ID   VMAT2_MOUSE             Reviewed;         517 AA.
AC   Q8BRU6; Q8CC55;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Synaptic vesicular amine transporter;
DE   AltName: Full=Monoamine transporter;
DE   AltName: Full=Solute carrier family 18 member 2;
DE   AltName: Full=Vesicular amine transporter 2;
DE            Short=VAT2;
GN   Name=Slc18a2; Synonyms=Vmat2;
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   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Gilsbach R., Bonisch H., Bruess M.;
RT   "Molecular cloning and pharmacological characterization of the mouse
RT   vesicular monoamine transporter 2 (mVMAT2).";
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Aorta, Diencephalon, and Vein;
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   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=9427251; DOI=10.1016/s0896-6273(00)80419-5;
RA   Wang Y.M., Gainetdinov R.R., Fumagalli F., Xu F., Jones S.R., Bock C.B.,
RA   Miller G.W., Wightman R.M., Caron M.G.;
RT   "Knockout of the vesicular monoamine transporter 2 gene results in neonatal
RT   death and supersensitivity to cocaine and amphetamine.";
RL   Neuron 19:1285-1296(1997).
RN   [4]
RP   FUNCTION.
RX   PubMed=10618388; DOI=10.1073/pnas.97.1.162;
RA   Travis E.R., Wang Y.M., Michael D.J., Caron M.G., Wightman R.M.;
RT   "Differential quantal release of histamine and 5-hydroxytryptamine from
RT   mast cells of vesicular monoamine transporter 2 knockout mice.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:162-167(2000).
RN   [5]
RP   INTERACTION WITH SLC6A3.
RX   PubMed=19357284; DOI=10.1523/jneurosci.4559-08.2009;
RA   Egana L.A., Cuevas R.A., Baust T.B., Parra L.A., Leak R.K., Hochendoner S.,
RA   Pena K., Quiroz M., Hong W.C., Dorostkar M.M., Janz R., Sitte H.H.,
RA   Torres G.E.;
RT   "Physical and functional interaction between the dopamine transporter and
RT   the synaptic vesicle protein synaptogyrin-3.";
RL   J. Neurosci. 29:4592-4604(2009).
CC   -!- FUNCTION: Electrogenic antiporter that exchanges one cationic monoamine
CC       with two intravesicular protons across the membrane of secretory and
CC       synaptic vesicles. Uses the electrochemical proton gradient established
CC       by the V-type proton-pump ATPase to accumulate high concentrations of
CC       monoamines inside the vesicles prior to their release via exocytosis.
CC       Transports a variety of catecholamines such as dopamine, adrenaline and
CC       noradrenaline, histamine, and indolamines such as serotonin
CC       (PubMed:10618388) (By similarity). Regulates the transvesicular
CC       monoaminergic gradient that determines the quantal size. Mediates
CC       somatodendritic dopamine release in hippocampal neurons, likely as part
CC       of a regulated secretory pathway that integrates retrograde synaptic
CC       signals (By similarity). Acts as a primary transporter for striatal
CC       dopamine loading ensuring impulse-dependent release of dopamine at the
CC       synaptic cleft (PubMed:9427251). Responsible for histamine and
CC       serotonin storage and subsequent corelease from mast cell granules
CC       (PubMed:10618388) (By similarity). {ECO:0000250|UniProtKB:Q01827,
CC       ECO:0000269|PubMed:10618388, ECO:0000269|PubMed:9427251}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+)(out) + serotonin(in) = 2 H(+)(in) + serotonin(out);
CC         Xref=Rhea:RHEA:73743, ChEBI:CHEBI:15378, ChEBI:CHEBI:350546;
CC         Evidence={ECO:0000250|UniProtKB:Q01827};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73744;
CC         Evidence={ECO:0000250|UniProtKB:Q01827};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dopamine(in) + 2 H(+)(out) = dopamine(out) + 2 H(+)(in);
CC         Xref=Rhea:RHEA:73739, ChEBI:CHEBI:15378, ChEBI:CHEBI:59905;
CC         Evidence={ECO:0000250|UniProtKB:Q01827};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73740;
CC         Evidence={ECO:0000250|UniProtKB:Q01827};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+)(out) + histamine(in) = 2 H(+)(in) + histamine(out);
CC         Xref=Rhea:RHEA:73755, ChEBI:CHEBI:15378, ChEBI:CHEBI:58432;
CC         Evidence={ECO:0000250|UniProtKB:Q01827};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73756;
CC         Evidence={ECO:0000250|UniProtKB:Q01827};
CC   -!- SUBUNIT: Interacts with SLC6A3. {ECO:0000269|PubMed:19357284}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC       vesicle membrane {ECO:0000269|PubMed:9427251}; Multi-pass membrane
CC       protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane
CC       {ECO:0000250|UniProtKB:Q01827}; Multi-pass membrane protein
CC       {ECO:0000255}. Cell projection, axon {ECO:0000250|UniProtKB:Q01827}.
