SNX33_XENTR
ID SNX33_XENTR Reviewed; 549 AA.
AC Q28GP7;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Sorting nexin-33;
DE AltName: Full=SH3 and PX domain-containing protein 3;
GN Name=snx33; Synonyms=sh3px3; ORFNames=TEgg059f08.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6; TISSUE=Lung;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in the reorganization of the cytoskeleton,
CC endocytosis and cellular vesicle trafficking, both during interphase
CC and at the end of mitotic cell divisions. Required for efficient
CC progress through mitosis and cytokinesis. Required for normal formation
CC of the cleavage furrow at the end of mitosis. Modulates endocytosis of
CC cell-surface proteins. Promotes membrane tubulation (in vitro). May
CC promote the formation of macropinosomes (By similarity). {ECO:0000250}.
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 -!- DOMAIN: The PX and BAR domains mediate association with membranes and
CC are required for membrane tubulation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; CR761284; CAJ81278.1; -; mRNA.
DR EMBL; BC127346; AAI27347.1; -; mRNA.
DR RefSeq; NP_001016368.1; NM_001016368.2.
DR RefSeq; XP_012822029.1; XM_012966575.2.
DR RefSeq; XP_017947573.1; XM_018092084.1.
DR AlphaFoldDB; Q28GP7; -.
DR SMR; Q28GP7; -.
DR STRING; 8364.ENSXETP00000012456; -.
DR PaxDb; Q28GP7; -.
DR DNASU; 549122; -.
DR GeneID; 549122; -.
DR KEGG; xtr:549122; -.
DR CTD; 257364; -.
DR Xenbase; XB-GENE-955365; snx33.
DR eggNOG; KOG2528; Eukaryota.
DR InParanoid; Q28GP7; -.
DR OMA; TENRIIC; -.
DR OrthoDB; 811995at2759; -.
DR PhylomeDB; Q28GP7; -.
DR TreeFam; TF314082; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000015279; Expressed in 4-cell stage embryo and 13 other tissues.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0044351; P:macropinocytosis; ISS:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0097320; P:plasma membrane tubulation; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; 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 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cytoplasm; Cytoplasmic vesicle; Endocytosis;
KW Membrane; Mitosis; Protein transport; Reference proteome; SH3 domain;
KW Transport.
FT CHAIN 1..549
FT /note="Sorting nexin-33"
FT /id="PRO_0000311951"
FT DOMAIN 1..61
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 205..315
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 346..549
FT /note="BAR"
FT REGION 66..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..104
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 549 AA; 63298 MW; 6B710F060621699A CRC64;
MALKARALYS FQGENKEEIN ILENEELHLF SDVSLDGWLQ GTNSRGQTGL FPASYVEILR
PRSGSVQVDY SGHTQGYTDS PHQGSYDDDE EDDDDWDDWD DGQTVVDEPS GSNGVSRSQL
QHHHHYPRPE YTHRPRPALE RQDSIASGKR GSVVGRNLNR FSSFVRSGVE AFVLGDVPQF
GGVSESHAIE MGPKGPQWKA NPRPFSCSVE EPTKQTKFKG IKSYISYRLT PDPCNSPVYR
RYKHFDWLYN RLLHKFTVIS VPHLPEKQAT GRFEEDFIQK RKRRLVLWMD HMTSHPVLSQ
YDGFQHFLSC QDEKQWKAGK RRAERDELVG ASFLLTLQLP TEHQDLQDVE ERVDVFKAFS
KKMDENVLQL SSVVSELARK HLGGFRKEFQ RLGAALQGLS HSFQLDPPYS SEPLVGAISH
TGRTYEAVGE MFAEQPKNDQ FRFLDTLSLY QGLLSNFPDI IHLQKGAFAK VKESQRMSDE
GRMEQDEADG IRKRCRVVGF ALQAEINHFH QRRLQDFKQA IQHYLKEQIL FYRRVSQELE
KTLHMYDDL
