ID   HSP7E_HUMAN             Reviewed;         509 AA.
AC   Q0VDF9; A8K8F8; B0YIY9; Q9P0X2; Q9UI07;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   28-JAN-2026, entry version 142.
DE   RecName: Full=Heat shock 70 kDa protein 14;
DE   AltName: Full=HSP70-like protein 1;
DE   AltName: Full=Heat shock protein HSP60;
DE   AltName: Full=Heat shock protein family A member 14;
GN   Name=HSPA14; Synonyms=HSP60, HSP70L1;
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].
RX   PubMed=14592822; DOI=10.1182/blood-2003-08-2828;
RA   Wan T., Zhou X., Chen G., An H., Chen T., Zhang W., Liu S., Jiang Y.,
RA   Yang F., Wu Y., Cao X.;
RT   "Novel heat shock protein Hsp70L1 activates dendritic cells and acts as a
RT   Th1 polarizing adjuvant.";
RL   Blood 103:1747-1754(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Adrenal gland;
RX   PubMed=10931946; DOI=10.1073/pnas.160270997;
RA   Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA   Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA   Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA   Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA   Chen M.-D., Chen J.-L.;
RT   "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT   and full-length cDNA cloning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NHLBI resequencing and genotyping service (RS&G);
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
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].
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   IMMUNOADJUVANT ABILITY.
RX   PubMed=15930317; DOI=10.1158/0008-5472.can-04-3912;
RA   Wu Y., Wan T., Zhou X., Wang B., Yang F., Li N., Chen G., Dai S., Liu S.,
RA   Zhang M., Cao X.;
RT   "Hsp70-like protein 1 fusion protein enhances induction of carcinoembryonic
RT   antigen-specific CD8+ CTL response by dendritic cell vaccine.";
RL   Cancer Res. 65:4947-4954(2005).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE RAC COMPLEX, AND
RP   INTERACTION WITH DNAJC2.
RX   PubMed=16002468; DOI=10.1073/pnas.0504400102;
RA   Otto H., Conz C., Maier P., Wolfle T., Suzuki C.K., Jeno P., Rucknagel P.,
RA   Stahl J., Rospert S.;
RT   "The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated
RT   complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10064-10069(2005).
RN   [10]
RP   IDENTIFICATION.
RX   PubMed=15802566; DOI=10.1126/science.1109247;
RA   Hundley H.A., Walter W., Bairstow S., Craig E.A.;
RT   "Human Mpp11 J protein: ribosome-tethered molecular chaperones are
RT   ubiquitous.";
RL   Science 308:1032-1034(2005).
RN   [11]
RP   IMMUNOADJUVANT ABILITY.
RX   PubMed=18851947; DOI=10.1016/j.bbrc.2008.10.002;
RA   Zeng R., Zhang Z., Mei X., Gong W., Wei L.;
RT   "Protective effect of a RSV subunit vaccine candidate G1F/M2 was enhanced
RT   by a HSP70-Like protein in mice.";
RL   Biochem. Biophys. Res. Commun. 377:495-499(2008).
RN   [12]
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   [13]
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   [14]
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).
RN   [15]
RP   VARIANT [LARGE SCALE ANALYSIS] VAL-85.
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).
CC   -!- FUNCTION: Component of the ribosome-associated complex (RAC), a complex
CC       involved in folding or maintaining nascent polypeptides in a folding-
CC       competent state. In the RAC complex, binds to the nascent polypeptide
CC       chain, while DNAJC2 stimulates its ATPase activity.
CC       {ECO:0000269|PubMed:16002468}.
CC   -!- SUBUNIT: Component of ribosome-associated complex (RAC), a heterodimer
CC       composed of Hsp70/DnaK-type chaperone HSPA14 and Hsp40/DnaJ-type
CC       chaperone DNAJC2. {ECO:0000269|PubMed:16002468}.
