2759; -.
DR   PhylomeDB; Q9UGC7; -.
DR   TreeFam; TF313720; -.
DR   PathwayCommons; Q9UGC7; -.
DR   Reactome; R-HSA-5419276; Mitochondrial translation termination.
DR   SignaLink; Q9UGC7; -.
DR   BioGRID-ORCS; 54516; 200 hits in 1155 CRISPR screens.
DR   ChiTaRS; MTRF1L; human.
DR   GeneWiki; MTRF1L; -.
DR   GenomeRNAi; 54516; -.
DR   Pharos; Q9UGC7; Tbio.
DR   PRO; PR:Q9UGC7; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9UGC7; Protein.
DR   Bgee; ENSG00000112031; Expressed in left ventricle myocardium and 195 other cell types or tissues.
DR   ExpressionAtlas; Q9UGC7; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0003747; F:translation release factor activity; IDA:UniProtKB.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IDA:UniProtKB.
DR   GO; GO:0070126; P:mitochondrial translational termination; IDA:UniProtKB.
DR   Gene3D; 3.30.160.20; -; 1.
DR   Gene3D; 3.30.70.1660; -; 1.
DR   Gene3D; 6.10.140.1950; -; 1.
DR   InterPro; IPR005139; PCRF.
DR   InterPro; IPR000352; Pep_chain_release_fac_I.
DR   InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR   PANTHER; PTHR43804; LD18447P; 1.
DR   PANTHER; PTHR43804:SF3; PEPTIDE CHAIN RELEASE FACTOR 1-LIKE, MITOCHONDRIAL; 1.
DR   Pfam; PF03462; PCRF; 1.
DR   Pfam; PF00472; RF-1; 1.
DR   SMART; SM00937; PCRF; 1.
DR   SUPFAM; SSF75620; Release factor; 1.
DR   PROSITE; PS00745; RF_PROK_I; 1.
DR   Genevisible; Q9UGC7; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil; Methylation;
KW   Mitochondrion; Protein biosynthesis; Reference proteome; Transit peptide.
FT   TRANSIT         1..26
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..380
FT                   /note="Peptide chain release factor 1-like, mitochondrial"
FT                   /id="PRO_0000330944"
FT   REGION          236..300
FT                   /note="GGQ domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q80VP5"
FT   COILED          63..117
FT                   /evidence="ECO:0000255"
FT   MOTIF           250..252
FT                   /note="GGQ"
FT                   /evidence="ECO:0000269|PubMed:37141370"
FT   MOD_RES         252
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000269|PubMed:18541145,
FT                   ECO:0000269|PubMed:35260756"
FT   VAR_SEQ         1..142
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_033139"
FT   VAR_SEQ         139..174
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033140"
FT   VAR_SEQ         269..271
FT                   /note="GVV -> DWK (in isoform 2 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033141"
FT   VAR_SEQ         272..380
FT                   /note="Missing (in isoform 2 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033142"
FT   VARIANT         38
FT                   /note="T -> A (in dbSNP:rs3818125)"
FT                   /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT                   /id="VAR_042725"
FT   VARIANT         76
FT                   /note="R -> Q (in dbSNP:rs3818123)"
FT                   /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT                   /id="VAR_042726"
FT   VARIANT         177
FT                   /note="L -> F (in dbSNP:rs12660881)"
FT                   /id="VAR_042727"
FT   VARIANT         214
FT                   /note="V -> I (in dbSNP:rs3192723)"
FT                   /id="VAR_042728"
FT   MUTAGEN         250..251
FT                   /note="GG->AA: Impaired mitochondrial peptide chain release
FT                   factor activity."
FT                   /evidence="ECO:0000269|PubMed:37141370"
SQ   SEQUENCE   380 AA;  43600 MW;  69632427972521C3 CRC64;
     MRSRVLWGAA RWLWPRRAVG PARRPLSSGS PPLEELFTRG GPLRTFLERQ AGSEAHLKVR
     RPELLAVIKL LNEKERELRE TEHLLHDENE DLRKLAENEI TLCQKEITQL KHQIILLLVP
     SEETDENDLI LEVTAGVGGQ EAMLFTSEIF DMYQQYAAFK RWHFETLEYF PSELGGLRHA
     SASIGGSEAY RHMKFEGGVH RVQRVPKTEK QGRVHTSTMT VAILPQPTEI NLVINPKDLR
     IDTKRASGAG GQHVNTTDSA VRIVHLPTGV VSECQQERSQ LKNKELAMTK LRAKLYSMHL
     EEEINKRQNA RKIQIGSKGR SEKIRTYNFP QNRVTDHRIN KTLHDLETFM QGDYLLDELV
     QSLKEYADYE SLVEIISQKV
//