ID   NFX1_MOUSE              Reviewed;        1114 AA.
AC   B1AY10; Q3U2A7; Q3UK95; Q3UMW1; Q7TPT4; Q8CC59; Q9DBC8; Q9JKW7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   RecName: Full=Transcriptional repressor NF-X1;
DE            Short=m-Nfx.1;
DE            EC=2.3.2.-;
DE   AltName: Full=Nuclear transcription factor, X box-binding protein 1;
GN   Name=Nfx1;
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 [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=12047746; DOI=10.1046/j.1365-2567.2002.01416.x;
RA   Arlotta P., Miyazaki D., Copeland N.G., Gilbert D.J., Jenkins N.A.,
RA   Ono S.J.;
RT   "Murine NFX.1: isolation and characterization of its messenger RNA, mapping
RT   of its chromosomal location and assessment of its developmental
RT   expression.";
RL   Immunology 106:173-181(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Diencephalon, Liver, Lung, and Placenta;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Egg;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81; SER-126 AND SER-130, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Pancreas, and Spleen;
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).
CC   -!- FUNCTION: Binds to the X-box motif of MHC class II genes and represses
CC       their expression. May play an important role in regulating the duration
CC       of an inflammatory response by limiting the period in which MHC class
CC       II molecules are induced by interferon-gamma. Together with PABPC1 or
CC       PABPC4, acts as a coactivator for TERT expression. Mediates E2-
CC       dependent ubiquitination. {ECO:0000269|PubMed:12047746}.
CC   -!- SUBUNIT: Interacts with PABPC1 and PABPC4. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=B1AY10-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=B1AY10-2; Sequence=VSP_033694, VSP_033695;
CC       Name=3;
CC         IsoId=B1AY10-3; Sequence=VSP_033693, VSP_033696;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC       thymus. {ECO:0000269|PubMed:12047746}.
CC   -!- DEVELOPMENTAL STAGE: Ubiquitously expressed at 12 dpc and 14 dpc.
CC       {ECO:0000269|PubMed:12047746}.
CC   -!- DOMAIN: The RING-type zinc finger domain interacts with an ubiquitin-
CC       conjugating enzyme (E2) and facilitates ubiquitination. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NFX1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF34700.1; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF223576; AAF34700.1; ALT_FRAME; mRNA.
DR   EMBL; AK005038; BAB23765.1; -; mRNA.
DR   EMBL; AK033850; BAC28494.1; -; mRNA.
DR   EMBL; AK144647; BAE25987.1; -; mRNA.
DR   EMBL; AK146108; BAE26907.1; -; mRNA.
DR   EMBL; AK155387; BAE33235.1; -; mRNA.
DR   EMBL; AL837521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC053709; AAH53709.1; -; mRNA.
DR   CCDS; CCDS18054.1; -. [B1AY10-1]
DR   CCDS; CCDS71359.1; -. [B1AY10-2]
DR   CCDS; CCDS71360.1; -. [B1AY10-3]
DR   RefSeq; NP_001277377.1; NM_001290448.1. [B1AY10-3]
DR   RefSeq; NP_001277378.1; NM_001290449.1. [B1AY10-2]
DR   RefSeq; NP_076228.2; NM_023739.3. [B1AY10-1]
DR   AlphaFoldDB; B1AY10; -.
DR   SMR; B1AY10; -.
DR   BioGRID; 216539; 18.
DR   IntAct; B1AY10; 2.
DR   MINT; B1AY10; -.
DR   STRING; 10090.ENSMUSP00000095747; -.
DR   iPTMnet; B1AY10; -.
DR   PhosphoSitePlus; B1AY10; -.
DR   SwissPalm; B1AY10; -.
DR   EPD; B1AY10; -.
DR   jPOST; B1AY10; -.
DR   MaxQB; B1AY10; -.
DR   PaxDb; 10090-ENSMUSP00000095747; -.
DR   PeptideAtlas; B1AY10; -.
DR   ProteomicsDB; 287501; -. [B1AY10-1]
DR   ProteomicsDB; 287502; -. [B1AY10-2]
DR   ProteomicsDB; 287503; -. [B1AY10-3]
DR   Pumba; B1AY10; -.
