ESYT2_MOUSE
ID ESYT2_MOUSE Reviewed; 845 AA.
AC Q3TZZ7; B2RSN5; Q9D5Y7;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Extended synaptotagmin-2;
DE Short=E-Syt2;
GN Name=Esyt2; Synonyms=D12Ertd551e, Fam62b;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Retina, and Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-685, AND IDENTIFICATION BY
RP 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 [4]
RP CALCIUM-BINDING.
RX PubMed=18977228; DOI=10.1016/j.febslet.2008.10.038;
RA Groer G.J., Haslbeck M., Roessle M., Gessner A.;
RT "Structural characterization of soluble E-Syt2.";
RL FEBS Lett. 582:3941-3947(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662; SER-682 AND SER-685, AND
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-660; SER-662; SER-663;
RP SER-667; SER-679; SER-682 AND SER-685, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
CC -!- FUNCTION: Tethers the endoplasmic reticulum to the cell membrane and
CC promotes the formation of appositions between the endoplasmic reticulum
CC and the cell membrane. Binds glycerophospholipids in a barrel-like
CC domain and may play a role in cellular lipid transport. Plays a role in
CC FGF signaling via its role in the rapid internalization of FGFR1 that
CC has been activated by FGF1 binding; this occurs most likely via the AP-
CC 2 complex (By similarity). Promotes the localization of SACM1L at
CC endoplasmic reticulum-plasma membrane contact sites (EPCS) (By
CC similarity). {ECO:0000250|UniProtKB:A0FGR8}.
CC -!- SUBUNIT: Homodimer. Interacts with ESYT1 and ESYT3. Interacts with
CC FGFR1 that has been activated by FGF1 binding. Interacts with the AP-2
CC complex; identified in a complex with the AP-2 complex and FGFR1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A0FGR8};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:A0FGR8}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:A0FGR8}; Multi-pass membrane
CC protein {ECO:0000255}. Note=Localizes to endoplasmic reticulum-plasma
CC membrane contact sites (EPCS). Recruited to the cell membrane via the
CC third C2 domain (By similarity). {ECO:0000250|UniProtKB:A0FGR8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3TZZ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TZZ7-2; Sequence=VSP_023243;
CC -!- DOMAIN: Anchored to the endoplasmic reticulum membrane by a
CC transmembrane hairpin structure; both N-terminus and C-terminus are
CC cytoplasmic. {ECO:0000250}.
CC -!- DOMAIN: The C2 domains mediate lipid and calcium binding. The N-
CC terminal C2 domain binds calcium ions and is important for calcium-
CC dependent lipid binding and interaction with membranes. Two calcium
CC ions are bound at a high-affinity site and a third calcium ion is bound
CC with lower affinity. May bind up to four calcium ions. In contrast, the
CC second C2 domain apparently does not bind calcium. The third C2 domain
CC mediates interaction with membranes enriched in phosphatidylinositol
CC 4,5-bisphosphate and is required for location at the cell membrane (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The SMP-LTD domain is a barrel-like domain that binds
CC glycerophospholipids in its interior; can bind two lipid molecules
CC simultaneously. Binds a variety of lipids, including
CC phosphatidylethanolamine, phosphatidylcholine and phosphatidylinositol
CC (By similarity). {ECO:0000250|UniProtKB:A0FGR8}.
CC -!- SIMILARITY: Belongs to the extended synaptotagmin family.
CC {ECO:0000305}.
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DR EMBL; AK014813; BAB29565.1; -; mRNA.
DR EMBL; AK044360; BAC31884.1; -; mRNA.
DR EMBL; AK157352; BAE34059.1; -; mRNA.
DR EMBL; BC052440; AAH52440.1; -; mRNA.
DR EMBL; BC054797; AAH54797.1; -; mRNA.
DR EMBL; BC059230; AAH59230.1; -; mRNA.
DR EMBL; BC138937; AAI38938.1; -; mRNA.
DR CCDS; CCDS26211.1; -. [Q3TZZ7-1]
DR RefSeq; NP_083007.2; NM_028731.5. [Q3TZZ7-1]
DR RefSeq; XP_017170617.1; XM_017315128.1.
DR AlphaFoldDB; Q3TZZ7; -.
DR SMR; Q3TZZ7; -.
DR BioGRID; 206705; 4.
DR IntAct; Q3TZZ7; 1.
DR MINT; Q3TZZ7; -.
DR STRING; 10090.ENSMUSP00000098548; -.
DR iPTMnet; Q3TZZ7; -.
DR PhosphoSitePlus; Q3TZZ7; -.
DR SwissPalm; Q3TZZ7; -.
DR EPD; Q3TZZ7; -.
DR jPOST; Q3TZZ7; -.
DR MaxQB; Q3TZZ7; -.
DR PaxDb; Q3TZZ7; -.
DR PeptideAtlas; Q3TZZ7; -.
DR PRIDE; Q3TZZ7; -.
DR ProteomicsDB; 275482; -. [Q3TZZ7-1]
DR ProteomicsDB; 275483; -. [Q3TZZ7-2]
DR Antibodypedia; 950; 109 antibodies from 21 providers.
