SNX10_HUMAN
ID SNX10_HUMAN Reviewed; 201 AA.
AC Q9Y5X0; E9PFH5; Q8IYT5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Sorting nexin-10;
GN Name=SNX10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND VARIANT
RP ILE-187.
RX PubMed=11485546; DOI=10.1042/0264-6021:3580007;
RA Teasdale R.D., Loci D., Houghton F., Karlsson L., Gleeson P.A.;
RT "A large family of endosome-localized proteins related to sorting nexin
RT 1.";
RL Biochem. J. 358:7-16(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-53; LYS-79 AND
RP ARG-94.
RX PubMed=17012226; DOI=10.1074/jbc.m608884200;
RA Qin B., He M., Chen X., Pei D.;
RT "Sorting nexin 10 induces giant vacuoles in mammalian cells.";
RL J. Biol. Chem. 281:36891-36896(2006).
RN [8]
RP FUNCTION IN CILIOGENESIS, INTERACTION WITH ATP6V1D, AND SUBCELLULAR
RP LOCATION.
RX PubMed=21844891; DOI=10.1038/cr.2011.134;
RA Chen Y., Wu B., Xu L., Li H., Xia J., Yin W., Li Z., Shi D., Li S., Lin S.,
RA Shu X., Pei D.;
RT "A SNX10/V-ATPase pathway regulates ciliogenesis in vitro and in vivo.";
RL Cell Res. 22:333-345(2012).
RN [9]
RP SUBCELLULAR LOCATION.
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).
RN [10]
RP INVOLVEMENT IN OPTB8.
RX PubMed=23123320; DOI=10.1016/j.ejmg.2012.10.010;
RA Megarbane A., Pangrazio A., Villa A., Chouery E., Maarawi J., Sabbagh S.,
RA Lefranc G., Sobacchi C.;
RT "Homozygous stop mutation in the SNX10 gene in a consanguineous Iraqi boy
RT with osteopetrosis and corpus callosum hypoplasia.";
RL Eur. J. Med. Genet. 56:32-35(2013).
RN [11]
RP VARIANT OPTB8 GLN-51, CHARACTERIZATION OF VARIANT OPTB8 GLN-51, AND
RP FUNCTION IN BONE RESORPTION.
RX PubMed=22499339; DOI=10.1136/jmedgenet-2011-100520;
RA Aker M., Rouvinski A., Hashavia S., Ta-Shma A., Shaag A., Zenvirt S.,
RA Israel S., Weintraub M., Taraboulos A., Bar-Shavit Z., Elpeleg O.;
RT "An SNX10 mutation causes malignant osteopetrosis of infancy.";
RL J. Med. Genet. 49:221-226(2012).
RN [12]
RP VARIANTS OPTB8 LEU-16; SER-32 AND PRO-51.
RX PubMed=23280965; DOI=10.1002/jbmr.1849;
RA Pangrazio A., Fasth A., Sbardellati A., Orchard P.J., Kasow K.A., Raza J.,
RA Albayrak C., Albayrak D., Vanakker O.M., De Moerloose B., Vellodi A.,
RA Notarangelo L.D., Schlack C., Strauss G., Kuehl J.S., Caldana E.,
RA Lo Iacono N., Susani L., Kornak U., Schulz A., Vezzoni P., Villa A.,
RA Sobacchi C.;
RT "SNX10 mutations define a subgroup of human autosomal recessive
RT osteopetrosis with variable clinical severity.";
RL J. Bone Miner. Res. 28:1041-1049(2013).
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:17012226, ECO:0000269|PubMed:21844891,
CC ECO:0000269|PubMed:22499339}.
CC -!- SUBUNIT: Interacts with ATP6V1D; may play a role in ciliogenesis.
CC {ECO:0000269|PubMed:21844891}.
CC -!- INTERACTION:
CC Q9Y5X0; Q15041: ARL6IP1; NbExp=6; IntAct=EBI-10329478, EBI-714543;
CC Q9Y5X0; Q92993: KAT5; NbExp=3; IntAct=EBI-10329478, EBI-399080;
CC Q9Y5X0; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-10329478, EBI-11742507;
CC Q9Y5X0; P17252: PRKCA; NbExp=3; IntAct=EBI-10329478, EBI-1383528;
CC Q9Y5X0; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-10329478, EBI-712367;
CC Q9Y5X0; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-10329478, EBI-9090795;
CC Q9Y5X0; O95070: YIF1A; NbExp=3; IntAct=EBI-10329478, EBI-2799703;
CC Q9Y5X0; P61981: YWHAG; NbExp=3; IntAct=EBI-10329478, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane; Peripheral membrane
CC protein; Cytoplasmic side. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Note=May also localize to nucleus and
CC endoplasmic reticulum.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y5X0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y5X0-2; Sequence=VSP_045920;
CC -!- DOMAIN: The PX domain mediates interaction with membranes enriched in
CC phosphatidylinositol 3-phosphate.
