ESYT1_MOUSE
ID ESYT1_MOUSE Reviewed; 1092 AA.
AC Q3U7R1; Q8C8R1; Q91X62; Q9CVH0; Q9Z1X5; Q9Z1X6;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Extended synaptotagmin-1;
DE Short=E-Syt1;
DE AltName: Full=Membrane-bound C2 domain-containing protein;
GN Name=Esyt1; Synonyms=Fam62a, Mbc2;
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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-632 AND 955-1092 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Retina, and Small intestine;
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] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 392-1092 (ISOFORM 1).
RC TISSUE=Mammary gland;
RX PubMed=10350628; DOI=10.1016/s0167-4838(99)00068-0;
RA Morris N.J., Ross S.A., Neveu J.M., Lane W.S., Lienhard G.E.;
RT "Cloning and preliminary characterization of a 121 kDa protein with
RT multiple predicted C2 domains.";
RL Biochim. Biophys. Acta 1431:525-530(1999).
RN [4]
RP PHOSPHORYLATION AT SER-314, IDENTIFICATION BY MASS SPECTROMETRY,
RP MUTAGENESIS OF SER-314, AND INTERACTION WITH SLC2A4.
RX PubMed=19255425; DOI=10.1073/pnas.0900218106;
RA Lalioti V., Muruais G., Dinarina A., van Damme J., Vandekerckhove J.,
RA Sandoval I.V.;
RT "The atypical kinase Cdk5 is activated by insulin, regulates the
RT association between GLUT4 and E-Syt1, and modulates glucose transport in
RT 3T3-L1 adipocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:4249-4253(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-951, AND IDENTIFICATION BY
RP MASS 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: Binds glycerophospholipids in a barrel-like domain and may
CC play a role in cellular lipid transport (By similarity). Binds calcium
CC (via the C2 domains) and translocates to sites of contact between the
CC endoplasmic reticulum and the cell membrane in response to increased
CC cytosolic calcium levels. Helps tether the endoplasmic reticulum to the
CC cell membrane and promotes the formation of appositions between the
CC endoplasmic reticulum and the cell membrane (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ESYT2 and ESYT3 (By similarity). Interacts
CC (phosphorylated form) with SLC2A4. {ECO:0000250,
CC ECO:0000269|PubMed:19255425}.
CC -!- INTERACTION:
CC Q3U7R1; P14142: Slc2a4; NbExp=2; IntAct=EBI-8398881, EBI-7540210;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9BSJ8}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9BSJ8}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:Q9BSJ8}. Note=Localizes
CC primarily to the endoplasmic reticulum. Recruited to sites of contact
CC between the endoplasmic reticulum and the cell membrane in response to
CC increased cytosolic calcium levels. {ECO:0000250|UniProtKB:Q9BSJ8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3U7R1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U7R1-2; Sequence=VSP_018278, VSP_018279;
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 translocation to the cell membrane
CC in response to increased cytosolic calcium levels (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The SMP-LTD domain is a barrel-like domain that binds
CC glycerophospholipids in its interior (By similarity).
CC {ECO:0000250|UniProtKB:A0FGR8}.
CC -!- PTM: Phosphorylated on Ser residues in insulin-treated adipocytes (in
CC vitro); this promotes interaction with SLC2A4.
CC {ECO:0000269|PubMed:19255425}.
CC -!- SIMILARITY: Belongs to the extended synaptotagmin family.
CC {ECO:0000305}.
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DR EMBL; AK008224; BAB25542.1; -; mRNA.
DR EMBL; AK044656; BAC32020.1; -; mRNA.
DR EMBL; AK152482; BAE31254.1; -; mRNA.
DR EMBL; AK152554; BAE31308.1; -; mRNA.
DR EMBL; BC011482; AAH11482.1; -; mRNA.
DR EMBL; AF098633; AAD10189.1; -; mRNA.
DR EMBL; AF098634; AAD10190.1; -; mRNA.
