DNJC9_HUMAN
ID DNJC9_HUMAN Reviewed; 260 AA.
AC Q8WXX5; B2RMW6;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=DnaJ homolog subfamily C member 9;
DE Short=HDJC9 {ECO:0000303|PubMed:17182002};
DE AltName: Full=DnaJ protein SB73;
GN Name=DNAJC9;
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, INTERACTION WITH HSPA1A; HSPA1B AND
RP HSPA8, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Dendritic cell {ECO:0000303|PubMed:17182002};
RX PubMed=17182002; DOI=10.1016/j.bbrc.2006.12.013;
RA Han C., Chen T., Li N., Yang M., Wan T., Cao X.;
RT "HDJC9, a novel human type C DnaJ/HSP40 member interacts with and
RT cochaperones HSP70 through the J domain.";
RL Biochem. Biophys. Res. Commun. 353:280-285(2007).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-215, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION BY
RP 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).
RN [11]
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 [12] {ECO:0007744|PDB:7CIZ, ECO:0007744|PDB:7CJ0}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 171-249 MUTANT CYS-243 IN COMPLEX
RP WITH MCM2 61-130 AND HISTONES H3.3 58-136 AND H4, IDENTIFICATION BY MASS
RP SPECTROMETRY, FUNCTION, IDENTIFICATION IN A CO-CHAPERONE COMPLEX WITH MCM2
RP AND HISTONES H3.3 AND H4, INTERACTION WITH MCM2; H3.3; H3.2; H3.1; H4;
RP TONSL; HSPA8; BAG2 AND HSPA1B, DOMAIN, AND MUTAGENESIS OF 43-HIS--ASP-45;
RP 195-GLU--ALA-200; 216-LEU--ILE-220; 224-GLN--TYR-242; 224-GLN--ARG-227;
RP ARG-227; 234-PHE-LEU-235; 238-MET--TYR-242 AND CYS-243.
RX PubMed=33857403; DOI=10.1016/j.molcel.2021.03.041;
RA Hammond C.M., Bao H., Hendriks I.A., Carraro M., Garcia-Nieto A., Liu Y.,
RA Reveron-Gomez N., Spanos C., Chen L., Rappsilber J., Nielsen M.L.,
RA Patel D.J., Huang H., Groth A.;
RT "DNAJC9 integrates heat shock molecular chaperones into the histone
RT chaperone network.";
RL Mol. Cell 0:0-0(2021).
CC -!- FUNCTION: Acts as a dual histone chaperone and heat shock co-chaperone
CC (PubMed:33857403). As a histone chaperone, forms a co-chaperone complex
CC with MCM2 and histone H3-H4 heterodimers; and may thereby assist MCM2
CC in histone H3-H4 heterodimer recognition and facilitate the assembly of
CC histones into nucleosomes (PubMed:33857403). May also act as a histone
CC co-chaperone together with TONSL (PubMed:33857403). May recruit histone
CC chaperones ASF1A, NASP and SPT2 to histone H3-H4 heterodimers
CC (PubMed:33857403). Also plays a role as co-chaperone of the HSP70
CC family of molecular chaperone proteins, such as HSPA1A, HSPA1B and
CC HSPA8 (PubMed:17182002, PubMed:33857403). As a co-chaperone, may play a
CC role in the recruitment of HSP70-type molecular chaperone machinery to
CC histone H3-H4 substrates, thereby maintaining the histone structural
CC integrity (PubMed:33857403). Exhibits activity to assemble histones
CC onto DNA in vitro (PubMed:33857403). {ECO:0000269|PubMed:17182002,
CC ECO:0000269|PubMed:33857403}.
CC -!- SUBUNIT: Forms a co-chaperone complex with MCM2 and histone H3.3-H4
CC heterodimers (PubMed:33857403). Within the complex, interacts (via C-
CC terminus) with MCM2 (via N-terminus); the interaction is histone-
CC dependent (PubMed:33857403). Within the complex, interacts (via C-
CC terminus) with histone H3.3-H4 heterodimers; the interaction is direct
CC (PubMed:33857403). Interacts with histones H4, H3.3, H3.2 and H3.1, but
CC not with CENPA or the testis-specific histone H3.1t (PubMed:33857403).
