SNX21_MOUSE
ID SNX21_MOUSE Reviewed; 363 AA.
AC Q3UR97;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Sorting nexin-21 {ECO:0000305};
GN Name=Snx21 {ECO:0000312|MGI:MGI:1917729};
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=Embryo;
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] {ECO:0000312|Ensembl:ENSMUSP00000054137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Ensembl:ENSMUSP00000054137};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0007744|PDB:4YMR}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 230-363, SUBUNIT, SUBCELLULAR
RP LOCATION, DOMAIN, AND MUTAGENESIS OF ARG-161.
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: Binds to membranes enriched in phosphatidylinositol 3-
CC phosphate (PtdIns(P3)) and phosphatidylinositol 4,5-bisphosphate
CC (PubMed:25882846). May be involved in several stages of intracellular
CC trafficking. {ECO:0000269|PubMed:25882846, ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:25882846}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000305|PubMed:25882846}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Early endosome membrane
CC {ECO:0000269|PubMed:25882846}; Peripheral membrane protein
CC {ECO:0000269|PubMed:25882846}; Cytoplasmic side
CC {ECO:0000269|PubMed:25882846}.
CC -!- DOMAIN: The PX domain mediates specific binding to membranes enriched
CC in phosphatidylinositol 3-phosphate (PtdIns(P3)).
CC {ECO:0000269|PubMed:25882846}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL591127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK141663; BAE24791.1; -; mRNA.
DR CCDS; CCDS38328.1; -.
DR RefSeq; NP_598685.2; NM_133924.3.
DR PDB; 4YMR; X-ray; 2.40 A; A/B=230-363.
DR PDBsum; 4YMR; -.
DR AlphaFoldDB; Q3UR97; -.
DR SMR; Q3UR97; -.
DR STRING; 10090.ENSMUSP00000054137; -.
DR iPTMnet; Q3UR97; -.
DR PhosphoSitePlus; Q3UR97; -.
DR MaxQB; Q3UR97; -.
DR PaxDb; Q3UR97; -.
DR PeptideAtlas; Q3UR97; -.
DR PRIDE; Q3UR97; -.
DR ProteomicsDB; 261541; -.
DR Antibodypedia; 27775; 82 antibodies from 17 providers.
DR DNASU; 101113; -.
DR Ensembl; ENSMUST00000056181; ENSMUSP00000054137; ENSMUSG00000050373.
DR GeneID; 101113; -.
DR KEGG; mmu:101113; -.
DR UCSC; uc008nwc.1; mouse.
DR CTD; 90203; -.
DR MGI; MGI:1917729; Snx21.
DR VEuPathDB; HostDB:ENSMUSG00000050373; -.
DR eggNOG; KOG2101; Eukaryota.
DR GeneTree; ENSGT00530000063759; -.
DR HOGENOM; CLU_059132_0_0_1; -.
DR InParanoid; Q3UR97; -.
DR OMA; EAQEHCD; -.
DR OrthoDB; 1322681at2759; -.
DR PhylomeDB; Q3UR97; -.
DR TreeFam; TF326807; -.
DR BioGRID-ORCS; 101113; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Snx21; mouse.
DR PRO; PR:Q3UR97; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q3UR97; protein.
DR Bgee; ENSMUSG00000050373; Expressed in hindlimb stylopod muscle and 200 other tissues.
DR ExpressionAtlas; Q3UR97; baseline and differential.
DR Genevisible; Q3UR97; MM.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
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 3D-structure; Cytoplasmic vesicle; Endosome; Lipid-binding; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..363
FT /note="Sorting nexin-21"
FT /id="PRO_0000434600"
FT DOMAIN 119..236
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..73
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 161
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 163
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 188
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 202
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 MUTAGEN 161
FT /note="R->Q: Abolishes location on endosome membranes.
FT Abolishes binding to membranes enriched in
FT phosphatidylinositol 3-phosphate. No significant effect on
FT binding to membranes enriched in phosphatidylinositol 4,5-
FT bisphosphate."
FT /evidence="ECO:0000269|PubMed:25882846"
FT HELIX 231..243
FT /evidence="ECO:0007829|PDB:4YMR"
FT HELIX 246..262
FT /evidence="ECO:0007829|PDB:4YMR"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:4YMR"
FT HELIX 271..285
FT /evidence="ECO:0007829|PDB:4YMR"
FT HELIX 289..304
FT /evidence="ECO:0007829|PDB:4YMR"
FT HELIX 312..325
FT /evidence="ECO:0007829|PDB:4YMR"
FT HELIX 331..341
FT /evidence="ECO:0007829|PDB:4YMR"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:4YMR"
FT HELIX 353..359
FT /evidence="ECO:0007829|PDB:4YMR"
SQ SEQUENCE 363 AA; 40308 MW; 076DEBEA6EA7AC4F CRC64;
MASRLLHRLR HALASDGPGE AAAGPEAEQF PESSELEDDD AEGLSSRLSG TLSFTSAEDD
PDDEDEDDEA GLDSPPSGDG ASGEDAERSP PPDGQRSSQL LARQLQDFWK KSRNTLVPQR
LLFEVTSANV VKDPPSKYVL YTLAVMGPGP PDRQPAQISR RYSDFERLHR NLQRQFRGPM
SAISFPRKRL RRNFTAETIA RRSRAFEQFL GHLQAVPELR QAPDLQDFFV LPELRRAQSL
TCTGLYREAL ALWANAWQLQ TQLGTPSGPD RPLLTLAGLA VCHQELEDPG EARACSEKAL
QLLGDKRPHP FLAPFLEAHV RLSWRLGLDK RQSEAQLQAL QEAGLTSTPP PSLKELLIKE
VLD