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Database: UniProt
Entry: A0A087YBV5_POEFO
LinkDB: A0A087YBV5_POEFO
Original site: A0A087YBV5_POEFO 
ID   A0A087YBV5_POEFO        Unreviewed;       568 AA.
AC   A0A087YBV5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 2.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Sorting nexin {ECO:0000256|PIRNR:PIRNR027744};
GN   Name=SNX18 {ECO:0000313|Ensembl:ENSPFOP00000015508.2};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000015508.2, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000015508.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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, ECO:0000256|PIRNR:PIRNR027744}.
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DR   EMBL; AYCK01009774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A087YBV5; -.
DR   STRING; 48698.ENSPFOP00000015508; -.
DR   Ensembl; ENSPFOT00000015530.1; ENSPFOP00000015508.2; ENSPFOG00000015453.1.
DR   eggNOG; KOG2528; Eukaryota.
DR   GeneTree; ENSGT00940000157724; -.
DR   OMA; MGVNYCL; -.
DR   Proteomes; UP000028760; 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: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:SF4; SORTING NEXIN-18; 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   ECO:0000256|PIRNR:PIRNR027744};
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR027744};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028760};
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          224..334
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   BINDING         260
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         262
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         300
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   568 AA;  64257 MW;  4EC7173B6EE9C3C2 CRC64;
     AMALQARVIY DFNSENPGEL SVKESEILTL ICEQDIDGWL EGTNSKGDRG LVPASYVEIL
     RSEAALNSYN INAEPRYSNI PAGGFDKLQN FSKPPPVGLT AYTAPIQEHH NNKHHIQGSD
     DDWDDDWDDN STVADEPGNV GGRYQDSEGS TYRMTTHISP RGNAAQVKSS ATVGRNLNRF
     STFVKSGGEA FVLGEASGFV KDGDKLCVVM GQHGPEWQEN PYPFSCTIDD PTKQTKFKGM
     KSYISYKLTP THTQNPVSRR YKHFDWLYAR LAEKFPVISV PHLPEKQATG RFEEDFISKR
     RKGLIWWMNH MTSHPVLSKC DVFQHFLTCT DEKAWKQGKR KAEKDELVGA NFFLTISTPP
     APLDFQEVES KIDGFKTFTK RMDDSTMQLN ATVNEFARKQ MGGFKKEYQK VGMSFKALSQ
     AFEMDQQTYS SGLNHAISFT GDAYEAIGEY FYEQPSKDLD PVMDLLALYQ GHLANFPDVI
     HVQKGALTKV KESQKHVEEG KMDRAQADGI NDRCNIISCA TLAEIQHFHH IRVRDFKAQM
     QHHLQQQIAF FQKITGKLEE ALQKYDNA
//
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