DJB14_HUMAN
ID DJB14_HUMAN Reviewed; 379 AA.
AC Q8TBM8; Q6UXN1; Q7Z3P0; Q86TA7; Q86TM0; Q9GZU9;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=DnaJ homolog subfamily B member 14 {ECO:0000312|HGNC:HGNC:25881};
GN Name=DNAJB14 {ECO:0000312|HGNC:HGNC:25881};
GN ORFNames=UNQ9427/PRO34683 {ECO:0000303|PubMed:12975309};
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 2).
RC TISSUE=Testis;
RA Sha J.H., Zhou Z.M., Xu M.;
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-101 (ISOFORM 1).
RC TISSUE=Fetal kidney, and Spinal cord;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 107-379.
RC TISSUE=Placenta;
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 [7]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=21673190; DOI=10.1128/mbio.00101-11;
RA Goodwin E.C., Lipovsky A., Inoue T., Magaldi T.G., Edwards A.P.,
RA Van Goor K.E., Paton A.W., Paton J.C., Atwood W.J., Tsai B., DiMaio D.;
RT "BiP and multiple DNAJ molecular chaperones in the endoplasmic reticulum
RT are required for efficient simian virus 40 infection.";
RL MBio 2:E00101-E00111(2011).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND INTERACTION WITH HSPA8.
RX PubMed=23018488; DOI=10.1247/csf.12017;
RA Sopha P., Kadokura H., Yamamoto Y.H., Takeuchi M., Saito M., Tsuru A.,
RA Kohno K.;
RT "A novel mammalian ER-located J-protein, DNAJB14, can accelerate ERAD of
RT misfolded membrane proteins.";
RL Cell Struct. Funct. 37:177-187(2012).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HSPA8, AND MUTAGENESIS OF
RP HIS-136.
RX PubMed=24732912; DOI=10.1371/journal.pone.0094322;
RA Goodwin E.C., Motamedi N., Lipovsky A., Fernandez-Busnadiego R., DiMaio D.;
RT "Expression of DNAJB12 or DNAJB14 causes coordinate invasion of the nucleus
RT by membranes associated with a novel nuclear pore structure.";
RL PLoS ONE 9:E94322-E94322(2014).
RN [10]
RP FUNCTION (MICROBIAL INFECTION), AND IDENTIFICATION IN A COMPLEX WITH
RP DNAJB12.
RX PubMed=24675744; DOI=10.1371/journal.ppat.1004007;
RA Walczak C.P., Ravindran M.S., Inoue T., Tsai B.;
RT "A cytosolic chaperone complexes with dynamic membrane J-proteins and
RT mobilizes a nonenveloped virus out of the endoplasmic reticulum.";
RL PLoS Pathog. 10:E1004007-E1004007(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]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27916661; DOI=10.1016/j.molcel.2016.10.027;
RA Li K., Jiang Q., Bai X., Yang Y.F., Ruan M.Y., Cai S.Q.;
RT "Tetrameric assembly of K(+) channels requires ER-located chaperone
RT proteins.";
RL Mol. Cell 65:52-65(2017).
CC -!- FUNCTION: Acts as a co-chaperone with HSPA8/Hsc70; required to promote
CC protein folding and trafficking, prevent aggregation of client
CC proteins, and promote unfolded proteins to endoplasmic reticulum-
CC associated degradation (ERAD) pathway (PubMed:24732912). Acts by
CC determining HSPA8/Hsc70's ATPase and polypeptide-binding activities
CC (PubMed:24732912). Can also act independently of HSPA8/Hsc70: together
CC with DNAJB12, acts as a chaperone that promotes maturation of potassium
CC channels KCND2 and KCNH2 by stabilizing nascent channel subunits and
CC assembling them into tetramers (PubMed:27916661). While stabilization
CC of nascent channel proteins is dependent on HSPA8/Hsc70, the process of
CC oligomerization of channel subunits is independent of HSPA8/Hsc70
CC (PubMed:27916661). When overexpressed, forms membranous structures
CC together with DNAJB12 and HSPA8/Hsc70 within the nucleus; the role of
CC these structures, named DJANGOs, is still unclear (PubMed:24732912).
