SNX4_PONAB
ID SNX4_PONAB Reviewed; 450 AA.
AC Q5R4C2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Sorting nexin-4 {ECO:0000250|UniProtKB:O95219};
GN Name=SNX4 {ECO:0000250|UniProtKB:O95219};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the regulation of endocytosis and in several
CC stages of intracellular trafficking. Plays a role in recycling
CC endocytosed transferrin receptor and prevent its degradation. Involved
CC in autophagosome assembly by regulating trafficking and recycling of
CC phospholipid scramblase ATG9A. {ECO:0000250|UniProtKB:O95219}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with SNX7 or SNX30. Interacts
CC with WWC1/KIBRA. Identified in a complex with WWC1/KIBRA and dynein
CC components DYNLL1 and DYNC1I2. Interacts with BIN1.
CC {ECO:0000250|UniProtKB:O95219}.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000250|UniProtKB:O95219}.
CC Early endosome membrane {ECO:0000250|UniProtKB:O95219}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:O95219}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O95219}. Note=Also detected on a juxtanuclear
CC endocytic recycling compartment (ERC). {ECO:0000250|UniProtKB:O95219}.
CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is
CC necessary for peripheral membrane localization.
CC {ECO:0000250|UniProtKB:Q96L94}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; CR861330; CAH93394.1; -; mRNA.
DR RefSeq; NP_001126992.1; NM_001133520.1.
DR AlphaFoldDB; Q5R4C2; -.
DR SMR; Q5R4C2; -.
DR STRING; 9601.ENSPPYP00000015056; -.
DR GeneID; 100174015; -.
DR KEGG; pon:100174015; -.
DR CTD; 8723; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_057138_0_0_1; -.
DR InParanoid; Q5R4C2; -.
DR OMA; QKSGHYL; -.
DR OrthoDB; 632390at2759; -.
DR TreeFam; TF328543; -.
DR Proteomes; UP000001595; Chromosome 3.
DR GO; GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0031201; C:SNARE complex; IEA:Ensembl.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IEA:Ensembl.
DR GO; GO:0005158; F:insulin receptor binding; IEA:Ensembl.
DR GO; GO:1990460; F:leptin receptor binding; IEA:Ensembl.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR GO; GO:1990459; F:transferrin receptor binding; IEA:Ensembl.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; ISS:UniProtKB.
DR GO; GO:1903595; P:positive regulation of histamine secretion by mast cell; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR CDD; cd07622; BAR_SNX4; 1.
DR CDD; cd06864; PX_SNX4; 1.
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; IPR034902; PX_SNX4.
DR InterPro; IPR034783; SNX4.
DR InterPro; IPR037430; SNX4_BAR.
DR PANTHER; PTHR46596; PTHR46596; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Endosome; Lipid-binding; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..450
FT /note="Sorting nexin-4"
FT /id="PRO_0000213843"
FT DOMAIN 61..187
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106
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 108
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 132
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 154
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"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O95219"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95219"
SQ SEQUENCE 450 AA; 51967 MW; B2259BD469A292F1 CRC64;
MEQAPPDPER QLQPAPLEPL GSPDAVLGAA VGKETEGAGE ESSGVDTMTH NNFWLKKIEI
SVSEAEKRTG RNAMNMQETY TAYLIETRSI EHTDGQSVLT DSLWRRYSEF ELLRSYLLVY
YPHIVVPPLP EKRAEFVWHK LSADNMDPDF VERRRIGLEN FLLRIASHPL LCRDKIFYLF
LTQEGNWKET VNETGFQLKA DSRLKALNAT FRVKNPDKRF TDLKHYSDEL QSVISHLLRV
RARVADRLYG VYKVHGNYGR VFSEWSAIEK EMGDGLQSAG HHMDVYASSI DDILEDEEHY
ADQLKEYLFY AEALRAVCRK HELMQYDLEM AAQDLASKKQ QCEELATGTV RTFSLKGMTT
KLFGQETPEQ REARIKVLEE QINEGEQQLK SKNLEGREFV KNAWADIERF KEQKNRDLKE
ALISYAVMQI SMCKKGIQVW TNAKECFSKM
