SNX10_BOVIN
ID SNX10_BOVIN Reviewed; 200 AA.
AC Q0IIL5;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Sorting nexin-10;
GN Name=SNX10;
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=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable phosphoinositide-binding protein involved in protein
CC sorting and membrane trafficking in endosomes. Plays a role in cilium
CC biogenesis through regulation of the transport and the localization of
CC proteins to the cilium. Required for the localization to the cilium of
CC V-ATPase subunit ATP6V1D and ATP6V0D1, and RAB8A. Involved in
CC osteoclast differentiation and therefore bone resorption (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ATP6V1D; may play a role in ciliogenesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endosome membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Note=May also localize to nucleus and
CC endoplasmic reticulum. {ECO:0000250}.
CC -!- DOMAIN: The PX domain mediates interaction with membranes enriched in
CC phosphatidylinositol 3-phosphate. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; BC122586; AAI22587.1; -; mRNA.
DR RefSeq; NP_001068843.1; NM_001075375.1.
DR RefSeq; XP_005205585.1; XM_005205528.1.
DR RefSeq; XP_005205586.1; XM_005205529.2.
DR RefSeq; XP_005205588.1; XM_005205531.3.
DR AlphaFoldDB; Q0IIL5; -.
DR SMR; Q0IIL5; -.
DR STRING; 9913.ENSBTAP00000002383; -.
DR PaxDb; Q0IIL5; -.
DR Ensembl; ENSBTAT00000002383; ENSBTAP00000002383; ENSBTAG00000001822.
DR Ensembl; ENSBTAT00000072909; ENSBTAP00000064069; ENSBTAG00000001822.
DR GeneID; 508836; -.
DR KEGG; bta:508836; -.
DR CTD; 29887; -.
DR VEuPathDB; HostDB:ENSBTAG00000001822; -.
DR VGNC; VGNC:35091; SNX10.
DR eggNOG; KOG2527; Eukaryota.
DR GeneTree; ENSGT00940000156007; -.
DR HOGENOM; CLU_057172_4_0_1; -.
DR InParanoid; Q0IIL5; -.
DR OMA; NIRIWDE; -.
DR OrthoDB; 1407986at2759; -.
DR TreeFam; TF332117; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000001822; Expressed in monocyte and 106 other tissues.
DR GO; GO:0090651; C:apical cytoplasm; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0031313; C:extrinsic component of endosome membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0030141; C:secretory granule; IEA:Ensembl.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IBA:GO_Central.
DR GO; GO:0035630; P:bone mineralization involved in bone maturation; IEA:Ensembl.
DR GO; GO:0045453; P:bone resorption; IEA:Ensembl.
DR GO; GO:0055074; P:calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0019725; P:cellular homeostasis; IEA:Ensembl.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:Ensembl.
DR GO; GO:0007032; P:endosome organization; ISS:UniProtKB.
DR GO; GO:0001696; P:gastric acid secretion; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0030316; P:osteoclast differentiation; ISS:UniProtKB.
DR GO; GO:0071539; P:protein localization to centrosome; ISS:UniProtKB.
DR GO; GO:0061512; P:protein localization to cilium; ISS:UniProtKB.
DR GO; GO:0097178; P:ruffle assembly; IEA:Ensembl.
DR GO; GO:0044691; P:tooth eruption; IEA:Ensembl.
DR GO; GO:0016050; P:vesicle organization; IBA:GO_Central.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR043544; SNX10/11.
DR PANTHER; PTHR46209; PTHR46209; 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 Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Endosome;
KW Lipid-binding; Membrane; Protein transport; Reference proteome; Transport.
FT CHAIN 1..200
FT /note="Sorting nexin-10"
FT /id="PRO_0000290186"
FT DOMAIN 10..127
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 8..125
FT /note="Required for interaction with ATP6V1D"
FT /evidence="ECO:0000250"
FT REGION 156..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 53
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"
FT BINDING 79
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"
FT BINDING 94
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"
SQ SEQUENCE 200 AA; 23522 MW; A1D8EDDD3B942BB2 CRC64;
MFPEQQKEEF VSVWVRDPRI QKEDFWHSYI DYEICIHTNS MCFTMKTSCV RRRYREFVWL
RQRLQSNALL VQLPELPSKN LFFNMNNRQH VDQRRQGLED FLRKVLQNAL LLSDSSLHLF
LQSHLNSEDI EACVSGQTKY SVEEAIHKFA LMNRRFPEEE EGKKENDIDY DSESSSSGFG
HSSDDSSSHG CKMSTAPQES