CC {ECO:0000269|PubMed:23018488, ECO:0000269|PubMed:24732912,
CC ECO:0000269|PubMed:27916661}.
CC -!- FUNCTION: (Microbial infection) In case of infection by polyomavirus,
CC involved in the virus endoplasmic reticulum membrane penetration and
CC infection (PubMed:21673190, PubMed:24675744).
CC {ECO:0000269|PubMed:21673190, ECO:0000269|PubMed:24675744}.
CC -!- SUBUNIT: Interacts (via J domain) with HSPA8/Hsc70 (PubMed:23018488,
CC PubMed:24732912, PubMed:27916661). Forms a multiprotein complex, at
CC least composed of DNAJB12, DNAJB14, HSPA8/Hsc70 and SGTA; interaction
CC with DNAJB14 and HSPA8/Hsc70 is direct (PubMed:24675744).
CC {ECO:0000269|PubMed:23018488, ECO:0000269|PubMed:24675744,
CC ECO:0000269|PubMed:24732912, ECO:0000269|PubMed:27916661}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23018488, ECO:0000269|PubMed:24732912,
CC ECO:0000269|PubMed:27916661}; Single-pass membrane protein
CC {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:24732912}; Single-
CC pass membrane protein {ECO:0000255}. Note=Localizes to the endoplasmic
CC reticulum membrane (PubMed:23018488, PubMed:24732912, PubMed:27916661).
CC When overexpressed, forms membranous structures in the nucleus
CC (PubMed:24732912). {ECO:0000269|PubMed:23018488,
CC ECO:0000269|PubMed:24732912, ECO:0000269|PubMed:27916661}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TBM8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TBM8-2; Sequence=VSP_024006, VSP_024007;
CC -!- SIMILARITY: Belongs to the DnaJ family. DNAJB12/DNAJB14 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ88639.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14645.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14893.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD97796.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AY186740; AAO31693.1; -; mRNA.
DR EMBL; AY358272; AAQ88639.1; ALT_SEQ; mRNA.
DR EMBL; AL833076; CAD89928.1; -; mRNA.
DR EMBL; BX537609; CAD97796.1; ALT_SEQ; mRNA.
DR EMBL; AC097460; AAY41012.1; -; Genomic_DNA.
DR EMBL; BC022248; AAH22248.1; -; mRNA.
DR EMBL; AK024343; BAB14893.1; ALT_SEQ; mRNA.
DR EMBL; AK023700; BAB14645.1; ALT_INIT; mRNA.
DR CCDS; CCDS34035.1; -. [Q8TBM8-1]
DR RefSeq; NP_001026893.1; NM_001031723.3. [Q8TBM8-1]
DR RefSeq; NP_001265239.1; NM_001278310.1.
DR RefSeq; XP_011530564.1; XM_011532262.2. [Q8TBM8-2]
DR RefSeq; XP_011530565.1; XM_011532263.2.
DR AlphaFoldDB; Q8TBM8; -.
DR SMR; Q8TBM8; -.
DR BioGRID; 123047; 90.
DR IntAct; Q8TBM8; 5.
DR MINT; Q8TBM8; -.
DR STRING; 9606.ENSP00000404381; -.
DR TCDB; 1.P.1.1.1; the polyoma virus sv40 er penetration channel (vpec) family.
DR iPTMnet; Q8TBM8; -.
DR PhosphoSitePlus; Q8TBM8; -.
DR BioMuta; DNAJB14; -.
DR DMDM; 74751385; -.
DR EPD; Q8TBM8; -.
DR jPOST; Q8TBM8; -.
DR MassIVE; Q8TBM8; -.
DR MaxQB; Q8TBM8; -.
DR PaxDb; Q8TBM8; -.
DR PeptideAtlas; Q8TBM8; -.
DR PRIDE; Q8TBM8; -.
DR ProteomicsDB; 74031; -. [Q8TBM8-1]
DR ProteomicsDB; 74032; -. [Q8TBM8-2]
DR Antibodypedia; 45017; 101 antibodies from 22 providers.