DR Ensembl; ENSMUST00000100986; ENSMUSP00000098548; ENSMUSG00000021171. [Q3TZZ7-1]
DR Ensembl; ENSMUST00000220816; ENSMUSP00000152444; ENSMUSG00000021171. [Q3TZZ7-1]
DR GeneID; 52635; -.
DR KEGG; mmu:52635; -.
DR UCSC; uc007pho.1; mouse. [Q3TZZ7-1]
DR UCSC; uc007phq.1; mouse. [Q3TZZ7-2]
DR CTD; 57488; -.
DR MGI; MGI:1261845; Esyt2.
DR VEuPathDB; HostDB:ENSMUSG00000021171; -.
DR eggNOG; KOG1012; Eukaryota.
DR GeneTree; ENSGT00940000156086; -.
DR HOGENOM; CLU_012047_0_0_1; -.
DR InParanoid; Q3TZZ7; -.
DR OMA; MKKDIGV; -.
DR OrthoDB; 52746at2759; -.
DR PhylomeDB; Q3TZZ7; -.
DR TreeFam; TF324255; -.
DR Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR BioGRID-ORCS; 52635; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Esyt2; mouse.
DR PRO; PR:Q3TZZ7; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q3TZZ7; protein.
DR Bgee; ENSMUSG00000021171; Expressed in dorsal pancreas and 224 other tissues.
DR ExpressionAtlas; Q3TZZ7; baseline and differential.
DR Genevisible; Q3TZZ7; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0140268; C:endoplasmic reticulum-plasma membrane contact site; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0044232; C:organelle membrane contact site; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISS:UniProtKB.
DR GO; GO:0008429; F:phosphatidylethanolamine binding; ISS:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd08391; C2A_C2C_Synaptotagmin_like; 1.
DR CDD; cd04050; C2B_Synaptotagmin-like; 1.
DR CDD; cd04030; C2C_KIAA1228; 1.
DR Gene3D; 2.60.40.150; -; 3.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037752; C2C_KIAA1228.
DR InterPro; IPR037733; Ext_Synaptotagmin_C2A.
DR InterPro; IPR037749; Ext_Synaptotagmin_C2B.
DR InterPro; IPR031468; SMP_LBD.
DR InterPro; IPR039010; Synaptotagmin_SMP.
DR Pfam; PF00168; C2; 3.
DR Pfam; PF17047; SMP_LBD; 1.
DR SMART; SM00239; C2; 3.
DR SUPFAM; SSF49562; SSF49562; 3.
DR PROSITE; PS50004; C2; 3.
DR PROSITE; PS51847; SMP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Endocytosis;
KW Endoplasmic reticulum; Lipid transport; Lipid-binding; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..845
FT /note="Extended synaptotagmin-2"
FT /id="PRO_0000278259"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..51
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..845
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 115..294
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01194"
FT DOMAIN 293..413
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 442..563
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 710..832
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..764
FT /note="Required for phosphatidylinositol 4,5-bisphosphate-
FT dependent location at the cell membrane"
FT /evidence="ECO:0000250"
FT COMPBIAS 613..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 324
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A0FGR8"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A0FGR8"
FT MOD_RES 629
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A0FGR8"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 663
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..487
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023243"
SQ SEQUENCE 845 AA; 94139 MW; 988F3D97D7F3CF6C CRC64;
MSSAGGEGPE AGPGRAGGRS EPEAPGSALS VDLPGLLGQL ARSFALLLPV YALGYLGLSF
SWVLLALGLL AWCRRSRGLK ASRLCRALAL LEDEEQAVRL GVRACDLPAW VHFPDTERAE
WLNKTVKHMW PFICQFIEKL FRETIEPAVR GANAHLSTFS FTKVDVGQQP LRVNGVKVYT
ENVDKRQIIL DLQISFVGNC EIDLEIKRYF CRAGVKSIQI HGTMRVILEP LIGDMPLVGA
LSIFFLRKPL LEINWTGLTN LLDIPGLNGL SDTIILDIIS NYLVLPNRIT VPLVSEVQIA
QLRFPIPKGV LRIHFIEAQD LQGKDTYLKG LVKGKSDPYG IIRVGNQIFQ SKVIKENLSP
KWNEVYEALV YEHPGQELEI ELFDEDPDKD DFLGSLMIDL IEVEKERLLD EWFTLDEVPK
GKLHLKLEWL TLMPDAANLD KVLADIRADK DQASDGLSSA LLILYLDSAR NLPSGKKINS
NPNPLVQMSV GHKAQESKIR YKTSEPVWEE NFTFFIHNPR RQDLEVEVKD EQHQCSLGSL
RIPLSQLLTS DNMTINQRFQ LSNSGPNSTL KMKIALRVLH LEKQERPPDY QHSAQVKRPS
VSKEGRKMPI KSQMSASPGT GGANTAPSTP VMGVDDKPAM EEKPQPPEAS PLGHRDLGRS
SSSLLASPSH IAAKEPTPSI ASDISLPIAT QELRQRLRQL ENGTTLGQSP LGQIQLTIRH
SSQRNKLIVV VHSCRNLIAF SEDGSDPYVR MYLLPDKRRS GRRKTHVSKK TLNPVFDQSF
DFSVSLPEVQ RRTLDVAVKN SGGFLSKDKG LLGKVLVVLA SEELAKGWTQ WYDLTEDGTR
PQVIT
