ID   DNJC5_MOUSE             Reviewed;         198 AA.
AC   P60904; P54101;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 1.
DT   12-OCT-2022, entry version 158.
DE   RecName: Full=DnaJ homolog subfamily C member 5 {ECO:0000305};
DE   AltName: Full=Cysteine string protein {ECO:0000250|UniProtKB:Q9H3Z4};
DE            Short=CSP {ECO:0000250|UniProtKB:Q9H3Z4};
DE   AltName: Full=Cysteine-string protein isoform alpha {ECO:0000303|PubMed:20847230};
GN   Name=Dnajc5 {ECO:0000312|MGI:MGI:892995};
GN   Synonyms=Cspalpha {ECO:0000303|PubMed:20847230};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Qin N., Lin T., Birnbaumer L.;
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF 8-24 AND 42-72, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   INTERACTION WITH HSC70 AND SGTA, SUBCELLULAR LOCATION, PALMITOYLATION, AND
RP   MUTAGENESIS OF CYS-113; CYS-118; CYS-121; PHE-129 AND LYS-135.
RX   PubMed=17034881; DOI=10.1016/j.bbamcr.2006.08.054;
RA   Boal F., Le Pevelen S., Cziepluch C., Scotti P., Lang J.;
RT   "Cysteine-string protein isoform beta (Cspbeta) is targeted to the trans-
RT   Golgi network as a non-palmitoylated CSP in clonal beta-cells.";
RL   Biochim. Biophys. Acta 1773:109-119(2007).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT   chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-151, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [11]
RP   FUNCTION, INTERACTION WITH SYT1; SYT5; SYT7; SYT9 AND HSC70, MUTAGENESIS OF
RP   SER-10 AND GLU-93, AND PHOSPHORYLATION AT SER-10.
RX   PubMed=20847230; DOI=10.1096/fj.09-152033;
RA   Boal F., Laguerre M., Milochau A., Lang J., Scotti P.A.;
RT   "A charged prominence in the linker domain of the cysteine-string protein
RT   Cspalpha mediates its regulated interaction with the calcium sensor
RT   synaptotagmin 9 during exocytosis.";
RL   FASEB J. 25:132-143(2011).
RN   [12]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=22187053; DOI=10.1038/emboj.2011.467;
RA   Sharma M., Burre J., Bronk P., Zhang Y., Xu W., Suedhof T.C.;
RT   "CSPalpha knockout causes neurodegeneration by impairing SNAP-25
RT   function.";
RL   EMBO J. 31:829-841(2012).
RN   [13]
RP   INTERACTION WITH ZDHHC13 AND ZDHHC17.
RX   PubMed=25253725; DOI=10.1091/mbc.e14-06-1169;
RA   Lemonidis K., Gorleku O.A., Sanchez-Perez M.C., Grefen C.,
RA   Chamberlain L.H.;
RT   "The Golgi S-acylation machinery comprises zDHHC enzymes with major
RT   differences in substrate affinity and S-acylation activity.";
RL   Mol. Biol. Cell 25:3870-3883(2014).
RN   [14]
RP   INTERACTION WITH ZDHHC17 AND ZDHHC13.
RX   PubMed=26198635; DOI=10.1074/jbc.m115.657668;
RA   Lemonidis K., Sanchez-Perez M.C., Chamberlain L.H.;
RT   "Identification of a novel sequence motif recognized by the ankyrin repeat
RT   domain of zDHHC17/13 S-acyltransferases.";
RL   J. Biol. Chem. 290:21939-21950(2015).
RN   [15]
RP   REVIEW.
RX   PubMed=25800794; DOI=10.1016/j.semcdb.2015.03.008;
RA   Burgoyne R.D., Morgan A.;
RT   "Cysteine string protein (CSP) and its role in preventing
RT   neurodegeneration.";
RL   Semin. Cell Dev. Biol. 40:153-159(2015).
RN   [16]
RP   STRUCTURE BY NMR OF 5-100.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of J-domain from mouse DnaJ subfamily C member 5.";
RL   Submitted (NOV-2005) to the PDB data bank.
CC   -!- FUNCTION: Acts as a co-chaperone for the SNARE protein SNAP-25
CC       (PubMed:22187053). Involved in the calcium-mediated control of a late
CC       stage of exocytosis (PubMed:20847230). Acts as a general chaperone in
CC       regulated exocytosis (By similarity). May have an important role in
CC       presynaptic function (By similarity). May be involved in calcium-
CC       dependent neurotransmitter release at nerve endings (By similarity).
CC       {ECO:0000250|UniProtKB:Q29455, ECO:0000269|PubMed:20847230,
CC       ECO:0000269|PubMed:22187053}.
CC   -!- SUBUNIT: Homodimer (Probable). Interacts with the chaperone complex
CC       consisting of HSC70 and SGTA (PubMed:17034881, PubMed:20847230).
