ID   DNJB4_HUMAN             Reviewed;         337 AA.
AC   Q9UDY4; B2R824; Q13431;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   28-JAN-2026, entry version 190.
DE   RecName: Full=DnaJ homolog subfamily B member 4;
DE   AltName: Full=Heat shock 40 kDa protein 1 homolog;
DE            Short=HSP40 homolog;
DE            Short=Heat shock protein 40 homolog;
DE   AltName: Full=Human liver DnaJ-like protein;
GN   Name=DNAJB4; Synonyms=DNAJW, HLJ1;
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], INDUCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=9546042; DOI=10.1016/s0167-4838(97)00207-0;
RA   Hoe K.L., Won M., Chung K.S., Jang Y.J., Lee S.B., Kim D.U., Lee J.W.,
RA   Yun J.H., Yoo H.S.;
RT   "Isolation of a new member of DnaJ-like heat shock protein 40 (Hsp40) from
RT   human liver.";
RL   Biochim. Biophys. Acta 1383:4-8(1998).
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.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].
RC   TISSUE=Lymph;
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   PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RA   Won M., Moon K.-M., Lee C.-E., Yoo H.-S.;
RL   Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PROTEIN SEQUENCE OF 2-13; 45-59; 166-177; 219-236; 260-275 AND 293-302,
RP   CLEAVAGE OF INITIATOR METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RA   Bienvenut W.V., Waridel P., Quadroni M.;
RL   Submitted (MAR-2009) to UniProtKB.
RN   [7]
RP   HOMODIMERIZATION.
RX   PubMed=15661747; DOI=10.1074/jbc.m408349200;
RA   Borges J.C., Fischer H., Craievich A.F., Ramos C.H.I.;
RT   "Low resolution structural study of two human HSP40 chaperones in solution.
RT   DJA1 from subfamily A and DJB4 from subfamily B have different quaternary
RT   structures.";
RL   J. Biol. Chem. 280:13671-13681(2005).
RN   [8]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH OPRM1.
RX   PubMed=16542645; DOI=10.1016/j.brainres.2006.01.125;
RA   Ancevska-Taneva N., Onoprishvili I., Andria M.L., Hiller J.M., Simon E.J.;
RT   "A member of the heat shock protein 40 family, hlj1, binds to the carboxyl
RT   tail of the human mu opioid receptor.";
RL   Brain Res. 1081:28-33(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION BY
RP   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   [10]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18837411;
RA   Lin X., Ma L., Wang J., Tan Y., Wen Q., Luo W., Su J., Lin Y., Wang X.;
RT   "Preparation of the anti-HLJ1 monoclonal antibodies and establishment of
RT   method for detection of the antigen.";
RL   Sheng Wu Gong Cheng Xue Bao 24:1293-1299(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-148, AND
RP   IDENTIFICATION BY 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   [12]
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   [13]
RP   INTERACTION WITH SDIM1.
RX   PubMed=21255413; DOI=10.1186/1750-1326-6-9;
RA   Lei J.X., Cassone C.G., Luebbert C., Liu Q.Y.;
RT   "A novel neuron-enriched protein SDIM1 is down regulated in Alzheimer's
RT   brains and attenuates cell death induced by DNAJB4 over-expression in
RT   neuro-progenitor cells.";
RL   Mol. Neurodegener. 6:9-9(2011).
RN   [14]
RP   FUNCTION.
RX   PubMed=24318877; DOI=10.1074/jbc.m113.521997;
RA   Rauch J.N., Gestwicki J.E.;
RT   "Binding of human nucleotide exchange factors to heat shock protein 70
RT   (Hsp70) generates functionally distinct complexes in vitro.";
RL   J. Biol. Chem. 289:1402-1414(2014).
RN   [15]
RP   INVOLVEMENT IN CMYO21, AND VARIANT CMYO21 GLY-61.
RX   PubMed=36344539; DOI=10.1038/s41598-022-22036-z;
RA   Al-Kasbi G., Al-Murshedi F., Al-Kindi A., Al-Hashimi N., Al-Thihli K.,
RA   Al-Saegh A., Al-Futaisi A., Al-Mamari W., Al-Asmi A., Bruwer Z.,
RA   Al-Kharusi K., Al-Rashdi S., Zadjali F., Al-Yahyaee S., Al-Maawali A.;
RT   "The diagnostic yield, candidate genes, and pitfalls for a genetic study of
RT   intellectual disability in 118 middle eastern families.";
RL   Sci. Rep. 12:18862-18862(2022).
RN   [16]
RP   VARIANTS CMYO21 GLN-25; SER-262 AND 286-LYS--SER-337 DEL, CHARACTERIZATION
RP   OF VARIANTS CMYO21 GLN-25; SER-262 AND 286-LYS--SER-337 DEL, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=36264506; DOI=10.1007/s00401-022-02510-8;
RA   Weihl C.C., Toepf A., Bengoechea R., Duff J., Charlton R., Garcia S.K.,
RA   Dominguez-Gonzalez C., Alsaman A., Hernandez-Lain A., Franco L.V.,
RA   Sanchez M.E.P., Beecroft S.J., Goullee H., Daw J., Bhadra A., True H.,
RA   Inoue M., Findlay A.R., Laing N., Olive M., Ravenscroft G., Straub V.;
RT   "Loss of function variants in DNAJB4 cause a myopathy with early
RT   respiratory failure.";
RL   Acta Neuropathol. 145:127-143(2023).
