ID Q5U4P8_XENTR Unreviewed; 585 AA.
AC Q5U4P8;
DT 07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=Sorting nexin {ECO:0000256|PIRNR:PIRNR027744};
GN Name=snx18 {ECO:0000313|RefSeq:NP_001011173.1,
GN ECO:0000313|Xenbase:XB-GENE-958823};
GN Synonyms=sh3px2 {ECO:0000313|RefSeq:NP_001011173.1}, sh3pxd3b
GN {ECO:0000313|RefSeq:NP_001011173.1}, snag1
GN {ECO:0000313|EMBL:AAH84999.1, ECO:0000313|RefSeq:NP_001011173.1},
GN snx18-a {ECO:0000313|RefSeq:NP_001011173.1}, snx18-b
GN {ECO:0000313|RefSeq:NP_001011173.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|EMBL:AAH84999.1};
RN [1] {ECO:0000313|RefSeq:NP_001011173.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAH84999.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000313|EMBL:AAH84999.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001011173.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004180}.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883, ECO:0000256|PIRNR:PIRNR027744}.
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DR EMBL; BC084999; AAH84999.1; -; mRNA.
DR RefSeq; NP_001011173.1; NM_001011173.1.
DR DNASU; 496591; -.
DR GeneID; 496591; -.
DR KEGG; xtr:496591; -.
DR AGR; Xenbase:XB-GENE-958823; -.
DR CTD; 112574; -.
DR Xenbase; XB-GENE-958823; snx18.
DR OMA; QLWVDRM; -.
DR OrthoDB; 5401713at2759; -.
DR Proteomes; UP000008143; Chromosome 1.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd11897; SH3_SNX18; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035557; SNX18_SH3.
DR InterPro; IPR014536; Snx9_fam.
DR InterPro; IPR019497; Sorting_nexin_WASP-bd-dom.
DR PANTHER; PTHR45827; SORTING NEXIN; 1.
DR PANTHER; PTHR45827:SF4; SORTING NEXIN-18; 1.
DR Pfam; PF10456; BAR_3_WASP_bdg; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PIRSF; PIRSF027744; Snx9; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW ECO:0000256|PIRNR:PIRNR027744};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR027744};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000008143};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transport {ECO:0000256|ARBA:ARBA00022927}.
FT DOMAIN 1..61
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 239..349
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 61..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 275
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000256|PIRSR:PIRSR027744-1"
FT BINDING 277
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000256|PIRSR:PIRSR027744-1"
FT BINDING 315
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000256|PIRSR:PIRSR027744-1"
SQ SEQUENCE 585 AA; 65213 MW; 76EFB2ACFB9A2894 CRC64;
MALRARALYD FRAENPGEVS LRESEVLSLC SEQDIEGWLE GLNSRGERGL FPASYVEVLR
GEPAGPPPPP PPALGDSRYA NLPSGGYEPA QPFQSAAAPQ LGLAFQPRAP PGGYPASQPS
DDDWDDEWDD SSSTAADEPA AQPGGSYPGG YHDYEGSSRY RVSTRSDMPP GPSSLASSQA
AGKGSATVSR NLNRFSAFVK SGGEAFVLGE AAGFVRDGDK LCVVPGAEGP EWQENPYPFR
CSIDEPTKQT KFKGMKSYIS YRLLPSHTGL QVHRRYKHFD WLYARLLDKF PVVSVPRIPE
KQATGRFEED FISKRKKGLV WWMEHMCSHP VLARCDAFQH FLSCTDEKAW KQGKRKCERD
EMVGANFFLT LSLPPGSPVL EPHDVDGRLD GFKVFTKRMD EGVLQLSQTA GEFARKQAAG
FKKEYQKVGQ AVRGLGQAFE MDHMVFSAGL NRAMAFTGEA YEAIGEMFAE QPRQDLDPIM
DLLAVYQGHL ANFPDIIHVQ RGALTKVRES KKQVEEGKLE LQKAGEIQER CNVISYATLA
EIHHFHKIRV RDFKSQMQHF LQQQICFFQK VTLKLEEALQ KYDAA
//
