SNX11_MOUSE
ID SNX11_MOUSE Reviewed; 271 AA.
AC Q91WL6; Q3V3A6;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Sorting nexin-11;
GN Name=Snx11;
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=Skin, and Thymus;
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; TISSUE=Kidney;
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].
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: Phosphoinositide-binding protein involved in protein sorting
CC and membrane trafficking in endosomes. {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endosome
CC {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; AK042409; BAE20632.1; -; mRNA.
DR EMBL; AK076332; BAC36302.1; -; mRNA.
DR EMBL; BC014719; AAH14719.1; -; mRNA.
DR CCDS; CCDS25302.1; -.
DR RefSeq; NP_001156861.1; NM_001163389.1.
DR RefSeq; NP_083241.1; NM_028965.4.
DR RefSeq; XP_006534438.1; XM_006534375.3.
DR RefSeq; XP_011247591.1; XM_011249289.2.
DR AlphaFoldDB; Q91WL6; -.
DR SMR; Q91WL6; -.
DR STRING; 10090.ENSMUSP00000021246; -.
DR iPTMnet; Q91WL6; -.
DR PhosphoSitePlus; Q91WL6; -.
DR SwissPalm; Q91WL6; -.
DR EPD; Q91WL6; -.
DR MaxQB; Q91WL6; -.
DR PaxDb; Q91WL6; -.
DR PRIDE; Q91WL6; -.
DR ProteomicsDB; 261300; -.
DR Antibodypedia; 30244; 137 antibodies from 21 providers.
DR DNASU; 74479; -.
DR Ensembl; ENSMUST00000021246; ENSMUSP00000021246; ENSMUSG00000020876.
DR Ensembl; ENSMUST00000107661; ENSMUSP00000103288; ENSMUSG00000020876.
DR GeneID; 74479; -.
DR KEGG; mmu:74479; -.
DR UCSC; uc007lci.2; mouse.
DR CTD; 29916; -.
DR MGI; MGI:1921729; Snx11.
DR VEuPathDB; HostDB:ENSMUSG00000020876; -.
DR eggNOG; KOG2527; Eukaryota.
DR GeneTree; ENSGT00940000160113; -.
DR HOGENOM; CLU_057172_3_0_1; -.
DR InParanoid; Q91WL6; -.
DR OMA; DQPNSCC; -.
DR OrthoDB; 1407986at2759; -.
DR PhylomeDB; Q91WL6; -.
DR TreeFam; TF332117; -.
DR BioGRID-ORCS; 74479; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Snx11; mouse.
DR PRO; PR:Q91WL6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q91WL6; protein.
DR Bgee; ENSMUSG00000020876; Expressed in granulocyte and 141 other tissues.
DR ExpressionAtlas; Q91WL6; baseline and differential.
DR Genevisible; Q91WL6; MM.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016050; P:vesicle organization; ISS:UniProtKB.
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 Endosome; Lipid-binding; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..271
FT /note="Sorting nexin-11"
FT /id="PRO_0000213857"
FT DOMAIN 16..132
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 135..139
FT /note="Important for membrane trafficking"
FT /evidence="ECO:0000250"
FT REGION 185..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59
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 85
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 99
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 271 AA; 30431 MW; D1921CBD70477456 CRC64;
MGLWYRMLEN QDLEEVITVR VQDPRVQNEG SWNSYVDYKI FLHTNSKAFT AKTSCVRRRY
REFVWLRKQL QRNAGLVPVP ELPGKSTFFG GSDEFIEKRR QGLQHFLEKV LQSVVLLSDS
QLHLFLQSQL SVPEIEACVQ GRGAMTVSDA ILSYAMSNCG WAQEERQSTS HLAKGDQLNS
CCFLPRSGRR SSPSPPLSEE KEQLETWAPV MDSEGPSSES PTLLPSSSLP ACWDPARPEE
GLSVSQPARR AVAADQAGPM EPTQLDTAWD K
