ID   TIM14_HUMAN             Reviewed;         116 AA.
AC   Q96DA6; B2R4B1; C9JBV1;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 171.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit TIM14;
DE   AltName: Full=DnaJ homolog subfamily C member 19;
GN   Name=DNAJC19; Synonyms=TIM14, TIMM14;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Thalamus;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
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] (ISOFORM 1).
RC   TISSUE=Colon, and Lung;
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   PROTEIN SEQUENCE OF 2-20 AND 62-75, CLEAVAGE OF INITIATOR METHIONINE,
RP   ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RA   Bienvenut W.V.;
RL   Submitted (JUN-2005) to UniProtKB.
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=12592411; DOI=10.1038/nbt793;
RA   Taylor S.W., Fahy E., Zhang B., Glenn G.M., Warnock D.E., Wiley S.,
RA   Murphy A.N., Gaucher S.P., Capaldi R.A., Gibson B.W., Ghosh S.S.;
RT   "Characterization of the human heart mitochondrial proteome.";
RL   Nat. Biotechnol. 21:281-286(2003).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, 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   [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-39 AND SER-70, 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   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   INVOLVEMENT IN MGCA5.
RX   PubMed=16055927; DOI=10.1136/jmg.2005.036657;
RA   Davey K.M., Parboosingh J.S., McLeod D.R., Chan A., Casey R., Ferreira P.,
RA   Snyder F.F., Bridge P.J., Bernier F.P.;
RT   "Mutation of DNAJC19, a human homologue of yeast inner mitochondrial
RT   membrane co-chaperones, causes DCMA syndrome, a novel autosomal recessive
RT   Barth syndrome-like condition.";
RL   J. Med. Genet. 43:385-393(2006).
CC   -!- FUNCTION: Mitochondrial co-chaperone which forms a complex with
CC       prohibitins to regulate cardiolipin remodeling (By similarity). May be
CC       a component of the PAM complex, a complex required for the
CC       translocation of transit peptide-containing proteins from the inner
CC       membrane into the mitochondrial matrix in an ATP-dependent manner. May
CC       act as a co-chaperone that stimulate the ATP-dependent activity (By
CC       similarity). {ECO:0000250|UniProtKB:Q07914,
CC       ECO:0000250|UniProtKB:Q9CQV7}.
CC   -!- SUBUNIT: Interacts with PHB2; the interaction associates DNAJC19 with
CC       the prohibitin complex. Interacts with TIMM16/PAM16 (By similarity).
CC       May be a component of the PAM complex at least composed of a
CC       mitochondrial HSP70 protein, GRPEL1 or GRPEL2, TIMM44, TIMM16/PAM16 and
CC       TIMM14/DNAJC19 (By similarity). {ECO:0000250|UniProtKB:Q07914,
CC       ECO:0000250|UniProtKB:Q9CQV7}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000305|PubMed:12592411}; Single-pass membrane protein
CC       {ECO:0000305|PubMed:12592411}; Matrix side
CC       {ECO:0000250|UniProtKB:Q9CQV7}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96DA6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96DA6-2; Sequence=VSP_047119;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- DISEASE: 3-methylglutaconic aciduria 5 (MGCA5) [MIM:610198]: An
CC       autosomal recessive disorder characterized by early-onset dilated
CC       cardiomyopathy, growth failure, cerebellar ataxia causing significant
CC       motor delays, testicular dysgenesis, growth failure and significant
CC       increases in urine organic acids, particularly 3-methylglutaconic acid
CC       and 3-methylglutaric acid. {ECO:0000269|PubMed:16055927}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the TIM14 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK311765; BAG34708.1; -; mRNA.
DR   EMBL; AC008009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471052; EAW78358.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78360.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78362.1; -; Genomic_DNA.
DR   EMBL; BC073989; AAH73989.1; -; mRNA.
DR   EMBL; BC009702; AAH09702.1; -; mRNA.
DR   CCDS; CCDS33895.1; -. [Q96DA6-1]
DR   CCDS; CCDS54684.1; -. [Q96DA6-2]
DR   RefSeq; NP_001177162.1; NM_001190233.1. [Q96DA6-2]
DR   RefSeq; NP_660304.1; NM_145261.3. [Q96DA6-1]
DR   AlphaFoldDB; Q96DA6; -.
DR   SMR; Q96DA6; -.
DR   BioGRID; 126272; 199.
DR   ComplexPortal; CPX-6129; TIM23 mitochondrial inner membrane pre-sequence translocase complex, TIM17A variant.
DR   ComplexPortal; CPX-6130; TIM23 mitochondrial inner membrane pre-sequence translocase complex, TIM17B variant.
DR   DIP; DIP-62091N; -.
DR   IntAct; Q96DA6; 22.
DR   MINT; Q96DA6; -.
DR   STRING; 9606.ENSP00000372005; -.
DR   iPTMnet; Q96DA6; -.
DR   PhosphoSitePlus; Q96DA6; -.
DR   BioMuta; DNAJC19; -.
DR   DMDM; 74760780; -.
DR   EPD; Q96DA6; -.
DR   jPOST; Q96DA6; -.
