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   27-MAR-2024, entry version 144.
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; 16.
DR   STRING; 10090.ENSMUSP00000023502; -.
DR   iPTMnet; Q91YJ2; -.
DR   PhosphoSitePlus; Q91YJ2; -.
DR   SwissPalm; Q91YJ2; -.
DR   EPD; Q91YJ2; -.
DR   jPOST; Q91YJ2; -.
DR   MaxQB; Q91YJ2; -.
DR   PaxDb; 10090-ENSMUSP00000023502; -.
DR   PeptideAtlas; Q91YJ2; -.
DR   ProteomicsDB; 261304; -.
DR   Pumba; Q91YJ2; -.
DR   Antibodypedia; 1370; 306 antibodies from 32 providers.
DR   DNASU; 69150; -.
DR   Ensembl; ENSMUST00000023502.6; ENSMUSP00000023502.5; ENSMUSG00000022808.6.
DR   GeneID; 69150; -.
DR   KEGG; mmu:69150; -.
DR   UCSC; uc007yzz.1; mouse.
DR   AGR; MGI:1916400; -.
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; 5475877at2759; -.
DR   PhylomeDB; Q91YJ2; -.
DR   TreeFam; TF328543; -.
DR   BioGRID-ORCS; 69150; 3 hits in 77 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 263 other cell types or tissues.
DR   ExpressionAtlas; Q91YJ2; baseline and differential.
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:0098830; C:presynaptic endosome; IDA:SynGO.
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; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 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; SORTING NEXIN-4; 1.
DR   PANTHER; PTHR46596:SF1; SORTING NEXIN-4; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   PROSITE; PS50195; PX; 1.
DR   Genevisible; Q91YJ2; MM.
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
//