ID   SNX25_HUMAN             Reviewed;         840 AA.
AC   Q9H3E2; Q3ZT30; Q8N6K3;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 2.
DT   27-NOV-2024, entry version 178.
DE   RecName: Full=Sorting nexin-25;
GN   Name=SNX25; ORFNames=MSTP043;
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   Hao X., Chang Z., Zhu S.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 275-840 (ISOFORM 1).
RC   TISSUE=Heart;
RA   Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y.,
RA   Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y.,
RA   Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C.,
RA   Zhao M.S., Hui R.T.;
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 303-840 (ISOFORM 1).
RA   Hong W.;
RT   "MSTP043 as a new member (SNX25) of the sorting nexin family.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=14975938; DOI=10.1165/rcmb.2003-0238oc;
RA   Bard M.P., Hegmans J.P., Hemmes A., Luider T.M., Willemsen R.,
RA   Severijnen L.A., van Meerbeeck J.P., Burgers S.A., Hoogsteden H.C.,
RA   Lambrecht B.N.;
RT   "Proteomic analysis of exosomes isolated from human malignant pleural
RT   effusions.";
RL   Am. J. Respir. Cell Mol. Biol. 31:114-121(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
CC   -!- FUNCTION: May be involved in several stages of intracellular
CC       trafficking. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:14975938};
CC       Peripheral membrane protein {ECO:0000269|PubMed:14975938}.
CC       Note=Detected in endosome-derived secreted vesicles (exosomes) from
CC       malignant pleural effusions.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9H3E2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H3E2-2; Sequence=VSP_057156, VSP_057157;
CC   -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG39294.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY601647; AAT98627.1; -; mRNA.
DR   EMBL; BC029868; AAH29868.2; -; mRNA.
DR   EMBL; AF113223; AAG39294.1; ALT_INIT; mRNA.
DR   EMBL; AY044656; AAK98770.1; -; mRNA.
DR   CCDS; CCDS34116.1; -. [Q9H3E2-1]
DR   RefSeq; NP_001304710.1; NM_001317781.1. [Q9H3E2-1]
DR   PDB; 5WOE; NMR; -; A=506-628.
DR   PDB; 7SR1; X-ray; 2.40 A; A/B=282-405.
DR   PDB; 7SR2; X-ray; 2.42 A; A/B=282-405.
DR   PDBsum; 5WOE; -.
DR   PDBsum; 7SR1; -.
DR   PDBsum; 7SR2; -.
DR   AlphaFoldDB; Q9H3E2; -.
DR   SMR; Q9H3E2; -.
DR   BioGRID; 123802; 23.
DR   IntAct; Q9H3E2; 13.
DR   STRING; 9606.ENSP00000426255; -.
DR   TCDB; 3.A.34.1.1; the sorting nexins of the escrt complexes (sn-escrt).
DR   GlyGen; Q9H3E2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9H3E2; -.
DR   PhosphoSitePlus; Q9H3E2; -.
DR   BioMuta; SNX25; -.
DR   DMDM; 212276473; -.
DR   jPOST; Q9H3E2; -.
DR   MassIVE; Q9H3E2; -.
DR   PaxDb; 9606-ENSP00000426255; -.
DR   PeptideAtlas; Q9H3E2; -.
DR   ProteomicsDB; 80704; -. [Q9H3E2-1]
DR   Pumba; Q9H3E2; -.
DR   Antibodypedia; 28920; 147 antibodies from 26 providers.
DR   DNASU; 83891; -.
DR   Ensembl; ENST00000264694.13; ENSP00000264694.8; ENSG00000109762.17. [Q9H3E2-1]
DR   Ensembl; ENST00000504273.5; ENSP00000426255.1; ENSG00000109762.17. [Q9H3E2-1]
DR   Ensembl; ENST00000618785.4; ENSP00000483653.1; ENSG00000109762.17. [Q9H3E2-2]
DR   GeneID; 83891; -.
DR   KEGG; hsa:83891; -.
