ID ESYT1_HUMAN Reviewed; 1104 AA. AC Q9BSJ8; A0FGR7; A8K2S2; O94848; Q6PJN4; Q9H6J1; Q9H6W2; Q9Y416; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 29-OCT-2014, entry version 115. DE RecName: Full=Extended synaptotagmin-1; DE Short=E-Syt1; DE AltName: Full=Membrane-bound C2 domain-containing protein; GN Name=ESYT1; Synonyms=FAM62A, KIAA0747, MBC2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND RP 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 1). RC TISSUE=Hepatoma, Kidney, and Tongue; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Kidney; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-1104 (ISOFORM 2). RC TISSUE=Brain; RX PubMed=9872452; DOI=10.1093/dnares/5.5.277; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., RA Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XI. RT The complete sequences of 100 new cDNA clones from brain which code RT for large proteins in vitro."; RL DNA Res. 5:277-286(1998). RN [6] RP PROTEIN SEQUENCE OF 308-323; 446-457 AND 551-586, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma, and Platelet; RA Bienvenut W.V., Claeys D.; RL Submitted (NOV-2005) to UniProtKB. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 379-1104 (ISOFORM 1). RC TISSUE=Uterus; 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., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer RT cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-963 AND SER-1034, AND RP 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 [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [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 [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-817, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820 AND SER-963, 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] 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., RA Buerckstuemmer T., 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 [15] RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, LIPID-BINDING, MUTAGENESIS RP OF ASP-663; ASP-675 AND 722-ASP--ASP-729, AND INTERACTION WITH ESYT2 RP AND ESYT3. RX PubMed=23791178; DOI=10.1016/j.cell.2013.05.026; RA Giordano F., Saheki Y., Idevall-Hagren O., Colombo S.F., RA Pirruccello M., Milosevic I., Gracheva E.O., Bagriantsev S.N., RA Borgese N., De Camilli P.; RT "PI(4,5)P(2)-dependent and Ca(2+)-regulated ER-PM interactions RT mediated by the extended synaptotagmins."; RL Cell 153:1494-1509(2013). RN [16] RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-406 AND RP ASP-724. RX PubMed=24183667; DOI=10.1016/j.celrep.2013.09.038; RA Chang C.L., Hsieh T.S., Yang T.T., Rothberg K.G., Azizoglu D.B., RA Volk E., Liao J.C., Liou J.; RT "Feedback regulation of receptor-induced Ca2+ signaling mediated by E- RT Syt1 and Nir2 at endoplasmic reticulum-plasma membrane junctions."; RL Cell Rep. 5:813-825(2013). CC -!