CC       Cell projection, dendrite {ECO:0000250|UniProtKB:Q01827}. Note=Sorted
CC       to large dense core granules in neuroendocrine cells, presumably at the
CC       level of the trans-Golgi network. In neurons it is predominantly
CC       detected in somatodendritic tubulovesicular membranes, a distinct
CC       population of secretory vesicles that undergo calcium-dependent
CC       exocytosis in axons and dendrites upon depolarization. Localized at
CC       synaptic vesicles in axons. {ECO:0000250|UniProtKB:Q01827}.
CC   -!- TISSUE SPECIFICITY: Expressed in striata and substantia nigra.
CC       {ECO:0000269|PubMed:9427251}.
CC   -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate. The
CC       homozygous mutants show severe growth retardation and the majority die
CC       shortly after birth. {ECO:0000269|PubMed:9427251}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Vesicular
CC       transporter 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; AJ555564; CAD88262.1; -; mRNA.
DR   EMBL; AK033871; BAC28501.1; -; mRNA.
DR   EMBL; AK041274; BAC30887.1; -; mRNA.
DR   CCDS; CCDS29935.1; -.
DR   RefSeq; NP_766111.1; NM_172523.3.
DR   AlphaFoldDB; Q8BRU6; -.
DR   SMR; Q8BRU6; -.
DR   MINT; Q8BRU6; -.
DR   STRING; 10090.ENSMUSP00000026084; -.
DR   BindingDB; Q8BRU6; -.
DR   ChEMBL; CHEMBL4295886; -.
DR   DrugBank; DB01126; Dutasteride.
DR   GlyCosmos; Q8BRU6; 5 sites, No reported glycans.
DR   GlyGen; Q8BRU6; 6 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8BRU6; -.
DR   PhosphoSitePlus; Q8BRU6; -.
DR   EPD; Q8BRU6; -.
DR   MaxQB; Q8BRU6; -.
DR   PaxDb; 10090-ENSMUSP00000026084; -.
DR   ProteomicsDB; 297607; -.
DR   Antibodypedia; 2802; 444 antibodies from 38 providers.
DR   DNASU; 214084; -.
DR   Ensembl; ENSMUST00000026084.5; ENSMUSP00000026084.4; ENSMUSG00000025094.9.
DR   GeneID; 214084; -.
DR   KEGG; mmu:214084; -.
DR   UCSC; uc008ibi.2; mouse.
DR   AGR; MGI:106677; -.
DR   CTD; 6571; -.
DR   MGI; MGI:106677; Slc18a2.
DR   VEuPathDB; HostDB:ENSMUSG00000025094; -.
DR   eggNOG; KOG3764; Eukaryota.
DR   GeneTree; ENSGT00940000157593; -.
DR   HOGENOM; CLU_001265_10_9_1; -.
DR   InParanoid; Q8BRU6; -.
DR   OMA; ATMYIAL; -.
DR   OrthoDB; 5388206at2759; -.
DR   PhylomeDB; Q8BRU6; -.
DR   TreeFam; TF313494; -.
DR   Reactome; R-MMU-181429; Serotonin Neurotransmitter Release Cycle.
DR   Reactome; R-MMU-181430; Norepinephrine Neurotransmitter Release Cycle.
DR   Reactome; R-MMU-212676; Dopamine Neurotransmitter Release Cycle.
DR   Reactome; R-MMU-442660; Na+/Cl- dependent neurotransmitter transporters.
DR   BioGRID-ORCS; 214084; 3 hits in 80 CRISPR screens.
DR   PRO; PR:Q8BRU6; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q8BRU6; Protein.
DR   Bgee; ENSMUSG00000025094; Expressed in ventral tegmental area and 166 other cell types or tissues.
DR   GO; GO:0030424; C:axon; ISS:UniProtKB.
DR   GO; GO:0043679; C:axon terminus; ISO:MGI.
DR   GO; GO:0044297; C:cell body; ISO:MGI.
DR   GO; GO:0042995; C:cell projection; ISO:MGI.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0031045; C:dense core granule; ISO:MGI.
DR   GO; GO:0098691; C:dopaminergic synapse; IDA:SynGO.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0098992; C:neuronal dense core vesicle; ISO:MGI.
DR   GO; GO:0099012; C:neuronal dense core vesicle membrane; ISO:MGI.
