ZDHC2_MOUSE
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 03-AUG-2022, entry version 125.
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: 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 AlphaFoldDB; P59267; -.
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 ProteomicsDB; 302053; -.
DR Antibodypedia; 22244; 128 antibodies from 23 providers.
DR DNASU; 70546; -.
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 VEuPathDB; HostDB:ENSMUSG00000039470; -.
DR eggNOG; KOG1315; Eukaryota.
DR GeneTree; ENSGT00940000153716; -.
DR HOGENOM; CLU_027721_1_3_1; -.
DR InParanoid; P59267; -.
DR OMA; DFPTRSD; -.
DR OrthoDB; 1491968at2759; -.
DR PhylomeDB; P59267; -.
DR TreeFam; TF316044; -.
DR Reactome; R-MMU-5683826; Surfactant metabolism.
DR BioGRID-ORCS; 70546; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Zdhhc2; mouse.
DR PRO; PR:P59267; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P59267; protein.
DR Bgee; ENSMUSG00000039470; Expressed in cranial nerve and 272 other tissues.
DR Genevisible; P59267; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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 membrane; Endoplasmic reticulum; Endosome;
KW Golgi apparatus; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Synapse; Transferase; Transmembrane; 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 296..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 COMPBIAS 296..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