CC   -!- FUNCTION: Probable chaperone. Stimulates ATP hydrolysis and the folding
CC       of unfolded proteins mediated by HSPA1A/B (in vitro) (PubMed:24318877).
CC       {ECO:0000269|PubMed:24318877}.
CC   -!- SUBUNIT: Homodimer. The C-terminal section interacts with the C-
CC       terminal tail of OPRM1. Also interacts with SDIM1.
CC       {ECO:0000269|PubMed:16542645, ECO:0000269|PubMed:21255413}.
CC   -!- INTERACTION:
CC       Q9UDY4; P54253: ATXN1; NbExp=3; IntAct=EBI-356960, EBI-930964;
CC       Q9UDY4; P42858: HTT; NbExp=3; IntAct=EBI-356960, EBI-466029;
CC       Q9UDY4; Q9Y230: RUVBL2; NbExp=3; IntAct=EBI-356960, EBI-352939;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18837411}. Cell
CC       membrane {ECO:0000269|PubMed:16542645}. Cytoplasm, myofibril,
CC       sarcomere, Z line {ECO:0000269|PubMed:36264506}. Note=Cytoplasmic
CC       according to PubMed:18837411 and membrane-associated according to
CC       PubMed:16542645.
CC   -!- TISSUE SPECIFICITY: Expressed in heart, pancreas and skeletal muscle,
CC       and to a lesser extent in brain, placenta and liver.
CC       {ECO:0000269|PubMed:9546042}.
CC   -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:9546042}.
CC   -!- DISEASE: Congenital myopathy 21 with early respiratory failure (CMYO21)
CC       [MIM:620326]: An autosomal recessive muscle disorder characterized by
CC       diaphragmatic weakness, respiratory impairment, and spinal rigidity.
CC       Disease onset ranges from early childhood to adulthood and severity is
CC       variable. Death from respiratory failure may occur in severe cases.
CC       Some affected individuals may show developmental delay and hypertrophic
CC       cardiomyopathy. {ECO:0000269|PubMed:36264506,
CC       ECO:0000269|PubMed:36344539}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
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DR   EMBL; U40992; AAC14483.2; -; mRNA.
DR   EMBL; AK313205; BAG36021.1; -; mRNA.
DR   EMBL; CH471059; EAX06354.1; -; Genomic_DNA.
DR   EMBL; BC034721; AAH34721.1; -; mRNA.
DR   EMBL; U41290; AAB07346.1; ALT_FRAME; Genomic_DNA.
DR   CCDS; CCDS684.1; -.
DR   PIR; G02272; G02272.
DR   RefSeq; NP_001304028.1; NM_001317099.2.
DR   RefSeq; NP_001304029.1; NM_001317100.1.
DR   RefSeq; NP_001304030.1; NM_001317101.1.
DR   RefSeq; NP_001304031.1; NM_001317102.1.
DR   RefSeq; NP_001304032.1; NM_001317103.1.
DR   RefSeq; NP_008965.2; NM_007034.4.
DR   AlphaFoldDB; Q9UDY4; -.
DR   SMR; Q9UDY4; -.
DR   BioGRID; 116263; 172.
DR   FunCoup; Q9UDY4; 2538.
DR   IntAct; Q9UDY4; 119.
DR   MINT; Q9UDY4; -.
DR   STRING; 9606.ENSP00000359799; -.
DR   GlyGen; Q9UDY4; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9UDY4; -.
DR   PhosphoSitePlus; Q9UDY4; -.
DR   BioMuta; DNAJB4; -.
DR   DMDM; 8928155; -.
DR   jPOST; Q9UDY4; -.
DR   MassIVE; Q9UDY4; -.
DR   PaxDb; 9606-ENSP00000359799; -.
DR   PeptideAtlas; Q9UDY4; -.
DR   ProteomicsDB; 84132; -.
DR   Pumba; Q9UDY4; -.
DR   Antibodypedia; 33498; 269 antibodies from 31 providers.
DR   DNASU; 11080; -.
DR   Ensembl; ENST00000370763.6; ENSP00000359799.5; ENSG00000162616.10.
DR   GeneID; 11080; -.
DR   KEGG; hsa:11080; -.
DR   MANE-Select; ENST00000370763.6; ENSP00000359799.5; NM_007034.5; NP_008965.2.
DR   UCSC; uc001dij.4; human.
DR   AGR; HGNC:14886; -.
DR   ClinPGx; PA27416; -.
DR   CTD; 11080; -.
DR   DisGeNET; 11080; -.
DR   GeneCards; DNAJB4; -.
DR   HGNC; HGNC:14886; DNAJB4.
DR   HPA; ENSG00000162616; Low tissue specificity.
