ID ESYT2_HUMAN Reviewed; 921 AA. AC A0FGR8; A4D229; Q69YJ2; Q6UKI4; Q6ZTU0; Q6ZVU1; Q9BQS0; Q9NW47; Q9ULJ2; DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2006, sequence version 1. DT 27-MAR-2024, entry version 152. DE RecName: Full=Extended synaptotagmin-2 {ECO:0000305}; DE Short=E-Syt2 {ECO:0000303|PubMed:29469807}; DE AltName: Full=Chr2Syt; GN Name=ESYT2 {ECO:0000312|HGNC:HGNC:22211}; Synonyms=FAM62B, KIAA1228; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, RP CALCIUM-DEPENDENT LIPID-BINDING, AND TISSUE SPECIFICITY. RX PubMed=17360437; DOI=10.1073/pnas.0611725104; RA Min S.-W., Chang W.-P., Suedhof T.C.; RT "E-Syts, a family of membranous Ca2+-sensor proteins with multiple C2 RT domains."; RL Proc. Natl. Acad. Sci. U.S.A. 104:3823-3828(2007). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Shan Y.X., Yu L.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 511-921 (ISOFORMS 1/2), AND VARIANT GLY-638. RC TISSUE=Esophageal carcinoma, and Thymus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-921 (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10574462; DOI=10.1093/dnares/6.5.337; RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XV. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:337-345(1999). RN [6] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 141-921. RC TISSUE=Melanoma; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 454-921 (ISOFORM 6). RC TISSUE=Colon; 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 [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 747-904. RC TISSUE=Brain; RX PubMed=11543631; DOI=10.1006/geno.2001.6619; RA Craxton M.A.; RT "Genomic analysis of synaptotagmin genes."; RL Genomics 77:43-49(2001). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743; SER-758 AND SER-761, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743; SER-755; SER-758 AND RP SER-761, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691; SER-739; SER-748; RP SER-755; SER-758 AND SER-761, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [15] RP INTERACTION WITH FGFR1 AND AP2B1, SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=20833364; DOI=10.1016/j.devcel.2010.08.007; RA Jean S., Mikryukov A., Tremblay M.G., Baril J., Guillou F., Bellenfant S., RA Moss T.; RT "Extended-synaptotagmin-2 mediates FGF receptor endocytosis and ERK RT activation in vivo."; RL Dev. Cell 19:426-439(2010). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743; SER-758 AND SER-761, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-758 AND SER-761, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [19] RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, LIPID-BINDING, DOMAIN, RP MUTAGENESIS OF 833-LYS--LYS-840, AND INTERACTION WITH ESYT1 AND ESYT3. RX PubMed=23791178; DOI=10.1016/j.cell.2013.05.026; RA Giordano F., Saheki Y., Idevall-Hagren O., Colombo S.F., Pirruccello M., RA Milosevic I., Gracheva E.O., Bagriantsev S.N., Borgese N., De Camilli P.; RT "PI(4,5)P(2)-dependent and Ca(2+)-regulated ER-PM interactions mediated by RT the extended synaptotagmins."; RL Cell 153:1494-1509(2013). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691; SER-736; SER-739; RP SER-743 AND SER-761, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-693; THR-705 AND SER-761, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [23] RP SUBCELLULAR LOCATION. RX PubMed=30220461; DOI=10.1016/j.cell.2018.08.033; RA Sandhu J., Li S., Fairall L., Pfisterer S.G., Gurnett J.E., Xiao X., RA Weston T.A., Vashi D., Ferrari A., Orozco J.L., Hartman C.L., RA Strugatsky D., Lee S.D., He C., Hong C., Jiang H., Bentolila L.A., RA Gatta A.T., Levine T.P., Ferng A., Lee R., Ford D.A., Young S.G., RA Ikonen E., Schwabe J.W.R., Tontonoz P.; RT "Aster proteins facilitate nonvesicular plasma membrane to ER cholesterol RT transport in mammalian cells."; RL Cell 175:514-529(2018). RN [24] RP SUBCELLULAR LOCATION. RX PubMed=29469807; DOI=10.7554/elife.31019; RA Besprozvannaya M., Dickson E., Li H., Ginburg K.S., Bers D.M., Auwerx J., RA Nunnari J.; RT "GRAM domain proteins specialize functionally distinct ER-PM contact sites RT in human cells."; RL Elife 7:0-0(2018). RN [25] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=27044890; DOI=10.1083/jcb.201508106; RA Dickson E.J., Jensen J.B., Vivas O., Kruse M., Traynor-Kaplan A.E., RA Hille B.; RT "Dynamic formation of ER-PM junctions presents a lipid phosphatase to RT regulate phosphoinositides."; RL J. Cell Biol. 213:33-48(2016). RN [26] RP STRUCTURE BY NMR OF 222-350. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the third C2 domain of KIAA1228 protein."; RL Submitted (OCT-2006) to the PDB data bank. RN [27] RP X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 191-662 IN COMPLEX WITH RP PHOSPHATIDYLETHANOLAMINE, LIPID-BINDING, FUNCTION, DOMAIN, AND SUBUNIT. RX PubMed=24847877; DOI=10.1038/nature13269; RA Schauder C.M., Wu X., Saheki Y., Narayanaswamy P., Torta F., Wenk M.R., RA De Camilli P., Reinisch K.M.; RT "Structure of a lipid-bound extended synaptotagmin indicates a role in RT lipid transfer."; RL Nature 510:552-555(2014). RN [28] RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 363-660 IN COMPLEX WITH CALCIUM, RP DOMAIN, CALCIUM-BINDING, AND MUTAGENESIS OF ASP-401; ASP-413 AND ASP-466. RX PubMed=24373768; DOI=10.1016/j.str.2013.11.011; RA Xu J., Bacaj T., Zhou A., Tomchick D.R., Sudhof T.C., Rizo J.; RT "Structure and Ca(2+)-binding properties of the tandem C(2) domains of E- RT Syt2."; RL Structure 22:269-280(2014). 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. Promotes the localization of SACM1L at endoplasmic CC reticulum-plasma membrane contact sites (EPCS) (PubMed:27044890). CC {ECO:0000269|PubMed:17360437, ECO:0000269|PubMed:20833364, CC ECO:0000269|PubMed:23791178, ECO:0000269|PubMed:24847877, CC ECO:0000269|PubMed:27044890}. 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. CC {ECO:0000269|PubMed:20833364, ECO:0000269|PubMed:23791178, CC ECO:0000269|PubMed:24373768, ECO:0000269|PubMed:24847877}. CC -!- INTERACTION: CC A0FGR8; Q9BSJ8: ESYT1; NbExp=6; IntAct=EBI-3184170, EBI-355956; CC A0FGR8; A0FGR8: ESYT2; NbExp=3; IntAct=EBI-3184170, EBI-3184170; CC A0FGR8; A0FGR9: ESYT3; NbExp=4; IntAct=EBI-3184170, EBI-8771391; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17360437, CC ECO:0000269|PubMed:20833364, ECO:0000269|PubMed:23791178, CC ECO:0000269|PubMed:29469807}; Peripheral membrane protein CC {ECO:0000269|PubMed:17360437}. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:23791178, ECO:0000269|PubMed:29469807}; Multi-pass CC membrane protein {ECO:0000255}. Note=Localizes to endoplasmic CC reticulum-plasma membrane contact sites (EPCS) (PubMed:29469807, CC PubMed:23791178, PubMed:30220461, PubMed:27044890). Recruited to the CC cell membrane via the third C2 domain (PubMed:17360437). CC {ECO:0000269|PubMed:17360437, ECO:0000269|PubMed:23791178, CC ECO:0000269|PubMed:29469807, ECO:0000269|PubMed:30220461}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=A0FGR8-1; Sequence=Displayed; CC Name=2; CC IsoId=A0FGR8-2; Sequence=VSP_023239; CC Name=4; CC IsoId=A0FGR8-4; Sequence=VSP_023238, VSP_023241, VSP_023242; CC Name=5; CC IsoId=A0FGR8-5; Sequence=VSP_023236, VSP_023240; CC Name=6; CC IsoId=A0FGR8-6; Sequence=VSP_038324; CC -!