DR   Antibodypedia; 25201; 163 antibodies from 29 providers.
DR   DNASU; 74164; -.
DR   Ensembl; ENSMUST00000030133.15; ENSMUSP00000030133.9; ENSMUSG00000028423.16. [B1AY10-3]
DR   Ensembl; ENSMUST00000091614.7; ENSMUSP00000089203.7; ENSMUSG00000028423.16. [B1AY10-2]
DR   Ensembl; ENSMUST00000098143.11; ENSMUSP00000095747.5; ENSMUSG00000028423.16. [B1AY10-1]
DR   GeneID; 74164; -.
DR   KEGG; mmu:74164; -.
DR   UCSC; uc008sic.2; mouse. [B1AY10-2]
DR   UCSC; uc008sid.2; mouse. [B1AY10-3]
DR   UCSC; uc008sie.2; mouse. [B1AY10-1]
DR   AGR; MGI:1921414; -.
DR   CTD; 4799; -.
DR   MGI; MGI:1921414; Nfx1.
DR   VEuPathDB; HostDB:ENSMUSG00000028423; -.
DR   eggNOG; KOG1952; Eukaryota.
DR   GeneTree; ENSGT00940000156325; -.
DR   HOGENOM; CLU_005714_1_2_1; -.
DR   InParanoid; B1AY10; -.
DR   OMA; PRTSCED; -.
DR   OrthoDB; 1412at2759; -.
DR   PhylomeDB; B1AY10; -.
DR   TreeFam; TF105889; -.
DR   BioGRID-ORCS; 74164; 2 hits in 81 CRISPR screens.
DR   ChiTaRS; Nfx1; mouse.
DR   PRO; PR:B1AY10; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; B1AY10; Protein.
DR   Bgee; ENSMUSG00000028423; Expressed in cumulus cell and 258 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045347; P:negative regulation of MHC class II biosynthetic process; IDA:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0051865; P:protein autoubiquitination; ISO:MGI.
DR   CDD; cd06008; NF-X1-zinc-finger; 6.
DR   CDD; cd02643; R3H_NF-X1; 1.
DR   CDD; cd16696; RING-CH-C4HC3_NFX1; 1.
DR   Gene3D; 3.30.1370.50; R3H-like domain; 1.
DR   InterPro; IPR034078; NFX1_fam.
DR   InterPro; IPR001374; R3H_dom.
DR   InterPro; IPR036867; R3H_dom_sf.
DR   InterPro; IPR034076; R3H_NF-X1.
DR   InterPro; IPR000967; Znf_NFX1.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR001841; Znf_RING.
DR   PANTHER; PTHR12360; NUCLEAR TRANSCRIPTION FACTOR, X-BOX BINDING 1 NFX1; 1.
DR   PANTHER; PTHR12360:SF12; TRANSCRIPTIONAL REPRESSOR NF-X1; 1.
DR   Pfam; PF01424; R3H; 1.
DR   Pfam; PF01422; zf-NF-X1; 7.
DR   SMART; SM00393; R3H; 1.
DR   SMART; SM00438; ZnF_NFX; 9.
