SNX30_MOUSE
ID SNX30_MOUSE Reviewed; 437 AA.
AC Q8CE50; Q3UHE6;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Sorting nexin-30 {ECO:0000305};
GN Name=Snx30 {ECO:0000312|MGI:MGI:2443882};
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, and NOD;
RC TISSUE=Brain, Dendritic cell, Skin, and Submandibular gland;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38 AND SER-40, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in the regulation of endocytosis and in several
CC stages of intracellular trafficking. Together with SNX4, involved in
CC autophagosome assembly. {ECO:0000250|UniProtKB:Q5VWJ9}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with SNX4.
CC {ECO:0000250|UniProtKB:Q5VWJ9}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000250|UniProtKB:Q5VWJ9}; 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; AK029012; BAC26242.1; -; mRNA.
DR EMBL; AK147437; BAE27911.1; -; mRNA.
DR EMBL; AK165619; BAE38299.1; -; mRNA.
DR EMBL; AK170774; BAE42020.1; -; mRNA.
DR EMBL; AK170999; BAE42170.1; -; mRNA.
DR EMBL; AL831738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC099674; AAH99674.1; -; mRNA.
DR CCDS; CCDS18226.1; -.
DR RefSeq; NP_766056.1; NM_172468.2.
DR AlphaFoldDB; Q8CE50; -.
DR SMR; Q8CE50; -.
DR BioGRID; 229049; 4.
DR STRING; 10090.ENSMUSP00000030080; -.
DR iPTMnet; Q8CE50; -.
DR PhosphoSitePlus; Q8CE50; -.
DR EPD; Q8CE50; -.
DR MaxQB; Q8CE50; -.
DR PaxDb; Q8CE50; -.
DR PeptideAtlas; Q8CE50; -.
DR PRIDE; Q8CE50; -.
DR ProteomicsDB; 257283; -.
DR Antibodypedia; 7509; 100 antibodies from 19 providers.
DR DNASU; 209131; -.
DR Ensembl; ENSMUST00000030080; ENSMUSP00000030080; ENSMUSG00000028385.
DR GeneID; 209131; -.
DR KEGG; mmu:209131; -.
DR UCSC; uc008tae.1; mouse.
DR CTD; 401548; -.
DR MGI; MGI:2443882; Snx30.
DR VEuPathDB; HostDB:ENSMUSG00000028385; -.
DR eggNOG; KOG2273; Eukaryota.
DR GeneTree; ENSGT00940000158994; -.
DR HOGENOM; CLU_040655_1_0_1; -.
DR InParanoid; Q8CE50; -.
DR OMA; FIWLRQK; -.
DR OrthoDB; 947320at2759; -.
DR PhylomeDB; Q8CE50; -.
DR TreeFam; TF328543; -.
DR BioGRID-ORCS; 209131; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Snx30; mouse.
DR PRO; PR:Q8CE50; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8CE50; protein.
DR Bgee; ENSMUSG00000028385; Expressed in humerus cartilage element and 209 other tissues.
DR Genevisible; Q8CE50; MM.
DR GO; GO:0005769; C:early endosome; ISS: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; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; ISS: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; IPR004148; BAR_dom.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR028649; SNX30.
DR PANTHER; PTHR45949:SF1; PTHR45949:SF1; 1.
DR Pfam; PF03114; BAR; 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_0000284534"
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..45
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:0007744|PubMed:21183079"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 19
FT /note="D -> G (in Ref. 1; BAE27911)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 437 AA; 49520 MW; 52805380D0E0D158 CRC64;
MAGGPPKALP STGPQSLRDM PHPLAGSSSE EAVGGDSTPS PDLLMARSFG DKDLILPNGG
TPAGTASPAS SSSLLNRLQL DDDIDGEARD LFVTVDDPKK HVCTMETYIT YRITTKSTRV
EFDLPEYSVR RRYQDFDWLR NKLEESQPTH LIPPLPEKFV VKGVVDRFSE EFVETRRKAL
DKFLKRITDH PVLSFNEHFN VFLTAKDLNA YKKQGIALLS RVGESVKHVT GGYKLRSRPL
EFAAISDYLD TFALKLGTID RIAQRIIKEE IEYLVELREY GPVYSTWSAL EGELAEPLEG
VSACIGNCST ALEELTDDIT EEFLPVLREY VLYSDSMKGV LKKRDQVQAE YEAKLEAVAL
RKEERPKVPA DVEKCQDRME CFNADLKADM ERWQSNKRHD FRQLLVGLAD KNIQYYEKCL
MAWESIIPLL QEKQETK
