ID   ZDHC2_MOUSE             Reviewed;         366 AA.
AC   P59267;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2003, sequence version 1.
DT   07-OCT-2020, entry version 118.
DE   RecName: Full=Palmitoyltransferase ZDHHC2 {ECO:0000305};
DE            EC=2.3.1.225 {ECO:0000269|PubMed:28167757};
DE   AltName: Full=Acyltransferase ZDHHC2 {ECO:0000305|PubMed:28167757};
DE            EC=2.3.1.- {ECO:0000305|PubMed:28167757};
DE   AltName: Full=Zinc finger DHHC domain-containing protein 2 {ECO:0000312|MGI:MGI:1923452};
DE            Short=DHHC-2;
GN   Name=Zdhhc2 {ECO:0000312|MGI:MGI:1923452};
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
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   [2]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=15603741; DOI=10.1016/j.neuron.2004.12.005;
RA   Fukata M., Fukata Y., Adesnik H., Nicoll R.A., Bredt D.S.;
RT   "Identification of PSD-95 palmitoylating enzymes.";
RL   Neuron 44:987-996(2004).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=21343290; DOI=10.1074/jbc.m110.193763;
RA   Jia L., Linder M.E., Blumer K.J.;
RT   "Gi/o signaling and the palmitoyltransferase DHHC2 regulate palmitate
RT   cycling and shuttling of RGS7 family-binding protein.";
RL   J. Biol. Chem. 286:13695-13703(2011).
RN   [4]
RP   SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF CYS-156, AND REGION.
RX   PubMed=21471008; DOI=10.1091/mbc.e10-11-0924;
RA   Greaves J., Carmichael J.A., Chamberlain L.H.;
RT   "The palmitoyl transferase DHHC2 targets a dynamic membrane cycling
RT   pathway: regulation by a C-terminal domain.";
RL   Mol. Biol. Cell 22:1887-1895(2011).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=25589740; DOI=10.1523/jneurosci.2243-14.2015;
RA   Woolfrey K.M., Sanderson J.L., Dell'Acqua M.L.;
RT   "The palmitoyl acyltransferase DHHC2 regulates recycling endosome
RT   exocytosis and synaptic potentiation through palmitoylation of
RT   AKAP79/150.";
RL   J. Neurosci. 35:442-456(2015).
RN   [6]
RP   SUBCELLULAR LOCATION, MUTAGENESIS OF SER-330; 334-LEU-LEU-335;
RP   340-THR--THR-342; 344-SER-SER-345; SER-356; ASN-357; PRO-358 AND THR-361,
RP   AND MOTIF.
RX   PubMed=28768144; DOI=10.1016/j.mcn.2017.07.007;
RA   Salaun C., Ritchie L., Greaves J., Bushell T.J., Chamberlain L.H.;
RT   "The C-terminal domain of zDHHC2 contains distinct sorting signals that
RT   regulate intracellular localisation in neurons and neuroendocrine cells.";
RL   Mol. Cell. Neurosci. 85:235-246(2017).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, MUTAGENESIS OF
RP   CYS-156, AND ACTIVE SITE.
RX   PubMed=28167757; DOI=10.1073/pnas.1612254114;
RA   Greaves J., Munro K.R., Davidson S.C., Riviere M., Wojno J., Smith T.K.,
RA   Tomkinson N.C., Chamberlain L.H.;
RT   "Molecular basis of fatty acid selectivity in the zDHHC family of S-
RT   acyltransferases revealed by click chemistry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:E1365-E1374(2017).
