ID   DNJC8_HUMAN             Reviewed;         253 AA.
AC   O75937; B4DUU4; D3DPM0; Q6IBA4; Q8N4Z5; Q9P051; Q9P067;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   29-MAY-2024, entry version 170.
DE   RecName: Full=DnaJ homolog subfamily C member 8;
DE   AltName: Full=Splicing protein spf31;
GN   Name=DNAJC8; Synonyms=SPF31; ORFNames=HSPC315, HSPC331;
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], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP   WITH HSP70, AND TISSUE SPECIFICITY.
RX   PubMed=27133716; DOI=10.1016/j.bbrc.2016.03.152;
RA   Ito N., Kamiguchi K., Nakanishi K., Sokolovskya A., Hirohashi Y.,
RA   Tamura Y., Murai A., Yamamoto E., Kanaseki T., Tsukahara T., Kochin V.,
RA   Chiba S., Shimohama S., Sato N., Torigoe T.;
RT   "A novel nuclear DnaJ protein, DNAJC8, can suppress the formation of
RT   spinocerebellar ataxia 3 polyglutamine aggregation in a J-domain
RT   independent manner.";
RL   Biochem. Biophys. Res. Commun. 474:626-633(2016).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   King A., Ajuh P., Schrotz-King P., Lamond A., Mann M.;
RT   "spf31: a protein involved in splicing.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
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].
RC   TISSUE=Uterus;
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 [LARGE SCALE MRNA] OF 96-253.
RC   TISSUE=Umbilical cord blood;
RA   Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
RA   Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RT   "Human partial CDS from CD34+ stem cells.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [9]
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=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [10]
RP   INTERACTION WITH SRPK1.
RX   PubMed=19240134; DOI=10.1101/gad.1752109;
RA   Zhong X.Y., Ding J.H., Adams J.A., Ghosh G., Fu X.D.;
RT   "Regulation of SR protein phosphorylation and alternative splicing by
RT   modulating kinetic interactions of SRPK1 with molecular chaperones.";
RL   Genes Dev. 23:482-495(2009).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-146, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [14]
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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [16]
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).
CC   -!- FUNCTION: Suppresses polyglutamine (polyQ) aggregation of ATXN3 in
CC       neuronal cells (PubMed:27133716). {ECO:0000269|PubMed:27133716}.
CC   -!- SUBUNIT: Interacts with SRPK1 (PubMed:19240134). Interacts with HSP70
CC       (HSPA1A or HSPA1B) (PubMed:27133716). {ECO:0000269|PubMed:19240134,
CC       ECO:0000269|PubMed:27133716}.
CC   -!- INTERACTION:
CC       O75937; P30556: AGTR1; NbExp=2; IntAct=EBI-1045911, EBI-6623016;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27133716}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:27133716}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC35352.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAG33181.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF083190; AAC35352.1; ALT_INIT; mRNA.
DR   EMBL; CR456900; CAG33181.1; ALT_INIT; mRNA.
DR   EMBL; AK300797; BAG62456.1; -; mRNA.
DR   EMBL; AL353354; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL353622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471059; EAX07707.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX07710.1; -; Genomic_DNA.
DR   EMBL; BC033159; AAH33159.1; -; mRNA.
DR   EMBL; AF161433; AAF28993.1; -; mRNA.
DR   EMBL; AF161449; AAF29009.1; -; mRNA.
DR   CCDS; CCDS41292.1; -.
DR   RefSeq; NP_055095.2; NM_014280.2.
DR   PDB; 7VPX; EM; 3.00 A; J=1-253.
DR   PDBsum; 7VPX; -.
DR   AlphaFoldDB; O75937; -.
DR   EMDB; EMD-32074; -.
DR   SMR; O75937; -.
DR   BioGRID; 116501; 234.
DR   CORUM; O75937; -.
DR   IntAct; O75937; 30.
DR   MINT; O75937; -.
DR   STRING; 9606.ENSP00000263697; -.
DR   GlyGen; O75937; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O75937; -.
DR   PhosphoSitePlus; O75937; -.
DR   BioMuta; DNAJC8; -.
DR   EPD; O75937; -.
DR   jPOST; O75937; -.