DR   UCSC; uc003ixh.4; human. [Q9H3E2-1]
DR   AGR; HGNC:21883; -.
DR   CTD; 83891; -.
DR   DisGeNET; 83891; -.
DR   GeneCards; SNX25; -.
DR   HGNC; HGNC:21883; SNX25.
DR   HPA; ENSG00000109762; Low tissue specificity.
DR   neXtProt; NX_Q9H3E2; -.
DR   OpenTargets; ENSG00000109762; -.
DR   PharmGKB; PA134988505; -.
DR   VEuPathDB; HostDB:ENSG00000109762; -.
DR   eggNOG; KOG2101; Eukaryota.
DR   GeneTree; ENSGT00950000182856; -.
DR   HOGENOM; CLU_005899_0_1_1; -.
DR   InParanoid; Q9H3E2; -.
DR   OrthoDB; 5392990at2759; -.
DR   PhylomeDB; Q9H3E2; -.
DR   TreeFam; TF324055; -.
DR   PathwayCommons; Q9H3E2; -.
DR   SignaLink; Q9H3E2; -.
DR   BioGRID-ORCS; 83891; 17 hits in 1148 CRISPR screens.
DR   ChiTaRS; SNX25; human.
DR   GenomeRNAi; 83891; -.
DR   Pharos; Q9H3E2; Tbio.
DR   PRO; PR:Q9H3E2; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q9H3E2; protein.
DR   Bgee; ENSG00000109762; Expressed in oocyte and 184 other cell types or tissues.
DR   ExpressionAtlas; Q9H3E2; baseline and differential.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0032801; P:receptor catabolic process; IMP:UniProtKB.
DR   CDD; cd06878; PX_SNX25; 1.
DR   CDD; cd08720; RGS_SNX25; 1.
DR   FunFam; 3.30.1520.10:FF:000033; Sorting nexin 25; 1.
DR   FunFam; 1.10.167.10:FF:000013; sorting nexin-25 isoform X1; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR   InterPro; IPR003114; Phox_assoc.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR044926; RGS_subdomain_2.
DR   InterPro; IPR037899; SNX25_PX.
DR   InterPro; IPR013937; Sorting_nexin_C.
DR   PANTHER; PTHR22775; SORTING NEXIN; 1.
DR   PANTHER; PTHR22775:SF29; SORTING NEXIN-25; 1.
DR   Pfam; PF08628; Nexin_C; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF02194; PXA; 1.
DR   Pfam; PF00615; RGS; 1.
DR   SMART; SM00312; PX; 1.
DR   SMART; SM00313; PXA; 1.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR   PROSITE; PS50195; PX; 1.
DR   PROSITE; PS51207; PXA; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil; Endosome; Membrane;
KW   Phosphoprotein; Protein transport; Proteomics identification;
KW   Reference proteome; Transport.