DR   MassIVE; Q96DA6; -.
DR   MaxQB; Q96DA6; -.
DR   PaxDb; 9606-ENSP00000372005; -.
DR   PeptideAtlas; Q96DA6; -.
DR   ProteomicsDB; 76265; -. [Q96DA6-1]
DR   ProteomicsDB; 9509; -.
DR   Pumba; Q96DA6; -.
DR   TopDownProteomics; Q96DA6-1; -. [Q96DA6-1]
DR   Antibodypedia; 33761; 202 antibodies from 27 providers.
DR   DNASU; 131118; -.
DR   Ensembl; ENST00000382564.8; ENSP00000372005.2; ENSG00000205981.9. [Q96DA6-1]
DR   Ensembl; ENST00000479269.5; ENSP00000419191.1; ENSG00000205981.9. [Q96DA6-2]
DR   Ensembl; ENST00000491873.5; ENSP00000420767.1; ENSG00000205981.9. [Q96DA6-2]
DR   GeneID; 131118; -.
DR   KEGG; hsa:131118; -.
DR   MANE-Select; ENST00000382564.8; ENSP00000372005.2; NM_145261.4; NP_660304.1.
DR   UCSC; uc003fkt.4; human. [Q96DA6-1]
DR   AGR; HGNC:30528; -.
DR   CTD; 131118; -.
DR   DisGeNET; 131118; -.
DR   GeneCards; DNAJC19; -.
DR   HGNC; HGNC:30528; DNAJC19.
DR   HPA; ENSG00000205981; Low tissue specificity.
DR   MalaCards; DNAJC19; -.
DR   MIM; 608977; gene.
DR   MIM; 610198; phenotype.
DR   neXtProt; NX_Q96DA6; -.
DR   OpenTargets; ENSG00000205981; -.
DR   Orphanet; 66634; Dilated cardiomyopathy with ataxia.
DR   PharmGKB; PA142671967; -.
DR   VEuPathDB; HostDB:ENSG00000205981; -.
DR   eggNOG; KOG0723; Eukaryota.
DR   GeneTree; ENSGT00940000154384; -.
DR   HOGENOM; CLU_017633_13_3_1; -.
DR   InParanoid; Q96DA6; -.
DR   OMA; MRQMPNA; -.
DR   OrthoDB; 160310at2759; -.
DR   PhylomeDB; Q96DA6; -.
DR   TreeFam; TF320584; -.
DR   PathwayCommons; Q96DA6; -.
DR   Reactome; R-HSA-1268020; Mitochondrial protein import.
DR   SignaLink; Q96DA6; -.
DR   SIGNOR; Q96DA6; -.
DR   BioGRID-ORCS; 131118; 147 hits in 1122 CRISPR screens.
DR   ChiTaRS; DNAJC19; human.
DR   GeneWiki; DNAJC19; -.
DR   GenomeRNAi; 131118; -.
DR   Pharos; Q96DA6; Tbio.
DR   PRO; PR:Q96DA6; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q96DA6; Protein.
DR   Bgee; ENSG00000205981; Expressed in tendon of biceps brachii and 181 other cell types or tissues.
DR   ExpressionAtlas; Q96DA6; baseline and differential.
DR   GO; GO:0098800; C:inner mitochondrial membrane protein complex; ISS:UniProtKB.
DR   GO; GO:0099617; C:matrix side of mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0001405; C:PAM complex, Tim23 associated import motor; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IDA:GO_Central.
DR   GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; NAS:ComplexPortal.
DR   GO; GO:0001671; F:ATPase activator activity; IBA:GO_Central.
DR   GO; GO:0048806; P:genitalia development; IMP:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; NAS:ComplexPortal.
DR   GO; GO:0006457; P:protein folding; NAS:UniProtKB.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0006626; P:protein targeting to mitochondrion; NAS:UniProtKB.
DR   GO; GO:1900208; P:regulation of cardiolipin metabolic process; ISS:UniProtKB.
DR   GO; GO:0007601; P:visual perception; IMP:UniProtKB.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR036869; J_dom_sf.
DR   PANTHER; PTHR12763:SF56; MITOCHONDRIAL IMPORT INNER MEMBRANE TRANSLOCASE SUBUNIT TIM14; 1.
DR   PANTHER; PTHR12763; UNCHARACTERIZED; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   Genevisible; Q96DA6; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cardiomyopathy; Chaperone;
KW   Direct protein sequencing; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Phosphoprotein; Protein transport;
KW   Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:25944712"
FT   CHAIN           2..116
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit TIM14"
FT                   /id="PRO_0000071100"
FT   TOPO_DOM        2..3
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        25..116
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          62..116
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:25944712"
FT   MOD_RES         39
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         70
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..25
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_047119"
SQ   SEQUENCE   116 AA;  12499 MW;  FEEFD5D2AE5D15F2 CRC64;
     MASTVVAVGL TIAAAGFAGR YVLQAMKHME PQVKQVFQSL PKSAFSGGYY RGGFEPKMTK
     REAALILGVS PTANKGKIRD AHRRIMLLNH PDKGGSPYIA AKINEAKDLL EGQAKK
//