ID   SNX24_HUMAN             Reviewed;         169 AA.
AC   Q9Y343; Q6UY33;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   24-JAN-2024, entry version 161.
DE   RecName: Full=Sorting nexin-24;
GN   Name=SNX24; ORFNames=SBBI31, UNQ654/PRO1284;
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 [MRNA] (ISOFORM 1).
RA   Zhang W., Wan T., Cao X.;
RT   "Hypothetical human protein SBBI31.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Hong W.;
RT   "SBBI31 as a new member (SNX24) of the sorting nexin family.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Kidney, and Lung;
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: May be involved in several stages of intracellular
CC       trafficking. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9Y343; P14859-6: POU2F1; NbExp=3; IntAct=EBI-727113, EBI-11526590;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Y343-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y343-2; Sequence=VSP_012034;
CC   -!- DOMAIN: The PX domain mediates specific binding to membranes enriched
CC       in phosphatidylinositol 3-phosphate (PtdIns(P3)). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR   EMBL; AF139461; AAD32668.1; -; mRNA.
DR   EMBL; AY044655; AAK98769.1; -; mRNA.
DR   EMBL; AY358098; AAQ88465.1; -; mRNA.
DR   EMBL; BC069012; AAH69012.1; -; mRNA.
DR   EMBL; BC010886; AAH10886.1; -; mRNA.
DR   CCDS; CCDS4132.1; -. [Q9Y343-1]
DR   RefSeq; NP_054754.1; NM_014035.2. [Q9Y343-1]
DR   PDB; 4AZ9; X-ray; 1.75 A; A/B=1-107.
DR   PDBsum; 4AZ9; -.
DR   AlphaFoldDB; Q9Y343; -.
DR   SMR; Q9Y343; -.
DR   BioGRID; 118791; 34.
DR   IntAct; Q9Y343; 24.
DR   MINT; Q9Y343; -.
DR   STRING; 9606.ENSP00000261369; -.
DR   TCDB; 3.A.34.1.1; the sorting nexins of the escrt complexes (sn-escrt).
DR   iPTMnet; Q9Y343; -.
DR   PhosphoSitePlus; Q9Y343; -.
DR   BioMuta; SNX24; -.
DR   DMDM; 20140349; -.
DR   EPD; Q9Y343; -.
DR   jPOST; Q9Y343; -.
DR   MassIVE; Q9Y343; -.
DR   MaxQB; Q9Y343; -.
DR   PaxDb; 9606-ENSP00000261369; -.
DR   PeptideAtlas; Q9Y343; -.
DR   ProteomicsDB; 85973; -. [Q9Y343-1]
DR   ProteomicsDB; 85974; -. [Q9Y343-2]
DR   Pumba; Q9Y343; -.
DR   Antibodypedia; 25654; 176 antibodies from 23 providers.
DR   DNASU; 28966; -.
DR   Ensembl; ENST00000261369.9; ENSP00000261369.4; ENSG00000064652.11. [Q9Y343-1]
DR   Ensembl; ENST00000506996.5; ENSP00000422535.1; ENSG00000064652.11. [Q9Y343-2]
DR   Ensembl; ENST00000513881.5; ENSP00000424149.1; ENSG00000064652.11. [Q9Y343-2]
DR   GeneID; 28966; -.
DR   KEGG; hsa:28966; -.
DR   MANE-Select; ENST00000261369.9; ENSP00000261369.4; NM_014035.4; NP_054754.1.
DR   UCSC; uc003ktf.3; human. [Q9Y343-1]
DR   AGR; HGNC:21533; -.
DR   CTD; 28966; -.
DR   DisGeNET; 28966; -.
DR   GeneCards; SNX24; -.
DR   HGNC; HGNC:21533; SNX24.
DR   HPA; ENSG00000064652; Low tissue specificity.
DR   neXtProt; NX_Q9Y343; -.
DR   OpenTargets; ENSG00000064652; -.
DR   PharmGKB; PA134980773; -.
DR   VEuPathDB; HostDB:ENSG00000064652; -.
DR   eggNOG; KOG2101; Eukaryota.
DR   GeneTree; ENSGT00390000001280; -.
DR   HOGENOM; CLU_117250_1_0_1; -.
DR   InParanoid; Q9Y343; -.
DR   OMA; TVFRIDV; -.
DR   OrthoDB; 48886at2759; -.
DR   PhylomeDB; Q9Y343; -.
DR   TreeFam; TF332414; -.
DR   PathwayCommons; Q9Y343; -.
DR   SignaLink; Q9Y343; -.
DR   BioGRID-ORCS; 28966; 8 hits in 1164 CRISPR screens.
DR   ChiTaRS; SNX24; human.
DR   GenomeRNAi; 28966; -.
DR   Pharos; Q9Y343; Tbio.
DR   PRO; PR:Q9Y343; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9Y343; Protein.
DR   Bgee; ENSG00000064652; Expressed in oocyte and 190 other cell types or tissues.
DR   ExpressionAtlas; Q9Y343; baseline and differential.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:1901981; F:phosphatidylinositol phosphate binding; IBA:GO_Central.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:Ensembl.
DR   GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IEA:Ensembl.
DR   GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IEA:Ensembl.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd06880; PX_SNX22; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   PANTHER; PTHR15813; SORTING NEXIN-22 AND 24; 1.
DR   PANTHER; PTHR15813:SF10; SORTING NEXIN-24; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   PROSITE; PS50195; PX; 1.
DR   Genevisible; Q9Y343; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasmic vesicle;
KW   Lipid-binding; Membrane; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..169
FT                   /note="Sorting nexin-24"
FT                   /id="PRO_0000213872"
FT   DOMAIN          1..125
FT                   /note="PX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT   BINDING         38
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"
FT   BINDING         40
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"
FT   BINDING         61
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"
FT   BINDING         74
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"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         113
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CRB0"
FT   MOD_RES         116
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CRB0"
FT   VAR_SEQ         148..169
FT                   /note="DFPNVVIEGVLHGIFYPHLQPR -> GNQTCHLLTALY (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:12975309,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_012034"
FT   STRAND          2..11
FT                   /evidence="ECO:0007829|PDB:4AZ9"
FT   STRAND          19..28
FT                   /evidence="ECO:0007829|PDB:4AZ9"
FT   STRAND          31..38
FT                   /evidence="ECO:0007829|PDB:4AZ9"
FT   HELIX           39..49
FT                   /evidence="ECO:0007829|PDB:4AZ9"
FT   TURN            50..52
FT                   /evidence="ECO:0007829|PDB:4AZ9"
FT   HELIX           68..88
FT                   /evidence="ECO:0007829|PDB:4AZ9"
FT   HELIX           94..99
FT                   /evidence="ECO:0007829|PDB:4AZ9"
SQ   SEQUENCE   169 AA;  19818 MW;  651B3964493AFE5D CRC64;
     MEVYIPSFRY EESDLERGYT VFKIEVLMNG RKHFVEKRYS EFHALHKKLK KCIKTPEIPS
     KHVRNWVPKV LEQRRQGLET YLQAVILENE ELPKLFLDFL NVRHLPSLPK AESCGSFDET
     ESEESSKLSH QPVLLFLRDP YVLPAASDFP NVVIEGVLHG IFYPHLQPR
//