DR   SUPFAM; SSF82708; R3H domain; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51061; R3H; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   Genevisible; B1AY10; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Transferase; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..1114
FT                   /note="Transcriptional repressor NF-X1"
FT                   /id="PRO_0000334614"
FT   DOMAIN          988..1056
FT                   /note="R3H"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT   ZN_FING         352..403
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         447..465
FT                   /note="NF-X1-type 1"
FT   ZN_FING         500..519
FT                   /note="NF-X1-type 2"
FT   ZN_FING         561..580
FT                   /note="NF-X1-type 3"
FT   ZN_FING         626..649
FT                   /note="NF-X1-type 4"
FT   ZN_FING         688..707
FT                   /note="NF-X1-type 5"
FT   ZN_FING         715..734
FT                   /note="NF-X1-type 6"
FT   ZN_FING         826..848
FT                   /note="NF-X1-type 7"
FT   ZN_FING         857..878
FT                   /note="NF-X1-type 8"
FT   REGION          9..26
FT                   /note="Interaction with PABPC1 and PABC4"
FT                   /evidence="ECO:0000250"
FT   REGION          20..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          232..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1071..1095
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..161
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..205
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..257
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         50
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12986"
FT   MOD_RES         81
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         92
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12986"
FT   MOD_RES         126
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         130
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         147
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12986"
FT   MOD_RES         320
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12986"
FT   VAR_SEQ         803..818
FT                   /note="LRSNIPCHLVDISCGL -> ELTIKKLWTFKETLDF (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_033693"
FT   VAR_SEQ         803..804
FT                   /note="LR -> RQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_033694"
FT   VAR_SEQ         805..1114
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_033695"
FT   VAR_SEQ         819..1114
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_033696"
FT   CONFLICT        49
FT                   /note="S -> N (in Ref. 2; BAC28494)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141
FT                   /note="T -> A (in Ref. 2; BAE33235)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        273
FT                   /note="S -> P (in Ref. 4; AAH53709)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        455
FT                   /note="C -> Y (in Ref. 2; BAE33235)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        590
FT                   /note="C -> R (in Ref. 4; AAH53709)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1114 AA;  123811 MW;  A31013ACC6FB31F4 CRC64;
     MAEAPPVSGT FKFNTDAAEF IPQERKTSGL NCGTQRRLDS SRIGRRNYSS SPPCHLPRHI
     PYEDISAVHQ HSYASGSKPK SPQGFFQSSN KSLKNHGLQN QPWQKARNEK HQNRNKKAQG
     LSEQTSDTSS LESVARSESG TNPREHSPSE SEKEVVIADP RGAKPKKAAQ LTYNYGRGPK
     AKGRLRSEWG NRMSPKSEDE NTRPVAISHT DSSDASCRKP VVDPCVCRRN EQRRYPQKRP
     PWEVEGARPR PGRNPPKQES QRHINAGPKT NMSPIPKDNL RERPTKSACD TGNLAVVSKS
     SRRVNQEKTA VRRQDPQVLS PFPRGKQNHM LKNVETHTGS LIEQLTTEKY ECMVCCELVQ
     VTAPVWSCQS CFHVFHLNCI KKWARSPASH ADGQSGWRCP ACQNVSAHVP NTYTCFCGKV
     KNPEWSRNEI PHSCGEVCRK KQPGQDCPHS CNLLCHPGPC PPCPAFTTKT CECGRTRHTV
     RCGQPVSVHC SNACENILNC GQHHCAELCH GGQCQPCRII LNQVCYCGST SRDVLCGTDV
     GKSDGFGDFS CLKICGKDLK CGSHTCSQVC HPQPCQPCPR LPHLVRYCPC GQTPLSQLLE
     HGSNARKTCM DPVPSCGKVC GKPLACGSSD FIHTCEKLCH EGDCGPCSRT SVISCRCSFR
     TKELPCTSLK SEDATFMCDK RCNKKRLCGR HKCNEICCVD KEHKCPLICG RKLRCGLHRC
     EEPCHRGNCQ TCWQASFDEL TCHCGASVIY PPVPCGTRPP ECTQTCARIH ECDHPVYHSC
     HSEEKCPPCT FLTQKWCMGK HELRSNIPCH LVDISCGLPC SAMLPCGMHK CQRLCHKGEC
     LVDEACKQPC TTPRGDCGHP CMAPCHPSLP CPVTACKAKV ELQCECGRRK EMVICSEASG
     TYQRIVAISM ASKITDMQLG DSVEISKLIT KKEVQQARLQ CDEECAALER RKRLAEAFDI
     TDDSDPFNVR SSASKFSDSL KDDARKDLKF VSDVEKEMET LVEAVNKGKN NKKSHCFPPM
     NRDHRRIIHD LAQVYGLESI SYDSEPKRNV VVTAVRGKSV CPPTTLTSVI ERETQTRPPP
     PIPHHRHQAD KAPGSSTLQK IVKEAVIDYF DVQD
//