STX3_MOUSE
ID STX3_MOUSE Reviewed; 289 AA.
AC Q64704; Q3TBP0; Q8R1B7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Syntaxin-3;
GN Name=Stx3; Synonyms=Stx3a;
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] (ISOFORMS 3A; 3C AND 3D), AND NUCLEOTIDE
RP SEQUENCE [MRNA] OF 1-283 (ISOFORM 3B).
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=7598732; DOI=10.1006/bbrc.1995.1910;
RA Ibaraki K., Horikawa H.P.M., Morita T., Mori H., Sakimura K., Mishina M.,
RA Saisu H., Abe T.;
RT "Identification of four different forms of syntaxin 3.";
RL Biochem. Biophys. Res. Commun. 211:997-1005(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3A).
RC STRAIN=NOD; TISSUE=Dendritic cell;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3B).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
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 [7]
RP INTERACTION WITH PRPH2; ROM1; SNAP25 AND VAMP2, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=26406599; DOI=10.1371/journal.pone.0138508;
RA Zulliger R., Conley S.M., Mwoyosvi M.L., Stuck M.W., Azadi S., Naash M.I.;
RT "SNAREs Interact with Retinal Degeneration Slow and Rod Outer Segment
RT Membrane Protein-1 during Conventional and Unconventional Outer Segment
RT Targeting.";
RL PLoS ONE 10:E0138508-E0138508(2015).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH REEP6, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28369466; DOI=10.1093/hmg/ddx111;
RA Veleri S., Nellissery J., Mishra B., Manjunath S.H., Brooks M.J., Dong L.,
RA Nagashima K., Qian H., Gao C., Sergeev Y.V., Huang X.F., Qu J., Lu F.,
RA Cideciyan A.V., Li T., Jin Z.B., Fariss R.N., Ratnapriya R., Jacobson S.G.,
RA Swaroop A.;
RT "REEP6 mediates trafficking of a subset of Clathrin-coated vesicles and is
RT critical for rod photoreceptor function and survival.";
RL Hum. Mol. Genet. 26:2218-2230(2017).
RN [9]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=33974130; DOI=10.1007/s00439-021-02284-1;
RA Janecke A.R., Liu X., Adam R., Punuru S., Viestenz A., Strauss V.,
RA Laass M., Sanchez E., Adachi R., Schatz M.P., Saboo U.S., Mittal N.,
RA Rohrschneider K., Escher J., Ganesh A., Al Zuhaibi S., Al Murshedi F.,
RA AlSaleem B., Alfadhel M., Al Sinani S., Alkuraya F.S., Huber L.A.,
RA Mueller T., Heidelberger R., Janz R.;
RT "Pathogenic STX3 variants affecting the retinal and intestinal transcripts
RT cause an early-onset severe retinal dystrophy in microvillus inclusion
RT disease subjects.";
RL Hum. Genet. 140:1143-1156(2021).
CC -!- FUNCTION: Potentially involved in docking of synaptic vesicles at
CC presynaptic active zones. Apical receptor involved in membrane fusion
CC of apical vesicles (By similarity). Essential for survival of retinal
CC photoreceetors (PubMed:33974130). {ECO:0000250|UniProtKB:Q13277,
CC ECO:0000269|PubMed:33974130}.
CC -!- SUBUNIT: Interacts with REEP6 (PubMed:28369466). Isoform 3B interacts
CC with PRPH2 in rod and cone photoreceptors (PubMed:26406599). Isoform 3B
CC interacts with ROM1 (PubMed:26406599). Isoform 3B interacts with SNAP25
CC (PubMed:26406599). Isoform 3B interacts with VAMP2 (PubMed:26406599).
CC {ECO:0000269|PubMed:26406599, ECO:0000269|PubMed:28369466}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type IV
CC membrane protein {ECO:0000305}. Note=Localized to the inner and outer
CC plexiform layers, the cell body and the inner segments of
CC photoreceptors. {ECO:0000269|PubMed:28369466}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3B]: Photoreceptor inner segment
CC {ECO:0000269|PubMed:26406599}. Cell projection, cilium, photoreceptor
CC outer segment {ECO:0000269|PubMed:26406599}. Note=Colocalizes with
CC SNAP25 and ROM1 in the inner segment and outer nuclear layer of the
CC retina (at protein level) (PubMed:26406599). Partially colocalizes with
CC PRPH2 in the inner segment of the retina (at protein level)
CC (PubMed:26406599). {ECO:0000269|PubMed:26406599}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=3A {ECO:0000303|PubMed:7598732};
CC IsoId=Q64704-1; Sequence=Displayed;
CC Name=3B {ECO:0000303|PubMed:7598732};
CC IsoId=Q64704-2; Sequence=VSP_006346;
CC Name=3C {ECO:0000303|PubMed:7598732};
CC IsoId=Q64704-3; Sequence=VSP_006341, VSP_006346;
CC Name=3D {ECO:0000303|PubMed:7598732};
CC IsoId=Q64704-4; Sequence=VSP_006342, VSP_006344;
CC -!- TISSUE SPECIFICITY: Expressed in the retina (at protein level).