FT   CHAIN           1..840
FT                   /note="Sorting nexin-25"
FT                   /id="PRO_0000213875"
FT   DOMAIN          1..164
FT                   /note="PXA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147,
FT                   ECO:0000255|PROSITE-ProRule:PRU00553"
FT   DOMAIN          287..401
FT                   /note="RGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT   DOMAIN          508..628
FT                   /note="PX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT   COILED          434..499
FT                   /evidence="ECO:0000255"
FT   MOD_RES         665
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983"
FT   VAR_SEQ         1..229
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_057156"
FT   VAR_SEQ         604..658
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_057157"
FT   VARIANT         318
FT                   /note="E -> K (in dbSNP:rs35700132)"
FT                   /id="VAR_047057"
FT   VARIANT         586
FT                   /note="I -> V (in dbSNP:rs3756275)"
FT                   /id="VAR_047058"
FT   VARIANT         725
FT                   /note="T -> I (in dbSNP:rs34120554)"
FT                   /id="VAR_047059"
FT   HELIX           288..293
FT                   /evidence="ECO:0007829|PDB:7SR1"
FT   HELIX           295..307
FT                   /evidence="ECO:0007829|PDB:7SR1"
FT   HELIX           311..324
FT                   /evidence="ECO:0007829|PDB:7SR1"
FT   TURN            328..330
FT                   /evidence="ECO:0007829|PDB:7SR1"
FT   HELIX           331..342
FT                   /evidence="ECO:0007829|PDB:7SR1"
FT   HELIX           351..354
FT                   /evidence="ECO:0007829|PDB:7SR1"
FT   HELIX           356..361
FT                   /evidence="ECO:0007829|PDB:7SR1"
FT   HELIX           366..386
FT                   /evidence="ECO:0007829|PDB:7SR1"
FT   HELIX           388..392
FT                   /evidence="ECO:0007829|PDB:7SR1"
FT   HELIX           397..400
FT                   /evidence="ECO:0007829|PDB:7SR1"
FT   STRAND          510..522
FT                   /evidence="ECO:0007829|PDB:5WOE"
FT   STRAND          525..536
FT                   /evidence="ECO:0007829|PDB:5WOE"
FT   STRAND          545..552
FT                   /evidence="ECO:0007829|PDB:5WOE"
FT   HELIX           553..566
FT                   /evidence="ECO:0007829|PDB:5WOE"
FT   HELIX           569..572
FT                   /evidence="ECO:0007829|PDB:5WOE"
FT   STRAND          582..584
FT                   /evidence="ECO:0007829|PDB:5WOE"
FT   HELIX           588..607
FT                   /evidence="ECO:0007829|PDB:5WOE"
FT   HELIX           609..613
FT                   /evidence="ECO:0007829|PDB:5WOE"
FT   HELIX           615..621
FT                   /evidence="ECO:0007829|PDB:5WOE"
SQ   SEQUENCE   840 AA;  97945 MW;  D75682A660DEF124 CRC64;
     MDKALKEVFD YSYRDYILSW YGNLSRDEGQ LYHLLLEDFW EIARQLHHRL SHVDVVKVVC
     NDVVRTLLTH FCDLKAANAR HEEQPRPFVL HACLRNSDDE VRFLQTCSRV LVFCLLPSKD
     VQSLSLRIML AEILTTKVLK PVVELLSNPD YINQMLLAQL AYREQMNEHH KRAYTYAPSY
     EDFIKLINSN SDVEFLKQLR YQIVVEIIQA TTISSFPQLK RHKGKETAAM KADLLRARNM
     KRYINQLTVA KKQCEKRIRI LGGPAYDQQE DGALDEGEGP QSQKILQFED ILANTFYREH
     FGMYMERMDK RALISFWESV EHLKNANKNE IPQLVGEIYQ NFFVESKEIS VEKSLYKEIQ
     QCLVGNKGIE VFYKIQEDVY ETLKDRYYPS FIVSDLYEKL LIKEEEKHAS QMISNKDEMG
     PRDEAGEEAV DDGTNQINEQ ASFAVNKLRE LNEKLEYKRQ ALNSIQNAPK PDKKIVSKLK
     DEIILIEKER TDLQLHMART DWWCENLGMW KASITSGEVT EENGEQLPCY FVMVSLQEVG
     GVETKNWTVP RRLSEFQNLH RKLSECVPSL KKVQLPSLSK LPFKSIDQKF MEKSKNQLNK
     FLQNLLSDER LCQSEALYAF LSPSPDYLKV IDVQGKKNSF SLSSFLERLP RDFFSHQEEE
     TEEDSDLSDY GDDVDGRKDA LAEPCFMLIG EIFELRGMFK WVRRTLIALV QVTFGRTINK
     QIRDTVSWIF SEQMLVYYIN IFRDAFWPNG KLAPPTTIRS KEQSQETKQR AQQKLLENIP
     DMLQSLVGQQ NARHGIIKIF NALQETRANK HLLYALMELL LIELCPELRV HLDQLKAGQV
//