SNX4_MOUSE
ID SNX4_MOUSE Reviewed; 450 AA.
AC Q91YJ2;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Sorting nexin-4 {ECO:0000303|PubMed:12668730};
GN Name=Snx4 {ECO:0000303|PubMed:12668730, ECO:0000312|MGI:MGI:1916400};
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;
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=Czech II; TISSUE=Mammary tumor;
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 INTERACTION WITH BIN1.
RX PubMed=12668730; DOI=10.1242/jcs.00403;
RA Leprince C., Le Scolan E., Meunier B., Fraisier V., Brandon N.,
RA De Gunzburg J., Camonis J.;
RT "Sorting nexin 4 and amphiphysin 2, a new partnership between endocytosis
RT and intracellular trafficking.";
RL J. Cell Sci. 116:1937-1948(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC 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: Involved in the regulation of endocytosis and in several
CC stages of intracellular trafficking. Plays a role in recycling
CC endocytosed transferrin receptor and prevent its degradation. Involved
CC in autophagosome assembly by regulating trafficking and recycling of
CC phospholipid scramblase ATG9A. {ECO:0000250|UniProtKB:O95219}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with SNX7 or SNX30 (By
CC similarity). Interacts with WWC1/KIBRA (By similarity). Identified in a
CC complex with WWC1/KIBRA and dynein components DYNLL1 and DYNC1I2 (By
CC similarity). Interacts with BIN1 (PubMed:12668730).
CC {ECO:0000250|UniProtKB:O95219, ECO:0000269|PubMed:12668730}.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000250|UniProtKB:O95219}.
CC Early endosome membrane {ECO:0000250|UniProtKB:O95219}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:O95219}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O95219}. Note=Also detected on a juxtanuclear
CC endocytic recycling compartment (ERC). {ECO:0000250|UniProtKB:O95219}.
CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is
CC necessary for peripheral membrane localization.
CC {ECO:0000250|UniProtKB:Q96L94}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; AK135356; BAE22501.1; -; mRNA.
DR EMBL; BC016599; AAH16599.1; -; mRNA.
DR CCDS; CCDS28129.1; -.
DR RefSeq; NP_542124.1; NM_080557.2.
DR AlphaFoldDB; Q91YJ2; -.
DR SMR; Q91YJ2; -.
DR BioGRID; 213257; 15.
DR STRING; 10090.ENSMUSP00000023502; -.
DR iPTMnet; Q91YJ2; -.
DR PhosphoSitePlus; Q91YJ2; -.
DR EPD; Q91YJ2; -.
DR jPOST; Q91YJ2; -.
DR MaxQB; Q91YJ2; -.
DR PaxDb; Q91YJ2; -.
DR PeptideAtlas; Q91YJ2; -.
DR PRIDE; Q91YJ2; -.
DR ProteomicsDB; 261304; -.
DR Antibodypedia; 1370; 272 antibodies from 32 providers.
DR DNASU; 69150; -.
DR Ensembl; ENSMUST00000023502; ENSMUSP00000023502; ENSMUSG00000022808.
DR GeneID; 69150; -.
DR KEGG; mmu:69150; -.
DR UCSC; uc007yzz.1; mouse.
DR CTD; 8723; -.
DR MGI; MGI:1916400; Snx4.
DR VEuPathDB; HostDB:ENSMUSG00000022808; -.
DR eggNOG; KOG2273; Eukaryota.
DR GeneTree; ENSGT00930000151029; -.
DR HOGENOM; CLU_057138_0_0_1; -.
DR InParanoid; Q91YJ2; -.
DR OMA; QKSGHYL; -.
DR OrthoDB; 632390at2759; -.
DR PhylomeDB; Q91YJ2; -.
DR TreeFam; TF328543; -.
DR BioGRID-ORCS; 69150; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Snx4; mouse.
DR PRO; PR:Q91YJ2; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q91YJ2; protein.
DR Bgee; ENSMUSG00000022808; Expressed in atrioventricular valve and 259 other tissues.
DR ExpressionAtlas; Q91YJ2; baseline and differential.
DR Genevisible; Q91YJ2; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0031201; C:SNARE complex; ISO:MGI.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; ISO:MGI.
DR GO; GO:0005158; F:insulin receptor binding; ISO:MGI.
DR GO; GO:1990460; F:leptin receptor binding; ISO:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR GO; GO:1990459; F:transferrin receptor binding; ISO:MGI.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; ISS:UniProtKB.
DR GO; GO:1903595; P:positive regulation of histamine secretion by mast cell; ISO:MGI.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR CDD; cd07622; BAR_SNX4; 1.
DR CDD; cd06864; PX_SNX4; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR034902; PX_SNX4.
DR InterPro; IPR034783; SNX4.
DR InterPro; IPR037430; SNX4_BAR.
DR PANTHER; PTHR46596; PTHR46596; 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 Acetylation; Endosome; Lipid-binding; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..450
FT /note="Sorting nexin-4"
FT /id="PRO_0000236197"
FT DOMAIN 61..187
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106
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:Q3UR97"
FT BINDING 108
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 132
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 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O95219"
SQ SEQUENCE 450 AA; 51778 MW; 533F8305BFE077EE CRC64;
MEQAPPDPEK LLQPGPLEPL GGPGAVLEAA VGEENEGTRE DGSGVDTMTG NNFWLKKIEI
SVSEAEKRTG RNAVNMQETY TAYLIETRSV EHADGQSVLT DSLWRRYSEF ELLRNYLLVY
YPHVVVPPLP EKRAEFVWHK LSADNMDPDF VERRRVGLEN FLLRVASHPV LCRDKIFYSF
LTQEGNWKET VNETGFQLKA DSRLKALNAT FRVKNPDKRF TELRHYSDEL QSVISHLLRV
RARVADRLYG VYKVHGNYGR VFSEWSAIEK EMGDGLQSAG HHMDVYASSI DDILEDEEHY
ADQLKEYLFY AEALRAVCRK HELMQYDLET AAQDLAAKKQ QCEELATGTV RTFSLKGMTT
KLFGQETPEQ REARIKVLEE QINEGEQQLK SKNLEGREFV KNAWADIERF KEQKNRDLKE
ALISYAVMQI SMCKKGIQVW TNAKECFSKM
