ID A0A087XFN2_POEFO Unreviewed; 613 AA.
AC A0A087XFN2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Sorting nexin {ECO:0000256|PIRNR:PIRNR027744};
GN Name=SNX9 {ECO:0000313|Ensembl:ENSPFOP00000004585.2};
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:ENSPFOP00000004585.2, 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:ENSPFOP00000004585.2}
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}.
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; AYCK01005085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007552920.1; XM_007552858.2.
DR AlphaFoldDB; A0A087XFN2; -.
DR STRING; 48698.ENSPFOP00000004585; -.
DR Ensembl; ENSPFOT00000004593.2; ENSPFOP00000004585.2; ENSPFOG00000004400.2.
DR GeneID; 103138599; -.
DR KEGG; pfor:103138599; -.
DR CTD; 558917; -.
DR eggNOG; KOG2528; Eukaryota.
DR GeneTree; ENSGT00940000156557; -.
DR OrthoDB; 5401713at2759; -.
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:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:InterPro.
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; 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 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 268..378
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 95..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 304
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 306
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 345
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 613 AA; 68142 MW; 066A88C06D61F358 CRC64;
MALKAQVLYD FTAEPGNNEL TVKEGETITV TNKSIGGGWI EAQNSRGEVG LVPEDYIEFK
NEFPAASTAP PSNAGNAAYP DLSVFDAFAP VSTPAQNQVD SGALSPVPDT PDTPVTPFFP
SPEEASNGND PWSAWNADPS GGTNNNWASN PEGTQTGKSA PDPWGNVSQG HPQAYQGPAA
EDDEWDDEWD EMKSSAGYAE SESGEAGGIQ RGGMHASSMK ISLNKFPGFS KSGPELYLLC
KQIAKGKDKL SIYVGEVGPV WSYPETQIDC IVADPKKGSK MYGLKSYIEY QITPNTTNRP
VNHRYKHFDW LYERLLDKFG SAIPIPSLPD KQVTGRFEEE FIKMRMERLQ GWMSRMCRHP
VISGSDVFQL FLTYKDEKDW KTGKRKAEKD ETVGVMIFTT IEPEAADLDP LEVEQKCEQF
SKFTKAMDDS VKEILTVGNE HWKRCTGPLP KEYQRIGKAL QNLSTVFTSS GYQGESTLTD
ALTAAGKTYE EIAQLVAEQP KKDLHFLMET NNEYKGLLGC FPDTIGVHKA AIDKVKEGDK
LVAANKITTQ DKVAMSKRLS TMSYTLQAEM NHFHSNRIYD YNRVMQQYLE EQVKFYETIA
GKLRQAHGQF TTM
//