CC       Interacts with ZDHHC13 (via ANK repeats) (PubMed:25253725,
CC       PubMed:26198635). Interacts with ZDHHC17 (via ANK repeats)
CC       (PubMed:25253725, PubMed:26198635). Interacts with SYT1, SYT5 and SYT7,
CC       and with SYT9, forming a complex with SNAP25 (PubMed:20847230). The
CC       interaction with SYT9 is stimulated tenfold in presence of calcium
CC       (PubMed:20847230). {ECO:0000269|PubMed:17034881,
CC       ECO:0000269|PubMed:20847230, ECO:0000269|PubMed:25253725,
CC       ECO:0000269|PubMed:26198635, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q29455}. Membrane {ECO:0000269|PubMed:17034881};
CC       Lipid-anchor {ECO:0000269|PubMed:17034881}. Cytoplasmic vesicle,
CC       secretory vesicle, chromaffin granule membrane
CC       {ECO:0000250|UniProtKB:Q29455}. Melanosome
CC       {ECO:0000250|UniProtKB:Q9H3Z4}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q9H3Z4}. Note=The association with membranes is
CC       regulated by palmitoylation (By similarity). Colocalizes with insulin
CC       granules, when overexpressed in an islet cell line (PubMed:17034881).
CC       {ECO:0000250|UniProtKB:Q29455, ECO:0000269|PubMed:17034881}.
CC   -!- PTM: Formation of the chaperone complex DNAJC5/HSC70 is not regulated
CC       by phosphorylation (PubMed:20847230). Ser-10 phosphorylation induces an
CC       order-to-disorder transition triggering the interaction with Lys-58 (By
CC       similarity). This conformational switch modulates DNAJC5's cellular
CC       functions by reducing binding to syntaxin and synaptogamin without
CC       altering HSC70 interactions (By similarity).
CC       {ECO:0000250|UniProtKB:Q9H3Z4, ECO:0000269|PubMed:20847230}.
CC   -!- PTM: Palmitoylated (PubMed:17034881). Could be palmitoylated by DHHC3,
CC       DHHC7, DHHC15 and DHHC17 (By similarity). Palmitoylation occurs
CC       probably in the cysteine-rich domain and regulates DNAJC5 membrane
CC       attachment (PubMed:17034881). {ECO:0000250|UniProtKB:Q29455,
CC       ECO:0000269|PubMed:17034881}.
CC   -!- DISRUPTION PHENOTYPE: Defective SNAP-25 function, which causes
CC       neurodegeneration by impairing SNARE-complex assembly
CC       (PubMed:22187053). {ECO:0000269|PubMed:22187053}.
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DR   EMBL; AF032115; AAB87080.1; -; mRNA.
DR   EMBL; AK029006; BAC26236.1; -; mRNA.
DR   EMBL; AK032373; BAC27841.1; -; mRNA.
DR   CCDS; CCDS17215.1; -.
DR   RefSeq; NP_001258513.1; NM_001271584.1.
DR   RefSeq; NP_001258514.1; NM_001271585.1.
DR   RefSeq; NP_058055.1; NM_016775.3.
DR   RefSeq; XP_011238225.1; XM_011239923.2.
DR   PDB; 2CTW; NMR; -; A=5-100.
DR   PDBsum; 2CTW; -.
DR   AlphaFoldDB; P60904; -.
DR   SMR; P60904; -.
DR   BioGRID; 198948; 7.
DR   CORUM; P60904; -.
DR   IntAct; P60904; 7.
DR   MINT; P60904; -.
DR   STRING; 10090.ENSMUSP00000072175; -.
DR   TCDB; 8.A.192.1.1; the dnaj homolog (dnaj) family.
DR   iPTMnet; P60904; -.
DR   PhosphoSitePlus; P60904; -.
DR   SwissPalm; P60904; -.
DR   EPD; P60904; -.
DR   jPOST; P60904; -.
DR   MaxQB; P60904; -.
DR   PaxDb; P60904; -.
DR   PeptideAtlas; P60904; -.
DR   PRIDE; P60904; -.
DR   ProteomicsDB; 277354; -.
DR   Antibodypedia; 2284; 255 antibodies from 32 providers.
DR   DNASU; 13002; -.
DR   Ensembl; ENSMUST00000072334; ENSMUSP00000072175; ENSMUSG00000000826.
DR   Ensembl; ENSMUST00000108796; ENSMUSP00000104424; ENSMUSG00000000826.
DR   Ensembl; ENSMUST00000108797; ENSMUSP00000104425; ENSMUSG00000000826.
DR   GeneID; 13002; -.
DR   KEGG; mmu:13002; -.
DR   UCSC; uc008omp.2; mouse.
DR   CTD; 80331; -.
DR   MGI; MGI:892995; Dnajc5.
DR   VEuPathDB; HostDB:ENSMUSG00000000826; -.
DR   eggNOG; KOG0716; Eukaryota.
