ID   SNX20_BOVIN             Reviewed;         316 AA.
AC   Q2T9W1;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Sorting nexin-20;
GN   Name=SNX20;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in cellular vesicle trafficking. Has been
CC       proposed to function as a sorting protein that targets SELPLG into
CC       endosomes, but has no effect on SELPLG internalization from the cell
CC       surface, or on SELPLG-mediated cell-cell adhesion.
CC       {ECO:0000250|UniProtKB:Q7Z614}.
CC   -!- SUBUNIT: Interacts with SELPLG. Interaction with SELPLG is
CC       controversial. {ECO:0000250|UniProtKB:Q7Z614}.
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane
CC       {ECO:0000250|UniProtKB:Q7Z614}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q7Z614}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q7Z614}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q7Z614}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q7Z614}. Nucleus {ECO:0000250|UniProtKB:Q7Z614}.
CC   -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is
CC       necessary for localization to the endosomes.
CC       {ECO:0000250|UniProtKB:Q7Z614}.
CC   -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR   EMBL; BC111240; AAI11241.1; -; mRNA.
DR   RefSeq; NP_001033122.1; NM_001038033.2.
DR   RefSeq; XP_005218532.1; XM_005218475.3.
DR   AlphaFoldDB; Q2T9W1; -.
DR   SMR; Q2T9W1; -.
DR   STRING; 9913.ENSBTAP00000005164; -.
DR   PaxDb; Q2T9W1; -.
DR   PRIDE; Q2T9W1; -.
DR   Ensembl; ENSBTAT00000005164; ENSBTAP00000005164; ENSBTAG00000003961.
DR   Ensembl; ENSBTAT00000085893; ENSBTAP00000067421; ENSBTAG00000003961.
DR   GeneID; 505256; -.
DR   KEGG; bta:505256; -.
DR   CTD; 124460; -.
DR   VEuPathDB; HostDB:ENSBTAG00000003961; -.
DR   VGNC; VGNC:35101; SNX20.
DR   eggNOG; KOG2101; Eukaryota.
DR   GeneTree; ENSGT00530000063759; -.
DR   HOGENOM; CLU_059132_0_0_1; -.
DR   InParanoid; Q2T9W1; -.
DR   OMA; ATRCVRH; -.
DR   OrthoDB; 1322681at2759; -.
DR   TreeFam; TF326807; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000003961; Expressed in neutrophil and 81 other tissues.
DR   GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:1901981; F:phosphatidylinositol phosphate binding; IBA:GO_Central.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1520.10; -; 1.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR039937; SNX20/SNX21.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR20939; PTHR20939; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   SUPFAM; SSF64268; SSF64268; 1.
DR   PROSITE; PS50195; PX; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasm; Endosome; Lipid-binding; Membrane; Nucleus;
KW   Phosphoprotein; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..316
FT                   /note="Sorting nexin-20"
FT                   /id="PRO_0000325819"
FT   DOMAIN          74..191
FT                   /note="PX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         116
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   BINDING         118
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         143
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         157
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         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5BK61"
SQ   SEQUENCE   316 AA;  36172 MW;  3864DBA23ED24339 CRC64;
     MASHKHPGSP GWTGPICQDM AGTTPKASAP RPDLPRPGPE DHLEAQGSPS SNSSMTTREL
     QEYWRAQKCC WKHVKLLFEI ASARIEERKV SKFVMYQIVV IQTGSFDSNK AVLERRYSDF
     ETLQKKLLKT FREEIEDVVF PKKHLIGNFT EEMISERKLA LKEYLSVLYA IRCVRRSREF
     IDFLTRPELK EAFGCLRAGQ YTKALDILMR VVPLQEKLTA HCPVLLVPAL CAMLVCHRDL
     DRPAEAFAVG ERALQCLQAR EGHRYYAPLL DAMARLAYLL GKDFVSLQKR LEESQLRKPA
     LRGFTLKELT VQEYLS