CC   -!- FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate
CC       onto various protein substrates and is involved in a variety of
CC       cellular processes (PubMed:15603741). Has no stringent fatty acid
CC       selectivity and in addition to palmitate can also transfer onto target
CC       proteins myristate from tetradecanoyl-CoA and stearate from
CC       octadecanoyl-CoA (Probable). In the nervous system, plays a role in
CC       long term synaptic potentiation by palmitoylating AKAP5 through which
CC       it regulates protein trafficking from the dendritic recycling endosomes
CC       to the plasma membrane and controls both structural and functional
CC       plasticity at excitatory synapses (PubMed:25589740). In dendrites,
CC       mediates the palmitoylation of DLG4 when synaptic activity decreases
CC       and induces synaptic clustering of DLG4 and associated AMPA-type
CC       glutamate receptors (PubMed:15603741). Also mediates the de novo and
CC       turnover palmitoylation of RGS7BP, a shuttle for Gi/o-specific GTPase-
CC       activating proteins/GAPs, promoting its localization to the plasma
CC       membrane in response to the activation of G protein-coupled receptors.
CC       Through the localization of these GTPase-activating proteins/GAPs, it
CC       also probably plays a role in G protein-coupled receptors signaling in
CC       neurons (PubMed:21343290). Also probably plays a role in cell adhesion
CC       by palmitoylating CD9 and CD151 to regulate their expression and
CC       function. Palmitoylates the endoplasmic reticulum protein CKAP4 and
CC       regulates its localization to the plasma membrane. Could also
CC       palmitoylate LCK and regulate its localization to the plasma membrane
CC       (By similarity). {ECO:0000250|UniProtKB:Q9UIJ5,
CC       ECO:0000269|PubMed:15603741, ECO:0000269|PubMed:21343290,
CC       ECO:0000269|PubMed:25589740, ECO:0000305|PubMed:28167757}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-
CC         hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-
CC         COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151;
CC         EC=2.3.1.225; Evidence={ECO:0000305|PubMed:28167757};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC         Evidence={ECO:0000305|PubMed:28167757};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-cysteinyl-[protein] + tetradecanoyl-CoA = CoA + S-
CC         tetradecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59736, Rhea:RHEA-
CC         COMP:10131, Rhea:RHEA-COMP:15433, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:143199;
CC         Evidence={ECO:0000305|PubMed:28167757};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737;
CC         Evidence={ECO:0000305|PubMed:28167757};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-cysteinyl-[protein] + octadecanoyl-CoA = CoA + S-
CC         octadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59740, Rhea:RHEA-
CC         COMP:10131, Rhea:RHEA-COMP:15434, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:143200;
CC         Evidence={ECO:0000305|PubMed:28167757};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741;
CC         Evidence={ECO:0000305|PubMed:28167757};
CC   -!- SUBUNIT: Monomer. Homodimer. The monomeric form has a higher catalytic
CC       activity. {ECO:0000250|UniProtKB:Q9UIJ5}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic density
CC       {ECO:0000250|UniProtKB:Q9JKR5}. Postsynaptic recycling endosome
CC       membrane {ECO:0000269|PubMed:25589740, ECO:0000269|PubMed:28768144};
CC       Multi-pass membrane protein {ECO:0000305|PubMed:21471008}. Cell
CC       membrane {ECO:0000269|PubMed:21343290, ECO:0000269|PubMed:21471008,
CC       ECO:0000269|PubMed:28768144}; Multi-pass membrane protein
CC       {ECO:0000305|PubMed:21471008}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9UIJ5}; Multi-pass membrane protein
CC       {ECO:0000305|PubMed:21471008}. Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q9UIJ5}; Multi-pass membrane protein
CC       {ECO:0000305|PubMed:21471008}. Note=Translocates to postsynaptic
CC       density when synaptic activity decreases.
CC       {ECO:0000250|UniProtKB:Q9JKR5}.
CC   -!- TISSUE SPECIFICITY: Expressed in all brain regions.
CC       {ECO:0000269|PubMed:15603741, ECO:0000269|PubMed:21343290}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC       {ECO:0000250|UniProtKB:Q8IUH5}.
CC   -!- PTM: Autopalmitoylated. {ECO:0000250|UniProtKB:Q9UIJ5}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AK030662; BAC27068.1; -; mRNA.
DR   CCDS; CCDS22252.1; -.
