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Database: UniProt
Entry: A0A3Q3CYX3_HAPBU
LinkDB: A0A3Q3CYX3_HAPBU
Original site: A0A3Q3CYX3_HAPBU 
ID   A0A3Q3CYX3_HAPBU        Unreviewed;       532 AA.
AC   A0A3Q3CYX3;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Sorting nexin-9-like {ECO:0000313|Ensembl:ENSHBUP00000033908.1};
GN   Name=SNX9 {ECO:0000313|Ensembl:ENSHBUP00000033908.1};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000033908.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000033908.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_005950281.1; XM_005950219.2.
DR   AlphaFoldDB; A0A3Q3CYX3; -.
DR   STRING; 8153.ENSHBUP00000033908; -.
DR   Ensembl; ENSHBUT00000035303.1; ENSHBUP00000033908.1; ENSHBUG00000021094.1.
DR   GeneID; 102309516; -.
DR   GeneTree; ENSGT00940000156557; -.
DR   OMA; CIIADPK; -.
DR   OrthoDB; 5401713at2759; -.
DR   Proteomes; UP000264840; Unplaced.
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:0000278; P:mitotic cell cycle; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; IPR014536; Snx9_fam.
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; 2.
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:UP000264840};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Transport {ECO:0000256|ARBA:ARBA00022927}.
FT   DOMAIN          1..62
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          187..297
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   REGION          74..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         223
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         225
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         264
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"
SQ   SEQUENCE   532 AA;  59856 MW;  F687C810BAE6F439 CRC64;
     MAAQALVLYD FTAEPGNNEL SVREGETITV TDQTVGGGWI QAQNSSGQTG LVPEGYLQIR
     NTGGVGGGGD LSSGGGAFVS HTQGWDSRGY NPTQHAVQDD DGEWDDEWDD QSVSSYHDNN
     QPEGEAGASG RSAHGPSVKI SLNKFSFSKG PSPEVFMLAR PPADSRERLP VYMGEVGPVW
     LYPTSPLDCV IADPKKESKM YGLKSFIEYQ ITPNTTNSPV NHRYKHFDWL YERLLEKFGS
     ILPIPSLPDK QVTGRFDDDF IRMRMEGLQA WMTRMCRHPI VSQSEVFQLF LTHRDEKEWK
     AGKRKAEKDE TVGPMMFSLV EPEAAELDVI QVEQRCEHYS RFTKSMDDGV RELLNVGHAH
     WKRCTGPLPK EYERIGQAFR NLSTVFITSK YPGEATLTDA LTAAGKTYEE IAEVVAQQPQ
     KDLHFLLETN SEYKGLLACF PDIIAVHKAA ADKVKEGDRL VSAGKMNNSD RKCMNQRLSC
     MSYALQAEMN HFHSNRIYDY NRVMQLYLEQ QVTFYQQIAD KLREALSQFT TL
//
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