CC Interacts (via J domain) with HSPA1A, HSPA1B and HSPA8
CC (PubMed:17182002, PubMed:33857403). May interact with TONSL; the
CC interaction seems to be histone-dependent (PubMed:33857403). May
CC interact with HSPA8 and BAG2; the interactions seem to be histone-
CC dependent (PubMed:33857403). {ECO:0000269|PubMed:17182002,
CC ECO:0000269|PubMed:33857403}.
CC -!- INTERACTION:
CC Q8WXX5; Q6NXT2: H3-5; NbExp=3; IntAct=EBI-2349100, EBI-2868501;
CC Q8WXX5; P68431: H3C12; NbExp=7; IntAct=EBI-2349100, EBI-79722;
CC Q8WXX5; Q8NDC4: MORN4; NbExp=3; IntAct=EBI-2349100, EBI-10269566;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17182002}. Cytoplasm
CC {ECO:0000269|PubMed:17182002}. Cell membrane
CC {ECO:0000269|PubMed:17182002}. Note=Predominantly nuclear. Translocates
CC to the cytoplasm and membrane after heat shock.
CC {ECO:0000269|PubMed:17182002}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, placenta, liver, skeletal
CC muscle, kidney, pancreas, thymus, ovary, colon and peripheral blood.
CC {ECO:0000269|PubMed:17182002}.
CC -!- INDUCTION: By heat shock, bacterial lipopolysaccharides (LPS), phorbol
CC 12-myristate 13-acetate (PMA), and the cytokine TNF (at protein level).
CC {ECO:0000269|PubMed:17182002}.
CC -!- DOMAIN: The functional J domain is required for the release from
CC histone-dependent chromatin-binding. {ECO:0000269|PubMed:33857403}.
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DR EMBL; AF327347; AAL56008.1; -; mRNA.
DR EMBL; AK074420; BAB85076.1; -; mRNA.
DR EMBL; AK094162; BAG52832.1; -; mRNA.
DR EMBL; CH471083; EAW54483.1; -; Genomic_DNA.
DR EMBL; BC136507; AAI36508.1; -; mRNA.
DR CCDS; CCDS7322.1; -.
DR RefSeq; NP_056005.1; NM_015190.4.
DR PDB; 7CIZ; X-ray; 1.80 A; D/H/L=180-249.
DR PDB; 7CJ0; X-ray; 2.50 A; A/D=171-249.
DR PDBsum; 7CIZ; -.
DR PDBsum; 7CJ0; -.
DR AlphaFoldDB; Q8WXX5; -.
DR SMR; Q8WXX5; -.
DR BioGRID; 116839; 229.
DR IntAct; Q8WXX5; 42.
DR MINT; Q8WXX5; -.
DR STRING; 9606.ENSP00000362041; -.
DR GlyGen; Q8WXX5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WXX5; -.
DR PhosphoSitePlus; Q8WXX5; -.
DR SwissPalm; Q8WXX5; -.
DR BioMuta; DNAJC9; -.
DR DMDM; 52782787; -.
DR EPD; Q8WXX5; -.
DR jPOST; Q8WXX5; -.
DR MassIVE; Q8WXX5; -.
DR MaxQB; Q8WXX5; -.
DR PaxDb; Q8WXX5; -.
DR PeptideAtlas; Q8WXX5; -.
DR PRIDE; Q8WXX5; -.
DR ProteomicsDB; 75112; -.
DR Antibodypedia; 29351; 139 antibodies from 25 providers.
DR DNASU; 23234; -.
DR Ensembl; ENST00000372950.6; ENSP00000362041.4; ENSG00000213551.7.
DR GeneID; 23234; -.
DR KEGG; hsa:23234; -.
DR MANE-Select; ENST00000372950.6; ENSP00000362041.4; NM_015190.5; NP_056005.1.
DR UCSC; uc010qkg.2; human.
DR CTD; 23234; -.
DR DisGeNET; 23234; -.
DR GeneCards; DNAJC9; -.
DR HGNC; HGNC:19123; DNAJC9.
DR HPA; ENSG00000213551; Tissue enhanced (bone).
DR MIM; 611206; gene.
DR neXtProt; NX_Q8WXX5; -.
DR OpenTargets; ENSG00000213551; -.
DR PharmGKB; PA38797; -.
DR VEuPathDB; HostDB:ENSG00000213551; -.
DR eggNOG; KOG0719; Eukaryota.
DR GeneTree; ENSGT00390000014549; -.
DR HOGENOM; CLU_055868_1_0_1; -.
DR InParanoid; Q8WXX5; -.
DR OMA; DLWSKIF; -.
DR OrthoDB; 1416483at2759; -.