CC {ECO:0000269|PubMed:26406599, ECO:0000269|PubMed:28369466,
CC ECO:0000269|PubMed:33974130}.
CC -!- DISRUPTION PHENOTYPE: Knockout animals show progressive photoreceptor
CC degeneration. At 5 weeks of age, an approximately 60% decrease in
CC thickness of the outer nuclear layer (ONL) and in the number of ONL
CC neuronal somata is observed, indicating that a large number of
CC photoreceptors have died. In some of the remaining rods, rhodopsin is
CC appropriately localized to the outer segments, but a marked amount of
CC rhodopsin mislocalized to the outer plexiform layer. At 8 and 12 weeks
CC of age, increasing cell loss and further ectopic expression of
CC rhodopsin are observed. Cone photoreceptor loss and ectopic expression
CC of opsin in cones is also observed. Quantification of the progressive
CC degenerative phenotype reveals a rapid loss in the number of neuronal
CC somata in the ONL, indicative of photoreceptor death, whereas the
CC number of cells in the inner nuclear layer, including horizontal,
CC bipolar, and amacrine cells, is no different from that of controls.
CC {ECO:0000269|PubMed:33974130}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; D29797; BAA06180.1; -; mRNA.
DR EMBL; D29798; BAA06181.1; -; mRNA.
DR EMBL; D29799; BAA06182.1; -; mRNA.
DR EMBL; D29800; BAA06183.1; -; mRNA.
DR EMBL; D38375; BAA07454.1; -; mRNA.
DR EMBL; AK171135; BAE42269.1; -; mRNA.
DR EMBL; AC126036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC126266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466534; EDL41444.1; -; Genomic_DNA.
DR EMBL; BC024844; AAH24844.1; -; mRNA.
DR CCDS; CCDS29611.1; -. [Q64704-2]
DR CCDS; CCDS29612.1; -. [Q64704-3]
DR CCDS; CCDS29613.1; -. [Q64704-1]
DR PIR; I60170; I60170.
DR PIR; I83197; I83197.
DR PIR; I83198; I83198.
DR RefSeq; NP_001020478.1; NM_001025307.1. [Q64704-2]
DR RefSeq; NP_001273472.1; NM_001286543.1.
DR RefSeq; NP_035632.1; NM_011502.3. [Q64704-3]
DR RefSeq; NP_689344.1; NM_152220.2. [Q64704-1]
DR AlphaFoldDB; Q64704; -.
DR SMR; Q64704; -.
DR BioGRID; 203562; 7.
DR STRING; 10090.ENSMUSP00000069529; -.
DR iPTMnet; Q64704; -.
DR PhosphoSitePlus; Q64704; -.
DR jPOST; Q64704; -.
DR MaxQB; Q64704; -.
DR PaxDb; Q64704; -.
DR PeptideAtlas; Q64704; -.
DR PRIDE; Q64704; -.
DR ProteomicsDB; 254766; -. [Q64704-1]
DR ProteomicsDB; 254767; -. [Q64704-2]
DR ProteomicsDB; 254768; -. [Q64704-3]
DR ProteomicsDB; 254769; -. [Q64704-4]
DR Antibodypedia; 724; 150 antibodies from 30 providers.
DR DNASU; 20908; -.
DR Ensembl; ENSMUST00000069285; ENSMUSP00000069529; ENSMUSG00000041488. [Q64704-1]
DR Ensembl; ENSMUST00000075304; ENSMUSP00000074776; ENSMUSG00000041488. [Q64704-2]
DR Ensembl; ENSMUST00000211641; ENSMUSP00000147398; ENSMUSG00000041488. [Q64704-3]
DR GeneID; 20908; -.
DR KEGG; mmu:20908; -.
DR UCSC; uc008gsy.1; mouse.
DR UCSC; uc008gsz.1; mouse. [Q64704-3]
DR UCSC; uc008gtb.2; mouse. [Q64704-1]
DR CTD; 6809; -.
DR MGI; MGI:103077; Stx3.
