ESYT2_HUMAN » Extended synaptotagmin-2

ESYT2_HUMAN » Extended synaptotagmin-2
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Topology in Endoplasmic reticulum membrane
Topologylumenal side
cytoplasmic side
ESYT2_HUMAN » Extended synaptotagmin-2 » E-Syt2; Chr2Syt;
Hydrophobic Thickness 24.8 ± 4.2 Å
Tilt Angle 4 ± 2°
ΔGtransfer -36.4 kcal/mol
ΔGfold -14.6 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, HMDB
Topology Out
TM Segments 129-149 (126-153)
Pathways none
PDB 4npk (363-660), 2dmg (785-913), 4p42 (A/B=191-662), 4npj (A/B=363-660)
OPM 2dmg, 4npk, 4p42
Complexes

ESYT2:ESYT2_HUMAN

Interactions

ESYT1, Complex: ESYT2:ESYT1, PubMed

ESYT2, Complex: Homodimer of extended synaptotagmin-2, PDBID: 4P42

ESYT3, Complex: ESYT2:ESYT3, PubMed

Domains

AA: 191-370, PDBID: 4P42, Subunit B, Seq Identity:100%, Synaptotagmin-like mitochondrial-lipid-binding domain

AA: 385-491, PDBID: 4NPJ, Subunit A, Seq Identity:100%, C2 domain

AA: 536-635, PDBID: 4NPJ, Subunit A, Seq Identity:100%, C2 domain

AA: 801-910, PDBID: 2DMG, Subunit A, Seq Identity:100%, C2 domain

UniProt annotation for ESYT2_HUMAN » Extended synaptotagmin-2
FUNCTION: Tethers the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane. Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport. Plays a role in FGF signaling via its role in the rapid internalization of FGFR1 that has been activated by FGF1 binding; this occurs most likely via the AP-2 complex.

SUBUNIT: Homodimer. Interacts with ESYT1 and ESYT3. Interacts with FGFR1 that has been activated by FGF1 binding. Interacts with the AP-2 complex; identified in a complex with the AP-2 complex and FGFR1.

TISSUE SPECIFICITY: Widely expressed with high level in cerebellum.

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 (PubMed). 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 binds glycerophospholipids in its interior; can bind two lipid molecules simultaneously. Binds a variety of lipids, including phosphatidylethanolamine, phosphatidylcholine and phosphatidylinositol (PubMed).

UniProt features for ESYT2_HUMAN » Extended synaptotagmin-2
CHAIN 1 921 Extended synaptotagmin-2.
DOMAIN 372 473 C2 1.
DOMAIN 523 617 C2 2.
DOMAIN 788 892 C2 3.
Amino Acid Sequence for ESYT2_HUMAN » Extended synaptotagmin-2
MTANRDAALS SHRHPGCAQR PRTPTFASSS QRRSAFGFDD GNFPGLGERS HAPGSRLGAR RRAKTARGLR GHRQRGAGAG LSRPGSARAP SPPRPGGPEN PGGVLSVELP GLLAQLARSF ALLLPVYALG YLGLSFSWVL LALALLAWCR RSRGLKALRL CRALALLEDE ERVVRLGVRA CDLPAWVHFP DTERAEWLNK TVKHMWPFIC QFIEKLFRET IEPAVRGANT HLSTFSFTKV DVGQQPLRIN GVKVYTENVD KRQIILDLQI SFVGNCEIDL EIKRYFCRAG VKSIQIHGTM RVILEPLIGD MPLVGALSIF FLRKPLLEIN WTGLTNLLDV PGLNGLSDTI ILDIISNYLV LPNRITVPLV SEVQIAQLRF PVPKGVLRIH FIEAQDLQGK DTYLKGLVKG KSDPYGIIRV GNQIFQSRVI KENLSPKWNE VYEALVYEHP GQELEIELFD EDPDKDDFLG SLMIDLIEVE KERLLDEWFT LDEVPKGKLH LRLEWLTLMP NASNLDKVLT DIKADKDQAN DGLSSALLIL YLDSARNLPS GKKISSNPNP VVQMSVGHKA QESKIRYKTN EPVWEENFTF FIHNPKRQDL EVEVRDEQHQ CSLGNLKVPL SQLLTSEDMT VSQRFQLSNS GPNSTIKMKI ALRVLHLEKR ERPPDHQHSA QVKRPSVSKE GRKTSIKSHM SGSPGPGGSN TAPSTPVIGG SDKPGMEEKA QPPEAGPQGL HDLGRSSSSL LASPGHISVK EPTPSIASDI SLPIATQELR QRLRQLENGT TLGQSPLGQI QLTIRHSSQR NKLIVVVHAC RNLIAFSEDG SDPYVRMYLL PDKRRSGRRK THVSKKTLNP VFDQSFDFSV SLPEVQRRTL DVAVKNSGGF LSKDKGLLGK VLVALASEEL AKGWTQWYDL TEDGTRPQAM T