- TISSUE SPECIFICITY: Widely expressed with high level in cerebellum. CC {ECO:0000269|PubMed:17360437}. CC -!- DOMAIN: Anchored to the endoplasmic reticulum membrane by a CC transmembrane hairpin structure; both N-terminus and C-terminus are CC cytoplasmic. {ECO:0000269|PubMed:23791178}. 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 (PubMed:24373768). CC The third C2 domain mediates interaction with membranes enriched in CC phosphatidylinositol 4,5-bisphosphate and is required for location at CC the cell membrane (PubMed:23791178). {ECO:0000269|PubMed:23791178, CC ECO:0000269|PubMed:24373768}. 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 (PubMed:24847877). {ECO:0000269|PubMed:24847877}. CC -!- SIMILARITY: Belongs to the extended synaptotagmin family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA91539.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC85769.1; Type=Frameshift; Evidence={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; DQ993201; ABJ97706.1; -; mRNA. DR EMBL; AY368150; AAR89381.1; -; mRNA. DR EMBL; AK001181; BAA91539.1; ALT_INIT; mRNA. DR EMBL; AK124091; BAC85769.1; ALT_FRAME; mRNA. DR EMBL; AK126214; BAC86489.1; -; mRNA. DR EMBL; CH236954; EAL23931.1; -; Genomic_DNA. DR EMBL; AB033054; BAA86542.2; -; mRNA. DR EMBL; AL833233; CAH10642.1; -; mRNA. DR EMBL; BC013957; AAH13957.2; -; mRNA. DR EMBL; AJ303365; CAC33887.1; -; mRNA. DR RefSeq; NP_065779.1; NM_020728.2. DR PDB; 2DMG; NMR; -; A=785-913. DR PDB; 4NPJ; X-ray; 2.10 A; A/B=363-660. DR PDB; 4NPK; X-ray; 2.55 A; A=363-660. DR PDB; 4P42; X-ray; 2.44 A; A/B=191-662. DR PDBsum; 2DMG; -. DR PDBsum; 4NPJ; -. DR PDBsum; 4NPK; -. DR PDBsum; 4P42; -. DR AlphaFoldDB; A0FGR8; -. DR SMR; A0FGR8; -. DR BioGRID; 121556; 381. DR CORUM; A0FGR8; -. DR DIP; DIP-61039N; -. DR IntAct; A0FGR8; 62. DR MINT; A0FGR8; -. DR STRING; 9606.ENSP00000499020; -. DR TCDB; 9.A.57.1.2; the extended-synaptotagmin (e-syt) family. DR GlyCosmos; A0FGR8; 1 site, 1 glycan. DR GlyGen; A0FGR8; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; A0FGR8; -. DR PhosphoSitePlus; A0FGR8; -. DR SwissPalm; A0FGR8; -. DR BioMuta; ESYT2; -. DR EPD; A0FGR8; -. DR jPOST; A0FGR8; -. DR MassIVE; A0FGR8; -. DR MaxQB; A0FGR8; -. DR PaxDb; 9606-ENSP00000251527; -. DR PeptideAtlas; A0FGR8; -. DR ProteomicsDB; 30; -. [A0FGR8-1] DR ProteomicsDB; 31; -. [A0FGR8-2] DR ProteomicsDB; 32; -. [A0FGR8-4] DR ProteomicsDB; 33; -. [A0FGR8-5] DR ProteomicsDB; 34; -. [A0FGR8-6] DR Pumba; A0FGR8; -. DR Antibodypedia; 950; 127 antibodies from 21 providers. DR DNASU; 57488; -. DR Ensembl; ENST00000652148.1; ENSP00000499020.1; ENSG00000117868.18. [A0FGR8-2] DR GeneID; 57488; -. DR KEGG; hsa:57488; -. DR UCSC; uc003wob.2; human. [A0FGR8-1] DR AGR; HGNC:22211; -. DR CTD; 57488; -. DR DisGeNET; 57488; -. DR GeneCards; ESYT2; -. DR HGNC; HGNC:22211; ESYT2. DR HPA; ENSG00000117868; Low tissue specificity. DR neXtProt; NX_A0FGR8; -. DR OpenTargets; ENSG00000117868; -. DR PharmGKB; PA165617947; -. DR VEuPathDB; HostDB:ENSG00000117868; -. DR eggNOG; KOG1012; Eukaryota. DR GeneTree; ENSGT00940000156086; -. DR InParanoid; A0FGR8; -. DR OrthoDB; 944695at2759; -. DR PhylomeDB; A0FGR8; -. DR TreeFam; TF324255; -. DR PathwayCommons; A0FGR8; -. DR Reactome; R-HSA-9840309; Glycosphingolipid biosynthesis. DR SignaLink; A0FGR8; -. DR BioGRID-ORCS; 57488; 16 hits in 1153 CRISPR screens. DR ChiTaRS; ESYT2; human. DR EvolutionaryTrace; A0FGR8; -. DR GeneWiki; FAM62B; -. DR GenomeRNAi; 57488; -. DR Pharos; A0FGR8; Tbio. DR PRO; PR:A0FGR8; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; A0FGR8; Protein. DR Bgee; ENSG00000117868; Expressed in layer of synovial tissue and 191 other cell types or tissues. DR ExpressionAtlas; A0FGR8; baseline and differential. