SNX4_BOVIN
ID SNX4_BOVIN Reviewed; 450 AA.
AC A1A4L0;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Sorting nexin-4 {ECO:0000250|UniProtKB:O95219};
GN Name=SNX4 {ECO:0000250|UniProtKB:O95219};
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=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) 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; BC126650; AAI26651.1; -; mRNA.
DR RefSeq; NP_001073750.1; NM_001080281.2.
DR AlphaFoldDB; A1A4L0; -.
DR SMR; A1A4L0; -.
DR STRING; 9913.ENSBTAP00000015120; -.
DR PaxDb; A1A4L0; -.
DR PRIDE; A1A4L0; -.
DR Ensembl; ENSBTAT00000015120; ENSBTAP00000015120; ENSBTAG00000011383.
DR GeneID; 519597; -.
DR KEGG; bta:519597; -.
DR CTD; 8723; -.
DR VEuPathDB; HostDB:ENSBTAG00000011383; -.
DR VGNC; VGNC:35111; SNX4.
DR eggNOG; KOG2273; Eukaryota.
DR GeneTree; ENSGT00930000151029; -.
DR HOGENOM; CLU_057138_0_0_1; -.
DR InParanoid; A1A4L0; -.
DR OMA; QKSGHYL; -.
DR OrthoDB; 632390at2759; -.
DR TreeFam; TF328543; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000011383; Expressed in caput epididymis and 111 other tissues.
DR ExpressionAtlas; A1A4L0; baseline and differential.
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; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
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; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..450
FT /note="Sorting nexin-4"
FT /id="PRO_0000290184"
FT DOMAIN 61..187
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..53
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"
SQ SEQUENCE 450 AA; 52194 MW; C02B701A1EE9E606 CRC64;
MEQAAPDPER LWQPAPLEPL SHPDAGLESM VGEETKGARD EGPGDGTMTE NNFSLKKIEI
SVSEAEKRTG RNAMNMQETY TAYLIETRSV EHNDGQSVLT DSLWRRYSEF ELLRNYLLVY
YPHIVVPPLP EKRAEFVWHK LSADNMDPDF VERRRIGLEN FLLRVASHPI LCRDKIFYLF
LTQEGNWKET VNETGFQLKA DSRLKALNAT FRVKNPDKRF IELKHYSDEL QSVISHLLRV
RARVADRLYG VYKVHGNYGR VFSEWSAIEK EMGDGLQSAG HHMDVYASSI DDILEDEEHY
ADQLKEYLFY AEALRAVCRK HELMQYDLEM AAQDLASKKQ QCEELATGTV RTFSLKGMTT
KLFGQETPEQ REARIKMLEE QIKEGEQQLK SKNLEGREFV RNAWADIERF KEQKNHDLKE
ALISYAVMQI SMCKKGIQVW TNAKECFSKM