DR   MalaCards; DNAJB4; -.
DR   MIM; 611327; gene.
DR   MIM; 620326; phenotype.
DR   OpenTargets; ENSG00000162616; -.
DR   Orphanet; 700170; Asymetric thumb-handgrip weakness-distal myopathy.
DR   VEuPathDB; HostDB:ENSG00000162616; -.
DR   eggNOG; KOG0714; Eukaryota.
DR   GeneTree; ENSGT00940000156826; -.
DR   HOGENOM; CLU_017633_0_0_1; -.
DR   InParanoid; Q9UDY4; -.
DR   OMA; MPIRKEG; -.
DR   OrthoDB; 550424at2759; -.
DR   PAN-GO; Q9UDY4; 4 GO annotations based on evolutionary models.
DR   PhylomeDB; Q9UDY4; -.
DR   PathwayCommons; Q9UDY4; -.
DR   SignaLink; Q9UDY4; -.
DR   Agora; ENSG00000162616; -.
DR   BioGRID-ORCS; 11080; 9 hits in 1151 CRISPR screens.
DR   CD-CODE; 91857CE7; Nucleolus.
DR   CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities.
DR   ChiTaRS; DNAJB4; human.
DR   GeneWiki; DNAJB4; -.
DR   GenomeRNAi; 11080; -.
DR   Pharos; Q9UDY4; Tbio.
DR   PRO; PR:Q9UDY4; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9UDY4; protein.
DR   Bgee; ENSG00000162616; Expressed in skeletal muscle tissue of rectus abdominis and 211 other cell types or tissues.
DR   ExpressionAtlas; Q9UDY4; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR   GO; GO:0001671; F:ATPase activator activity; IDA:UniProtKB.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IPI:UniProtKB.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0009408; P:response to heat; TAS:ProtInc.
DR   GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd10747; DnaJ_C; 1.
DR   FunFam; 1.10.287.110:FF:000005; DnaJ (Hsp40) homolog, subfamily B, member 4; 1.
DR   FunFam; 2.60.260.20:FF:000002; Dnaj homolog subfamily b member; 1.
DR   FunFam; 2.60.260.20:FF:000007; dnaJ homolog subfamily B member 5; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR051339; DnaJ_subfamily_B.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR036869; J_dom_sf.
DR   PANTHER; PTHR24078:SF288; DNAJ HOMOLOG SUBFAMILY B MEMBER 4; 1.
DR   PANTHER; PTHR24078; DNAJ HOMOLOG SUBFAMILY C MEMBER; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Chaperone; Cytoplasm; Direct protein sequencing;
KW   Disease variant; Membrane; Phosphoprotein; Proteomics identification;
KW   Reference proteome; Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.6"
FT   CHAIN           2..337
FT                   /note="DnaJ homolog subfamily B member 4"
FT                   /id="PRO_0000071021"
FT   DOMAIN          2..70
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   MOD_RES         122
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         148
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   VARIANT         25
FT                   /note="R -> Q (in CMYO21; loss of function in
FT                   chaperone-mediated protein folding; in cells subjected to
FT                   heat shock, it results in increased protein aggregation and
FT                   cell death compared to the wild type; unable to complement
FT                   growth defects in a yeast complementation assay; does not
FT                   affect subcellular location at the Z line;
FT                   dbSNP:rs1660297324)"
FT                   /evidence="ECO:0000269|PubMed:36264506"
FT                   /id="VAR_088469"
FT   VARIANT         61
FT                   /note="R -> G (in CMYO21; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:36344539"
FT                   /id="VAR_088470"
FT   VARIANT         262
FT                   /note="L -> S (in CMYO21; severely decreased protein
FT                   abundance in homozygous patient cells; increased
FT                   degradation)"
FT                   /evidence="ECO:0000269|PubMed:36264506"
FT                   /id="VAR_088471"
FT   VARIANT         286..337
FT                   /note="Missing (in CMYO21; severely decreased protein
FT                   abundance in homozygous patient cells; increased
FT                   degradation)"
FT                   /evidence="ECO:0000269|PubMed:36264506"
FT                   /id="VAR_088472"
SQ   SEQUENCE   337 AA;  37807 MW;  C7A9C613F73BCDAC CRC64;
     MGKDYYCILG IEKGASDEDI KKAYRKQALK FHPDKNKSPQ AEEKFKEVAE AYEVLSDPKK
     REIYDQFGEE GLKGGAGGTD GQGGTFRYTF HGDPHATFAA FFGGSNPFEI FFGRRMGGGR
     DSEEMEIDGD PFSAFGFSMN GYPRDRNSVG PSRLKQDPPV IHELRVSLEE IYSGCTKRMK
     ISRKRLNADG RSYRSEDKIL TIEIKKGWKE GTKITFPREG DETPNSIPAD IVFIIKDKDH
     PKFKRDGSNI IYTAKISLRE ALCGCSINVP TLDGRNIPMS VNDIVKPGMR RRIIGYGLPF
     PKNPDQRGDL LIEFEVSFPD TISSSSKEVL RKHLPAS
//