SNX3_BOVIN
ID SNX3_BOVIN Reviewed; 162 AA.
AC Q1RMH8;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Sorting nexin-3;
GN Name=SNX3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphoinositide-binding protein required for multivesicular
CC body formation. Specifically binds phosphatidylinositol 3-phosphate
CC (PtdIns(P3)). Can also bind phosphatidylinositol 4-phosphate
CC (PtdIns(P4)), phosphatidylinositol 5-phosphate (PtdIns(P5)) and
CC phosphatidylinositol 3,5-biphosphate (PtdIns(3,5)P2). Plays a role in
CC protein transport between cellular compartments. Together with RAB7A
CC facilitates endosome membrane association of the retromer cargo-
CC selective subcomplex (CSC). May act in part as component of the SNX3-
CC retromer complex which mediates the retrograde endosome-to-TGN
CC transport of WLS distinct from the SNX-BAR retromer pathway. Promotes
CC stability and cell surface expression of epithelial sodium channel
CC (ENAC) subunits SCNN1A and SCNN1G. Not involved in EGFR degradation.
CC Involved in the regulation of phagocytosis in dendritic cells possibly
CC by regulating EEA1 recruitment to the nascent phagosomes. Involved in
CC iron homeostasis through regulation of endocytic recycling of the
CC transferrin receptor Tfrc presuambly by delivering the
CC transferrin:transferrin receptor complex to recycling endosomes; the
CC function may involve the CSC retromer subcomplex. Involved in
CC regulation of neurite outgrowth in primary neurons.
CC {ECO:0000250|UniProtKB:O60493, ECO:0000250|UniProtKB:O70492}.
CC -!- SUBUNIT: Interacts with VPS26A, VPS29 and VPS35; the interaction with
CC VPS35 is direct. The association with the retromer CSC subcomplex
CC subunits is proposed to represent a functional distinct retromer
CC variant described as SNX3-retromer complex. Interacts with USP10 and
CC SCNN1A. Interacts with TRFC. Interacts with SNX8; 2 molecules of SNX8
CC seems to associate with one molecule of SNX3. Interacts with PTPRU (By
CC similarity). Interacts with MON2 and DOP1B.
CC {ECO:0000250|UniProtKB:O60493, ECO:0000250|UniProtKB:O70492}.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000250|UniProtKB:O60493,
CC ECO:0000250|UniProtKB:O70492}. Cytoplasmic vesicle, phagosome
CC {ECO:0000250|UniProtKB:O60493}. Note=Colocalizes to clathrin-coated
CC endosomal vesicles morphologically distinct from retromer-decorated
CC non-branched endosomal tubule structures. Colocalizes with EEA1 on
CC nascent phagosomes in dendritic cells but competes with EEA1 for
CC binding to phagosomal membrane (By similarity).
CC {ECO:0000250|UniProtKB:O60493, ECO:0000250|UniProtKB:O70492}.
CC -!- DOMAIN: The PX domain mediates specific binding to phosphatidylinositol
CC 3-phosphate (PtdIns(P3)). {ECO:0000250|UniProtKB:O60493}.
CC -!- PTM: Ubiquitinated, leading to its proteasomal degradation.
CC Deubiquitinated by USP10 (By similarity).
CC {ECO:0000250|UniProtKB:O70492}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; BC114888; AAI14889.1; -; mRNA.
DR RefSeq; NP_001073246.1; NM_001079778.1.
DR AlphaFoldDB; Q1RMH8; -.
DR SMR; Q1RMH8; -.
DR STRING; 9913.ENSBTAP00000025026; -.
DR PaxDb; Q1RMH8; -.
DR PeptideAtlas; Q1RMH8; -.
DR PRIDE; Q1RMH8; -.
DR Ensembl; ENSBTAT00000025026; ENSBTAP00000025026; ENSBTAG00000018801.
DR GeneID; 528265; -.
DR KEGG; bta:528265; -.
DR CTD; 8724; -.
DR VEuPathDB; HostDB:ENSBTAG00000018801; -.
DR VGNC; VGNC:35107; SNX3.
DR eggNOG; KOG2527; Eukaryota.
DR GeneTree; ENSGT00940000153609; -.
DR HOGENOM; CLU_057172_2_2_1; -.
DR InParanoid; Q1RMH8; -.
DR OMA; MFLQDEF; -.
DR OrthoDB; 1407986at2759; -.
DR TreeFam; TF314980; -.
DR Reactome; R-BTA-3238698; WNT ligand biogenesis and trafficking.
DR Proteomes; UP000009136; Chromosome 9.
DR Bgee; ENSBTAG00000018801; Expressed in occipital lobe and 104 other tissues.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IBA:GO_Central.
DR GO; GO:0032009; C:early phagosome; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0030904; C:retromer complex; IBA:GO_Central.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISS:UniProtKB.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; ISS:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR GO; GO:1905394; F:retromer complex binding; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:0070676; P:intralumenal vesicle formation; IEA:Ensembl.
DR GO; GO:0034499; P:late endosome to Golgi transport; IBA:GO_Central.
DR GO; GO:0010324; P:membrane invagination; IEA:Ensembl.
DR GO; GO:2000642; P:negative regulation of early endosome to late endosome transport; IEA:Ensembl.
DR GO; GO:0050765; P:negative regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0051224; P:negative regulation of protein transport; IEA:Ensembl.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IEA:Ensembl.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0022615; P:protein to membrane docking; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0030111; P:regulation of Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR CDD; cd07293; PX_SNX3; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR042137; PX_SNX3_Vert.
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; Cytoplasmic vesicle; Endosome; Isopeptide bond; Lipid-binding;
KW Methylation; Phosphoprotein; Protein transport; Reference proteome;
KW Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O60493"
FT CHAIN 2..162
FT /note="Sorting nexin-3"
FT /id="PRO_0000245489"
FT DOMAIN 27..151
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 147..162
FT /note="Binds predominantly to PtdIns(P5) and weaker to
FT PtdIns(P3) abd PtdIns(P4); involved in neurite outgrowth
FT regulation"
FT /evidence="ECO:0000250|UniProtKB:O70492"
FT BINDING 70
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 72
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 95
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 118
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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O60493"
FT MOD_RES 43
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O60493"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60493"
FT CROSSLNK 95
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60493"
SQ SEQUENCE 162 AA; 18762 MW; 983D422FCA6E07BC CRC64;
MAETVADTRR LITKPQNLND AYGPPSNFLE IDVSNPQTVG VGRGRFTTYE IRVKTNLPIF
KLKESTVRRR YSDFEWLRSE LERESKVVVP PLPGKAFLRQ LPFRGDDGIF DDNFIEERKQ
GLEQFINKVA GHPLAQNERC LHMFLQDEII DKSYTPSKIR HA
