SNX30_HUMAN
ID SNX30_HUMAN Reviewed; 437 AA.
AC Q5VWJ9;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Sorting nexin-30 {ECO:0000303|PubMed:32513819};
GN Name=SNX30 {ECO:0000303|PubMed:32513819, ECO:0000312|HGNC:HGNC:23685};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SNX4.
RX PubMed=32513819; DOI=10.1242/jcs.246306;
RA Anton Z., Betin V.M.S., Simonetti B., Traer C.J., Attar N., Cullen P.J.,
RA Lane J.D.;
RT "A heterodimeric SNX4--SNX7 SNX-BAR autophagy complex coordinates ATG9A
RT trafficking for efficient autophagosome assembly.";
RL J. Cell Sci. 133:0-0(2020).
CC -!- FUNCTION: Involved in the regulation of endocytosis and in several
CC stages of intracellular trafficking (PubMed:32513819). Together with
CC SNX4, involved in autophagosome assembly (PubMed:32513819).
CC {ECO:0000269|PubMed:32513819}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with SNX4.
CC {ECO:0000269|PubMed:32513819}.
CC -!- INTERACTION:
CC Q5VWJ9; O95219: SNX4; NbExp=3; IntAct=EBI-8099676, EBI-724909;
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000269|PubMed:32513819}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O95219}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O95219}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; AL390067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL360235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS43865.1; -.
DR RefSeq; NP_001013012.1; NM_001012994.1.
DR AlphaFoldDB; Q5VWJ9; -.
DR SMR; Q5VWJ9; -.
DR BioGRID; 135142; 19.
DR IntAct; Q5VWJ9; 5.
DR MINT; Q5VWJ9; -.
DR STRING; 9606.ENSP00000363349; -.
DR iPTMnet; Q5VWJ9; -.
DR MetOSite; Q5VWJ9; -.
DR PhosphoSitePlus; Q5VWJ9; -.
DR BioMuta; SNX30; -.
DR DMDM; 74747407; -.
DR EPD; Q5VWJ9; -.
DR jPOST; Q5VWJ9; -.
DR MassIVE; Q5VWJ9; -.
DR MaxQB; Q5VWJ9; -.
DR PaxDb; Q5VWJ9; -.
DR PeptideAtlas; Q5VWJ9; -.
DR PRIDE; Q5VWJ9; -.
DR ProteomicsDB; 65531; -.
DR Antibodypedia; 7509; 100 antibodies from 19 providers.
DR DNASU; 401548; -.
DR Ensembl; ENST00000374232.8; ENSP00000363349.3; ENSG00000148158.17.
DR GeneID; 401548; -.
DR KEGG; hsa:401548; -.
DR MANE-Select; ENST00000374232.8; ENSP00000363349.3; NM_001012994.2; NP_001013012.1.
DR UCSC; uc004bgj.5; human.
DR CTD; 401548; -.
DR DisGeNET; 401548; -.
DR GeneCards; SNX30; -.
DR HGNC; HGNC:23685; SNX30.
DR HPA; ENSG00000148158; Tissue enhanced (brain).
DR neXtProt; NX_Q5VWJ9; -.
DR OpenTargets; ENSG00000148158; -.
DR PharmGKB; PA142670889; -.
DR VEuPathDB; HostDB:ENSG00000148158; -.
DR eggNOG; KOG2273; Eukaryota.
DR GeneTree; ENSGT00940000158994; -.
DR HOGENOM; CLU_040655_1_0_1; -.
DR InParanoid; Q5VWJ9; -.
DR OMA; FIWLRQK; -.
DR OrthoDB; 947320at2759; -.
DR PhylomeDB; Q5VWJ9; -.
DR TreeFam; TF328543; -.
DR PathwayCommons; Q5VWJ9; -.
DR SignaLink; Q5VWJ9; -.
DR BioGRID-ORCS; 401548; 10 hits in 1075 CRISPR screens.
DR ChiTaRS; SNX30; human.
DR GenomeRNAi; 401548; -.
DR Pharos; Q5VWJ9; Tdark.
DR PRO; PR:Q5VWJ9; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5VWJ9; protein.
DR Bgee; ENSG00000148158; Expressed in kidney epithelium and 174 other tissues.
DR ExpressionAtlas; Q5VWJ9; baseline and differential.
DR Genevisible; Q5VWJ9; HS.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IMP:UniProtKB.
DR GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
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; IPR028649; SNX30.
DR PANTHER; PTHR45949:SF1; PTHR45949:SF1; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Endosome; Membrane; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..437
FT /note="Sorting nexin-30"
FT /id="PRO_0000284533"
FT DOMAIN 89..210
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 234..437
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:Q3UR97"
FT BINDING 134
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 162
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 176
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 38
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8CE50"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT VARIANT 83
FT /note="D -> H (in dbSNP:rs2796036)"
FT /id="VAR_031771"
FT VARIANT 125
FT /note="P -> A (in dbSNP:rs10117709)"
FT /id="VAR_052483"
SQ SEQUENCE 437 AA; 49677 MW; 32496ED341C5E9A4 CRC64;
MAGGPPKALP STGPHSLRDM PHPLAGSSSE EAVGGDSTPS PDLLMARSFG DKDLILPNGG
TPAGTSSPAS SSSLLNRLQL DDDIDGETRD LFVIVDDPKK HVCTMETYIT YRITTKSTRV
EFDLPEYSVR RRYQDFDWLR SKLEESQPTH LIPPLPEKFV VKGVVDRFSE EFVETRRKAL
DKFLKRITDH PVLSFNEHFN IFLTAKDLNA YKKQGIALLT RMGESVKHVT GGYKLRTRPL
EFAAIGDYLD TFALKLGTID RIAQRIIKEE IEYLVELREY GPVYSTWSAL EGELAEPLEG
VSACIGNCST ALEELTDDMT EDFLPVLREY ILYSDSMKSV LKKRDQVQAE YEAKLEAVAL
RKEDRPKVPA DVEKCQDRME CFNADLKADM ERWQNNKRQD FRQLLMGMAD KNIQYYEKCL
MAWESIIPLL QEKQEAK
