SNX16_MOUSE
ID SNX16_MOUSE Reviewed; 344 AA.
AC Q8C080; Q9D525;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Sorting nexin-16;
GN Name=Snx16;
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; TISSUE=Medulla oblongata, and Testis;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Testis;
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).
CC -!- FUNCTION: May be involved in several stages of intracellular
CC trafficking. Plays a role in protein transport from early to late
CC endosomes. Plays a role in protein transport to the lysosome. Promotes
CC degradation of EGFR after EGF signaling (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer. Interacts with EGFR (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Late
CC endosome membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Lysosome {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; AK015872; BAB30011.1; -; mRNA.
DR EMBL; AK032055; BAC27673.1; -; mRNA.
DR EMBL; CH466577; EDL05159.1; -; Genomic_DNA.
DR EMBL; BC019424; AAH19424.1; -; mRNA.
DR CCDS; CCDS17244.1; -.
DR RefSeq; NP_083344.3; NM_029068.4.
DR AlphaFoldDB; Q8C080; -.
DR SMR; Q8C080; -.
DR BioGRID; 216968; 4.
DR STRING; 10090.ENSMUSP00000029047; -.
DR iPTMnet; Q8C080; -.
DR PhosphoSitePlus; Q8C080; -.
DR EPD; Q8C080; -.
DR jPOST; Q8C080; -.
DR MaxQB; Q8C080; -.
DR PaxDb; Q8C080; -.
DR PRIDE; Q8C080; -.
DR ProteomicsDB; 261596; -.
DR Antibodypedia; 12573; 139 antibodies from 29 providers.
DR DNASU; 74718; -.
DR Ensembl; ENSMUST00000029047; ENSMUSP00000029047; ENSMUSG00000027534.
DR GeneID; 74718; -.
DR KEGG; mmu:74718; -.
DR UCSC; uc008opw.3; mouse.
DR CTD; 64089; -.
DR MGI; MGI:1921968; Snx16.
DR VEuPathDB; HostDB:ENSMUSG00000027534; -.
DR eggNOG; KOG2101; Eukaryota.
DR GeneTree; ENSGT00390000005651; -.
DR InParanoid; Q8C080; -.
DR OMA; ENHETCW; -.
DR OrthoDB; 1094695at2759; -.
DR PhylomeDB; Q8C080; -.
DR TreeFam; TF324116; -.
DR BioGRID-ORCS; 74718; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Snx16; mouse.
DR PRO; PR:Q8C080; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8C080; protein.
DR Bgee; ENSMUSG00000027534; Expressed in facial nucleus and 245 other tissues.
DR ExpressionAtlas; Q8C080; baseline and differential.
DR Genevisible; Q8C080; MM.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031313; C:extrinsic component of endosome membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISS:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; ISS:UniProtKB.
DR GO; GO:0006622; P:protein targeting to lysosome; ISS:UniProtKB.
DR CDD; cd07276; PX_SNX16; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR037911; SNX16_PX.
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 Coiled coil; Cytoplasm; Endosome; Lipid-binding; Lysosome; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..344
FT /note="Sorting nexin-16"
FT /id="PRO_0000236204"
FT DOMAIN 105..218
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 223..278
FT /evidence="ECO:0000255"
FT COMPBIAS 13..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 144
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 146
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 184
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 MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 181
FT /note="L -> V (in Ref. 1; BAC27673)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 38817 MW; F8AD14C543A8EBC6 CRC64;
MATPYVPVPM PIGNSASSFT NNRNQRSSSF GSVSTSSTSS KGQLEDSAVG SLKQTNVQDQ
MDSASSMCGS PLIRTKFTGT DSSIEYSARP REAEEQHPEA VNWEDRPSTP TILGYEVMEE
RAKFTVYKIL VKKSPEESWV VFRRYTDFSR LNDKLKEMFP GFRLALPPKR WFKDNYNAEF
LEDRQLGLQA FLQNLVAHKD IANCLAVREF LCLDDPPGPF DSLEESRAFC ETLEETNYHL
QRELLEKQKE VESLKKLLGE KQLHIDALET RIRTLSLEPG ASLYVSRAEG GQILRVEPSV
LQVNRDVLDE ESRADHKPHF NSREAGSVIA GIEVAQLAYN AEDD
