SNX20_MOUSE
ID SNX20_MOUSE Reviewed; 313 AA.
AC Q9D2Y5; Q3U0B6; Q544B6; Q8CHQ3;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Sorting nexin-20;
GN Name=Snx20;
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 [MRNA].
RC STRAIN=C57BL/6J;
RA Hong W.;
RT "A new member (SNX20) of the sorting nexin protein family.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cecum, Spleen, 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Lung;
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 DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=18196517; DOI=10.1002/eji.200737777;
RA Schaff U.Y., Shih H.H., Lorenz M., Sako D., Kriz R., Milarski K., Bates B.,
RA Tchernychev B., Shaw G.D., Simon S.I.;
RT "SLIC-1/sorting nexin 20: a novel sorting nexin that directs subcellular
RT distribution of PSGL-1.";
RL Eur. J. Immunol. 38:550-564(2008).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ARG-113, AND LACK OF
RP INTERACTION WITH SELPLG.
RX PubMed=25882846; DOI=10.1074/jbc.m115.650598;
RA Clairfeuille T., Norwood S.J., Qi X., Teasdale R.D., Collins B.M.;
RT "Structure and membrane binding properties of the endosomal
RT tetratricopeptide repeat (TPR) domain-containing sorting nexins SNX20 and
RT SNX21.";
RL J. Biol. Chem. 290:14504-14517(2015).
CC -!- FUNCTION: May play a role in cellular vesicle trafficking
CC (PubMed:25882846). Has been proposed to function as a sorting protein
CC that targets SELPLG into endosomes, but has no effect on SELPLG
CC internalization from the cell surface, nor on SELPLG-mediated cell-cell
CC adhesion (PubMed:18196517). {ECO:0000269|PubMed:18196517,
CC ECO:0000305|PubMed:25882846}.
CC -!- SUBUNIT: Interacts with SELPLG (By similarity). Interaction with SELPLG
CC is controversial and was not detected in PubMed:25882846.
CC {ECO:0000250|UniProtKB:Q7Z614, ECO:0000269|PubMed:25882846}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000269|PubMed:25882846}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q7Z614}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q7Z614}. Cell membrane
CC {ECO:0000250|UniProtKB:Q7Z614}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q7Z614}. Nucleus {ECO:0000250|UniProtKB:Q7Z614}.
CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is
CC necessary for localization to the endosomes.
CC {ECO:0000269|PubMed:25882846}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice appear healthy and
CC normal. Neutrophils from mutant mice display unchanged Selplg-mediated
CC cell-cell adhesion and Selplg expression at the cell membrane is
CC unchanged. {ECO:0000269|PubMed:18196517}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; AF395844; AAK73125.1; -; mRNA.
DR EMBL; AK157032; BAE33939.1; -; mRNA.
DR EMBL; AK018632; BAB31317.1; -; mRNA.
DR EMBL; AK042068; BAC31150.1; -; mRNA.
DR EMBL; BC039809; AAH39809.1; -; mRNA.
DR CCDS; CCDS22512.1; -.
DR RefSeq; NP_082116.1; NM_027840.3.
DR RefSeq; XP_006531434.1; XM_006531371.2.
DR AlphaFoldDB; Q9D2Y5; -.
DR SMR; Q9D2Y5; -.
DR IntAct; Q9D2Y5; 1.
DR MINT; Q9D2Y5; -.
DR STRING; 10090.ENSMUSP00000034087; -.
DR iPTMnet; Q9D2Y5; -.
DR PhosphoSitePlus; Q9D2Y5; -.
DR EPD; Q9D2Y5; -.
DR MaxQB; Q9D2Y5; -.
DR PaxDb; Q9D2Y5; -.
DR PRIDE; Q9D2Y5; -.
DR ProteomicsDB; 261540; -.
DR GeneID; 71607; -.
DR KEGG; mmu:71607; -.
DR UCSC; uc009mrp.1; mouse.
DR CTD; 124460; -.
DR MGI; MGI:1918857; Snx20.
DR eggNOG; KOG2101; Eukaryota.
DR InParanoid; Q9D2Y5; -.
DR OrthoDB; 1322681at2759; -.
DR PhylomeDB; Q9D2Y5; -.
DR TreeFam; TF326807; -.
DR BioGRID-ORCS; 71607; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Snx20; mouse.
DR PRO; PR:Q9D2Y5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9D2Y5; protein.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IBA:GO_Central.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR039937; SNX20/SNX21.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR20939; PTHR20939; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Endosome; Lipid-binding; Membrane; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..313
FT /note="Sorting nexin-20"
FT /id="PRO_0000213869"
FT DOMAIN 71..188
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 113
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|PubMed:25882846"
FT BINDING 115
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|UniProtKB:Q96L94"
FT BINDING 140
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|UniProtKB:Q96L94"
FT BINDING 154
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|UniProtKB:Q6P4T1"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BK61"
FT MUTAGEN 113
FT /note="R->Q: Abolishes location on endosome membranes.
FT Abolishes binding to membranes enriched in
FT phosphatidylinositol 3-phosphate. Mildly decreases binding
FT to membranes enriched in phosphatidylinositol 4,5-
FT bisphosphate."
FT /evidence="ECO:0000269|PubMed:25882846"
FT CONFLICT 29..30
FT /note="PP -> LQ (in Ref. 3; BAE33939)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="P -> S (in Ref. 3; AAH39809)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="T -> A (in Ref. 1; AAK73125 and 2; BAC31150/
FT BAB31317)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 313 AA; 36028 MW; 1DF360401D821D69 CRC64;
MASPEHPGSP GWRGPINQCR TRTRQEVLPP GPDLPCPGPE EAQDGPSSNS SMTTRELQEH
WQKEKSRWKH VRLLFEIASA RIEERKVSKF VMYQVVVIQT GSFDSDKAVV ERRYSDFERL
QKALLKRFGP ELEDVTFPRK RLTGNLSAET ICERRRELRE YLRLLYAVRA VRRSREFLDF
LTRPELREAF GCLRAGQYAR ALELLGRALP LQEKLTAHCP SAAVPALCAA LVCLRDLERP
AEAFAVGERA LRCLRTRENH RYYAPLLDAM VRLAYALGKD FAALQSRLDE NQLRRPTHRD
ATLKELTVRE YLS