CC   -!- INTERACTION:
CC       Q0VDF9; Q99543: DNAJC2; NbExp=5; IntAct=EBI-8773684, EBI-11017224;
CC       Q0VDF9; Q8NET5: NFAM1; NbExp=2; IntAct=EBI-8773684, EBI-11990542;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16002468}.
CC   -!- MISCELLANEOUS: Acts as a potent immunoadjuvant, capable to interact
CC       with antigen-presenting cells and generating efficient CD8(+) T-cell
CC       responses. May be used as adjuvant to enhance effect of vaccine G1F/M2,
CC       a candidate vaccine against respiratory syncytial virus (RSV), a major
CC       respiratory pathogen in newborns (PubMed:18851947). May also be used as
CC       adjuvant to prepare antigenic fusion protein for the therapeutics of
CC       cancers (PubMed:15930317). {ECO:0000305|PubMed:15930317,
CC       ECO:0000305|PubMed:18851947}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; AF143723; AAF66640.1; -; mRNA.
DR   EMBL; AF112210; AAF17198.1; -; mRNA.
DR   EMBL; AK292323; BAF85012.1; -; mRNA.
DR   EMBL; EF444968; ACA05969.1; -; Genomic_DNA.
DR   EMBL; EF444968; ACA05970.1; -; Genomic_DNA.
DR   EMBL; AC069544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471072; EAW86258.1; -; Genomic_DNA.
DR   EMBL; BC119690; AAI19691.1; -; mRNA.
DR   CCDS; CCDS7103.1; -.
DR   RefSeq; NP_057383.2; NM_016299.4.
DR   AlphaFoldDB; Q0VDF9; -.
DR   SMR; Q0VDF9; -.
DR   BioGRID; 119358; 129.
DR   ComplexPortal; CPX-2642; Ribosome-associated complex.
DR   DIP; DIP-62114N; -.
DR   FunCoup; Q0VDF9; 3089.
DR   IntAct; Q0VDF9; 54.
DR   MINT; Q0VDF9; -.
DR   STRING; 9606.ENSP00000367623; -.
DR   ChEMBL; CHEMBL5169146; -.
DR   GlyGen; Q0VDF9; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; Q0VDF9; -.
DR   PhosphoSitePlus; Q0VDF9; -.
DR   SwissPalm; Q0VDF9; -.
DR   BioMuta; HSPA14; -.
DR   DMDM; 121948121; -.
DR   jPOST; Q0VDF9; -.
DR   MassIVE; Q0VDF9; -.
DR   PaxDb; 9606-ENSP00000367623; -.
DR   PeptideAtlas; Q0VDF9; -.
DR   ProteomicsDB; 58825; -.
DR   Pumba; Q0VDF9; -.
DR   Antibodypedia; 37843; 150 antibodies from 29 providers.
DR   DNASU; 51182; -.
DR   Ensembl; ENST00000378372.8; ENSP00000367623.3; ENSG00000187522.16.
DR   GeneID; 51182; -.
DR   KEGG; hsa:51182; -.
DR   MANE-Select; ENST00000378372.8; ENSP00000367623.3; NM_016299.4; NP_057383.2.
DR   UCSC; uc001inf.5; human.
DR   AGR; HGNC:29526; -.
DR   ClinPGx; PA134979057; -.
DR   CTD; 51182; -.
DR   DisGeNET; 51182; -.
DR   GeneCards; HSPA14; -.
DR   HGNC; HGNC:29526; HSPA14.
DR   HPA; ENSG00000187522; Low tissue specificity.
DR   MIM; 610369; gene.
DR   OpenTargets; ENSG00000187522; -.
DR   VEuPathDB; HostDB:ENSG00000187522; -.
DR   eggNOG; KOG0101; Eukaryota.
DR   GeneTree; ENSGT00940000156380; -.
DR   HOGENOM; CLU_005965_0_3_1; -.
DR   InParanoid; Q0VDF9; -.
DR   OMA; GSTCACA; -.
