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Database: UniProt
Entry: A0A091FJR8_9AVES
LinkDB: A0A091FJR8_9AVES
Original site: A0A091FJR8_9AVES 
ID   A0A091FJR8_9AVES        Unreviewed;       597 AA.
AC   A0A091FJR8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Sorting nexin-9 {ECO:0000313|EMBL:KFO70750.1};
DE   Flags: Fragment;
GN   ORFNames=N303_00654 {ECO:0000313|EMBL:KFO70750.1};
OS   Cuculus canorus (common cuckoo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX   NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO70750.1, ECO:0000313|Proteomes:UP000053760};
RN   [1] {ECO:0000313|EMBL:KFO70750.1, ECO:0000313|Proteomes:UP000053760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO70750.1};
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}.
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DR   EMBL; KL447196; KFO70750.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091FJR8; -.
DR   STRING; 55661.A0A091FJR8; -.
DR   Proteomes; UP000053760; 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; PF14604; SH3_9; 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:UP000053760};
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..198
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:KFO70750.1"
FT   NON_TER         597
FT                   /evidence="ECO:0000313|EMBL:KFO70750.1"
SQ   SEQUENCE   597 AA;  66631 MW;  7BB3D85C99BF372A CRC64;
     QARVMYDFAA EPGNNELTVS EGEIITITNP DVGGGWLEGK NSQGERGLVP TDYVEIISEG
     AKDGISCGNS LADQAFFDSL SSSTAQTNAA AKSSHQANNA SDPWSSWSTG KSGNWDNGNA
     VDSWATKPES AAGQRNSASN NWETAAAFGH PQAYQGPAAA DDDDWDDDWD DPKSASPSYL
     GYKETEASEA GGVQRGNSRG 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
     ADQPKKDLHF LMETNHEYKG FLGCFPDIIG AHKGAIERVK ESDKLVATSK ITPQDKQNMV
     KRVSTMAYAL QAEMNHFHSN RIYDYNSVIR LYLEQQAQFY ETIAQKLRQA LSRFPVM
//
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