DR   RefSeq; NP_848482.1; NM_178395.3.
DR   RefSeq; XP_006509548.1; XM_006509485.3.
DR   SMR; P59267; -.
DR   STRING; 10090.ENSMUSP00000041727; -.
DR   iPTMnet; P59267; -.
DR   PhosphoSitePlus; P59267; -.
DR   EPD; P59267; -.
DR   MaxQB; P59267; -.
DR   PaxDb; P59267; -.
DR   PRIDE; P59267; -.
DR   Antibodypedia; 22244; 114 antibodies.
DR   Ensembl; ENSMUST00000049389; ENSMUSP00000041727; ENSMUSG00000039470.
DR   Ensembl; ENSMUST00000128166; ENSMUSP00000123070; ENSMUSG00000039470.
DR   Ensembl; ENSMUST00000167766; ENSMUSP00000129996; ENSMUSG00000039470.
DR   GeneID; 70546; -.
DR   KEGG; mmu:70546; -.
DR   UCSC; uc009lmn.1; mouse.
DR   CTD; 51201; -.
DR   MGI; MGI:1923452; Zdhhc2.
DR   eggNOG; KOG1315; Eukaryota.
DR   GeneTree; ENSGT00940000153716; -.
DR   HOGENOM; CLU_027721_1_3_1; -.
DR   InParanoid; P59267; -.
DR   KO; K20028; -.
DR   OMA; DFPTRSD; -.
DR   OrthoDB; 1491968at2759; -.
DR   PhylomeDB; P59267; -.
DR   TreeFam; TF316044; -.
DR   Reactome; R-MMU-5683826; Surfactant metabolism.
DR   BioGRID-ORCS; 70546; 0 hits in 18 CRISPR screens.
DR   ChiTaRS; Zdhhc2; mouse.
DR   PRO; PR:P59267; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; P59267; protein.
DR   Bgee; ENSMUSG00000039470; Expressed in islet of Langerhans and 301 other tissues.
DR   Genevisible; P59267; MM.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR   GO; GO:0098837; C:postsynaptic recycling endosome; IDA:UniProtKB.
DR   GO; GO:0055038; C:recycling endosome membrane; IDA:MGI.
DR   GO; GO:0016409; F:palmitoyltransferase activity; IDA:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0019705; F:protein-cysteine S-myristoyltransferase activity; IC:UniProtKB.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; ISO:MGI.
DR   GO; GO:0140439; F:protein-cysteine S-stearoyltransferase activity; IC:UniProtKB.
DR   GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IDA:UniProtKB.
DR   GO; GO:1904719; P:positive regulation of AMPA glutamate receptor clustering; ISS:UniProtKB.
DR   GO; GO:1905751; P:positive regulation of endosome to plasma membrane protein transport; ISS:UniProtKB.
DR   GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISS:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
DR   GO; GO:1903539; P:protein localization to postsynaptic membrane; ISS:UniProtKB.
DR   GO; GO:0018345; P:protein palmitoylation; IDA:MGI.
DR   GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR   GO; GO:0022407; P:regulation of cell-cell adhesion; ISS:UniProtKB.
DR   GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISS:UniProtKB.
DR   GO; GO:0042176; P:regulation of protein catabolic process; ISS:UniProtKB.
DR   GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISO:MGI.