CC -!- DISEASE: Osteopetrosis, autosomal recessive 8 (OPTB8) [MIM:615085]: A
CC rare genetic disease characterized by abnormally dense bone, due to
CC defective resorption of immature bone. Osteopetrosis occurs in two
CC forms: a severe autosomal recessive form occurring in utero, infancy,
CC or childhood, and a benign autosomal dominant form occurring in
CC adolescence or adulthood. Recessive osteopetrosis commonly manifests in
CC early infancy with macrocephaly, feeding difficulties, evolving
CC blindness and deafness, bone marrow failure, severe anemia, and
CC hepatosplenomegaly. Deafness and blindness are generally thought to
CC represent effects of pressure on nerves. OPTB8 is clinically
CC characterized by dense bones with no distinction between outer and
CC inner plates, due to extensive encroachment of cortical bone into the
CC medullary space, increased head circumference, broad open fontanelle,
CC frontal bossing, and hepatosplenomegaly. Osteoclasts number is low and
CC their bone resorptive capacity is impaired.
CC {ECO:0000269|PubMed:22499339, ECO:0000269|PubMed:23123320,
CC ECO:0000269|PubMed:23280965}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; AF121860; AAD27833.1; -; mRNA.
DR EMBL; AK309162; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK312850; BAG35703.1; -; mRNA.
DR EMBL; AC004540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC074295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236948; EAL24234.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93849.1; -; Genomic_DNA.
DR EMBL; BC034992; AAH34992.1; -; mRNA.
DR CCDS; CCDS5399.1; -. [Q9Y5X0-1]
DR CCDS; CCDS56470.1; -. [Q9Y5X0-2]
DR RefSeq; NP_001186764.1; NM_001199835.1. [Q9Y5X0-1]
DR RefSeq; NP_001186766.1; NM_001199837.1.
DR RefSeq; NP_001186767.1; NM_001199838.1. [Q9Y5X0-2]
DR RefSeq; NP_001305127.1; NM_001318198.1.
DR RefSeq; NP_001305128.1; NM_001318199.1. [Q9Y5X0-1]
DR RefSeq; NP_037454.2; NM_013322.2. [Q9Y5X0-1]
DR RefSeq; XP_006715775.1; XM_006715712.2. [Q9Y5X0-1]
DR PDB; 4ON3; X-ray; 2.60 A; A/B=1-201.
DR PDB; 4PZG; X-ray; 2.80 A; A/B=1-201.
DR PDB; 6KOK; X-ray; 2.00 A; A/B=135-153.
DR PDBsum; 4ON3; -.
DR PDBsum; 4PZG; -.
DR PDBsum; 6KOK; -.
DR AlphaFoldDB; Q9Y5X0; -.
DR SMR; Q9Y5X0; -.
DR BioGRID; 118940; 5.
DR IntAct; Q9Y5X0; 9.
DR STRING; 9606.ENSP00000395474; -.
DR iPTMnet; Q9Y5X0; -.
DR PhosphoSitePlus; Q9Y5X0; -.
DR BioMuta; SNX10; -.
DR DMDM; 205371824; -.
DR EPD; Q9Y5X0; -.
DR jPOST; Q9Y5X0; -.
DR MassIVE; Q9Y5X0; -.
DR MaxQB; Q9Y5X0; -.
DR PaxDb; Q9Y5X0; -.
DR PeptideAtlas; Q9Y5X0; -.
DR PRIDE; Q9Y5X0; -.
DR ProteomicsDB; 20105; -.
DR ProteomicsDB; 86525; -. [Q9Y5X0-1]
DR Antibodypedia; 1917; 150 antibodies from 20 providers.
DR DNASU; 29887; -.
DR Ensembl; ENST00000338523.9; ENSP00000343709.5; ENSG00000086300.16. [Q9Y5X0-1]
DR Ensembl; ENST00000396376.5; ENSP00000379661.1; ENSG00000086300.16. [Q9Y5X0-1]
DR Ensembl; ENST00000409838.1; ENSP00000386540.1; ENSG00000086300.16. [Q9Y5X0-2]
DR Ensembl; ENST00000446848.6; ENSP00000395474.3; ENSG00000086300.16. [Q9Y5X0-1]
DR GeneID; 29887; -.
DR KEGG; hsa:29887; -.
DR MANE-Select; ENST00000338523.9; ENSP00000343709.5; NM_013322.3; NP_037454.2.
DR UCSC; uc003sxx.4; human. [Q9Y5X0-1]
DR CTD; 29887; -.
DR DisGeNET; 29887; -.
DR GeneCards; SNX10; -.
DR HGNC; HGNC:14974; SNX10.
DR HPA; ENSG00000086300; Tissue enhanced (liver).
DR MalaCards; SNX10; -.
DR MIM; 614780; gene.
DR MIM; 615085; phenotype.
DR neXtProt; NX_Q9Y5X0; -.
DR OpenTargets; ENSG00000086300; -.