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IMP:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0140268; C:endoplasmic reticulum-plasma membrane contact site; IDA:UniProtKB. DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0044232; C:organelle membrane contact site; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB. DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:FlyBase. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0031210; F:phosphatidylcholine binding; IDA:UniProtKB. DR GO; GO:0008429; F:phosphatidylethanolamine binding; IDA:UniProtKB. DR GO; GO:0035091; F:phosphatidylinositol binding; IDA: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 CDD; cd21680; SMP_ESyt2; 1. DR Gene3D; 2.60.40.150; C2 domain; 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 PANTHER; PTHR45761:SF2; EXTENDED SYNAPTOTAGMIN-2; 1. DR PANTHER; PTHR45761; EXTENDED SYNAPTOTAGMIN-LIKE PROTEIN 2, ISOFORM C; 1. DR Pfam; PF00168; C2; 3. DR Pfam; PF17047; SMP_LBD; 1. DR SMART; SM00239; C2; 3. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 3. DR PROSITE; PS50004; C2; 3. DR PROSITE; PS51847; SMP; 1. DR Genevisible; A0FGR8; HS. PE 1: Evidence at protein level; KW 3D-structure; 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..921 FT /note="Extended synaptotagmin-2" FT /id="PRO_0000278258" FT TOPO_DOM 1..103 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 104..124 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 125..127 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 128..148 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 149..921 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 191..370 FT /note="SMP-LTD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01194, FT ECO:0000269|PubMed:24847877" FT DOMAIN 369..489 FT /note="C2 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT DOMAIN 514..639 FT /note="C2 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT DOMAIN 786..908 FT /note="C2 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT REGION 1..103 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 660..754 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 833..840 FT /note="Required for phosphatidylinositol 4,5-bisphosphate- FT dependent location at the cell membrane" FT COMPBIAS 22..36 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 56..71 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 660..686 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 687..707 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 400 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:24373768" FT BINDING 401 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:24373768" FT BINDING 401 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:24373768" FT BINDING 413 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:24373768" FT BINDING 460 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:24373768" FT BINDING 460 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:24373768" FT BINDING 461 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:24373768" FT BINDING 462 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:24373768" FT BINDING 462 