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Database: UniProt
Entry: A0A2K6E084_MACNE
LinkDB: A0A2K6E084_MACNE
Original site: A0A2K6E084_MACNE 
ID   A0A2K6E084_MACNE        Unreviewed;       767 AA.
AC   A0A2K6E084;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Pleckstrin and Sec7 domain containing 2 {ECO:0000313|Ensembl:ENSMNEP00000041571.1};
GN   Name=PSD2 {ECO:0000313|Ensembl:ENSMNEP00000041571.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000041571.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000041571.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell projection, ruffle membrane
CC       {ECO:0000256|ARBA:ARBA00004632}.
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DR   AlphaFoldDB; A0A2K6E084; -.
DR   STRING; 9545.ENSMNEP00000041571; -.
DR   Ensembl; ENSMNET00000066070.1; ENSMNEP00000041571.1; ENSMNEG00000043579.1.
DR   GeneTree; ENSGT00940000159674; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000043579; Expressed in temporal lobe and 1 other cell type or tissue.
DR   GO; GO:0032154; C:cleavage furrow; IEA:Ensembl.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR   GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR   CDD; cd13295; PH_EFA6; 1.
DR   CDD; cd00171; Sec7; 1.
DR   Gene3D; 1.10.1000.11; Arf Nucleotide-binding Site Opener,domain 2; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR041681; PH_9.
DR   InterPro; IPR001605; PH_dom-spectrin-type.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR023394; Sec7_C_sf.
DR   InterPro; IPR000904; Sec7_dom.
DR   InterPro; IPR035999; Sec7_dom_sf.
DR   PANTHER; PTHR10663; GUANYL-NUCLEOTIDE EXCHANGE FACTOR; 1.
DR   PANTHER; PTHR10663:SF329; PH AND SEC7 DOMAIN-CONTAINING PROTEIN 2; 1.
DR   Pfam; PF15410; PH_9; 1.
DR   Pfam; PF01369; Sec7; 1.
DR   PRINTS; PR00683; SPECTRINPH.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00222; Sec7; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF48425; Sec7 domain; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50190; SEC7; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233120}.
FT   DOMAIN          289..462
FT                   /note="SEC7"
FT                   /evidence="ECO:0000259|PROSITE:PS50190"
FT   DOMAIN          512..625
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          108..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          184..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          731..767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          653..680
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        751..767
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   767 AA;  84027 MW;  C56EB2DB24E66A6B CRC64;
     MEEDKLLSAV PEEGDATHDP SPEPEEEPGV QNGMASEGLN SSLCSPGHER RGTPADTEEP
     TKDPDMAFRG LSLGLSLTNG LALGPDLNIL EDSTGSRSWR AGVLAEGDDA SRSLCPDAED
     PQLELDGPGE PDVRDGFSAT FEKILESELL RGTQYSSLDS LDGLSLTDES DSCVSFEAPL
     TPLIQQRARD SPEPGAGLGI GDMGFEGDMG AAGGDGELGS PLRRSISSSR SENVLSRLSL
     MAMPNGFHED GPQGPGGDED DDEEDTDKLL NSTSDPSLKD GLSDSDSELS SSEGLEPGSA
     DPLANGCQGV SEAARRLARR LYHLEGFQRC DVARQLGKNN EFSRLVAGEY LSFFDFSGLT
     LDRALRTFLK AFPLMGETQE RERVLTHFSR RYCQCNPDDS TSEDGIHTLT CALMLLNTDL
     HGHNIGKKMS CQQFIANLDQ LNDGQDFAKD LLKTLYNSIK NEKLEWAIDE DELRKSLSEL
     VDDKFGTGTK KVTRILDGGN PFLDVPQALS ATTYKHGVLT RKTHADMDGK RTPRGRRGWK
     KFYAVLKGTI LYLQKDEYRP DKALSEGDLK NAIRVHHALA TRASDYSKKS NVLKLKTADW
     RVFLFQAPSK EEMLSWILRI NLVAAIFSAP AFPAAVSSMK KFCRPLLPSC TTRLCQEEQL
     RSHENKLRQL TAELAEHRCH PVERGIKSKE AEEYRLKEHY LTFEVSLEGL DCKMIWSGLK
     ARLAHLLTEG STASPPLRKS TLKSCPPPAQ GPLTGSKTTK DATGLNT
//
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