ID A0A091JUW0_COLST Unreviewed; 597 AA.
AC A0A091JUW0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Sorting nexin-9 {ECO:0000313|EMBL:KFP27738.1};
DE Flags: Fragment;
GN ORFNames=N325_05682 {ECO:0000313|EMBL:KFP27738.1};
OS Colius striatus (Speckled mousebird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coliiformes; Coliidae; Colius.
OX NCBI_TaxID=57412 {ECO:0000313|EMBL:KFP27738.1, ECO:0000313|Proteomes:UP000053615};
RN [1] {ECO:0000313|EMBL:KFP27738.1, ECO:0000313|Proteomes:UP000053615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N325 {ECO:0000313|EMBL:KFP27738.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK530108; KFP27738.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091JUW0; -.
DR Proteomes; UP000053615; 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; SSF103657; BAR/IMD domain-like; 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:UP000053615};
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 87..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..195
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:KFP27738.1"
FT NON_TER 597
FT /evidence="ECO:0000313|EMBL:KFP27738.1"
SQ SEQUENCE 597 AA; 66776 MW; C4CED044D05DDE88 CRC64;
QARVMYDFAA EPGNNELTVS EGEIIIITNP DVGGGWLEGK NSQGERGLVP TDYVEIITEG
AKDGISCGNS LADQAFFDSL SSSTAQTNSA AKSNNQANNA SDPWSSWNVG KSGNWDNGNT
VDSWATKPES AAGQRNSASN NWEAAAAFGH PQAYQGPAAA DDDDWDDDWD DPKSTSPSYL
GYKETEASEA GGVQRGNSRA AAMKLPLNKF PGFAKPGMEQ YLLAKQLAKP KEKIPIIIGD
YGPMWVYPTS TFDCVVADPK KGSKMYGLKS YIEYQLTCTN TNRSVNHRYK HFDWLYERLL
VKFGLAIPIP SLPDKQVTGR FEEEFIKMRM ERLQAWMTRM CRHPVVSESE VFQQFLNFRD
EKEWKTGKRK AEKDETVGVL IFSTMEPEAP DLDMVEIEQK CDAVGRFTKA MDDGVRELLT
VGQEHWKRCT GPLPKEYQKI GKALQSLATV FSTSGYQGES DLNGAITEAG KTYEEIASLV
ADQPKKDLHF LMETNHEYKG FLGCFPDIIA AHKGAIERVK ESDKLVATSK ITPQDKQNMV
KRVSTMAYAL QAEMNHFHSN RIYDYNSVIR LYLEQQAQFY ETIAQKLRQA LSRFPVM
//
