SNX30_DANRE
ID SNX30_DANRE Reviewed; 430 AA.
AC Q566W7;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Sorting nexin-30;
GN Name=snx30; ORFNames=zgc:112424;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the regulation of endocytosis and in several
CC stages of intracellular trafficking. Together with snx4, involved in
CC autophagosome assembly. {ECO:0000250|UniProtKB:Q5VWJ9}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000250|UniProtKB:Q5VWJ9}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O95219}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O95219}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; BC093298; AAH93298.1; -; mRNA.
DR RefSeq; NP_001017798.1; NM_001017798.1.
DR AlphaFoldDB; Q566W7; -.
DR SMR; Q566W7; -.
DR STRING; 7955.ENSDARP00000050176; -.
DR PaxDb; Q566W7; -.
DR PRIDE; Q566W7; -.
DR GeneID; 550496; -.
DR KEGG; dre:550496; -.
DR CTD; 401548; -.
DR ZFIN; ZDB-GENE-050417-330; snx30.
DR eggNOG; KOG2273; Eukaryota.
DR InParanoid; Q566W7; -.
DR OrthoDB; 947320at2759; -.
DR PhylomeDB; Q566W7; -.
DR PRO; PR:Q566W7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR028649; SNX30.
DR PANTHER; PTHR45949:SF1; PTHR45949:SF1; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 2: Evidence at transcript level;
KW Endosome; Membrane; Protein transport; Reference proteome; Transport.
FT CHAIN 1..430
FT /note="Sorting nexin-30"
FT /id="PRO_0000284535"
FT DOMAIN 80..201
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 223..428
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 123
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250|UniProtKB:Q3UR97"
FT BINDING 125
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250|UniProtKB:Q3UR97"
FT BINDING 153
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250|UniProtKB:Q96L94"
FT BINDING 167
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250|UniProtKB:Q6P4T1"
SQ SEQUENCE 430 AA; 49470 MW; 6924F8A9025CEA59 CRC64;
MSNGGTPRSL PSSGQKSIQE ICHPLSAEES ARSRSPDVLN PGEKDLSLPN GTPVDTSSPA
SSSSLLNRLQ LDDDLDAETR DLFVTVDDPK KHVSTMETYI TYRVCTKTTR TEFDLPEYSV
RRRYQDFDWL RIKLEDSQPT HLIPPLPEKF VMKGVVDRFS EEFVETRRKA LDKFLKRVAD
HPVLSFNEHF NAFLSAKDLN KRQGLALLTK MGESVKYVTG GYKLRGRPVE FAAMGEYLDM
FTQKLGTIDR IAQRIIKEQT EFLMELREYG PVYSSWSSFE EDLHEPLEGV SGCVSNCSSA
LEELTEDMSE DFLPVLREYV LYIESMKNVL KKRDQVQAEY ETKLEAVVFR EDKKTPMPTD
VEKCQDRVEC FNADLKADWD RWQNNKRQDF RQLLTGMADK NIQYYEKCLA AWESLIPLLQ
DKQDAKGETN