ESYT3_XENTR
ID ESYT3_XENTR Reviewed; 889 AA.
AC Q5M7N9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Extended synaptotagmin-3;
DE Short=E-Syt3;
GN Name=esyt3; Synonyms=fam62c;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A0FGR9};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:A0FGR9}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:A0FGR9}; Multi-pass membrane
CC protein {ECO:0000255}. Note=Localizes to endoplasmic reticulum-plasma
CC membrane contact sites (EPCS). Recruited to the cell membrane via the
CC third C2 domain (By similarity). {ECO:0000250|UniProtKB:A0FGR9}.
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 -!- SIMILARITY: Belongs to the extended synaptotagmin family.
CC {ECO:0000305}.
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DR EMBL; BC088530; AAH88530.1; -; mRNA.
DR RefSeq; NP_001011364.1; NM_001011364.1.
DR AlphaFoldDB; Q5M7N9; -.
DR SMR; Q5M7N9; -.
DR PRIDE; Q5M7N9; -.
DR GeneID; 496831; -.
DR KEGG; xtr:496831; -.
DR CTD; 83850; -.
DR Xenbase; XB-GENE-5746165; esyt3.
DR InParanoid; Q5M7N9; -.
DR OrthoDB; 52746at2759; -.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0140268; C:endoplasmic reticulum-plasma membrane contact site; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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: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 Gene3D; 2.60.40.150; -; 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 Pfam; PF00168; C2; 3.
DR Pfam; PF17047; SMP_LBD; 1.
DR SMART; SM00239; C2; 3.
DR SUPFAM; SSF49562; SSF49562; 3.
DR PROSITE; PS50004; C2; 3.
DR PROSITE; PS51847; SMP; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell membrane; Endoplasmic reticulum; Lipid transport;
KW Lipid-binding; Membrane; Metal-binding; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..889
FT /note="Extended synaptotagmin-3"
FT /id="PRO_0000314901"
FT TOPO_DOM 1..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..889
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 155..333
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01194"
FT DOMAIN 331..452
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 468..618
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 757..879
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..811
FT /note="Required for phosphatidylinositol 4,5-bisphosphate-
FT dependent location at the cell membrane"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 363
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 376
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 423
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 423
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 424
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 427
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 429
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 889 AA; 99594 MW; C7A888F1C6E1DA54 CRC64;
MAQGDPGGQT PQAPQGTDKK PDEPKATEKP QGAGPQPRDP PGGEKGLRDP PGGEKGPRDP
GQGGAGEALA EALYGLGRPV LRAVLYLFPV YLCGRFGLSP TWLLFGLFLW MFWTRNKKFK
LARIQAAWDL HENEKLGVTR GLYLQQLPAW VNFPDVERVE WLNKVVGQMW PYIGMYVEKM
FQDKVEPLVR SSSAHLKAFT FTKVHLGEKF PRINGVKSYT KNVDKREVIL DLQLSYNGDV
EINVEVKKMC KAGVKGVQLH GTLRVILAPL LPDLPFVGAV TMFFIQRPHL DINWTGLTNV
LEIPGVSDFS DSMIVDMIAS HLVLPNRFTV PLSSQVQAAQ LRFPLPHGVL RLHLIEAEDL
IPKDNYLKGI IRGKSDPYAV LRIGNQNFKS RTIKENLNPK WGEMYEFVVH EVPGQDLEVD
LYDEDPDKDD FLGSLVIGLE GVMQDRVVDE WFPLSDVPSG SVHLRLEWLS LLPKSEKLSE
AKGGISTAML IVYLDSASAL PRNHFEYSSS EYTTRKQRHM TYTKTDKDPN SYVLMSVGKK
SVKSKTCTGS TEPVWGQAFA FFIQDVHMQH LHLEVKDSER QCALGMLDLP LHRLLGNEEL
TADQRFPLAN SGPNSTIKMK IVLRVLHVEA PEPESIYTGI NSLKQGPVSI KRAQSQQHKS
HGKSHQAHHQ AHQTQQNHTV QQPKAERKES ISTTSQQANT SSSNPAPNQN PNSTGAVPES
HTPSLKPLER IAPSLLSLNS IGSSVFDPND KRWPSEMTGE VEVSVRYASL RRCLVVLINS
CRNLIQCSSN GADPYVRIYL LPDRKWSGRK KTSVKRKTLN PQYNERFEFL VSQEEAKKRM
LDVAVKNNRG FGSHERKELG KVLVDLSCDD LVKGFTKWFE LTPTGLPTS
