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Database: UniProt
Entry: A0A2K5CPC1_AOTNA
LinkDB: A0A2K5CPC1_AOTNA
Original site: A0A2K5CPC1_AOTNA 
ID   A0A2K5CPC1_AOTNA        Unreviewed;       596 AA.
AC   A0A2K5CPC1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Sorting nexin {ECO:0000256|PIRNR:PIRNR027744};
GN   Name=SNX9 {ECO:0000313|Ensembl:ENSANAP00000010543.1};
OS   Aotus nancymaae (Ma's night monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000010543.1, ECO:0000313|Proteomes:UP000233020};
RN   [1] {ECO:0000313|Ensembl:ENSANAP00000010543.1}
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   AlphaFoldDB; A0A2K5CPC1; -.
DR   Ensembl; ENSANAT00000028346.1; ENSANAP00000010543.1; ENSANAG00000023218.1.
DR   GeneTree; ENSGT00940000156557; -.
DR   OMA; FDSAPMR; -.
DR   Proteomes; UP000233020; 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: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; PF07653; SH3_2; 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   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:UP000233020};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Transport {ECO:0000256|ARBA:ARBA00022927}.
FT   DOMAIN          1..63
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          251..362
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   REGION          92..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         287
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         289
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         328
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   596 AA;  66794 MW;  3912A024D61EB9A5 CRC64;
     MRTKPARVMY DFAAEPGNNE LTVNEGEIIT ITNPDVGGGW LEGRNIKGER GLVPTDYVEI
     LPSDGKDQFS CGNSVADQAF LDSLSASTTQ ASSSAASSNH QVGSGNDPWS AWSASKSGNW
     ESSEGWGAKP DGAGAQRNTN TPDNWDTAFG HPQAYQGPAT GDDDDWDEDW DGPKSSSYFK
     DSESADTGGV QRGNSRASAS SMKIPLNKFP GFAKPGTEQY LLAKQLAKPK EKIPIIVGDY
     GPMWVYPTST FDCVVADPRK GSKMYGLKSY IEYQLTPTNT NRSVNHRYKH FDWLYERLLV
     KFGSAIPIPS LPDKQVTGRF EEEFIKMRME RLQSWMTRMC RHPVISESEV FQQFLNFRDE
     KEWKTGKRKA ERDELAGVMI FSTMEPEAPD LDLVEIEQKC EAVGKFTKAM DDGVKELLTV
     GQEHWKRCTG PLPKEYQKIG KALQSLATVF SSSGYQGETD LNDAITEAGK TYEEIASLVA
     EQPKKDLHFL MECNHEYKGF LGCFPDIIGT HKGALEKVKE SDKLVATSKI TPQDKQNMVK
     RVSTMSYALQ AEMNHFHSNR IYDYNSVIRL YLEQQVQFYE TIAEKLRQAL SRFPVM
//
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