DR   OrthoDB; 29851at2759; -.
DR   PAN-GO; Q0VDF9; 15 GO annotations based on evolutionary models.
DR   PhylomeDB; Q0VDF9; -.
DR   PathwayCommons; Q0VDF9; -.
DR   Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR   SignaLink; Q0VDF9; -.
DR   Agora; ENSG00000187522; -.
DR   BioGRID-ORCS; 51182; 303 hits in 1167 CRISPR screens.
DR   ChiTaRS; HSPA14; human.
DR   GeneWiki; HSPA14; -.
DR   GenomeRNAi; 51182; -.
DR   Pharos; Q0VDF9; Tbio.
DR   PRO; PR:Q0VDF9; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q0VDF9; protein.
DR   Bgee; ENSG00000187522; Expressed in secondary oocyte and 194 other cell types or tissues.
DR   ExpressionAtlas; Q0VDF9; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR   GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0051083; P:'de novo' cotranslational protein folding; TAS:UniProtKB.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   CDD; cd10238; ASKHA_NBD_HSP70_HSPA14; 1.
DR   FunFam; 2.60.34.10:FF:000013; Heat shock 70 kDa protein 14; 1.
DR   FunFam; 3.30.30.30:FF:000008; heat shock 70 kDa protein 14; 1.
DR   FunFam; 3.90.640.10:FF:000010; heat shock 70 kDa protein 14; 1.
DR   FunFam; 3.30.420.40:FF:000171; Heat shock 70 kDa protein 4; 1.
DR   FunFam; 3.30.420.40:FF:000433; Heat shock protein family A (Hsp70) member 14; 1.
DR   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   Gene3D; 3.90.640.10; Actin, Chain A, domain 4; 1.
DR   Gene3D; 2.60.34.10; Substrate Binding Domain Of DNAk, Chain A, domain 1; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   InterPro; IPR042049; HSPA14_NBD.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding;
KW   Proteomics identification; Reference proteome.
FT   CHAIN           1..509
FT                   /note="Heat shock 70 kDa protein 14"
FT                   /id="PRO_0000289946"
FT   VARIANT         85
FT                   /note="A -> V (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs374837716)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036347"
FT   CONFLICT        6
FT                   /note="V -> A (in Ref. 3; BAF85012)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        15
FT                   /note="V -> E (in Ref. 1; AAF66640)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        282
FT                   /note="L -> P (in Ref. 2; AAF17198)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        312
FT                   /note="I -> L (in Ref. 2; AAF17198)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        350
FT                   /note="D -> G (in Ref. 3; BAF85012)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   509 AA;  54794 MW;  C3B685C7192B95C3 CRC64;
     MAAIGVHLGC TSACVAVYKD GRAGVVANDA GDRVTPAVVA YSENEEIVGL AAKQSRIRNI
     SNTVMKVKQI LGRSSSDPQA QKYIAESKCL VIEKNGKLRY EIDTGEETKF VNPEDVARLI
     FSKMKETAHS VLGSDANDVV ITVPFDFGEK QKNALGEAAR AAGFNVLRLI HEPSAALLAY
     GIGQDSPTGK SNILVFKLGG TSLSLSVMEV NSGIYRVLST NTDDNIGGAH FTETLAQYLA
     SEFQRSFKHD VRGNARAMMK LTNSAEVAKH SLSTLGSANC FLDSLYEGQD FDCNVSRARF
     ELLCSPLFNK CIEAIRGLLD QNGFTADDIN KVVLCGGSSR IPKLQQLIKD LFPAVELLNS
     IPPDEVIPIG AAIEAGILIG KENLLVEDSL MIECSARDIL VKGVDESGAS RFTVLFPSGT
     PLPARRQHTL QAPGSISSVC LELYESDGKN SAKEETKFAQ VVLQDLDKKE NGLRDILAVL
     TMKRDGSLHV TCTDQETGKC EAISIEIAS
//