DR   GO; GO:0016188; P:synaptic vesicle maturation; IBA:GO_Central.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Cell junction; Cell membrane; Endoplasmic reticulum;
KW   Endosome; Golgi apparatus; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Synapse; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..366
FT                   /note="Palmitoyltransferase ZDHHC2"
FT                   /id="PRO_0000212860"
FT   TOPO_DOM        1..15
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:21471008"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        37..47
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:21471008"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        69..169
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:21471008"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        191..207
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:21471008"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        229..366
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:21471008"
FT   DOMAIN          126..176
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   REGION          298..366
FT                   /note="Mediates localization to plasma membrane and
FT                   recycling endosomes"
FT                   /evidence="ECO:0000269|PubMed:21471008"
FT   MOTIF           334..335
FT                   /note="Non-canonical dileucine endocytic signal"
FT                   /evidence="ECO:0000269|PubMed:28768144"
FT   MOTIF           357..360
FT                   /note="NPxY-like endocytic signal"
FT                   /evidence="ECO:0000269|PubMed:28768144"
FT   ACT_SITE        156
FT                   /note="S-palmitoyl cysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067,
FT                   ECO:0000269|PubMed:28167757"
FT   MUTAGEN         156
FT                   /note="C->A: No effect on subcellular localization."
FT                   /evidence="ECO:0000269|PubMed:21471008"
FT   MUTAGEN         156
FT                   /note="C->S: Loss of protein-cysteine S-
FT                   palmitoyltransferase activity. Loss of autopalmitoylation."
FT                   /evidence="ECO:0000269|PubMed:28167757"
FT   MUTAGEN         330
FT                   /note="S->A: Increased localization to the plasma
FT                   membrane."
FT                   /evidence="ECO:0000269|PubMed:28768144"
FT   MUTAGEN         330
FT                   /note="S->D: No effect on subcellular localization."
FT                   /evidence="ECO:0000269|PubMed:28768144"
FT   MUTAGEN         334..335
FT                   /note="LL->AA: Increased localization to the plasma
FT                   membrane."
FT                   /evidence="ECO:0000269|PubMed:28768144"
FT   MUTAGEN         340..342
FT                   /note="TWT->AWA: Decreased localization to the plasma
FT                   membrane."
FT                   /evidence="ECO:0000269|PubMed:28768144"
FT   MUTAGEN         344..345
FT                   /note="SS->DD: Decreased localization to the plasma
FT                   membrane."
FT                   /evidence="ECO:0000269|PubMed:28768144"
FT   MUTAGEN         356
FT                   /note="S->A: No effect on subcellular localization."
FT                   /evidence="ECO:0000269|PubMed:28768144"
FT   MUTAGEN         356
FT                   /note="S->D: Loss of localization to the plasma membrane."
FT                   /evidence="ECO:0000269|PubMed:28768144"
FT   MUTAGEN         357
FT                   /note="N->A: Increased localization to the plasma
FT                   membrane."
FT                   /evidence="ECO:0000269|PubMed:28768144"
FT   MUTAGEN         358
FT                   /note="P->A: Increased localization to the plasma
FT                   membrane."
FT                   /evidence="ECO:0000269|PubMed:28768144"
FT   MUTAGEN         361
FT                   /note="T->A: No effect on subcellular localization."
FT                   /evidence="ECO:0000269|PubMed:28768144"
FT   MUTAGEN         361
FT                   /note="T->E: Loss of localization to the plasma membrane."
FT                   /evidence="ECO:0000269|PubMed:28768144"
SQ   SEQUENCE   366 AA;  41982 MW;  05DC0FCC7D786278 CRC64;
     MAPSGSGGVR RRCRRVLYWI PVVFISLLLG WSYYAYAIQL CIVSMENIGE QVVCLMAYHL
     LFAMFVWSYW KTIFTLPMNP SKEFHLSYAE KELLEREPRG EAHQEVLRRA AKDLPIYTRT
     MSGAIRYCDR CQLIKPDRCH HCSVCDKCIL KMDHHCPWVN NCVGFSNYKF FLLFLAYSLL
     YCLFIAATDL QYFIRFWTNG LPDTQAKFHI MFLFFAAAMF SVSLSSLFGY HCWLVSKNKS
     TLEAFRNPVF RHGTDKNGFS LGFSKNMRQV FGDEKKYWLL PVFSSQGDGC SFPTCLVNQD
     PEQPSTPAGL NSTVKNPENH QFPAKPLRES QSHLLKDSQT WTESSANPGK GKAGMSNPAL
     TMENET
//