SNX10_MOUSE
ID SNX10_MOUSE Reviewed; 201 AA.
AC Q9CWT3; Q8C1E0;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Sorting nexin-10;
GN Name=Snx10;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION IN OSTEOCLASTOGENESIS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=22174188; DOI=10.1002/jcb.24029;
RA Zhu C.H., Morse L.R., Battaglino R.A.;
RT "SNX10 is required for osteoclast formation and resorption activity.";
RL J. Cell. Biochem. 113:1608-1615(2012).
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.
CC {ECO:0000269|PubMed:22174188}.
CC -!- SUBUNIT: Interacts with ATP6V1D; may play a role in ciliogenesis.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22174188}. Endosome
CC membrane {ECO:0000269|PubMed:22174188}; Peripheral membrane protein
CC {ECO:0000269|PubMed:22174188}; Cytoplasmic side
CC {ECO:0000269|PubMed:22174188}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250}. Note=May also localize to
CC nucleus and endoplasmic reticulum.
CC -!- TISSUE SPECIFICITY: Expressed in femur, calvariae and teeth.
CC {ECO:0000269|PubMed:22174188}.
CC -!- DEVELOPMENTAL STAGE: Strongly up-regulated during osteoclastogenesis.
CC Expressed in calvariae and developing teeth as early as 16.5 dpc (at
CC protein level). {ECO:0000269|PubMed:22174188}.
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; AK010399; BAB26910.1; -; mRNA.
DR EMBL; AK028163; BAC25786.1; -; mRNA.
DR EMBL; BC010334; AAH10334.1; -; mRNA.
DR CCDS; CCDS20136.1; -.
DR RefSeq; NP_001120820.1; NM_001127348.1.
DR RefSeq; NP_001120821.1; NM_001127349.1.
DR RefSeq; NP_082311.3; NM_028035.4.
DR RefSeq; XP_006506716.1; XM_006506653.3.
DR RefSeq; XP_017177242.1; XM_017321753.1.
DR AlphaFoldDB; Q9CWT3; -.
DR SMR; Q9CWT3; -.
DR STRING; 10090.ENSMUSP00000044165; -.
DR iPTMnet; Q9CWT3; -.
DR PhosphoSitePlus; Q9CWT3; -.
DR MaxQB; Q9CWT3; -.
DR PaxDb; Q9CWT3; -.
DR PRIDE; Q9CWT3; -.
DR ProteomicsDB; 261538; -.
DR Antibodypedia; 1917; 150 antibodies from 20 providers.
DR DNASU; 71982; -.
DR Ensembl; ENSMUST00000049152; ENSMUSP00000044165; ENSMUSG00000038301.
DR Ensembl; ENSMUST00000114439; ENSMUSP00000110082; ENSMUSG00000038301.
DR Ensembl; ENSMUST00000179365; ENSMUSP00000136974; ENSMUSG00000038301.
DR GeneID; 71982; -.
DR KEGG; mmu:71982; -.
DR UCSC; uc009bxs.2; mouse.
DR CTD; 29887; -.
DR MGI; MGI:1919232; Snx10.
DR VEuPathDB; HostDB:ENSMUSG00000038301; -.
DR eggNOG; KOG2527; Eukaryota.
DR GeneTree; ENSGT00940000156007; -.
DR InParanoid; Q9CWT3; -.
DR OMA; NIRIWDE; -.
DR OrthoDB; 1407986at2759; -.
DR PhylomeDB; Q9CWT3; -.
DR TreeFam; TF332117; -.
DR BioGRID-ORCS; 71982; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Snx10; mouse.
DR PRO; PR:Q9CWT3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9CWT3; protein.
DR Bgee; ENSMUSG00000038301; Expressed in granulocyte and 249 other tissues.
DR ExpressionAtlas; Q9CWT3; baseline and differential.
DR Genevisible; Q9CWT3; MM.
DR GO; GO:0090651; C:apical cytoplasm; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA: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; IDA:UniProtKB.
DR GO; GO:0030141; C:secretory granule; IDA:MGI.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IBA:GO_Central.
DR GO; GO:0035630; P:bone mineralization involved in bone maturation; IMP:MGI.
DR GO; GO:0046849; P:bone remodeling; IMP:MGI.
DR GO; GO:0045453; P:bone resorption; IMP:MGI.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:MGI.
DR GO; GO:0019725; P:cellular homeostasis; IMP:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IMP:MGI.
DR GO; GO:0007032; P:endosome organization; ISS:UniProtKB.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0001696; P:gastric acid secretion; IMP:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0030316; P:osteoclast differentiation; IMP: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; IMP:MGI.
DR GO; GO:0044691; P:tooth eruption; IMP:MGI.
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 1: Evidence at protein level;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Endosome;
KW Lipid-binding; Membrane; Protein transport; Reference proteome; Transport.
FT CHAIN 1..201
FT /note="Sorting nexin-10"
FT /id="PRO_0000213855"
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 155..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..201
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"
FT CONFLICT 168
FT /note="D -> E (in Ref. 1; BAC25786)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 201 AA; 23542 MW; 34F853BE23D23D80 CRC64;
MFPEQQKEEF VSVWVRDPRI QKEDFWHSYI DYEICIHTNS MCFTMKTSCV RRRYREFVWL
RQRLQSNALL VQLPELPSKN LFFNMNNRQH VDQRRQGLED FLRKVLQNAL LLSDSSLHLF
LQSHLNSEDI EACVSGQTKY SVEEAIHKFA LMNRRFPEEE EEGKKDADVE YDSESSSSGL
GHSSDDSSSH GCKTSPALQE S
