SNX20_RAT
ID SNX20_RAT Reviewed; 313 AA.
AC Q5BK61;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Sorting nexin-20;
GN Name=Snx20;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; BC091194; AAH91194.1; -; mRNA.
DR RefSeq; NP_001020170.1; NM_001024999.1.
DR AlphaFoldDB; Q5BK61; -.
DR SMR; Q5BK61; -.
DR STRING; 10116.ENSRNOP00000019130; -.
DR iPTMnet; Q5BK61; -.
DR PhosphoSitePlus; Q5BK61; -.
DR PaxDb; Q5BK61; -.
DR Ensembl; ENSRNOT00000019130; ENSRNOP00000019130; ENSRNOG00000014202.
DR GeneID; 307742; -.
DR KEGG; rno:307742; -.
DR CTD; 124460; -.
DR RGD; 1307787; Snx20.
DR eggNOG; KOG2101; Eukaryota.
DR GeneTree; ENSGT00530000063759; -.
DR HOGENOM; CLU_059132_0_0_1; -.
DR InParanoid; Q5BK61; -.
DR OMA; ATRCVRH; -.
DR OrthoDB; 1322681at2759; -.
DR PhylomeDB; Q5BK61; -.
DR TreeFam; TF326807; -.
DR PRO; PR:Q5BK61; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000014202; Expressed in spleen and 19 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 PANTHER; PTHR20939; PTHR20939; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Endosome; Lipid-binding; Membrane; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..313
FT /note="Sorting nexin-20"
FT /id="PRO_0000325821"
FT DOMAIN 71..188
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 113
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 115
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 140
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 154
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:0007744|PubMed:22673903"
SQ SEQUENCE 313 AA; 35723 MW; 79D766A3B4F272B4 CRC64;
MASPQHPGGP GWTGPRNQCI TRTRQEVLPP GPDLPCPGPE EAQDGPTSNS NMTTRELQEH
WQKEKSRWKH VRLLFEIASA RIEERKVSKF VMYQVVVIQT GSFDSDKAVV ERRYSDFERL
QRALLKRFGP ELEDVTFPRK RLTGNLSAET ICERRLELRE YLRLLYAVRA VRRSREFADF
LTRPELCEAF GCLRAGQYAR ALDLLGRVVP LQEKLTAHCP SAPVPALCAM LVCLRDLERP
AEAFAVGERA LRRLGARESH RYYAPLLDAM VRLAYALGKD LASLQGRLDE SQLRRPTHRG
ATLKELTVRE YLS
