SNX4_SCHPO
ID SNX4_SCHPO Reviewed; 401 AA.
AC O14243; P78806;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Sorting nexin-4;
DE AltName: Full=Autophagy-related protein 24;
GN Name=snx4; Synonyms=atg24; ORFNames=SPAC6F6.12;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-295.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Sorting nexin, involved in the separation or division of
CC vacuoles throughout the entire life cycle of the cells. Involved in
CC retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-
CC Golgi network, for cytoplasm to vacuole transport (Cvt), autophagy,
CC mitophagy, and pexophagy. {ECO:0000250|UniProtKB:P47057}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P47057}. Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:P47057}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P47057}. Endosome membrane
CC {ECO:0000250|UniProtKB:P47057}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P47057}. Note=Endosome and other perivacuolar
CC punctate structures. Associates to phosphatidylinositol 3-phosphate,
CC necessary for peripheral membrane localization to the perivacuolar
CC punctate structures. {ECO:0000250|UniProtKB:P47057}.
CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is
CC necessary for peripheral membrane localization to the perivacuolar
CC punctate structures. {ECO:0000250|UniProtKB:Q96L94}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11735.1; -; Genomic_DNA.
DR EMBL; D89155; BAA13817.1; -; mRNA.
DR PIR; T39046; T39046.
DR PIR; T42515; T42515.
DR RefSeq; NP_593905.1; NM_001019335.2.
DR AlphaFoldDB; O14243; -.
DR SMR; O14243; -.
DR BioGRID; 278889; 12.
DR IntAct; O14243; 1.
DR STRING; 4896.SPAC6F6.12.1; -.
DR iPTMnet; O14243; -.
DR MaxQB; O14243; -.
DR PaxDb; O14243; -.
DR PRIDE; O14243; -.
DR EnsemblFungi; SPAC6F6.12.1; SPAC6F6.12.1:pep; SPAC6F6.12.
DR GeneID; 2542427; -.
DR KEGG; spo:SPAC6F6.12; -.
DR PomBase; SPAC6F6.12; -.
DR VEuPathDB; FungiDB:SPAC6F6.12; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_027221_0_0_1; -.
DR InParanoid; O14243; -.
DR OMA; QKSGHYL; -.
DR PhylomeDB; O14243; -.
DR PRO; PR:O14243; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005776; C:autophagosome; ISO:PomBase.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0000407; C:phagophore assembly site; IDA:PomBase.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISO:PomBase.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:PomBase.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:0099638; P:endosome to plasma membrane protein transport; IMP:PomBase.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; ISO:PomBase.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IBA:GO_Central.
DR GO; GO:0006623; P:protein targeting to vacuole; ISO:PomBase.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0061709; P:reticulophagy; IMP:PomBase.
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 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 Autophagy; Coiled coil; Cytoplasm; Endosome; Lipid-binding; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..401
FT /note="Sorting nexin-4"
FT /id="PRO_0000213817"
FT DOMAIN 17..139
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT COILED 190..292
FT /evidence="ECO:0000255"
FT BINDING 60
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 62
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 86
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 105
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 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 58
FT /note="R -> P (in Ref. 2; BAA13817)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="K -> R (in Ref. 2; BAA13817)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="R -> P (in Ref. 2; BAA13817)"
FT /evidence="ECO:0000305"
FT CONFLICT 293..295
FT /note="KLS -> SFL (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 401 AA; 46376 MW; 1732E3D08B85157C CRC64;
MSDSVNLDEP STNSTHFLQC LVTEPRKELQ GSRDTHVSYL IITKTNLSIF TRAECKVRRR
FSDFVKLQEI LSRMNEDCVV PPLPAKHKLE YIKGGRFSDN FINRRAKLLN RYITRCALHP
VLHQSPHFIA FLENPNWNNY VRFFIQPKLN NTSKLDEISD SLLNAFSKLK EEPTEFDIQR
DHVQQFMFGI SNLEGSIQKL LRLEKALESD YEDVSIQFDR LASLDQALDV PIESIQNALQ
QTGTEYANLT EKLTLLLDTI KDVESYAHSL KELLKRRDQK QQDVEALQEY SAKLSLERDK
ISSGGSNGFS LSKTLDDLRG IDHNDTRLKR LEHVQSELQA VEQAIQEASA VHDAFNQRVR
EESKLFDSVR QSEMLSAISD YANVHVEFFT NIRDLWIRVK Q
