SNX33_MOUSE
ID SNX33_MOUSE Reviewed; 574 AA.
AC Q4VAA7; Q8BPM5; Q8C832;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Sorting nexin-33;
DE AltName: Full=SH3 and PX domain-containing protein 3;
GN Name=Snx33; Synonyms=Sh3px3;
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=Eye, Head, and Heart;
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 TISSUE SPECIFICITY.
RX PubMed=18353773; DOI=10.1074/jbc.m801531200;
RA Schobel S., Neumann S., Hertweck M., Dislich B., Kuhn P.H., Kremmer E.,
RA Seed B., Baumeister R., Haass C., Lichtenthaler S.F.;
RT "A novel sorting nexin modulates endocytic trafficking and alpha-secretase
RT cleavage of the amyloid precursor protein.";
RL J. Biol. Chem. 283:14257-14268(2008).
RN [4]
RP INTERACTION WITH FCHSD1.
RX PubMed=26567222; DOI=10.1242/jcs.178699;
RA Ukken F.P., Bruckner J.J., Weir K.L., Hope S.J., Sison S.L.,
RA Birschbach R.M., Hicks L., Taylor K.L., Dent E.W., Gonsalvez G.B.,
RA O'Connor-Giles K.M.;
RT "BAR-SH3 sorting nexins are conserved interacting proteins of Nervous wreck
RT that organize synapses and promote neurotransmission.";
RL J. Cell Sci. 129:166-177(2016).
CC -!- FUNCTION: Plays a role in the reorganization of the cytoskeleton,
CC endocytosis and cellular vesicle trafficking via its interactions with
CC membranes, WASL, DNM1 and DNM2. Acts both during interphase and at the
CC end of mitotic cell divisions. Required for efficient progress through
CC mitosis and cytokinesis. Required for normal formation of the cleavage
CC furrow at the end of mitosis. Modulates endocytosis of cell-surface
CC proteins, such as APP and PRNP; this then modulates the secretion of
CC APP and PRNP peptides. Promotes membrane tubulation (in vitro). May
CC promote the formation of macropinosomes (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (via BAR domain). Interacts with ADAM15. Interacts
CC with FASLG. Interacts (via SH3 domain) with DNM1 and DNM2. Interacts
CC with WASL (By similarity). Interacts with FCHSD1 (via the F-BAR domain)
CC (PubMed:26567222). {ECO:0000250, ECO:0000269|PubMed:26567222}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Note=Primarily detected in the cytosol. A minor
CC proportion is membrane-bound (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level).
CC {ECO:0000269|PubMed:18353773}.
CC -!- DOMAIN: The PX and BAR domains mediate association with membranes and
CC are required for membrane tubulation. {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; AK048566; BAC33376.1; -; mRNA.
DR EMBL; AK053761; BAC35511.1; -; mRNA.
DR EMBL; AK142274; BAE25004.1; -; mRNA.
DR EMBL; BC096472; AAH96472.1; -; mRNA.
DR CCDS; CCDS23212.1; -.
DR RefSeq; NP_780692.2; NM_175483.5.
DR RefSeq; XP_006511154.1; XM_006511091.2.
DR AlphaFoldDB; Q4VAA7; -.
DR SMR; Q4VAA7; -.
DR BioGRID; 231655; 3.
DR IntAct; Q4VAA7; 1.
DR MINT; Q4VAA7; -.
DR STRING; 10090.ENSMUSP00000060225; -.
DR iPTMnet; Q4VAA7; -.
DR PhosphoSitePlus; Q4VAA7; -.
DR EPD; Q4VAA7; -.
DR jPOST; Q4VAA7; -.
DR MaxQB; Q4VAA7; -.
DR PaxDb; Q4VAA7; -.
DR PeptideAtlas; Q4VAA7; -.
DR PRIDE; Q4VAA7; -.
DR ProteomicsDB; 261303; -.
DR Antibodypedia; 27355; 136 antibodies from 23 providers.
DR DNASU; 235406; -.
DR Ensembl; ENSMUST00000050916; ENSMUSP00000060225; ENSMUSG00000032733.
