ESYT3_HUMAN » Extended synaptotagmin-3

ESYT3_HUMAN » Extended synaptotagmin-3
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Topology in Endoplasmic reticulum membrane
Topologylumenal side
cytoplasmic side
ESYT3_HUMAN » Extended synaptotagmin-3 » E-Syt3; Chr3Syt;
Hydrophobic Thickness 29.6 ± 3.0 Å
Tilt Angle 0 ± 0°
ΔGtransfer -37.3 kcal/mol
ΔGfold -16.9 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, HMDB
Topology Out
TM Segments 54-73 (48-77)
Pathways none
PDB none
OPM none
Complexes none
Interactions

ESYT1, Complex: ESYT3:ESYT1, PubMed

ESYT2, Complex: ESYT2:ESYT3, PubMed

Domains

AA: 114-291, PDBID: 4P42, Subunit B, Seq Identity:51%, Synaptotagmin-like mitochondrial-lipid-binding domain

AA: 306-410, PDBID: 4NPJ, Subunit A, Seq Identity:53%, C2 domain

AA: 445-564, PDBID: 4NPJ, Subunit A, Seq Identity:31%, C2 domain

AA: 769-878, PDBID: 2DMG, Subunit A, Seq Identity:49%, C2 domain

UniProt annotation for ESYT3_HUMAN » Extended synaptotagmin-3
FUNCTION: Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport (By similarity). Tethers the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane.

SUBUNIT: Interacts with ESYT1 and ESYT2.

TISSUE SPECIFICITY: Widely expressed with high level in cerebellum and skin.

DOMAIN: Anchored to the endoplasmic reticulum membrane by a transmembrane hairpin structure; both N-terminus and C-terminus are cytoplasmic.

DOMAIN: The C2 domains mediate lipid and calcium binding. The N- terminal C2 domain binds calcium ions and is important for calcium-dependent lipid binding and interaction with membranes. Two calcium ions are bound at a high-affinity site and a third calcium ion is bound with lower affinity. May bind up to four calcium ions. In contrast, the second C2 domain apparently does not bind calcium (By similarity). The third C2 domain mediates interaction with membranes enriched in phosphatidylinositol 4,5- bisphosphate and is required for location at the cell membrane (PubMed).

DOMAIN: Contains a barrel-like domain that can bind various types of glycerophospholipids in its interior.

UniProt features for ESYT3_HUMAN » Extended synaptotagmin-3
CHAIN 1 886 Extended synaptotagmin-3.
DOMAIN 293 392 C2 1.
DOMAIN 430 544 C2 2.
DOMAIN 756 860 C2 3.
Amino Acid Sequence for ESYT3_HUMAN » Extended synaptotagmin-3
MRAEEPCAPG APSALGAQRT PGPELRLSSQ LLPELCTFVV RVLFYLGPVY LAGYLGLSIT WLLLGALLWM WWRRNRRGKL GRLAAAFEFL DNEREFISRE LRGQHLPAWI HFPDVERVEW ANKIISQTWP YLSMIMESKF REKLEPKIRE KSIHLRTFTF TKLYFGQKCP RVNGVKAHTN TCNRRRVTVD LQICYIGDCE ISVELQKIQA GVNGIQLQGT LRVILEPLLV DKPFVGAVTV FFLQKPHLQI NWTGLTNLLD APGINDVSDS LLEDLIATHL VLPNRVTVPV KKGLDLTNLR FPLPCGVIRV HLLEAEQLAQ KDNFLGLRGK SDPYAKVSIG LQHFRSRTIY RNLNPTWNEV FEFMVYEVPG QDLEVDLYDE DTDRDDFLGS LQICLGDVMT NRVVDEWFVL NDTTSGRLHL RLEWLSLLTD QEVLTEDHGG LSTAILVVFL ESACNLPRNP FDYLNGEYRA KKLSRFARNK VSKDPSSYVK LSVGKKTHTS KTCPHNKDPV WSQVFSFFVH NVATERLHLK VLDDDQECAL GMLEVPLCQI LPYADLTLEQ RFQLDHSGLD SLISMRLVLR FLQVEERELG SPYTGPEALK KGPLLIKKVA TNQGPKAQPQ EEGPTDLPCP PDPASDTKDV SRSTTTTTSA TTVATEPTSQ ETGPEPKGKD SAKRFCEPIG EKKSPATIFL TVPGPHSPGP IKSPRPMKCP ASPFAWPPKR LAPSMSSLNS LASSCFDLAD ISLNIEGGDL RRRQLGEIQL TVRYVCLRRC LSVLINGCRN LTPCTSSGAD PYVRVYLLPE RKWACRKKTS VKRKTLEPLF DETFEFFVPM EEVKKRSLDV AVKNSRPLGS HRRKELGKVL IDLSKEDLIK GFSQWYELTP NGQPRS