DR DNASU; 79982; -.
DR Ensembl; ENST00000442697.7; ENSP00000404381.2; ENSG00000164031.17. [Q8TBM8-1]
DR GeneID; 79982; -.
DR KEGG; hsa:79982; -.
DR MANE-Select; ENST00000442697.7; ENSP00000404381.2; NM_001031723.4; NP_001026893.1.
DR UCSC; uc003hvl.5; human. [Q8TBM8-1]
DR CTD; 79982; -.
DR DisGeNET; 79982; -.
DR GeneCards; DNAJB14; -.
DR HGNC; HGNC:25881; DNAJB14.
DR HPA; ENSG00000164031; Low tissue specificity.
DR MIM; 617487; gene.
DR neXtProt; NX_Q8TBM8; -.
DR OpenTargets; ENSG00000164031; -.
DR PharmGKB; PA142671973; -.
DR VEuPathDB; HostDB:ENSG00000164031; -.
DR eggNOG; KOG0714; Eukaryota.
DR GeneTree; ENSGT00940000157887; -.
DR HOGENOM; CLU_043579_3_0_1; -.
DR InParanoid; Q8TBM8; -.
DR OMA; AYCRKPA; -.
DR OrthoDB; 1173544at2759; -.
DR PhylomeDB; Q8TBM8; -.
DR TreeFam; TF105145; -.
DR PathwayCommons; Q8TBM8; -.
DR SignaLink; Q8TBM8; -.
DR BioGRID-ORCS; 79982; 11 hits in 1074 CRISPR screens.
DR ChiTaRS; DNAJB14; human.
DR GenomeRNAi; 79982; -.
DR Pharos; Q8TBM8; Tbio.
DR PRO; PR:Q8TBM8; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8TBM8; protein.
DR Bgee; ENSG00000164031; Expressed in lateral nuclear group of thalamus and 202 other tissues.
DR ExpressionAtlas; Q8TBM8; baseline and differential.
DR Genevisible; Q8TBM8; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:UniProtKB.
DR GO; GO:0071218; P:cellular response to misfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IDA:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
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; IPR015399; DUF1977_DnaJ-like.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF09320; DUF1977; 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 Alternative splicing; Chaperone; Endoplasmic reticulum;
KW Host-virus interaction; Membrane; Nucleus; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..379
FT /note="DnaJ homolog subfamily B member 14"
FT /id="PRO_0000281478"
FT TOPO_DOM 1..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..379
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 108..172
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 55..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..85
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005, ECO:0000303|Ref.1"
FT /id="VSP_024006"
FT VAR_SEQ 86..102
FT /note="GEGGKGYTKDQVDGVLS -> MDIGTLIWDGGPVPNTH (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:17974005, ECO:0000303|Ref.1"
FT /id="VSP_024007"
FT MUTAGEN 136
FT /note="H->Q: Abolishes interaction with HSPA8/Hsc70."
FT /evidence="ECO:0000269|PubMed:24732912"
FT CONFLICT 143
FT /note="P -> L (in Ref. 6; BAB14893)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="N -> T (in Ref. 1; AAO31693)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 42516 MW; 02FB6D940DECA170 CRC64;
MEGNRDEAEK CVEIAREALN AGNREKAQRF LQKAEKLYPL PSARALLEII MKNGSTAGNS
PHCRKPSGSG DQSKPNCTKD STSGSGEGGK GYTKDQVDGV LSINKCKNYY EVLGVTKDAG
DEDLKKAYRK LALKFHPDKN HAPGATDAFK KIGNAYAVLS NPEKRKQYDL TGNEEQACNH
QNNGRFNFHR GCEADITPED LFNIFFGGGF PSGSVHSFSN GRAGYSQQHQ HRHSGHEREE
ERGDGGFSVF IQLMPIIVLI LVSLLSQLMV SNPPYSLYPR SGTGQTIKMQ TENLGVVYYV
NKDFKNEYKG MLLQKVEKSV EEDYVTNIRN NCWKERQQKT DMQYAAKVYR DDRLRRKADA
LSMDNCKELE RLTSLYKGG
