DJC21_HUMAN
ID DJC21_HUMAN Reviewed; 531 AA.
AC Q5F1R6; Q3B7J9; Q6P086; Q6ZS43; Q86VC6;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=DnaJ homolog subfamily C member 21;
DE AltName: Full=DnaJ homolog subfamily A member 5;
DE AltName: Full=Protein GS3;
GN Name=DNAJC21; Synonyms=DNAJA5;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=15067379;
RA Chen J., Yin G., Lu Y., Lou M., Cheng H., Ni X., Hu G., Luo C., Ying K.,
RA Xie Y., Mao Y.;
RT "Cloning and characterization of a novel human cDNA encoding a J-domain
RT protein (DNAJA5) from the fetal brain.";
RL Int. J. Mol. Med. 13:735-740(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Chen J., Xie Y., Mao Y.;
RT "Cloning and characterization of a novel GS3 protein.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 126-458 (ISOFORM 3).
RC TISSUE=Skin, and 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 116-531 (ISOFORM 2).
RC TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-302 AND SER-370, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283 AND SER-370, 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511, 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 [12]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-214.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [13]
RP VARIANT BMFS3 ALA-32, INVOLVEMENT IN BMFS3, INTERACTION WITH HSPA8; PA2G4
RP AND ZNF622, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT BMFS3 ALA-32,
RP AND FUNCTION.
RX PubMed=27346687; DOI=10.1016/j.ajhg.2016.05.002;
RA Tummala H., Walne A.J., Williams M., Bockett N., Collopy L., Cardoso S.,
RA Ellison A., Wynn R., Leblanc T., Fitzgibbon J., Kelsell D.P.,
RA van Heel D.A., Payne E., Plagnol V., Dokal I., Vulliamy T.;
RT "DNAJC21 mutations link a cancer-prone bone marrow failure syndrome to
RT corruption in 60S ribosome subunit maturation.";
RL Am. J. Hum. Genet. 99:115-124(2016).
CC -!- FUNCTION: May act as a co-chaperone for HSP70. May play a role in
CC ribosomal RNA (rRNA) biogenesis, possibly in the maturation of the 60S
CC subunit. Binds the precursor 45S rRNA. {ECO:0000269|PubMed:27346687}.
CC -!- SUBUNIT: Interacts with HSPA8, PA2G4 and ZNF622.
CC {ECO:0000269|PubMed:27346687}.
CC -!- INTERACTION:
CC Q5F1R6; P42858: HTT; NbExp=6; IntAct=EBI-2654581, EBI-466029;
CC Q5F1R6; Q99551: MTERF1; NbExp=2; IntAct=EBI-2654581, EBI-2690033;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27346687}. Nucleus
CC {ECO:0000269|PubMed:27346687}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:27346687}. Note=Within the nucleus, localizes
CC primarily to the nucleolus. {ECO:0000269|PubMed:27346687}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5F1R6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5F1R6-2; Sequence=VSP_024005;
CC Name=3;
CC IsoId=Q5F1R6-3; Sequence=VSP_024004;
CC -!- TISSUE SPECIFICITY: Expressed in brain, placenta, kidney and pancreas.
CC {ECO:0000269|PubMed:15067379}.
CC -!- DISEASE: Bone marrow failure syndrome 3 (BMFS3) [MIM:617052]: A form of
CC bone marrow failure syndrome, a heterogeneous group of life-threatening
CC disorders characterized by hematopoietic defects in association with a
CC range of variable extra-hematopoietic manifestations. BMFS3 is
CC characterized by pancytopenia with onset in early childhood. Some
CC patients have additional variable non-specific features, including poor
CC growth, microcephaly, and skin anomalies. BMFS3 inheritance is
CC autosomal recessive. {ECO:0000269|PubMed:27346687}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH65745.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAI07578.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAC87112.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY258422; AAP81807.1; -; mRNA.
DR EMBL; AY177688; AAO46910.1; -; mRNA.
DR EMBL; BC050472; AAH50472.1; -; mRNA.
DR EMBL; BC065745; AAH65745.1; ALT_SEQ; mRNA.
DR EMBL; BC107577; AAI07578.1; ALT_SEQ; mRNA.
DR EMBL; AK127749; BAC87112.1; ALT_INIT; mRNA.
DR CCDS; CCDS34144.1; -. [Q5F1R6-1]
DR CCDS; CCDS3907.2; -. [Q5F1R6-2]
DR CCDS; CCDS87294.1; -. [Q5F1R6-3]
DR RefSeq; NP_001012339.2; NM_001012339.2. [Q5F1R6-1]
DR RefSeq; NP_001335349.1; NM_001348420.1. [Q5F1R6-3]
DR RefSeq; NP_919259.3; NM_194283.3. [Q5F1R6-2]
DR AlphaFoldDB; Q5F1R6; -.
DR SMR; Q5F1R6; -.
DR BioGRID; 126389; 50.
DR IntAct; Q5F1R6; 14.
DR iPTMnet; Q5F1R6; -.
DR PhosphoSitePlus; Q5F1R6; -.
DR BioMuta; DNAJC21; -.
DR DMDM; 296434479; -.
DR EPD; Q5F1R6; -.
DR jPOST; Q5F1R6; -.
DR MassIVE; Q5F1R6; -.
DR MaxQB; Q5F1R6; -.
DR PeptideAtlas; Q5F1R6; -.
