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Database: UniProt
Entry: A0A3Q0J737_DIACI
LinkDB: A0A3Q0J737_DIACI
Original site: A0A3Q0J737_DIACI 
ID   A0A3Q0J737_DIACI        Unreviewed;       974 AA.
AC   A0A3Q0J737;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Regulating synaptic membrane exocytosis protein 1 {ECO:0000313|RefSeq:XP_026682530.1};
GN   Name=LOC103513566 {ECO:0000313|RefSeq:XP_026682530.1};
OS   Diaphorina citri (Asian citrus psyllid).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Psylloidea; Psyllidae;
OC   Diaphorininae; Diaphorina.
OX   NCBI_TaxID=121845 {ECO:0000313|Proteomes:UP000079169, ECO:0000313|RefSeq:XP_026682530.1};
RN   [1] {ECO:0000313|RefSeq:XP_026682530.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_026682530.1; XM_026826729.1.
DR   AlphaFoldDB; A0A3Q0J737; -.
DR   STRING; 121845.A0A3Q0J737; -.
DR   PaxDb; 121845-A0A3Q0J737; -.
DR   KEGG; dci:103513566; -.
DR   OrthoDB; 4502832at2759; -.
DR   Proteomes; UP000079169; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0045202; C:synapse; IEA:UniProt.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0006887; P:exocytosis; IEA:InterPro.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR039032; Rim-like.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR12157:SF24; FIFE, ISOFORM D; 1.
DR   PANTHER; PTHR12157; REGULATING SYNAPTIC MEMBRANE EXOCYTOSIS PROTEIN; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00239; C2; 2.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}; Reference proteome {ECO:0000313|Proteomes:UP000079169};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          88..136
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          502..593
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          649..774
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          829..958
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          59..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          623..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          781..824
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..77
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..218
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..296
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..346
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        792..816
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|RefSeq:XP_026682530.1"
SQ   SEQUENCE   974 AA;  107222 MW;  FA41D7DDD2403879 CRC64;
     NEQVGPGGTT DQGDSGTTLS KLRQTLSSSL NAAQDKVTKL NTASSRQCDI VTSLSETTLQ
     DSSQTTSPLQ STISPPKSDK PAARLGNCRV CLKSFKPDDY SRVCYECHQK VCEDCASYSK
     LDENQDENTW RCSICRRKLQ SRAQPVLSQN STDSLLDVPV LEALQRRHSD VKIGSANSGA
     HPANQGLAPP RSPELRRHSD VSPASLKELE KAVQKVKSEQ RGNLDWNQNN TPSINNNINV
     SHKKSSGSPG STPRVPSPSV EKRNENNWDS RLKPSHLDAD VEGDDHDDSD HKIRRGSKAG
     TTRRRKSRVV QKQHSYDDEI KNNNQAQSVN PQQAPPSHET SLGPSAQFSR RASAYDVFNR
     DSSASIIPPS QTRRSSCRQS TPADTEDISC TEQTSCRPLT LTLSDRPRSS VSCQSVKAPD
     IAAIKAGLHQ QRAGSDAILS NLPRGSVANI ATPRLQTEEQ AAPVTPPVLR QPSVTAGEDI
     KIVIHDVDYE SSFNNRQVSK RRVVLRRDVS DMAHRTRGFG MRVVGGKMGP DGRLFAYIVW
     TVPGGPAEKG GLQQGDKVLE WCGVGLTDRS FEEVCSIMDR TGDVAELLVE HGADLRMCDL
     LDEPMPGTVR KNSGDALGLQ LVDGDGSPAS PTRRKLPKTP EQLAKERQVS GRIQLQVYYN
     DEKNEIVVSV LAADDLAARD ETCGFGTLPQ AYVQLRLLPF TGDMNCIKTD IAEPATNPIW
     NTTVEVANVS GDQLLDKTIE VTLWDSKPDK EQVFLGETTI DLQKALIDDR PVWYRLEDPR
     QLRGGGANKS PRGSIQGDNT RTLTRGNRSL SGNHYEKSSV KLGPGQIQPR GYRLVPGGYI
     ELKIGLILTK GQLEVEVISA RGIPACEPQP DTYVKTYLRD RDNDRWIQKR KTRVVRNTSQ
     PQYKQTLKYN GNDVTDRTLL VMLWERQKGF EHNQGLGGAE IALNTVTNND STLSVGWYPL
     FPIHTLGSDS NDSP
//
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