- FUNCTION: Binds glycerophospholipids in a barrel-like domain and CC may play a role in cellular lipid transport (By similarity). Binds CC calcium (via the C2 domains) and translocates to sites of contact CC between the endoplasmic reticulum and the cell membrane in CC response to increased cytosolic calcium levels. Helps tether the CC endoplasmic reticulum to the cell membrane and promotes the CC formation of appositions between the endoplasmic reticulum and the CC cell membrane. {ECO:0000250, ECO:0000269|PubMed:23791178, CC ECO:0000269|PubMed:24183667}. CC -!- SUBUNIT: Interacts (phosphorylated form) with SLC2A4 (By CC similarity). Interacts with ESYT2 and ESYT3. {ECO:0000250, CC ECO:0000269|PubMed:23791178}. CC -!- INTERACTION: CC A0FGR8:ESYT2; NbExp=4; IntAct=EBI-355956, EBI-3184170; CC A0FGR9:ESYT3; NbExp=3; IntAct=EBI-355956, EBI-8771391; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein. Cell membrane; Peripheral membrane protein. CC Note=Localizes primarily to the endoplasmic reticulum. Recruited CC to sites of contact between the endoplasmic reticulum and the cell CC membrane in response to increased cytosolic calcium levels. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9BSJ8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BSJ8-2; Sequence=VSP_018277; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Widely expressed. 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 CC are 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 CC calcium-dependent lipid binding and interaction with membranes. CC Two calcium ions are bound at a high-affinity site and a third CC calcium ion is bound with lower affinity. May bind up to four CC calcium ions. In contrast, the second C2 domain apparently does CC not bind calcium (By similarity). The third C2 domain mediates CC interaction with membranes enriched in phosphatidylinositol 4,5- CC bisphosphate and is required for translocation to the cell CC membrane in response to increased cytosolic calcium levels CC (PubMed:24183667 and PubMed:23791178). {ECO:0000250}. CC -!- DOMAIN: Contains a barrel-like domain that can bind various types CC of glycerophospholipids in its interior. {ECO:0000250}. CC -!- PTM: Phosphorylated on Ser residues in insulin-treated adipocytes CC (in vitro); this promotes interaction with SLC2A4. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the extended synaptotagmin family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 5 C2 domains. {ECO:0000255|PROSITE- CC ProRule:PRU00041}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB15139.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAB15268.1; Type=Erroneous initiation; 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; DQ993200; ABJ97705.1; -; mRNA. DR EMBL; AK025463; BAB15139.1; ALT_INIT; mRNA. DR EMBL; AK025878; BAB15268.1; ALT_INIT; mRNA. DR EMBL; AK290337; BAF83026.1; -; mRNA. DR EMBL; CH471054; EAW96891.1; -; Genomic_DNA. DR EMBL; BC004998; AAH04998.1; -; mRNA. DR EMBL; AB018290; BAA34467.1; -; mRNA. DR EMBL; AL050134; CAB43284.1; -; mRNA. DR CCDS; CCDS53801.1; -. [Q9BSJ8-2] DR CCDS; CCDS8904.1; -. [Q9BSJ8-1] DR PIR; T08769; T08769. DR PIR; T13156; T13156. DR RefSeq; NP_001171725.1; NM_001184796.1. [Q9BSJ8-2] DR RefSeq; NP_056107.1; NM_015292.2. [Q9BSJ8-1] DR UniGene; Hs.632729; -. DR ProteinModelPortal; Q9BSJ8; -. DR SMR; Q9BSJ8; 135-599, 646-1103. DR BioGrid; 116927; 