ID A0A3Q0S8X6_AMPCI Unreviewed; 924 AA.
AC A0A3Q0S8X6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Extended synaptotagmin-like protein 1a {ECO:0000313|Ensembl:ENSACIP00000021249.1};
GN Name=ESYT1 {ECO:0000313|Ensembl:ENSACIP00000021249.1};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000021249.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000021249.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
CC -!- SIMILARITY: Belongs to the extended synaptotagmin family.
CC {ECO:0000256|ARBA:ARBA00005867}.
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DR AlphaFoldDB; A0A3Q0S8X6; -.
DR STRING; 61819.ENSACIP00000021249; -.
DR Ensembl; ENSACIT00000021798.1; ENSACIP00000021249.1; ENSACIG00000016467.1.
DR GeneTree; ENSGT00940000156561; -.
DR OMA; HPGQSKE; -.
DR Proteomes; UP000261340; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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; 2.
DR CDD; cd04050; C2B_Synaptotagmin-like; 1.
DR Gene3D; 2.60.40.150; C2 domain; 5.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
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:SF3; EXTENDED SYNAPTOTAGMIN-1; 1.
DR PANTHER; PTHR45761; EXTENDED SYNAPTOTAGMIN-LIKE PROTEIN 2, ISOFORM C; 1.
DR Pfam; PF00168; C2; 4.
DR Pfam; PF17047; SMP_LBD; 1.
DR SMART; SM00239; C2; 4.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 4.
DR PROSITE; PS50004; C2; 4.
DR PROSITE; PS51847; SMP; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|SAM:Phobius}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00023055}.
FT TRANSMEM 51..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 114..292
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 291..412
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 414..535
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 569..702
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 803..924
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 924 AA; 103780 MW; 0AD1332B76976C27 CRC64;
MPAADAEPGT GKSTEPLAPA SQSQPQGEHA VSVLWSFGKC LGALLPVYLA GYYGFSITVV
LFGLMIYMGW KHSRLEKMMK LKSAMYLLEN EREFTTQTVF RAKRDLPPWV NFPDVEKVEW
VNKILQQAWP FIGQYLEKLL VETIAPAIRT SSIHLQTLSF TKVNIGDKAL KVVGVKAHTE
QDKKQVMLDL YLSYAGDVEI NVEIKKYFCK AGVKGVQLHG KLRVILEPLI GDVPLVGAVT
MFFIRRPKLD INWTGLTNLL DIPGLNAMSD TMIMDAIASH LVLPNRLTIP LVADLHVAQL
RSPLPRGVVR IHLLEAEDLT AKDTVIKGLI DGKSDPYAVL RVGTQIFTSH HVDNNLNPQW
REMYEVIVHE VPGQELEVEV FDKDPDQDDF LGRYFCSHVL LLFLYQVIEK NQNLTSKIAD
PPSAAILAIY LDQAYQLPMR KGNKDPSPLV QISVQDTTKE SKTCYGTANP VWEDAFTFFI
QDPRKRDINI QVKDDDRALS LGSLTVPVTR LLGMPELTMD QWFQLENSGS ASRIYMKIVL
RVGILQSIAA QGGITSDQNS SGLGGLTKPQ LARPQHTTPD PEFATEGVLR IHLVEAQNLI
AKDNFMGGMV KGKSDPYVKI RVAGITFRSH TIKENLNPVW NELYEVILTQ LPGQEIQFEL
FDKDIDQDDF LGRCLLMLKK KKNSNISDVL YLKKNKKIKF WFFFAGLNLT CETSSAHNSL
IRCVLSHSWG QALGSLTLPL KEVLAETDLV LDRWLSLDGA LPESQILLRV TLKVLQTGCL
FSVCCSSFSW SNVIPNTDDN INSAGQVKLT IGYSADENRL FITVHSCRAL VARSKDGADP
YVSFILLPDK KATTKRKTAT KKKDLNPEFN ERFDFDFSLE ESLQRRLDLS VKNSVSFISR
ERELIGKLQL DLDQIDLKTG VTQW
//