DR   GO; GO:0098794; C:postsynapse; ISO:MGI.
DR   GO; GO:0030667; C:secretory granule membrane; ISS:UniProtKB.
DR   GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IDA:UniProtKB.
DR   GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR   GO; GO:0005275; F:amine transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR   GO; GO:1901363; F:heterocyclic compound binding; ISO:MGI.
DR   GO; GO:0015311; F:monoamine:proton antiporter activity; ISO:MGI.
DR   GO; GO:0005335; F:serotonin:sodium:chloride symporter activity; IBA:GO_Central.
DR   GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015842; P:aminergic neurotransmitter loading into synaptic vesicle; ISO:MGI.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISO:MGI.
DR   GO; GO:0002553; P:histamine secretion by mast cell; IMP:UniProtKB.
DR   GO; GO:0051615; P:histamine uptake; ISO:MGI.
DR   GO; GO:0030073; P:insulin secretion; ISO:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0015844; P:monoamine transport; ISO:MGI.
DR   GO; GO:0051589; P:negative regulation of neurotransmitter transport; ISO:MGI.
DR   GO; GO:0098700; P:neurotransmitter loading into synaptic vesicle; IDA:SynGO.
DR   GO; GO:0006836; P:neurotransmitter transport; ISO:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0001975; P:response to amphetamine; IMP:MGI.
DR   GO; GO:0009636; P:response to toxic substance; IMP:MGI.
DR   GO; GO:0002552; P:serotonin secretion by mast cell; IMP:UniProtKB.
DR   GO; GO:0051610; P:serotonin uptake; ISO:MGI.
DR   GO; GO:0099123; P:somato-dendritic dopamine secretion; ISS:UniProtKB.
DR   CDD; cd17384; MFS_SLC18A1_2_VAT1_2; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 2.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR004734; Multidrug-R.
DR   NCBIfam; TIGR00880; 2_A_01_02; 1.
DR   PANTHER; PTHR23506; -; 1.
DR   PANTHER; PTHR23506:SF30; SYNAPTIC VESICULAR AMINE TRANSPORTER; 1.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   Genevisible; Q8BRU6; MM.
PE   1: Evidence at protein level;
KW   Cell projection; Cytoplasmic vesicle; Disulfide bond; Glycoprotein;
KW   Membrane; Neurotransmitter transport; Phosphoprotein; Reference proteome;
KW   Synapse; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..517
FT                   /note="Synaptic vesicular amine transporter"
FT                   /id="PRO_0000127515"
FT   TOPO_DOM        1..20
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        42..132
FT                   /note="Lumenal, vesicle"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        154..162
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        184..192
FT                   /note="Lumenal, vesicle"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        214..222
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        246..251
FT                   /note="Lumenal, vesicle"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        275..294
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        295..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        315..331
FT                   /note="Lumenal, vesicle"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        332..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        356..360
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        361..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        382..392
FT                   /note="Lumenal, vesicle"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        393..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        414..417
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        418..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        439..443
FT                   /note="Lumenal, vesicle"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        444..465
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        466..517
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          100..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         514
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q01827"
FT   MOD_RES         516
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q01827"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        120..327
FT                   /evidence="ECO:0000250"
FT   CONFLICT        150
FT                   /note="P -> T (in Ref. 2; BAC28501)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   517 AA;  55754 MW;  97B40B65DE3DDBEE CRC64;
     MALSDLVLLR WLRDSRHSRK LILFIVFLAL LLDNMLLTVV VPIIPSYLYS IKHEKNTTEI
     QTARPALTAS TSESFHSIFS YYNNSTVFTG NATGGLPGGE SPKATTTQHT VTNTTVPPDC
     PSEDKDLLNE NVQVGLLFAS KATVQLLTNP FIGLLTNRIG YPIPMFAGFC IMFISTVMFA
     FSSSYAFLLI ARSLQGIGSS CSSVAGMGML ASVYTDDEER GNAMGIALGG LAMGVLVGPP
     FGSVLYEFVG KTAPFLVLAA LVLLDGAIQL FVLQPSRVQP ESQKGTPLTT LLKDPYILIA
     AGSICFANMG IAMLEPALPI WMMETMCSRK WQLGVAFLPA SISYLIGTNI FGILAHKMGR
     WLCALLGMIV VGISILCIPF AKNIYGLIAP NFGVGFAIGM VDSSMMPIMG YLVDLRHVSV
     YGSVYAIADV AFCMGYAIGP SAGGAIAKAI GFPWLMTIIG IIDIVFAPLC FFLRSPPAKE
     EKMAILMDHN CPIKTKMYTQ NNVQPYPVGD DEESESD
//