DR Orphanet; 667; Autosomal recessive malignant osteopetrosis.
DR PharmGKB; PA37950; -.
DR VEuPathDB; HostDB:ENSG00000086300; -.
DR eggNOG; KOG2527; Eukaryota.
DR GeneTree; ENSGT00940000156007; -.
DR HOGENOM; CLU_057172_4_0_1; -.
DR InParanoid; Q9Y5X0; -.
DR OMA; FPVEHEE; -.
DR OrthoDB; 24858at2759; -.
DR PhylomeDB; Q9Y5X0; -.
DR TreeFam; TF332117; -.
DR PathwayCommons; Q9Y5X0; -.
DR SignaLink; Q9Y5X0; -.
DR BioGRID-ORCS; 29887; 14 hits in 1077 CRISPR screens.
DR GenomeRNAi; 29887; -.
DR Pharos; Q9Y5X0; Tbio.
DR PRO; PR:Q9Y5X0; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9Y5X0; protein.
DR Bgee; ENSG00000086300; Expressed in lateral nuclear group of thalamus and 176 other tissues.
DR ExpressionAtlas; Q9Y5X0; baseline and differential.
DR Genevisible; Q9Y5X0; HS.
DR GO; GO:0090651; C:apical cytoplasm; IEA:Ensembl.
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; IDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030141; C:secretory granule; IEA:Ensembl.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; IMP:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:Ensembl.
DR GO; GO:0007032; P:endosome organization; IMP: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; IMP:UniProtKB.
DR GO; GO:0061512; P:protein localization to cilium; IMP: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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cilium biogenesis/degradation;
KW Cytoplasm; Cytoskeleton; Disease variant; Endosome; Lipid-binding;
KW Membrane; Osteopetrosis; Protein transport; Reference proteome; Transport.
FT CHAIN 1..201
FT /note="Sorting nexin-10"
FT /id="PRO_0000213854"
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:0000269|PubMed:21844891"
FT REGION 156..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..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:0000305"
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:0000305"
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:0000305"
FT VAR_SEQ 1..84
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045920"
FT VARIANT 16
FT /note="R -> L (in OPTB8; dbSNP:rs779298714)"
FT /evidence="ECO:0000269|PubMed:23280965"
FT /id="VAR_069299"
FT VARIANT 32
FT /note="Y -> S (in OPTB8; dbSNP:rs771038257)"
FT /evidence="ECO:0000269|PubMed:23280965"
FT /id="VAR_069300"
FT VARIANT 51
FT /note="R -> P (in OPTB8)"
FT /evidence="ECO:0000269|PubMed:23280965"
FT /id="VAR_069301"
FT VARIANT 51
FT /note="R -> Q (in OPTB8; increased expression, produces
FT extensive cytoplasmic vacuolation and impairs bone
FT resorptive function; dbSNP:rs398123011)"
FT /evidence="ECO:0000269|PubMed:22499339"
FT /id="VAR_069302"
FT VARIANT 187
FT /note="S -> I (in dbSNP:rs1053042)"
FT /evidence="ECO:0000269|PubMed:11485546"
FT /id="VAR_046098"
FT MUTAGEN 53
FT /note="R->A: Abolishes vacuolization induced by
FT overexpression."
FT /evidence="ECO:0000269|PubMed:17012226"
FT MUTAGEN 79
FT /note="K->A: Slightly reduced vacuolization induced by
FT overexpression."
FT /evidence="ECO:0000269|PubMed:17012226"
FT MUTAGEN 94
FT /note="R->A: Reduced vacuolization induced by
FT overexpression."
FT /evidence="ECO:0000269|PubMed:17012226"
FT STRAND 11..22
FT /evidence="ECO:0007829|PDB:4ON3"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:4PZG"
FT STRAND 29..38
FT /evidence="ECO:0007829|PDB:4ON3"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:4ON3"
FT HELIX 54..67
FT /evidence="ECO:0007829|PDB:4ON3"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:4ON3"
FT HELIX 88..106
FT /evidence="ECO:0007829|PDB:4ON3"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:4ON3"
FT HELIX 115..122
FT /evidence="ECO:0007829|PDB:4ON3"
FT HELIX 127..134
FT /evidence="ECO:0007829|PDB:4ON3"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:6KOK"
FT HELIX 142..153
FT /evidence="ECO:0007829|PDB:6KOK"
SQ SEQUENCE 201 AA; 23598 MW; 665B80734D5E5C72 CRC64;
MFPEQQKEEF VSVWVRDPRI QKEDFWHSYI DYEICIHTNS MCFTMKTSCV RRRYREFVWL
RQRLQSNALL VQLPELPSKN LFFNMNNRQH VDQRRQGLED FLRKVLQNAL LLSDSSLHLF
LQSHLNSEDI EACVSGQTKY SVEEAIHKFA LMNRRFPEED EEGKKENDID YDSESSSSGL
GHSSDDSSSH GCKVNTAPQE S