DR CCDS; CCDS24280.1; -. [Q3U7R1-1]
DR RefSeq; NP_035973.1; NM_011843.2. [Q3U7R1-1]
DR AlphaFoldDB; Q3U7R1; -.
DR SMR; Q3U7R1; -.
DR BioGRID; 204808; 10.
DR DIP; DIP-48746N; -.
DR IntAct; Q3U7R1; 5.
DR MINT; Q3U7R1; -.
DR STRING; 10090.ENSMUSP00000026427; -.
DR ChEMBL; CHEMBL3621032; -.
DR iPTMnet; Q3U7R1; -.
DR PhosphoSitePlus; Q3U7R1; -.
DR SwissPalm; Q3U7R1; -.
DR EPD; Q3U7R1; -.
DR jPOST; Q3U7R1; -.
DR MaxQB; Q3U7R1; -.
DR PaxDb; Q3U7R1; -.
DR PeptideAtlas; Q3U7R1; -.
DR PRIDE; Q3U7R1; -.
DR ProteomicsDB; 275692; -. [Q3U7R1-1]
DR ProteomicsDB; 275693; -. [Q3U7R1-2]
DR Antibodypedia; 3015; 249 antibodies from 33 providers.
DR Ensembl; ENSMUST00000026427; ENSMUSP00000026427; ENSMUSG00000025366. [Q3U7R1-1]
DR GeneID; 23943; -.
DR KEGG; mmu:23943; -.
DR UCSC; uc007hng.1; mouse. [Q3U7R1-1]
DR CTD; 23344; -.
DR MGI; MGI:1344426; Esyt1.
DR VEuPathDB; HostDB:ENSMUSG00000025366; -.
DR eggNOG; KOG1012; Eukaryota.
DR GeneTree; ENSGT00940000156561; -.
DR HOGENOM; CLU_012047_0_0_1; -.
DR InParanoid; Q3U7R1; -.
DR OMA; HPGQSKE; -.
DR OrthoDB; 52746at2759; -.
DR PhylomeDB; Q3U7R1; -.
DR TreeFam; TF324255; -.
DR Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR BioGRID-ORCS; 23943; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Esyt1; mouse.
DR PRO; PR:Q3U7R1; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q3U7R1; protein.
DR Bgee; ENSMUSG00000025366; Expressed in ectoplacental cone and 110 other tissues.
DR ExpressionAtlas; Q3U7R1; baseline and differential.
DR Genevisible; Q3U7R1; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR GO; GO:0008429; F:phosphatidylethanolamine binding; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0120014; F:phospholipid transfer activity; ISS:UniProtKB.
DR GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; IEA:InterPro.
DR GO; GO:0120009; P:intermembrane lipid transfer; ISS:UniProtKB.
DR CDD; cd08391; C2A_C2C_Synaptotagmin_like; 2.
DR CDD; cd04050; C2B_Synaptotagmin-like; 2.
DR CDD; cd04030; C2C_KIAA1228; 1.
DR Gene3D; 2.60.40.150; -; 5.
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; 5.
DR Pfam; PF17047; SMP_LBD; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR SMART; SM00239; C2; 5.
DR SUPFAM; SSF49562; SSF49562; 5.
DR PROSITE; PS50004; C2; 5.
DR PROSITE; PS51847; SMP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Calcium; Cell membrane;
KW Endoplasmic reticulum; Lipid transport; Lipid-binding; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1092
FT /note="Extended synaptotagmin-1"
FT /id="PRO_0000234345"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..52
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..1092
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 125..303
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01194"
FT DOMAIN 302..423
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 444..570
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 616..738
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 769..886
FT /note="C2 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 959..1081
FT /note="C2 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1013
FT /note="Required for phosphatidylinositol 4,5-bisphosphate-
FT dependent location at the cell membrane"
FT /evidence="ECO:0000250"
FT COMPBIAS 909..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 401
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSJ8"
FT MOD_RES 314
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000269|PubMed:19255425"
FT MOD_RES 804
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSJ8"
FT MOD_RES 807
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSJ8"
FT MOD_RES 937
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSJ8"
FT MOD_RES 951
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 997
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1X1"
FT VAR_SEQ 852..893
FT /note="VRGEGTGTLGSVSLPLSELLQEDQLCLDHWFALSGQGQVLMR -> ACFIHL
FT LFLFERGREQRTVFEFEVFGVNSFPPCGNLWATAHS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018278"
FT VAR_SEQ 894..1092
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018279"
FT MUTAGEN 314
FT /note="S->A: Abolished phosphorylation by CDK5."
