ID A0A3B3RIK6_9TELE Unreviewed; 573 AA.
AC A0A3B3RIK6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Sorting nexin {ECO:0000256|PIRNR:PIRNR027744};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000018472.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000018472.1}
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; A0A3B3RIK6; -.
DR STRING; 1676925.ENSPKIP00000018472; -.
DR Ensembl; ENSPKIT00000036216.1; ENSPKIP00000018472.1; ENSPKIG00000004006.1.
DR GeneTree; ENSGT00940000156557; -.
DR OrthoDB; 5401713at2759; -.
DR Proteomes; UP000261540; 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; PF00018; SH3_1; 1.
DR PIRSF; PIRSF027744; Snx9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
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 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 228..338
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 84..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT BINDING 266
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 305
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 573 AA; 65116 MW; FDC63493B2FDDB5F CRC64;
MAIKALVLYD FTAEPGNNEL TIKEGEMVTI TNQNIGGGWI EARNSQGETG LVPEEYIEVR
NVDPGSGRFT QSDFDPFAYT AASRTSNNQM SNGNDPWSPQ NTVNEQDSRL SGSAARQSYA
RNSWTVVEHP QAYQGPGAVD DDEWDDEWDD LNSPGPGSAE PEVEETGGSN KAEAQAASKK
INLNKFPSFS RSGPEVFLLA NLPPRGKDKI SVCMGEVGPV WLYPSLQMDC VVADPKKGSK
MYGLKSYIEY QVTPSTTNRP VNHRYKHFDW LYERLLEKFG SVIPIPSLPD KQVTGRFEEE
FIKLRMERLQ GWMTRMCRHP IVSDSEVLQL FLTYKDEKEW KSGKRRAEKD ETVGVMTFSL
IEPEAPELAV TEVEQKCESF SRFTKAMDDR VKELLTVGHD HWKRCTGPLP KQYQKIGKAF
QNLSTVFNSS RYQGEETLTN ALTATGKMYE EIANIVSEQP KKDMHFLVEL NNEYKSLLGC
FPDTINVHKA AIEKVKDSDK LVATNKINPQ DKHTMAKRLS NMSYSLQAEM NHFHSNRIHD
YNRVMQLYLT EQVKFYEMIA DKLREALNQF TTI
//
