ID A0A287BCJ5_PIG Unreviewed; 853 AA.
AC A0A287BCJ5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 3.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Extended synaptotagmin 2 {ECO:0000313|Ensembl:ENSSSCP00000054054.3};
GN Name=ESYT2 {ECO:0000313|Ensembl:ENSSSCP00000054054.3,
GN ECO:0000313|VGNC:VGNC:87797};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000054054.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000054054.3, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000054054.3,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000054054.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the extended synaptotagmin family.
CC {ECO:0000256|ARBA:ARBA00005867}.
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DR AlphaFoldDB; A0A287BCJ5; -.
DR STRING; 9823.ENSSSCP00000054054; -.
DR Ensembl; ENSSSCT00000063329.3; ENSSSCP00000054054.3; ENSSSCG00000016406.5.
DR VGNC; VGNC:87797; ESYT2.
DR GeneTree; ENSGT00940000156086; -.
DR InParanoid; A0A287BCJ5; -.
DR Reactome; R-SSC-9840309; Glycosphingolipid biosynthesis.
DR Proteomes; UP000008227; Chromosome 18.
DR Bgee; ENSSSCG00000016406; Expressed in heart and 44 other cell types or tissues.
DR ExpressionAtlas; A0A287BCJ5; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma 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; C2 domain; 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 PANTHER; PTHR45761:SF2; EXTENDED SYNAPTOTAGMIN-2; 1.
DR PANTHER; PTHR45761; EXTENDED SYNAPTOTAGMIN-LIKE PROTEIN 2, ISOFORM C; 1.
DR Pfam; PF00168; C2; 3.
DR Pfam; PF17047; SMP_LBD; 1.
DR SMART; SM00239; C2; 3.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 3.
DR PROSITE; PS50004; C2; 3.
DR PROSITE; PS51847; SMP; 1.
PE 1: Evidence at protein level;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A287BCJ5};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 46..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 97..277
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 276..396
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 421..567
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 718..840
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 585..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 853 AA; 94595 MW; 12977792B3342300 CRC64;
MSGPRAPGPE AGAAGAEPPG AALSVDVTGL LAQLARSFAL LLPVYALGYL GLSFSWVLLA
LGLLVWCRRS RGLKATRLCR ALALLEDEER AVRLGVRACD LPAWVHFPDT ERAEWLNKFI
EKLFRETIEP AVRGAHPHLS TFSFTRVDVG QQPLRINGVK VYTENVDKRQ IILDLQISFV
GNCEIDLEIK RYFCRAGVQS IQIHGTMRVI LEPLIGDMPL VGALSIFFLR KPLLEINWTG
LTNLLDIPGL NGLSDTIILD IISNYLVLPN RVTVPLVSEV QIAQLRFPVP KGVLRIHFIE
AQDLQGKDTY LKGLVKGKSD PYGVLRVGNQ IFQSKVIKES LSPKWNEVYE ALVYEHPGQE
LEIELFDEDP DKDDFLGSLM IDLIEVEKER LLDEWFALDE VPKGKLHLKL EWLTLVPNAV
NLEKVLTDIR ADKDQATDGL SSSLLILYLD SARNLPSNPL EFNADVLKKA AIQKALKSGK
KMNSNPSPLV QMSVGHKAQE SKIRYKTNEP VWEENFTFFI HNPKRQELEV EVRDEQHQCS
LGNLRIPLSQ LLASEDMTMN QRFQLSNSGP NSSLKMKLAL RVLHLEKQER SPDHQHSAQV
KRPSVSKEGR KIPVRPQMSA SPGTGDSSTA PSSPVVGGGD KPGVEERAPP AEASPQGPQD
LGRSSSSLQA SGTGSPSHIS VKEPTPSIAS DISLPIATQE LRQRLRQLEN GTTLGQSPLG
QIQLTIRHSS QRNKLVVVVH SCRNLIAFSE DGSDPYVRLY LLPDKRRSGR RKTHVSKKTL
NPVFDQSFDF SVSLPEAQRR TLDVAVKNSG GFLSKDKGLL GKVLVGLASE ELAKGWTQWY
DLTEDGTRPH VVT
//