DR   GeneTree; ENSGT00940000155597; -.
DR   InParanoid; P60904; -.
DR   OMA; CKPRPRD; -.
DR   OrthoDB; 1401920at2759; -.
DR   PhylomeDB; P60904; -.
DR   TreeFam; TF105164; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-888590; GABA synthesis, release, reuptake and degradation.
DR   BioGRID-ORCS; 13002; 2 hits in 74 CRISPR screens.
DR   ChiTaRS; Dnajc5; mouse.
DR   EvolutionaryTrace; P60904; -.
DR   PRO; PR:P60904; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P60904; protein.
DR   Bgee; ENSMUSG00000000826; Expressed in barrel cortex and 253 other tissues.
DR   ExpressionAtlas; P60904; baseline and differential.
DR   Genevisible; P60904; MM.
DR   GO; GO:0031225; C:anchored component of membrane; ISS:UniProtKB.
DR   GO; GO:0098993; C:anchored component of synaptic vesicle membrane; ISO:MGI.
DR   GO; GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0060203; C:clathrin-sculpted glutamate transport vesicle membrane; TAS:Reactome.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0098793; C:presynapse; IDA:SynGO.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR   GO; GO:0043008; F:ATP-dependent protein binding; ISO:MGI.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IDA:SynGO.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IGI:MGI.
DR   GO; GO:0051402; P:neuron apoptotic process; IGI:MGI.
DR   GO; GO:0098693; P:regulation of synaptic vesicle cycle; IDA:SynGO.
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   Pfam; PF00226; DnaJ; 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   3D-structure; Acetylation; Cell membrane; Chaperone; Cytoplasm;
KW   Cytoplasmic vesicle; Direct protein sequencing; Lipoprotein; Membrane;
KW   Palmitate; Phosphoprotein; Reference proteome.
FT   CHAIN           1..198
FT                   /note="DnaJ homolog subfamily C member 5"
FT                   /id="PRO_0000071053"
FT   DOMAIN          13..82
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3Z4"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19131326"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3Z4"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         17
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3Z4"
FT   MOD_RES         56
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H3Z4"
FT   MOD_RES         151
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MUTAGEN         10
FT                   /note="S->D: Reduced interaction with SYT9, but no effect
FT                   on the interaction with HSC70."
FT                   /evidence="ECO:0000269|PubMed:20847230"
FT   MUTAGEN         93
FT                   /note="E->V: Reduced interaction with SYT9."
FT                   /evidence="ECO:0000269|PubMed:20847230"
FT   MUTAGEN         113
FT                   /note="C->V: No effect on palmitoylation. No change in
FT                   subcellular location; when associated with G-118 and
FT                   F-121."
FT                   /evidence="ECO:0000269|PubMed:17034881"
FT   MUTAGEN         118
FT                   /note="C->G: No effect on palmitoylation. No change in
FT                   subcellular location; when associated with V-113 and
FT                   F-121."
FT                   /evidence="ECO:0000269|PubMed:17034881"
FT   MUTAGEN         121
FT                   /note="C->F: No effect on palmitoylation. No change in
FT                   subcellular location; when associated with V-113 and
FT                   G-118."
FT                   /evidence="ECO:0000269|PubMed:17034881"
FT   MUTAGEN         129
FT                   /note="F->C: No effect on palmitoylation. No change in
FT                   subcellular location; when associated with H-135."
FT                   /evidence="ECO:0000269|PubMed:17034881"
FT   MUTAGEN         135
FT                   /note="K->H: No effect on palmitoylation. No change in
FT                   subcellular location; when associated with C-129."
FT                   /evidence="ECO:0000269|PubMed:17034881"
FT   HELIX           16..20
FT                   /evidence="ECO:0007829|PDB:2CTW"
FT   HELIX           28..41
FT                   /evidence="ECO:0007829|PDB:2CTW"
FT   TURN            44..46
FT                   /evidence="ECO:0007829|PDB:2CTW"
FT   HELIX           51..67
FT                   /evidence="ECO:0007829|PDB:2CTW"
FT   HELIX           70..78
FT                   /evidence="ECO:0007829|PDB:2CTW"
FT   HELIX           81..89
FT                   /evidence="ECO:0007829|PDB:2CTW"
FT   HELIX           94..100
FT                   /evidence="ECO:0007829|PDB:2CTW"
SQ   SEQUENCE   198 AA;  22101 MW;  52F98261FBAD978F CRC64;
     MADQRQRSLS TSGESLYHVL GLDKNATSDD IKKSYRKLAL KYHPDKNPDN PEAADKFKEI
     NNAHAILTDA TKRNIYDKYG SLGLYVAEQF GEENVNTYFV LSSWWAKALF VVCGLLTCCY
     CCCCLCCCFN CCCGKCKPKA PEGEETEFYV SPEDLEAQLQ SDEREATDTP IVIQPASATE
     TTQLTADSHP SYHTDGFN
//