ESYT1_RAT
ID ESYT1_RAT Reviewed; 1088 AA.
AC Q9Z1X1; Q3T1L3;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Extended synaptotagmin-1;
DE Short=E-Syt1;
DE AltName: Full=Membrane-bound C2 domain-containing protein;
DE AltName: Full=vp115;
GN Name=Esyt1; Synonyms=Fam62a, Mbc2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 TYR-993, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- TISSUE SPECIFICITY: Ubiquitously expressed with a higher expression in
CC spleen and white adipose tissue. {ECO:0000269|PubMed:10350628}.
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}.
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; AF099138; AAD10051.1; -; mRNA.
DR EMBL; BC101857; AAI01858.1; -; mRNA.
DR RefSeq; NP_058945.2; NM_017249.2.
DR AlphaFoldDB; Q9Z1X1; -.
DR SMR; Q9Z1X1; -.
DR BioGRID; 248212; 2.
DR IntAct; Q9Z1X1; 1.
DR STRING; 10116.ENSRNOP00000006119; -.
DR iPTMnet; Q9Z1X1; -.
DR PhosphoSitePlus; Q9Z1X1; -.
DR jPOST; Q9Z1X1; -.
DR PaxDb; Q9Z1X1; -.
DR PRIDE; Q9Z1X1; -.
DR GeneID; 29579; -.
DR KEGG; rno:29579; -.
DR UCSC; RGD:3053; rat.
DR CTD; 23344; -.
DR RGD; 3053; Esyt1.
DR eggNOG; KOG1012; Eukaryota.
DR InParanoid; Q9Z1X1; -.
DR OrthoDB; 52746at2759; -.
DR PhylomeDB; Q9Z1X1; -.
DR TreeFam; TF324255; -.
DR Reactome; R-RNO-1660662; Glycosphingolipid metabolism.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013405; RHOD GTPase cycle.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR Reactome; R-RNO-9035034; RHOF GTPase cycle.
DR PRO; PR:Q9Z1X1; -.
DR Proteomes; UP000002494; Unplaced.
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:RGD.
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; Calcium; Cell membrane; Endoplasmic reticulum;
KW Lipid transport; Lipid-binding; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1088
FT /note="Extended synaptotagmin-1"
FT /id="PRO_0000234347"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..54
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..1088
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 127..305
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01194"
FT DOMAIN 304..425
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 446..572
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 618..740
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 771..888
FT /note="C2 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 955..1077
FT /note="C2 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1009
FT /note="Required for phosphatidylinositol 4,5-bisphosphate-
FT dependent location at the cell membrane"
FT /evidence="ECO:0000250"
FT COMPBIAS 606..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 349
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 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 402
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 403
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 316
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:Q3U7R1"
FT MOD_RES 806
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSJ8"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSJ8"
FT MOD_RES 933
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSJ8"
FT MOD_RES 947
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSJ8"
FT MOD_RES 993
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 373
FT /note="H -> R (in Ref. 2; AAI01858)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1088 AA; 121159 MW; E7E12D9737FFB89D CRC64;
MERSPEEGAG PEPSGQSPAT DSTRERDGGS GVPPAGPGAA SEALAVLTSF GRRLLVLVPV
YLAGAAGLSV GFVLFGLALY LGWRRVRDGK ERSLRAARQL LDDEERITAE TLYMSHRELP
AWVSFPDVEK AEWLNKIVVQ VWPFLGQYME KLLAETVAPA VRGANPHLQT FTFTRVELGE
KPVRIIGVKV HPSQRKDQIL LDLNVSYVGD LQIDVEVKKY FCKAGVKGMQ LHGVLRVILE
PLIGDLPIVG AVSMFFIKRP TLDINWTGMT NLLDIPGLSS LSDTMIMDSI AAFLVLPNRL
LVPLVPDLQD VAQLRSPLPR GIIRIHLLAA RGLSSKDKYV KGLIEGKSDP YALVRVGTQT
FCSRVIDEEL NPHWGETYEV IVHEVPGQEI EVEVFDKDPD KDDFLGRMKL DVGKVLQAGV
LDNWYPLQGG QGQVHLRLEW LSLLPDAEKL DQVLQWNRGI TSRPEPPSAA ILVVYLDRAQ
DLPLKKGNKE PNPMVQLSVQ DVTQESKATY STNCPVWEEA FRFFLQDPRS QELDVQVKDD
SRALTLGALT LPLARLLTAS ELTLDQWFQL SSSGPNSRLY MKLVMRILYL DSSEMRLPTE
PGAQDWDSES PETGSSVDAP PRPYHTTPNS HFGTENVLRI HVLEAQDLIA KDRFLGGLVK
GKSDPYVKLK VAGRSLRTHV VREDLNPRWN EVFEVIVTSI PGQELDIEVF DKDLDKDDFL
GRYKVGLTTV LNSGFLDEWL TLEDVPSGRL HLRLERLSPR PTAAELEEVL QVNSLIQTQK
SSELAAALLS VYLERSEDLP LRKGTKPPSP YAILTVGETS HKTKTVSQTS APIWEESASF
LIRKPHAESL ELQVRGEGTG TLGSISLPLS ELLQEEQLCL DRWFALSGQG QVLMRVQLGI
LVSQHSGVEA HSHSSSSLNE EPEVLGDPTH TASPVLEVRH RLTHGDSPSE ALIGPLGQVK
LTVWYHSDEQ KLISIIHSCR ALRQNGRDLP DPYVSVLLLP DKNRGTKRKT SQKKRTLNPE
FNERFEWDLP LDGTLRRKLD VSVKSNSSFM SRERELLGKV QLDLAEIDLS QGAAQWYDLI
DDRDKGGS
