ID F4WPD9_ACREC Unreviewed; 536 AA.
AC F4WPD9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Sorting nexin-9 {ECO:0000313|EMBL:EGI64034.1};
GN ORFNames=G5I_07615 {ECO:0000313|EMBL:EGI64034.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI64034.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883}.
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DR EMBL; GL888243; EGI64034.1; -; Genomic_DNA.
DR RefSeq; XP_011056934.1; XM_011058632.1.
DR AlphaFoldDB; F4WPD9; -.
DR STRING; 103372.F4WPD9; -.
DR EnsemblMetazoa; XM_011058632.1; XP_011056934.1; LOC105147542.
DR GeneID; 105147542; -.
DR KEGG; aec:105147542; -.
DR eggNOG; KOG2528; Eukaryota.
DR InParanoid; F4WPD9; -.
DR OrthoDB; 5401713at2759; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR CDD; cd07626; BAR_SNX9_like; 1.
DR CDD; cd06862; PX_SNX9_18_like; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR019497; Sorting_nexin_WASP-bd-dom.
DR PANTHER; PTHR45827; SORTING NEXIN; 1.
DR PANTHER; PTHR45827:SF1; SORTING NEXIN; 1.
DR Pfam; PF10456; BAR_3_WASP_bdg; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00312; PX; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..63
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 194..303
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 66..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 536 AA; 61496 MW; 61C0D3E1033E8648 CRC64;
MENQQVRALY DFTGESGTAE LSITAGELLT VIRDNVGDGW CEGFNQSGQS GLFPAAYVQV
VQVEQAASSN PMTSSQQSSG DYWDDDWDDD SEVGQTQAYV PPSQQQQQQP QISVSQQNNA
NDYGDPMHTI HSVIPERPIS TVPKKNNKFS TLIKSGEDSF LLGVKVVTVP DSEKIFIEEG
DGNRCTWLPT GESYSCVVTS PKKESKLKGL KSFIVYQLTP TFNNIQVSRR YKHFDWLHER
LEEKYCFIPI PPLPDKQISG RYEDAFIEHR RTQLQEFVDY VCRHPVLSRS RVWQHFITCT
DEKRWKAGKR QAEKDELLGV NYFNAIQSPD TPLDIIKMEL QTDAFNKFIN GLDPVVKNFM
AMAVDQAKKH QVLYKREFQK ISQSFTSLSH ALEADDNGRG KLTRALKATG DAYNDIGKLY
EEQPKFDWEP LSDKFHIYRG IISNFPDVTS IHKSAMQKRR DCERLVSEHK MEPQQLRDLS
HRTDVIARAL IAEEIHFQTE REVHVNKAVR THLTEQIAFY QKIVNKLREA LNTFDE
//