ID NEMF_MOUSE Reviewed; 1064 AA.
AC Q8CCP0; Q3TAS9; Q3UF46; Q66JX6; Q8C9R6; Q8CA65; Q8JZT9; Q8R072; Q9CW30;
AC Q9CYB8; Q9D4A9;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 27-MAR-2024, entry version 144.
DE RecName: Full=Ribosome quality control complex subunit NEMF {ECO:0000305};
DE AltName: Full=Nuclear export mediator factor {ECO:0000312|MGI:MGI:1918305};
GN Name=Nemf {ECO:0000303|PubMed:32934225, ECO:0000312|MGI:MGI:1918305};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-438 (ISOFORMS 1/2/3).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Cerebellum, Embryo, Olfactory bulb, Spinal cord, Spleen,
RC Sympathetic ganglion, Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 687-1064 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 1-443 AND 855-1064 (ISOFORM 1).
RC STRAIN=C57BL/6J, and NMRI; TISSUE=Embryo, Mammary tumor, and Retina;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND SER-737, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP MUTAGENESIS OF ARG-86; 106-ASP--LYS-1064 AND ARG-487.
RX PubMed=32934225; DOI=10.1038/s41467-020-18327-6;
RA Martin P.B., Kigoshi-Tansho Y., Sher R.B., Ravenscroft G., Stauffer J.E.,
RA Kumar R., Yonashiro R., Mueller T., Griffith C., Allen W., Pehlivan D.,
RA Harel T., Zenker M., Howting D., Schanze D., Faqeih E.A.,
RA Almontashiri N.A.M., Maroofian R., Houlden H., Mazaheri N., Galehdari H.,
RA Douglas G., Posey J.E., Ryan M., Lupski J.R., Laing N.G., Joazeiro C.A.P.,
RA Cox G.A.;
RT "NEMF mutations that impair ribosome-associated quality control are
RT associated with neuromuscular disease.";
RL Nat. Commun. 11:4625-4625(2020).
RN [6]
RP FUNCTION.
RX PubMed=33406423; DOI=10.1016/j.celrep.2020.108599;
RA Udagawa T., Seki M., Okuyama T., Adachi S., Natsume T., Noguchi T.,
RA Matsuzawa A., Inada T.;
RT "Failure to degrade CAT-tailed proteins disrupts neuronal morphogenesis and
RT cell survival.";
RL Cell Rep. 34:108599-108599(2021).
CC -!- FUNCTION: Key component of the ribosome quality control complex (RQC),
CC a ribosome-associated complex that mediates the extraction of
CC incompletely synthesized nascent chains from stalled ribosomes as well
CC as their ubiquitin-mediated proteasomal degradation (PubMed:33406423).
CC Thereby, frees 60S subunit ribosomes from the stalled translation
CC complex and prevents the accumulation of nascent polypeptide chains
CC that are potentially toxic for the cell (PubMed:33406423). Within the
CC RQC complex, NEMF specifically binds stalled 60S ribosomal subunits by
CC recognizing an exposed, nascent chain-conjugated tRNA moiety and
CC promotes the recruitment of LTN1 to stalled 60S subunits (By
CC similarity). Following binding to stalled 60S ribosomal subunits, NEMF
CC mediates CAT tailing by recruiting alanine-charged tRNA to the A-site
CC and directing the elongation of stalled nascent chains independently of
CC mRNA or 40S subunits, leading to non-templated C-terminal alanine
CC extensions (CAT tails) (PubMed:33406423). Mainly recruits alanine-
CC charged tRNAs, but can also other amino acid-charged tRNAs (By
CC similarity). CAT tailing is required to promote ubiquitination of
CC stalled nascent chains by different E3 ubiquitin-protein ligases (By
CC similarity). In the canonical RQC pathway (RQC-L), CAT tailing
CC facilitates LTN1-dependent ubiquitination by exposing lysine residues
CC that would otherwise remain buried in the ribosomal exit tunnel (By
CC similarity). In the alternative RQC pathway (RQC-C) CAT tailing creates
CC an C-degron mainly composed of alanine that is recognized by the
CC CRL2(KLHDC10) and RCHY1/PIRH2 E3 ligases, leading to ubiquitination and
CC degradation of stalled nascent chains (By similarity). NEMF may also
CC indirectly play a role in nuclear export (By similarity).
CC {ECO:0000250|UniProtKB:O60524, ECO:0000250|UniProtKB:Q12532,
CC ECO:0000269|PubMed:33406423}.
CC -!- SUBUNIT: Component of the ribosome quality control complex (RQC),
CC composed of the E3 ubiquitin ligase LTN1, TCF25 and NEMF associated
CC with the 60S ribosomal subunit (By similarity). The complex probably
CC also contains VCP/p97 and its ubiquitin-binding cofactors (By
CC similarity). Interacts (via its N-terminus) with XPO1 (By similarity).
