ESYT1_PONAB
ID ESYT1_PONAB Reviewed; 1104 AA.
AC Q5RAG2; Q5RA33;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Extended synaptotagmin-1;
DE Short=E-Syt1;
GN Name=ESYT1; Synonyms=FAM62A;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Interacts (phosphorylated
CC form) with SLC2A4 (By similarity). {ECO:0000250}.
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 -!- 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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the extended synaptotagmin family.
CC {ECO:0000305}.
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DR EMBL; CR859055; CAH91248.1; -; mRNA.
DR EMBL; CR859189; CAH91377.1; -; mRNA.
DR RefSeq; NP_001125737.1; NM_001132265.1.
DR RefSeq; NP_001128811.1; NM_001135339.1.
DR AlphaFoldDB; Q5RAG2; -.
DR SMR; Q5RAG2; -.
DR STRING; 9601.ENSPPYP00000005290; -.
DR PRIDE; Q5RAG2; -.
DR GeneID; 100172662; -.
DR GeneID; 100189719; -.
DR KEGG; pon:100172662; -.
DR CTD; 23344; -.
DR eggNOG; KOG1012; Eukaryota.
DR InParanoid; Q5RAG2; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Acetylation; Calcium; Cell membrane; Coiled coil; Endoplasmic reticulum;
KW Lipid transport; Lipid-binding; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1104
FT /note="Extended synaptotagmin-1"
FT /id="PRO_0000234346"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..62
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..1104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 135..313
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01194"
FT DOMAIN 312..433
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 460..580
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 627..751
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 777..899
FT /note="C2 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 971..1093
FT /note="C2 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1018..1025
FT /note="Required for phosphatidylinositol 4,5-bisphosphate-
FT dependent location at the cell membrane"
FT /evidence="ECO:0000250"
FT COILED 91..116
FT /evidence="ECO:0000255"
FT COMPBIAS 10..30
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 410
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 411
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 324
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:Q3U7R1"
FT MOD_RES 817
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSJ8"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSJ8"
FT MOD_RES 941
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSJ8"
FT MOD_RES 948
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSJ8"
FT MOD_RES 949
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSJ8"
FT MOD_RES 963
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSJ8"
FT MOD_RES 1009
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1X1"
FT MOD_RES 1034
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSJ8"
FT CONFLICT 179
FT /note="F -> V (in Ref. 1; CAH91377)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="R -> H (in Ref. 1; CAH91377)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="G -> R (in Ref. 1; CAH91248)"
FT /evidence="ECO:0000305"
FT CONFLICT 947
FT /note="V -> I (in Ref. 1; CAH91377)"
FT /evidence="ECO:0000305"
FT CONFLICT 1023
FT /note="K -> E (in Ref. 1; CAH91377)"
FT /evidence="ECO:0000305"
FT CONFLICT 1054
FT /note="K -> R (in Ref. 1; CAH91248)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1104 AA; 122544 MW; 531826E61DC1DB6F CRC64;
MERSPGEGPS PSPTDQPSAP SDPTGQPPAA HAKPDPGSGG QPAGPGAAGE ALAVLTSFGK
RLLVLIPVYL AGAVGLSVGF VLFGLALYLG WRRVRDEKER SLRAARQLLD DEEQLTAKTL
YMSHRELPAW VSFPDVEKAE WLNKIVAQVW PFLGQYMEKL LAETVAPAVR GSNPHLQTFT
FTRVELGEKP LRIIGVKVHP GQRKEQILLD LNISYVGDVQ IDVEVKKYFC KAGVKGMQLH
GVLRVILEPL IGDLPIVGAV SMFFIRRPTL DINWTGMTNL LDIPGLSSLS DTMIMDSIAA
FLVLPNRLLV PLVPDLQDVA QLRSPLPRGI IRIHLLAARG LTSKDKYVKG LIEGKSDPYA
LVRLGTQTFC SRVIDEELNP QWGETYEVMV HEVPGQEIEV EVFDKDPDKD DFLGRMKLDV
GKVLQAGVLD DWFPLQGGQG QVHLRLEWLS LLSDAEKLEQ VLQWNQGVSS RPEPPSAAIL
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 LGRCKVSLTT VLNSGFLDEW LTLEDVPSGR LHLRLERLTP RPTAAELEEV
LQVNSLIQTQ KSAELAAALL SIYMERAEDL PLRKGTKHPS PYATLTVGDT SHKTKTVSQT
SAPVWDESAS FLIRKPHTEN LELQVRGEGT GVLGSLSLPL SELLVADQLC LDRWFTLNSG
QGQVLLRAQL GILVSQHSGV EAHSHSYSHS SSSLSEEPEL SGGPPHVTSS APELRQRLTH
VDSSLEAPAG PLGQVKLTVW YYSEERKLVS IVHGCRALRQ NGRDPPDPYV SLLLLPDKNR
GTKRKTSQKK RTLSPEFNER FEWELPLDEA QRRKLDVSVK SNPSFMSRER ELLGKVQLDL
AETDLSQGVA RWYDLMDDKD KGSS