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:24373768" FT BINDING 462 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:24373768" FT BINDING 464 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:24373768" FT BINDING 466 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:24373768" FT BINDING 467 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:24373768" FT MOD_RES 691 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 693 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 705 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 736 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 738 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q3TZZ7" FT MOD_RES 739 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 743 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17924679, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 748 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 755 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 758 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 761 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..593 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_023236" FT VAR_SEQ 1..204 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_023238" FT VAR_SEQ 1..97 FT /note="MTANRDAALSSHRHPGCAQRPRTPTFASSSQRRSAFGFDDGNFPGLGERSHA FT PGSRLGARRRAKTARGLRGHRQRGAGAGLSRPGSARAPSPPRPGG -> MTPPSRAEAG FT VRRSRVPSEGRWRGAEPPGISASTQPASAGRAARHCGAMSGARGEGPEAGAGGAGGRAA FT (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_023239" FT VAR_SEQ 550 FT /note="S -> SNPLEFNPDVLKKTAVQRALKS (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_038324" FT VAR_SEQ 594..603 FT /note="NPKRQDLEVE -> MPVLPPCVLQ (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_023240" FT VAR_SEQ 706..731 FT /note="PVIGGSDKPGMEEKAQPPEAGPQGLH -> SQSRSRPPASPRTSRCPSPPRS FT CGKG (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_023241" FT VAR_SEQ 732..921 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_023242" FT VARIANT 210 FT /note="C -> S (in dbSNP:rs13233513)" FT /id="VAR_030725" FT VARIANT 638 FT /note="S -> G (in dbSNP:rs2305473)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_030726" FT MUTAGEN 401 FT /note="D->A: Abolishes calcium binding; when associated FT with A-413." FT /evidence="ECO:0000269|PubMed:24373768" FT MUTAGEN 413 FT /note="D->A: Abolishes calcium binding; when associated FT with A-401." FT /evidence="ECO:0000269|PubMed:24373768" FT MUTAGEN 413 FT /note="D->N: Strongly reduces calcium binding." FT /evidence="ECO:0000269|PubMed:24373768" FT MUTAGEN 466 FT /note="D->A: Impairs binding of the third calcium ion, but FT has no effect on the binding of the other two calcium FT ions." FT /evidence="ECO:0000269|PubMed:24373768" FT MUTAGEN 833..840 FT /note="KRRSGRRK->AAASGAAA: Abolishes location at the cell FT membrane." FT /evidence="ECO:0000269|PubMed:23791178" FT CONFLICT 141 FT /note="L -> V (in Ref. 7; CAH10642)" FT /evidence="ECO:0000305" FT CONFLICT 612 FT /note="S -> P (in Ref. 3; BAC85769)" FT /evidence="ECO:0000305" FT CONFLICT 615 FT /note="N -> S (in Ref. 3; BAC86489)" FT /evidence="ECO:0000305" FT CONFLICT 795 FT /note="R -> Q (in Ref. 3; BAC85769)" FT /evidence="ECO:0000305" FT HELIX 196..219 FT /evidence="ECO:0007829|PDB:4P42" FT HELIX 221..226 FT /evidence="ECO:0007829|PDB:4P42" FT HELIX 230..232 FT /evidence="ECO:0007829|PDB:4P42" FT STRAND 235..241 FT /evidence="ECO:0007829|PDB:4P42" FT STRAND 248..255 FT /evidence="ECO:0007829|PDB:4P42" FT STRAND 264..282 FT /evidence="ECO:0007829|PDB:4P42" FT TURN 283..286 FT /evidence="ECO:0007829|PDB:4P42" FT STRAND 287..304 FT /evidence="ECO:0007829|PDB:4P42" FT STRAND 316..323 FT /evidence="ECO:0007829|PDB:4P42" FT STRAND 326..333 FT /evidence="ECO:0007829|PDB:4P42" FT HELIX 334..337 FT /evidence="ECO:0007829|PDB:4P42" FT TURN 341..345 FT /evidence="ECO:0007829|PDB:4P42" FT HELIX 348..358 FT /evidence="ECO:0007829|PDB:4P42" FT STRAND 365..370 FT /evidence="ECO:0007829|PDB:4P42" FT HELIX 372..379 FT /evidence="ECO:0007829|PDB:4P42" FT STRAND 384..396 FT /evidence="ECO:0007829|PDB:4NPJ" FT TURN 405..407 FT /evidence="ECO:0007829|PDB:4P42" FT STRAND 414..420 FT /evidence="ECO:0007829|PDB:4NPJ" FT STRAND 423..426 FT /evidence="ECO:0007829|PDB:4NPJ" FT STRAND 437..446 FT /evidence="ECO:0007829|PDB:4NPJ" FT STRAND 453..460 FT /evidence="ECO:0007829|PDB:4NPJ" FT STRAND 463..465 FT /evidence="ECO:0007829|PDB:4NPJ" FT STRAND 467..475 FT /evidence="ECO:0007829|PDB:4NPJ" FT HELIX 476..482 FT /evidence="ECO:0007829|PDB:4NPJ" FT STRAND 483..490 FT /evidence="ECO:0007829|PDB:4NPJ" FT STRAND 494..496 FT /evidence="ECO:0007829|PDB:4NPJ" FT STRAND 498..512 FT /evidence="ECO:0007829|PDB:4NPJ" FT HELIX 515..524 FT /evidence="ECO:0007829|PDB:4NPJ" FT STRAND 535..547 FT /evidence="ECO:0007829|PDB:4NPJ" FT STRAND 552..554 FT /evidence="ECO:0007829|PDB:4P42" FT STRAND 560..566 FT /evidence="ECO:0007829|PDB:4NPJ" FT STRAND 569..572 FT /evidence="ECO:0007829|PDB:4NPJ" FT STRAND 583..593 FT /evidence="ECO:0007829|PDB:4NPJ" FT TURN 595..597 FT /evidence="ECO:0007829|PDB:4NPJ" FT STRAND 599..606 FT /evidence="ECO:0007829|PDB:4NPJ" FT TURN 607..609 FT /evidence="ECO:0007829|PDB:4NPJ" FT STRAND 612..619 FT /evidence="ECO:0007829|PDB:4NPJ" FT HELIX 621..624 FT /evidence="ECO:0007829|PDB:4NPJ" FT HELIX 627..629 FT /evidence="ECO:0007829|PDB:4NPJ" FT STRAND 630..636 FT /evidence="ECO:0007829|PDB:4NPJ" FT STRAND 638..640 FT /evidence="ECO:0007829|PDB:4NPJ" FT STRAND 645..656 FT /evidence="ECO:0007829|PDB:4NPJ" FT STRAND 789..797 FT /evidence="ECO:0007829|PDB:2DMG" FT TURN 798..801 FT /evidence="ECO:0007829|PDB:2DMG" FT STRAND 802..811 FT /evidence="ECO:0007829|PDB:2DMG" FT STRAND 823..831 FT /evidence="ECO:0007829|PDB:2DMG" FT STRAND 835..837 FT /evidence="ECO:0007829|PDB:2DMG" FT STRAND 851..858 FT /evidence="ECO:0007829|PDB:2DMG" FT HELIX 862..867 FT /evidence="ECO:0007829|PDB:2DMG" FT STRAND 869..876 FT /evidence="ECO:0007829|PDB:2DMG" FT STRAND 889..894 FT /evidence="ECO:0007829|PDB:2DMG" FT TURN 899..902 FT /evidence="ECO:0007829|PDB:2DMG" SQ SEQUENCE 921 AA; 102357 MW; D57F1BD9BB0A0C8A CRC64; MTANRDAALS SHRHPGCAQR PRTPTFASSS QRRSAFGFDD GNFPGLGERS HAPGSRLGAR RRAKTARGLR GHRQRGAGAG LSRPGSARAP SPPRPGGPEN PGGVLSVELP GLLAQLARSF ALLLPVYALG YLGLSFSWVL LALALLAWCR RSRGLKALRL CRALALLEDE ERVVRLGVRA CDLPAWVHFP DTERAEWLNK TVKHMWPFIC QFIEKLFRET IEPAVRGANT HLSTFSFTKV DVGQQPLRIN GVKVYTENVD KRQIILDLQI SFVGNCEIDL EIKRYFCRAG VKSIQIHGTM RVILEPLIGD MPLVGALSIF FLRKPLLEIN WTGLTNLLDV PGLNGLSDTI ILDIISNYLV LPNRITVPLV SEVQIAQLRF PVPKGVLRIH FIEAQDLQGK DTYLKGLVKG KSDPYGIIRV GNQIFQSRVI KENLSPKWNE VYEALVYEHP GQELEIELFD EDPDKDDFLG SLMIDLIEVE KERLLDEWFT LDEVPKGKLH LRLEWLTLMP NASNLDKVLT DIKADKDQAN DGLSSALLIL YLDSARNLPS GKKISSNPNP VVQMSVGHKA QESKIRYKTN EPVWEENFTF FIHNPKRQDL EVEVRDEQHQ CSLGNLKVPL SQLLTSEDMT VSQRFQLSNS GPNSTIKMKI ALRVLHLEKR ERPPDHQHSA QVKRPSVSKE GRKTSIKSHM SGSPGPGGSN TAPSTPVIGG SDKPGMEEKA QPPEAGPQGL HDLGRSSSSL LASPGHISVK EPTPSIASDI SLPIATQELR QRLRQLENGT TLGQSPLGQI QLTIRHSSQR NKLIVVVHAC RNLIAFSEDG SDPYVRMYLL PDKRRSGRRK THVSKKTLNP VFDQSFDFSV SLPEVQRRTL DVAVKNSGGF LSKDKGLLGK VLVALASEEL AKGWTQWYDL TEDGTRPQAM T //