CC {ECO:0000250|UniProtKB:O60524, ECO:0000250|UniProtKB:Q12532}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O60524}. Nucleus {ECO:0000250|UniProtKB:O60524}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8CCP0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CCP0-2; Sequence=VSP_008397, VSP_008398;
CC Name=3;
CC IsoId=Q8CCP0-3; Sequence=VSP_010465, VSP_010466;
CC Name=4;
CC IsoId=Q8CCP0-4; Sequence=VSP_010463, VSP_010464;
CC -!- MISCELLANEOUS: [Isoform 2]: Due to intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NEMF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27272.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH53488.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH53488.2; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB30366.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB30366.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC27849.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC27849.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AK005212; BAB23886.1; -; mRNA.
DR EMBL; AK016662; BAB30366.1; ALT_FRAME; mRNA.
DR EMBL; AK017826; BAB30959.1; -; mRNA.
DR EMBL; AK032388; BAC27849.1; ALT_SEQ; mRNA.
DR EMBL; AK039497; BAC30369.1; -; mRNA.
DR EMBL; AK041458; BAC30950.1; -; mRNA.
DR EMBL; AK089000; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK149005; BAE28715.1; -; mRNA.
DR EMBL; AK171652; BAE42589.1; -; mRNA.
DR EMBL; BC027272; AAH27272.1; ALT_INIT; mRNA.
DR EMBL; BC037106; AAH37106.2; -; mRNA.
DR EMBL; BC053488; AAH53488.2; ALT_FRAME; mRNA.
DR EMBL; BC080716; AAH80716.1; -; mRNA.
DR CCDS; CCDS25951.1; -. [Q8CCP0-1]
DR RefSeq; NP_079717.2; NM_025441.3. [Q8CCP0-1]
DR AlphaFoldDB; Q8CCP0; -.
DR SMR; Q8CCP0; -.
DR BioGRID; 211322; 2.
DR IntAct; Q8CCP0; 2.
DR MINT; Q8CCP0; -.
DR STRING; 10090.ENSMUSP00000021368; -.
DR ChEMBL; CHEMBL4879489; -.
DR iPTMnet; Q8CCP0; -.
DR PhosphoSitePlus; Q8CCP0; -.
DR SwissPalm; Q8CCP0; -.
DR EPD; Q8CCP0; -.
DR jPOST; Q8CCP0; -.
DR MaxQB; Q8CCP0; -.
DR PaxDb; 10090-ENSMUSP00000021368; -.
DR PeptideAtlas; Q8CCP0; -.
DR ProteomicsDB; 252882; -. [Q8CCP0-1]
DR ProteomicsDB; 252883; -. [Q8CCP0-2]
DR ProteomicsDB; 252884; -. [Q8CCP0-3]
DR ProteomicsDB; 252885; -. [Q8CCP0-4]
DR Pumba; Q8CCP0; -.
DR Antibodypedia; 140; 255 antibodies from 29 providers.
DR DNASU; 66244; -.
DR Ensembl; ENSMUST00000021368.10; ENSMUSP00000021368.9; ENSMUSG00000020982.10. [Q8CCP0-1]
DR GeneID; 66244; -.
DR KEGG; mmu:66244; -.
DR UCSC; uc007nse.2; mouse. [Q8CCP0-1]
DR UCSC; uc007nsg.2; mouse. [Q8CCP0-3]
DR UCSC; uc007nsh.2; mouse. [Q8CCP0-4]
DR AGR; MGI:1918305; -.
DR CTD; 9147; -.
DR MGI; MGI:1918305; Nemf.
DR VEuPathDB; HostDB:ENSMUSG00000020982; -.
DR eggNOG; KOG2030; Eukaryota.
DR GeneTree; ENSGT00390000018516; -.
DR HOGENOM; CLU_003612_1_0_1; -.
DR InParanoid; Q8CCP0; -.
DR OMA; MFLEFFA; -.
DR OrthoDB; 129892at2759; -.
DR PhylomeDB; Q8CCP0; -.
DR TreeFam; TF300515; -.
DR BioGRID-ORCS; 66244; 4 hits in 78 CRISPR screens.
DR ChiTaRS; Nemf; mouse.
DR PRO; PR:Q8CCP0; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8CCP0; Protein.
DR Bgee; ENSMUSG00000020982; Expressed in manus and 231 other cell types or tissues.
DR ExpressionAtlas; Q8CCP0; baseline and differential.
DR Genevisible; Q8CCP0; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:1990112; C:RQC complex; ISS:UniProtKB.
DR GO; GO:1904678; F:alpha-aminoacyl-tRNA binding; ISO:MGI.
DR GO; GO:0043023; F:ribosomal large subunit binding; ISO:MGI.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0140708; P:CAT tailing; IDA:UniProtKB.
DR GO; GO:0051168; P:nuclear export; ISO:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0072344; P:rescue of stalled ribosome; ISO:MGI.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR Gene3D; 2.30.310.10; ibrinogen binding protein from staphylococcus aureus domain; 1.
DR InterPro; IPR021846; NFACT-C.
DR InterPro; IPR008532; NFACT_RNA-bd.
DR PANTHER; PTHR15239; NUCLEAR EXPORT MEDIATOR FACTOR NEMF; 1.