DR PRIDE; Q5F1R6; -.
DR ProteomicsDB; 62776; -. [Q5F1R6-1]
DR ProteomicsDB; 62777; -. [Q5F1R6-2]
DR ProteomicsDB; 62778; -. [Q5F1R6-3]
DR Antibodypedia; 22862; 59 antibodies from 14 providers.
DR DNASU; 134218; -.
DR Ensembl; ENST00000382021.2; ENSP00000371451.2; ENSG00000168724.17. [Q5F1R6-2]
DR Ensembl; ENST00000642851.1; ENSP00000496545.1; ENSG00000168724.17. [Q5F1R6-3]
DR Ensembl; ENST00000648817.1; ENSP00000497410.1; ENSG00000168724.17. [Q5F1R6-1]
DR GeneID; 134218; -.
DR KEGG; hsa:134218; -.
DR MANE-Select; ENST00000648817.1; ENSP00000497410.1; NM_001012339.3; NP_001012339.2.
DR UCSC; uc003jjb.3; human. [Q5F1R6-1]
DR CTD; 134218; -.
DR DisGeNET; 134218; -.
DR GeneCards; DNAJC21; -.
DR GeneReviews; DNAJC21; -.
DR HGNC; HGNC:27030; DNAJC21.
DR HPA; ENSG00000168724; Low tissue specificity.
DR MalaCards; DNAJC21; -.
DR MIM; 617048; gene.
DR MIM; 617052; phenotype.
DR neXtProt; NX_Q5F1R6; -.
DR OpenTargets; ENSG00000168724; -.
DR Orphanet; 811; Shwachman-Diamond syndrome.
DR PharmGKB; PA162383874; -.
DR VEuPathDB; HostDB:ENSG00000168724; -.
DR eggNOG; KOG0714; Eukaryota.
DR eggNOG; KOG0717; Eukaryota.
DR GeneTree; ENSGT00510000047097; -.
DR HOGENOM; CLU_009539_1_0_1; -.
DR InParanoid; Q5F1R6; -.
DR OMA; SEYSENC; -.
DR OrthoDB; 858842at2759; -.
DR PhylomeDB; Q5F1R6; -.
DR TreeFam; TF314518; -.
DR PathwayCommons; Q5F1R6; -.
DR SignaLink; Q5F1R6; -.
DR BioGRID-ORCS; 134218; 56 hits in 1083 CRISPR screens.
DR ChiTaRS; DNAJC21; human.
DR GenomeRNAi; 134218; -.
DR Pharos; Q5F1R6; Tdark.
DR PRO; PR:Q5F1R6; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q5F1R6; protein.
DR Bgee; ENSG00000168724; Expressed in epithelial cell of pancreas and 183 other tissues.
DR ExpressionAtlas; Q5F1R6; baseline and differential.
DR Genevisible; Q5F1R6; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005840; C:ribosome; NAS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; NAS: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 InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR022755; Znf_C2H2_jaz.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF12171; zf-C2H2_jaz; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Cytoplasm; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..531
FT /note="DnaJ homolog subfamily C member 21"
FT /id="PRO_0000281475"
FT DOMAIN 3..69
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT ZN_FING 314..338
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 482..506
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 279..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..311
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 381
FT /note="K -> KVKYLTFRFIFALR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024004"
FT VAR_SEQ 395
FT /note="Q -> QDVPGKDSYLPAAHFQMAWGKKCVLGERRDGESEHKCAKMLLENRQ
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024005"
FT VARIANT 32
FT /note="P -> A (in BMFS3; loss of HSPA8-binding; no effect
FT on PA2G4-, nor on ZNF622-binding; dbSNP:rs879253818)"
FT /evidence="ECO:0000269|PubMed:27346687"
FT /id="VAR_076802"
FT VARIANT 214
FT /note="D -> N (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036163"
FT VARIANT 433
FT /note="E -> K (in dbSNP:rs34908091)"
FT /id="VAR_061145"
FT CONFLICT 509
FT /note="A -> V (in Ref. 1; AAP81807 and 2; AAO46910)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 531 AA; 62028 MW; D1D3ED9AD6505613 CRC64;
MKCHYEALGV RRDASEEELK KAYRKLALKW HPDKNLDNAA EAAEQFKLIQ AAYDVLSDPQ
ERAWYDNHRE ALLKGGFDGE YQDDSLDLLR YFTVTCYSGY GDDEKGFYTV YRNVFEMIAK
EELESVLEEE VDDFPTFGDS QSDYDTVVHP FYAYWQSFCT QKNFAWKEEY DTRQASNRWE
KRAMEKENKK IRDKARKEKN ELVRQLVAFI RKRDKRVQAH RKLVEEQNAE KARKAEEMRR
QQKLKQAKLV EQYREQSWMT MANLEKELQE MEARYEKEFG DGSDENEMEE HELKDEEDGK
DSDEAEDAEL YDDLYCPACD KSFKTEKAMK NHEKSKKHRE MVALLKQQLE EEEENFSRPQ
IDENPLDDNS EEEMEDAPKQ KLSKKQKKKK QKPAQNYDDN FNVNGPGEGV KVDPEDTNLN
QDSAKELEDS PQENVSVTEI IKPCDDPKSE AKSVPKPKGK KTKDMKKPVR VPAEPQTMSV
LISCTTCHSE FPSRNKLFDH LKATGHARAP SSSSLNSATS SQSKKEKRKN R