DR PhylomeDB; Q8WXX5; -.
DR TreeFam; TF105168; -.
DR PathwayCommons; Q8WXX5; -.
DR SignaLink; Q8WXX5; -.
DR BioGRID-ORCS; 23234; 586 hits in 1076 CRISPR screens.
DR ChiTaRS; DNAJC9; human.
DR GenomeRNAi; 23234; -.
DR Pharos; Q8WXX5; Tbio.
DR PRO; PR:Q8WXX5; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8WXX5; protein.
DR Bgee; ENSG00000213551; Expressed in secondary oocyte and 179 other tissues.
DR ExpressionAtlas; Q8WXX5; baseline and differential.
DR Genevisible; Q8WXX5; HS.
DR GO; GO:0101031; C:chaperone complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IDA:UniProtKB.
DR GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:UniProtKB.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Chaperone; Cytoplasm; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..260
FT /note="DnaJ homolog subfamily C member 9"
FT /id="PRO_0000071063"
FT DOMAIN 15..82
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 171..249
FT /note="Required for histone binding"
FT /evidence="ECO:0000269|PubMed:33857403"
FT REGION 185..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MUTAGEN 43..45
FT /note="HPD->QPN: Increased binding to histones H3 and H4.
FT Less integration of histones H3 and H4 in chromatin.
FT Increased recruitment of histone deposition factors to
FT chromatin. Trapped on chromatin throughout the cell cycle
FT in a manner depending on histone-binding. Released from
FT chromatin trap; when associated with Ala-224; Ala-227; Ala-
FT 238 and Ala-242."
FT /evidence="ECO:0000269|PubMed:33857403"
FT MUTAGEN 195..200
FT /note="EEAKEA->AAAKAE: Reduces the co-chaperone complex
FT formation with MCM2; histone H3.3 and H4."
FT /evidence="ECO:0000269|PubMed:33857403"
FT MUTAGEN 216..220
FT /note="LKAAI->AKAAA: Disrupts the formation of the co-
FT chaperone complex with MCM2 and histones H3.3 and H4."
FT /evidence="ECO:0000269|PubMed:33857403"
FT MUTAGEN 224..242
FT /note="QKDRQKEMDNFLAQMEAKY->AKDAQKEMDNFLAQAEAKA: Abolishes
FT the interaction with MCM2, TONSL and histones H3.3 and H4.
FT Disrupts the formation of the co-chaperone complex with
FT MCM2 and histones H3.3 and H4."
FT /evidence="ECO:0000269|PubMed:33857403"
FT MUTAGEN 224..227
FT /note="QKDR->AKDA: Partial loss of histone dimer H3-H4
FT interaction. Reduces the formation of the co-chaperone
FT complex with MCM2 and histones H3.3 and H4."
FT /evidence="ECO:0000269|PubMed:33857403"
FT MUTAGEN 234..235
FT /note="FL->AA: Reduces the formation of the co-chaperone
FT complex with MCM2 and histones H3.3 and H4."
FT /evidence="ECO:0000269|PubMed:33857403"
FT MUTAGEN 238..242
FT /note="MEAKY->AEAKA: Partial loss of histone dimer H3-H4
FT interaction. Reduces the co-chaperone complex formation
FT with MCM2; histone H3.3 and H4."
FT /evidence="ECO:0000269|PubMed:33857403"
FT MUTAGEN 243
FT /note="C->S: Does not affect interaction with histones."
FT /evidence="ECO:0000269|PubMed:33857403"
FT HELIX 175..207
FT /evidence="ECO:0007829|PDB:7CJ0"
FT HELIX 213..242
FT /evidence="ECO:0007829|PDB:7CIZ"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:7CJ0"
SQ SEQUENCE 260 AA; 29910 MW; 6C5C34774217863F CRC64;
MGLLDLCEEV FGTADLYRVL GVRREASDGE VRRGYHKVSL QVHPDRVGEG DKEDATRRFQ
ILGKVYSVLS DREQRAVYDE QGTVDEDSPV LTQDRDWEAY WRLLFKKISL EDIQAFEKTY
KGSEEELADI KQAYLDFKGD MDQIMESVLC VQYTEEPRIR NIIQQAIDAG EVPSYNAFVK
ESKQKMNARK RRAQEEAKEA EMSRKELGLD EGVDSLKAAI QSRQKDRQKE MDNFLAQMEA
KYCKSSKGGG KKSALKKEKK