DR PANTHER; PTHR15239:SF6; RIBOSOME QUALITY CONTROL COMPLEX SUBUNIT NEMF; 1.
DR Pfam; PF11923; NFACT-C; 1.
DR Pfam; PF05670; NFACT-R_1; 1.
DR Pfam; PF05833; NFACT_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1064
FT /note="Ribosome quality control complex subunit NEMF"
FT /id="PRO_0000097643"
FT REGION 420..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 296..359
FT /evidence="ECO:0000255"
FT COILED 481..512
FT /evidence="ECO:0000255"
FT COILED 858..882
FT /evidence="ECO:0000255"
FT COMPBIAS 731..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..916
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60524"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 412..415
FT /note="NPYL -> GGRW (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_010463"
FT VAR_SEQ 416..1064
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_010464"
FT VAR_SEQ 638..641
FT /note="KKNF -> NSLT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010465"
FT VAR_SEQ 642..1064
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010466"
FT VAR_SEQ 889..892
FT /note="SAGS -> VSII (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008397"
FT VAR_SEQ 893..1064
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008398"
FT MUTAGEN 86
FT /note="R->S: Induces an age-dependent neurodegenerative
FT phenotype."
FT /evidence="ECO:0000269|PubMed:32934225"
FT MUTAGEN 106..1064
FT /note="Missing: Induces an age-dependent neurodegenerative
FT phenotype."
FT /evidence="ECO:0000269|PubMed:32934225"
FT MUTAGEN 487
FT /note="R->G: Induces an age-dependent neurodegenerative
FT phenotype."
FT /evidence="ECO:0000269|PubMed:32934225"
FT CONFLICT 84
FT /note="S -> G (in Ref. 1; BAE42589)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="A -> P (in Ref. 1; BAB23886)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="H -> Q (in Ref. 1; BAB30959)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="L -> S (in Ref. 1; BAB23886)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="Q -> K (in Ref. 2; AAH80716)"
FT /evidence="ECO:0000305"
FT CONFLICT 789
FT /note="E -> G (in Ref. 1; BAB30366)"
FT /evidence="ECO:0000305"
FT CONFLICT 873
FT /note="K -> R (in Ref. 2; AAH53488)"
FT /evidence="ECO:0000305"
FT CONFLICT 1023
FT /note="H -> Y (in Ref. 2; AAH53488)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1064 AA; 121188 MW; F74F6ED7552AB183 CRC64;
MKSRFSTVDL RAVLAELNAS LLGMRVNNVY DVDNKTYLIR LQKPDFKATL LLESGIRIHT
TEFEWPKNMM PSSFAMKCRK HLKSRRLVSA KQLGVDRIVD FQFGSDEAAY HLIIELYDRG
NIVLTDYEYL ILNILRFRTD EADDVKFAVR ERYPIDHARA AEPLLTLERL TEVIAAAPKG
EVLKRVLNPL LPYGPALIEH CLIESGFSGN AKVDEKLESK DIEKILVCVQ RAEDYLRKTS
NFNGKGYIIQ KREAKPSLDA DKPAEDILTY EEFHPFLFSQ HLQCPYIEFE SFDKAVDEFY
SKIEGQKIDL KALQQEKQAL KKLDNVRKDH ENRLEALQQA QEIDKLKGEL IEMNLQIVDR
AIQVVRSALA NQIDWTEIGV IVKEAQAQGD PVACAIKELK LQTNHVTMLL RNPYLLSEEE
DGDGDASIEN SDAEAPKGKK KKQKNKQLQK PQKNKPLLVD VDLSLSAYAN AKKYYDHKRY
AAKKTQRTVE AAEKAFKSAE KKTKQTLKEV QTVTSIQKAR KVYWFEKFLW FISSENYLII
GGRDQQQNEI IVKRYLTPGD IYVHADLHGA TSCVIKNPTG EPIPPRTLTE AGTMALCYSA
AWDARVITSA WWVYHHQVSK TAPTGEYLTT GSFMIRGKKN FLPPSYLMMG FSFLFKVDES
CVWRHRGERK VRVQDEDMET LTSCTSELMA EEMEQLEGGD SSEEETEELH GMPGDVELMT
QVDQEDIAVH SGRDELSSED GEAKAVTKDQ EPIGEMKEEE EDTFEYPDTT IDLSHLQSQR
PLQKLAPREE SLNSNDSKSQ GRRHLSAKER REMKKKKLPC ESGDLEVIEE KDKERESAVH
TEAYQNTSKN VAAGQPMKRG QKSKMKKMKE KYKDQDDEDR ELIMKLLASA GSNKEEKGKK
GKKGKPKDEP VKKPPQKPRG GQRVLDVVKE PPSLQVLAHD LQDLAVDDPH DDKEEHDLDQ
QGNEENLFDS LTGQPHPEDV LMFAIPICAP YTIMTNYKYK VKLTPGVQKK GKAAKTALNS
FMHSKEATAR EKDLFRSVKD TDLSRNIPGK VKVSAPNLLH VKRK
//
