SNX33_XENLA
ID SNX33_XENLA Reviewed; 550 AA.
AC Q6NRL2;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Sorting nexin-33;
DE AltName: Full=SH3 and PX domain-containing protein 3;
GN Name=snx33; Synonyms=sh3px3;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2004) 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}.
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; BC070737; AAH70737.1; -; mRNA.
DR RefSeq; NP_001084772.1; NM_001091303.1.
DR RefSeq; XP_018109698.1; XM_018254209.1.
DR RefSeq; XP_018109699.1; XM_018254210.1.
DR AlphaFoldDB; Q6NRL2; -.
DR SMR; Q6NRL2; -.
DR MaxQB; Q6NRL2; -.
DR PRIDE; Q6NRL2; -.
DR DNASU; 431808; -.
DR GeneID; 431808; -.
DR KEGG; xla:431808; -.
DR CTD; 431808; -.
DR Xenbase; XB-GENE-955371; snx33.S.
DR OMA; TENRIIC; -.
DR OrthoDB; 811995at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 431808; Expressed in ovary and 19 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:0035091; F:phosphatidylinositol binding; IEA:InterPro.
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:0097320; P:plasma membrane tubulation; ISS:UniProtKB.
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 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..550
FT /note="Sorting nexin-33"
FT /id="PRO_0000311950"
FT DOMAIN 1..61
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 206..316
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 347..550
FT /note="BAR"
FT REGION 62..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..105
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 550 AA; 63323 MW; 0E323681395CAA5F CRC64;
MALKARALYS FQGENKEEIN LMENEELQLL SDVSLDGWLQ GTNSRGQTGL FPASYVEIQS
SRSGSVQVDY SGNAREYTDP PHQGSYDDDD EEDDDDWDDW DDGQTVVDEP SGSNGVSRSE
LQHHHHYSRP EYSHRPRPAL ERQDSIASGK RGSVVGRNLN RFSSFVRSGV EAFVLGDVPQ
FGGVAESHAI EMAPKGPQWK ANPRPFNCSV EEPTKQTKFK GIKSYISYRL TPDHSNSPVY
RRYKHFDWLY NRLLHKFTVI SLPHLPEKQA TGRFEEDFIQ KRKRRLVLWM DHMTSHPVLS
QYDGFQHFLG CQDEKQWKAG KRRAERDELV GASFLLTLQL PTEHQDLQDV EERVDVFKAF
SKKMDESVLQ LSSVVSELAR KHLGGFRKEF QKLGAAFQGL SHSFQLDPPY SSEPLVGAIS
HTGRTYEAVG EMFAEQPKND QFRFLDTLSL YQGLLSNFPD IIHLQKGAFA KVKDSQRMSD
EGRMEQDEAD GVRKRCRVVG FALQAEINHF HQRRLLDFKQ AIQHYLKEQI IFYRRVSQEL
EKTLHLYDEL
