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Database: UniProt
Entry: A0A0A0AB18_CHAVO
LinkDB: A0A0A0AB18_CHAVO
Original site: A0A0A0AB18_CHAVO 
ID   A0A0A0AB18_CHAVO        Unreviewed;       597 AA.
AC   A0A0A0AB18;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Sorting nexin-9 {ECO:0000313|EMBL:KGL91107.1};
DE   Flags: Fragment;
GN   ORFNames=N301_01766 {ECO:0000313|EMBL:KGL91107.1};
OS   Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX   NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL91107.1, ECO:0000313|Proteomes:UP000053858};
RN   [1] {ECO:0000313|EMBL:KGL91107.1, ECO:0000313|Proteomes:UP000053858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL91107.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC       {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004180}.
CC   -!- SIMILARITY: Belongs to the sorting nexin family.
CC       {ECO:0000256|ARBA:ARBA00010883}.
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DR   EMBL; KL871168; KGL91107.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A0AB18; -.
DR   STRING; 50402.A0A0A0AB18; -.
DR   Proteomes; UP000053858; Unassembled WGS sequence.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0000281; P:mitotic cytokinesis; IEA:InterPro.
DR   CDD; cd07668; BAR_SNX9; 1.
DR   CDD; cd07285; PX_SNX9; 1.
DR   CDD; cd11898; SH3_SNX9; 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; IPR037425; SNX9_BAR.
DR   InterPro; IPR014536; Snx9_fam.
DR   InterPro; IPR037426; SNX9_PX.
DR   InterPro; IPR035558; SNX9_SH3.
DR   InterPro; IPR019497; Sorting_nexin_WASP-bd-dom.
DR   PANTHER; PTHR45827; SORTING NEXIN; 1.
DR   PANTHER; PTHR45827:SF2; SORTING NEXIN-9; 1.
DR   Pfam; PF10456; BAR_3_WASP_bdg; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PIRSF; PIRSF027744; Snx9; 1.
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   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053858};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Transport {ECO:0000256|ARBA:ARBA00022927}.
FT   DOMAIN          1..59
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          252..362
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   REGION          88..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          153..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         288
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-4,5-bisphosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58456"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR027744-1"
FT   BINDING         290
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-4,5-bisphosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58456"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR027744-1"
FT   BINDING         329
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-4,5-bisphosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58456"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR027744-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KGL91107.1"
FT   NON_TER         597
FT                   /evidence="ECO:0000313|EMBL:KGL91107.1"
SQ   SEQUENCE   597 AA;  66702 MW;  7EABB1AB7EDF7E35 CRC64;
     QARVMYDFAA EPGNNELTVS EGEIIIITNP DVGGGWLEGK NSQGERGLVP TDYVEILTEG
     AKDGVSCGNS LADQAFFDSL SSNTAQTNSA AKSSNQANNA SDPWSSWNVG KSGNWDNGNA
     VDSWATKPES AAGQRNSASN NWEAAAAFGH PQAYQGPAAA DDDDWDDDWD DPKSTSPSYL
     GYKESEASEA GGVQRGNSRA AAMKLPLNKF PGFAKPGMEQ YLLAKQLAKP KEKIPIIIGD
     YGPMWVYPTS TFDCVVADPK KGSKMYGLKS YIEYQLTCTN TNRSVNHRYK HFDWLYERLL
     VKFGLAIPIP SLPDKQVTGR FEEEFIKMRM ERLQAWMTRM CRHPVVSESE VFQQFLNFRD
     EKEWKTGKRK AEKDETVGVL IFSTMEPEAP DLDMVEIEQK CDAVGRFTKA MDDGVKELLT
     VGQEHWKRCT GPLPKEYQKI GKALQSLALV FSTSGYQGES DLNGAITEAG KTYEEIASLV
     AEQPKKDLHF LMETNHEYKG FLGCFPDIIG AHKGAIERVK ESDKLVATSK ITPQDKQNMV
     KRVSTMAYAL QAEMNHFHSN RIYDYNSVIR LYLEQQAQFY ETIAQKLRQA LSRFPVM
//
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