DR VEuPathDB; HostDB:ENSMUSG00000041488; -.
DR eggNOG; KOG0810; Eukaryota.
DR GeneTree; ENSGT01030000234627; -.
DR HOGENOM; CLU_042423_2_2_1; -.
DR InParanoid; Q64704; -.
DR OMA; MIMICCV; -.
DR OrthoDB; 1033833at2759; -.
DR PhylomeDB; Q64704; -.
DR TreeFam; TF313763; -.
DR Reactome; R-MMU-449836; Other interleukin signaling.
DR BioGRID-ORCS; 20908; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Stx3; mouse.
DR PRO; PR:Q64704; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q64704; protein.
DR Bgee; ENSMUSG00000041488; Expressed in retinal neural layer and 264 other tissues.
DR ExpressionAtlas; Q64704; baseline and differential.
DR Genevisible; Q64704; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0042582; C:azurophil granule; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; IMP:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IMP:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0048787; C:presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0030141; C:secretory granule; IDA:MGI.
DR GO; GO:0031201; C:SNARE complex; IDA:MGI.
DR GO; GO:0042581; C:specific granule; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0042589; C:zymogen granule membrane; IDA:MGI.
DR GO; GO:0050544; F:arachidonic acid binding; ISO:MGI.
DR GO; GO:0005484; F:SNAP receptor activity; ISO:MGI.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; IDA:SynGO.
DR GO; GO:0006887; P:exocytosis; IMP:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
DR GO; GO:0061025; P:membrane fusion; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR GO; GO:0090174; P:organelle membrane fusion; ISS:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0050921; P:positive regulation of chemotaxis; ISO:MGI.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR GO; GO:0099003; P:vesicle-mediated transport in synapse; IDA:SynGO.
DR CDD; cd00179; SynN; 1.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR031186; Stx3.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR006011; Syntaxin_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR PANTHER; PTHR19957:SF34; PTHR19957:SF34; 1.
DR Pfam; PF05739; SNARE; 1.
DR Pfam; PF00804; Syntaxin; 1.
DR SMART; SM00503; SynN; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Coiled coil; Membrane;
KW Neurotransmitter transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..289
FT /note="Syntaxin-3"
FT /id="PRO_0000210200"
FT TOPO_DOM 1..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..283
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..289
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 191..253
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT COILED 32..111
FT /evidence="ECO:0000255"
FT VAR_SEQ 39..72
FT /note="IEETRLNIDKISEHVEEAKKLYSIILSAPIPEPK -> NFHGILSYLLRLSS
FT HE (in isoform 3C)"
FT /evidence="ECO:0000303|PubMed:7598732"
FT /id="VSP_006341"
FT VAR_SEQ 73..86
FT /note="TKDDLEQLTTEIKK -> LPWNPLLSPEIELT (in isoform 3D)"
FT /evidence="ECO:0000303|PubMed:7598732"
FT /id="VSP_006342"
FT VAR_SEQ 87..289
FT /note="Missing (in isoform 3D)"
FT /evidence="ECO:0000303|PubMed:7598732"
FT /id="VSP_006344"
FT VAR_SEQ 227..289
FT /note="EMLDNIELNVMHTVDHVEKARDETKRAMKYQGQARKKLIIIIVVVVVLLGIL
FT ALIIGLSVGLK -> AMIDRIENNMDQSVGFVERAVADTKKAVKYQSEARRKKIMIMIC
FT CIILAIILASTIGGIFA (in isoform 3B and isoform 3C)"
FT /evidence="ECO:0000303|PubMed:7598732"
FT /id="VSP_006346"
FT CONFLICT Q64704-4:75
FT /note="W -> R (in Ref. 1; BAA07454)"
FT /evidence="ECO:0000305|PubMed:7598732"
SQ SEQUENCE 289 AA; 33243 MW; 4A8EAFC2049EEE6F CRC64;
MKDRLEQLKA KQLTQDDDTD EVEIAIDNTA FMDEFFSEIE ETRLNIDKIS EHVEEAKKLY
SIILSAPIPE PKTKDDLEQL TTEIKKRANN VRNKLKSMEK HIEEDEVRSS ADLRIRKSQH
SVLSRKFVEV MTKYNEAQVD FRERSKGRIQ RQLEITGKKT TDEELEEMLE SGNPAIFTSG
IIDSQISKQA LSEIEGRHKD IVRLESSIKE LHDMFMDIAM LVENQGEMLD NIELNVMHTV
DHVEKARDET KRAMKYQGQA RKKLIIIIVV VVVLLGILAL IIGLSVGLK