DR GeneID; 235406; -.
DR KEGG; mmu:235406; -.
DR UCSC; uc009ptp.1; mouse.
DR CTD; 257364; -.
DR MGI; MGI:2443239; Snx33.
DR VEuPathDB; HostDB:ENSMUSG00000032733; -.
DR eggNOG; KOG2528; Eukaryota.
DR GeneTree; ENSGT00940000160162; -.
DR HOGENOM; CLU_021494_3_0_1; -.
DR InParanoid; Q4VAA7; -.
DR OMA; KHMMQSY; -.
DR OrthoDB; 811995at2759; -.
DR PhylomeDB; Q4VAA7; -.
DR TreeFam; TF314082; -.
DR BioGRID-ORCS; 235406; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q4VAA7; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q4VAA7; protein.
DR Bgee; ENSMUSG00000032733; Expressed in otolith organ and 189 other tissues.
DR Genevisible; Q4VAA7; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0036089; P:cleavage furrow formation; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
DR GO; GO:0007032; P:endosome organization; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0044351; P:macropinocytosis; ISS:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0045806; P:negative regulation of endocytosis; ISO:MGI.
DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; ISO:MGI.
DR GO; GO:0097320; P:plasma membrane tubulation; ISS:UniProtKB.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; ISO:MGI.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISO:MGI.
DR GO; GO:0017038; P:protein import; ISO:MGI.
DR CDD; cd07669; BAR_SNX33; 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; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR028642; SNX33.
DR InterPro; IPR037427; SNX33_BAR.
DR InterPro; IPR014536; Snx9_fam.
DR InterPro; IPR019497; Sorting_nexin_WASP-bd-dom.
DR PANTHER; PTHR45827:SF3; PTHR45827:SF3; 1.
DR Pfam; PF10456; BAR_3_WASP_bdg; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PIRSF; PIRSF027744; Snx9; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Cytoplasmic vesicle; Endocytosis;
KW Membrane; Mitosis; Phosphoprotein; Protein transport; Reference proteome;
KW SH3 domain; Transport.
FT CHAIN 1..574
FT /note="Sorting nexin-33"
FT /id="PRO_0000311949"
FT DOMAIN 1..61
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 230..340
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 371..574
FT /note="BAR"
FT REGION 79..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WV41"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WV41"
FT CONFLICT 10
FT /note="D -> Y (in Ref. 1; BAC35511)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="H -> N (in Ref. 1; BAC35511)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="K -> E (in Ref. 1; BAC33376)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 65315 MW; 9F4CED2567D7DB2E CRC64;
MALKGRALYD FHSENKEEIS IQQDEELVIF SETSLDGWLQ GQNSRGETGL FPASYVEIVR
PGISTNHVDY SNSPAGSLGT QGSLYSSPSM ASPARSGGGS GFLSNPGSFE DDDDDDWDDW
DDGCTVVEEP LAGGLGTNGH PPLNLSYPGA YPNQHMAFRP KAPLERQDSL ASAKRGSVVG
RNLNRFSCFV RSGVEAFILG DVPMMAKIAE TYSIEMGPRG PQWKANPHPF ACSIEDPTKQ
TKFKGIKSYI SYKLTPTHAG SPVYRRYKHF DWLYNRLLHK FTVISVPHLP EKQATGRFEE
DFIEKRKRRL ILWMDHMTSH PVLSQYEGFQ HFLSCLDDKQ WKMGKRRAEK DEMVGASFLL
TFQIPTEHQD LQDVEDRVDT FKAFSKKMDD SVLQLSNVAA ELVRKHVGGF RKEFQKLGSA
FQAISHAFQM DPPFRSDALN NAISHTGRTY ETVGEMFAEQ PKHDLFQMLD TLSLYQGLLS
NFPDIIHLQK GAFAKVKESQ RMSDEGRMAQ EEADGIRRRC RVVGFALQAE MNHFHQRREL
DFKHMMQSYL RQQILFYQRV GQQLEKTLHM YDHL