DR   MassIVE; O75937; -.
DR   MaxQB; O75937; -.
DR   PaxDb; 9606-ENSP00000263697; -.
DR   PeptideAtlas; O75937; -.
DR   ProteomicsDB; 50302; -.
DR   Pumba; O75937; -.
DR   TopDownProteomics; O75937; -.
DR   Antibodypedia; 30906; 119 antibodies from 22 providers.
DR   DNASU; 22826; -.
DR   Ensembl; ENST00000263697.6; ENSP00000263697.4; ENSG00000126698.11.
DR   GeneID; 22826; -.
DR   KEGG; hsa:22826; -.
DR   MANE-Select; ENST00000263697.6; ENSP00000263697.4; NM_014280.3; NP_055095.2.
DR   UCSC; uc001bpn.4; human.
DR   AGR; HGNC:15470; -.
DR   CTD; 22826; -.
DR   DisGeNET; 22826; -.
DR   GeneCards; DNAJC8; -.
DR   HGNC; HGNC:15470; DNAJC8.
DR   HPA; ENSG00000126698; Low tissue specificity.
DR   neXtProt; NX_O75937; -.
DR   OpenTargets; ENSG00000126698; -.
DR   PharmGKB; PA27425; -.
DR   VEuPathDB; HostDB:ENSG00000126698; -.
DR   eggNOG; KOG1150; Eukaryota.
DR   GeneTree; ENSGT00390000012569; -.
DR   HOGENOM; CLU_070940_2_0_1; -.
DR   InParanoid; O75937; -.
DR   OMA; EIVNKAW; -.
DR   OrthoDB; 205698at2759; -.
DR   PhylomeDB; O75937; -.
DR   TreeFam; TF105167; -.
DR   PathwayCommons; O75937; -.
DR   Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR   SignaLink; O75937; -.
DR   BioGRID-ORCS; 22826; 626 hits in 1155 CRISPR screens.
DR   ChiTaRS; DNAJC8; human.
DR   GenomeRNAi; 22826; -.
DR   Pharos; O75937; Tbio.
DR   PRO; PR:O75937; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; O75937; Protein.
DR   Bgee; ENSG00000126698; Expressed in ganglionic eminence and 103 other cell types or tissues.
DR   ExpressionAtlas; O75937; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0030544; F:Hsp70 protein binding; IPI:UniProtKB.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR042858; DNAJC8.
DR   InterPro; IPR036869; J_dom_sf.
DR   PANTHER; PTHR15606:SF4; DNAJ HOMOLOG SUBFAMILY C MEMBER 8; 1.
DR   PANTHER; PTHR15606; DNAJ HOMOLOG SUBFAMILY C MEMBER 8/LIPOPOLYSACCHARIDE SPECIFIC RESPONSE-7-RELATED; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Chaperone; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   CHAIN           2..253
FT                   /note="DnaJ homolog subfamily C member 8"
FT                   /id="PRO_0000071060"
FT   DOMAIN          57..124
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   REGION          181..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          232..253
FT                   /note="Essential for polyglutamine aggregation suppression"
FT                   /evidence="ECO:0000269|PubMed:27133716"
FT   MOTIF           189..192
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000305|PubMed:27133716"
FT   MOTIF           203..206
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000305|PubMed:27133716"
FT   COMPBIAS        181..221
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   MOD_RES         35
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         146
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         222
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CONFLICT        253
FT                   /note="E -> D (in Ref. 3; CAG33181)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   253 AA;  29842 MW;  C69D6189D69D1588 CRC64;
     MAASGESGTS GGGGSTEEAF MTFYSEVKQI EKRDSVLTSK NQIERLTRPG SSYFNLNPFE
     VLQIDPEVTD EEIKKRFRQL SILVHPDKNQ DDADRAQKAF EAVDKAYKLL LDQEQKKRAL
     DVIQAGKEYV EHTVKERKKQ LKKEGKPTIV EEDDPELFKQ AVYKQTMKLF AELEIKRKER
     EAKEMHERKR QREEEIEAQE KAKREREWQK NFEESRDGRV DSWRNFQANT KGKKEKKNRT
     FLRPPKVKME QRE
//