ESYT1_HUMAN » Extended synaptotagmin-1

ESYT1_HUMAN » Extended synaptotagmin-1
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Topology in Endoplasmic reticulum membrane
Topologylumenal side
cytoplasmic side
ESYT1_HUMAN » Extended synaptotagmin-1 » E-Syt1; Membrane-bound C2 domain-containing protein;
Hydrophobic Thickness 31.4 ± 3.9 Å
Tilt Angle 3 ± 4°
ΔGtransfer -16.1 kcal/mol
ΔGfold -13.1 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, HMDB
Topology Out
TM Segments 72-93 (68-95)
Pathways none
PDB none
OPM none
Complexes none
Interactions

CD3Z, Complex: CD3Z:ESYT1, PubMed

EDEM1, Complex: ESYT1:EDEM1

ESR1, Complex: ESYT1:ESR1, PubMed

ESYT2, Complex: ESYT2:ESYT1, PubMed

ESYT3, Complex: ESYT3:ESYT1, PubMed

ITA4, Complex: ITA4:ESYT1, PubMed

SYJ2B, Complex: SYJ2B:ESYT1

VCAM1, Complex: VCAM1:ESYT1, PubMed

Domains

AA: 135-313, PDBID: 4P42, Subunit B, Seq Identity:63%, Synaptotagmin-like mitochondrial-lipid-binding domain

AA: 329-435, PDBID: 4NPJ, Subunit A, Seq Identity:55%, C2 domain

AA: 478-578, PDBID: 4NPJ, Subunit A, Seq Identity:38%, C2 domain

AA: 647-753, PDBID: 4NPJ, Subunit A, Seq Identity:56%, C2 domain

AA: 798-897, PDBID: 4NPJ, Subunit A, Seq Identity:30%, C2 domain

AA: 986-1095, PDBID: 2DMG, Subunit A, Seq Identity:42%, C2 domain

UniProt annotation for ESYT1_HUMAN » Extended synaptotagmin-1
FUNCTION: Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport (By similarity). Binds calcium (via the C2 domains) and translocates to sites of contact between the endoplasmic reticulum and the cell membrane in response to increased cytosolic calcium levels. Helps tether the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane.

SUBUNIT: Interacts (phosphorylated form) with SLC2A4 (By similarity). Interacts with ESYT2 and ESYT3.

TISSUE SPECIFICITY: Widely expressed.

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 translocation to the cell membrane in response to increased cytosolic calcium levels (PubMed and PubMed).

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

UniProt features for ESYT1_HUMAN » Extended synaptotagmin-1
CHAIN 1 1104 Extended synaptotagmin-1.
DOMAIN 316 417 C2 1.
DOMAIN 465 558 C2 2.
DOMAIN 634 735 C2 3.
DOMAIN 785 877 C2 4.
DOMAIN 972 1077 C2 5.
COILED 91 116 Potential.
Amino Acid Sequence for ESYT1_HUMAN » Extended synaptotagmin-1
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