16. DR IntAct; Q9BSJ8; 8. DR MINT; MINT-1144538; -. DR STRING; 9606.ENSP00000267113; -. DR PhosphoSite; Q9BSJ8; -. DR DMDM; 74733019; -. DR OGP; Q9Y416; -. DR MaxQB; Q9BSJ8; -. DR PaxDb; Q9BSJ8; -. DR PRIDE; Q9BSJ8; -. DR DNASU; 23344; -. DR Ensembl; ENST00000267113; ENSP00000267113; ENSG00000139641. [Q9BSJ8-2] DR Ensembl; ENST00000394048; ENSP00000377612; ENSG00000139641. [Q9BSJ8-1] DR GeneID; 23344; -. DR KEGG; hsa:23344; -. DR UCSC; uc001sjq.3; human. [Q9BSJ8-1] DR UCSC; uc001sjr.3; human. [Q9BSJ8-2] DR CTD; 23344; -. DR GeneCards; GC12P056548; -. DR HGNC; HGNC:29534; ESYT1. DR HPA; HPA016858; -. DR neXtProt; NX_Q9BSJ8; -. DR PharmGKB; PA165512688; -. DR eggNOG; COG5038; -. DR GeneTree; ENSGT00550000074417; -. DR HOVERGEN; HBG055795; -. DR InParanoid; Q9BSJ8; -. DR OMA; SQHSGVE; -. DR OrthoDB; EOG7RNJZK; -. DR PhylomeDB; Q9BSJ8; -. DR TreeFam; TF324255; -. DR ChiTaRS; ESYT1; human. DR GeneWiki; FAM62A; -. DR GenomeRNAi; 23344; -. DR NextBio; 45301; -. DR PRO; PR:Q9BSJ8; -. DR Bgee; Q9BSJ8; -. DR CleanEx; HS_FAM62A; -. DR ExpressionAtlas; Q9BSJ8; baseline and differential. DR Genevestigator; Q9BSJ8; -. DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.150; -; 5. DR InterPro; IPR000008; C2_dom. DR Pfam; PF00168; C2; 5. DR PRINTS; PR00360; C2DOMAIN. DR SMART; SM00239; C2; 5. DR SUPFAM; SSF49562; SSF49562; 5. DR PROSITE; PS50004; C2; 5. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Calcium; Cell membrane; KW Coiled coil; Complete proteome; Direct protein sequencing; KW Endoplasmic reticulum; Lipid transport; Lipid-binding; Membrane; KW Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; KW Repeat; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 1104 Extended synaptotagmin-1. FT /FTId=PRO_0000234344. FT TOPO_DOM 1 38 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 39 59 Helical. {ECO:0000255}. FT TOPO_DOM 60 62 Lumenal. {ECO:0000255}. FT TRANSMEM 63 83 Helical. {ECO:0000255}. FT TOPO_DOM 84 1104 Cytoplasmic. {ECO:0000255}. FT DOMAIN 316 417 C2 1. {ECO:0000255|PROSITE- FT ProRule:PRU00041}. FT DOMAIN 465 558 C2 2. {ECO:0000255|PROSITE- FT ProRule:PRU00041}. FT DOMAIN 634 735 C2 3. {ECO:0000255|PROSITE- FT ProRule:PRU00041}. FT DOMAIN 785 877 C2 4. {ECO:0000255|PROSITE- FT ProRule:PRU00041}. FT DOMAIN 972 1077 C2 5. {ECO:0000255|PROSITE- FT ProRule:PRU00041}. FT REGION 139 313 Glycerophospholipid-binding barrel-like FT domain. {ECO:0000250}. FT REGION 1018 1025 Required for phosphatidylinositol 4,5- FT bisphosphate-dependent location at the FT cell membrane. {ECO:0000250}. FT COILED 91 116 {ECO:0000255}. FT COMPBIAS 924 935 Poly-Ser. FT COMPBIAS 1012 1015 Poly-Leu. FT METAL 344 344 Calcium 1; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 345 345 Calcium 1. {ECO:0000250}. FT METAL 345 345 Calcium 2. {ECO:0000250}. FT METAL 357 357 Calcium 2. {ECO:0000250}. FT METAL 404 404 Calcium 1. {ECO:0000250}. FT METAL 404 404 Calcium 2. {ECO:0000250}. FT METAL 406 406 Calcium 1. {ECO:0000250}. FT METAL 406 406 Calcium 2. {ECO:0000250}. FT METAL 406 406 Calcium 3; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 408 408 Calcium 3; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 410 410 Calcium 3. {ECO:0000250}. FT METAL 411 411 Calcium 1. {ECO:0000250}. FT MOD_RES 1 1 N-acetylmethionine. FT {ECO:0000269|PubMed:19413330}. FT MOD_RES 324 324 Phosphoserine; by CDK5. {ECO:0000250}. FT MOD_RES 817 817 N6-acetyllysine. FT {ECO:0000269|PubMed:19608861}. FT MOD_RES 820 820 Phosphoserine. FT {ECO:0000269|PubMed:20068231}. FT MOD_RES 963 963 Phosphoserine. FT {ECO:0000269|PubMed:18669648, FT ECO:0000269|PubMed:20068231}. FT MOD_RES 1034 1034 Phosphoserine. FT {ECO:0000269|PubMed:18669648}. FT VAR_SEQ 491 491 P -> PMVTSELYPPQ (in isoform 2). FT {ECO:0000303|PubMed:9872452}. FT /FTId=VSP_018277. FT VARIANT 764 764 R -> C (in dbSNP:rs35075600). FT /FTId=VAR_038190. FT MUTAGEN 406 406 D->A: No effect on translocation to sites FT of contact between the endoplasmic FT reticulum and the cell membrane. FT {ECO:0000269|PubMed:24183667}. FT MUTAGEN 663 663 D->A: Abolishes location at the cell FT membrane; when associated with A-675 and FT 722-A--A-729. FT {ECO:0000269|PubMed:23791178}. FT MUTAGEN 675 675 D->A: Abolishes location at the cell FT membrane; when associated with A-675 and FT 722-A--A-729. FT {ECO:0000269|PubMed:23791178}. FT MUTAGEN 722 729 DKDLDKDD->AKALAKAA: Abolishes location at FT the cell membrane; when associated with FT A-663 and A-675. FT {ECO:0000269|PubMed:23791178}. FT MUTAGEN 724 724 D->A: Loss of translocation to sites of FT contact between the endoplasmic reticulum FT and the cell membrane. FT {ECO:0000269|PubMed:24183667}. FT CONFLICT 133 133 F -> L (in Ref. 2; BAF83026). FT {ECO:0000305}. FT CONFLICT 489 489 D -> N (in Ref. 2; BAB15139). FT {ECO:0000305}. FT CONFLICT 738 738 L -> F (in Ref. 2; BAB15139). FT {ECO:0000305}. FT CONFLICT 785 785 S -> R (in Ref. 2; BAF83026). FT {ECO:0000305}. FT CONFLICT 998 998 L -> P (in Ref. 2; BAB15139). FT {ECO:0000305}. SQ SEQUENCE 1104 AA; 122856 MW; E72B20C458B96F19 CRC64; MERSPGEGPS PSPMDQPSAP SDPTDQPPAA HAKPDPGSGG QPAGPGAAGE ALAVLTSFGR RLLVLIPVYL AGAVGLSVGF VLFGLALYLG WRRVRDEKER SLRAARQLLD DEEQLTAKTL YMSHRELPAW VSFPDVEKAE WLNKIVAQVW PFLGQYMEKL LAETVAPAVR GSNPHLQTFT FTRVELGEKP LRIIGVKVHP GQRKEQILLD LNISYVGDVQ IDVEVKKYFC KAGVKGMQLH GVLRVILEPL IGDLPFVGAV SMFFIRRPTL DINWTGMTNL LDIPGLSSLS DTMIMDSIAA FLVLPNRLLV PLVPDLQDVA QLRSPLPRGI IRIHLLAARG LSSKDKYVKG LIEGKSDPYA LVRLGTQTFC SRVIDEELNP QWGETYEVMV HEVPGQEIEV EVFDKDPDKD DFLGRMKLDV GKVLQASVLD DWFPLQGGQG QVHLRLEWLS LLSDAEKLEQ VLQWNWGVSS RPDPPSAAIL VVYLDRAQDL PLKKGNKEPN PMVQLSIQDV TQESKAVYST NCPVWEEAFR FFLQDPQSQE LDVQVKDDSR ALTLGALTLP LARLLTAPEL ILDQWFQLSS SGPNSRLYMK LVMRILYLDS SEICFPTVPG CPGAWDVDSE NPQRGSSVDA PPRPCHTTPD SQFGTEHVLR IHVLEAQDLI AKDRFLGGLV KGKSDPYVKL KLAGRSFRSH VVREDLNPRW NEVFEVIVTS VPGQELEVEV FDKDLDKDDF LGRCKVRLTT VLNSGFLDEW LTLEDVPSGR LHLRLERLTP RPTAAELEEV LQVNSLIQTQ KSAELAAALL SIYMERAEDL PLRKGTKHLS PYATLTVGDS SHKTKTISQT SAPVWDESAS FLIRKPHTES LELQVRGEGT GVLGSLSLPL SELLVADQLC LDRWFTLSSG QGQVLLRAQL GILVSQHSGV EAHSHSYSHS SSSLSEEPEL SGGPPHITSS APELRQRLTH VDSPLEAPAG PLGQVKLTLW YYSEERKLVS IVHGCRSLRQ NGRDPPDPYV SLLLLPDKNR GTKRRTSQKK RTLSPEFNER FEWELPLDEA QRRKLDVSVK SNSSFMSRER ELLGKVQLDL AETDLSQGVA RWYDLMDNKD KGSS //