FT /evidence="ECO:0000269|PubMed:19255425"
FT CONFLICT 385
FT /note="G -> R (in Ref. 2; BAC32020)"
FT /evidence="ECO:0000305"
FT CONFLICT 392..394
FT /note="VFD -> IQH (in Ref. 3; AAD10190)"
FT /evidence="ECO:0000305"
FT CONFLICT 829..841
FT /note="APVWEESASFLIR -> GFGLEAKIRHEGG (in Ref. 3;
FT AAD10189)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1092 AA; 121554 MW; 71A397EC52DE6DA9 CRC64;
MEHSPEEGAS PEPSGQPPAT DSTRDGGSGV PPAGPGAASE ALAVLTSFGR RLLVLVPVYL
AGAAGLSVGF VLFGLALYLG WRRVRDGKER SLRAARQLLD DEERITAETL YMSHRELPAW
VSFPDVEKAE WLNKIVAQVW PFLGQYMEKL LAETVAPAVR GANPHLQTFT FTRVELGEKP
LRIIGVKVHP SQRKDQILLD LNVSYVGDVQ IDVEVKKYFC KAGVKGMQLH GVLRVILEPL
TGDLPIVGAV SMFFIKRPTL DINWTGMTNL LDIPGLSSLS DTMIMDSIAA FLVLPNRLLV
PLVPDLQDVA QLRSPLPRGI IRIHLLAARG LSSKDKYVKG LIEGKSDPYA LVRVGTQTFC
SRVIDEELNP HWGETYEVIV HEVPGQEIEV EVFDKDPDKD DFLGRMKLDV GKVLQAGVLD
NWYPLQGGQG QVHLRLEWLS LLPDAEKLDQ VLQWNRGITS RPEPPSAAIL VVYLDRAQDL
PLKKGNKEPN PMVQLSVQDV TRESKATYST NSPVWEEAFR FFLQDPRSQE LDVQVKDDSR
ALTLGALTLP LARLLTASEL TLDQWFQLSS SGPNSRLYMK LVMRILYLDY SEIRFPTVPG
AQDWDRESLE TGSSVDAPPR PYHTTPNSHF GTENVLRIHV LEAQDLIAKD RFLGGLVKGK
SDPYVKLKVA GKSFRTHVVR EDLNPRWNEV FEVIVTSIPG QELEIEVFDK DLDKDDFLGR
YKVSLTTVLN SGFLDEWLTL EDVPSGRLHL RLERLTPRPT AAELEEVLQV NSLIQTQKSS
ELAAALLSVF LERAEDLPLR KGTKPPSPYA TITVGETSHK TKTVSQSSAP VWEESASFLI
RKPHAESLEL QVRGEGTGTL GSVSLPLSEL LQEDQLCLDH WFALSGQGQV LMRAQLGILV
SQHSGVEAHS HSYSHSHSSS SLNDEPEALG GPTHPASPVL EVRHRLTHGD SPSEAPVGPL
GQVKLTVWYH SDEQKLISII HSCRALRQNG RDLPDPYVSV LLLPDKNRST KRKTPQKKRT
LNPEFNERFE WDLPLDGTLR RKLDVSVKSN SSFMSREREL LGKVQLDLAE IDLSQGAAQW
YDLMDDRDKG GS
