ID G3TTG2_LOXAF Unreviewed; 620 AA.
AC G3TTG2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Sorting nexin {ECO:0000256|PIRNR:PIRNR027744};
GN Name=SNX18 {ECO:0000313|Ensembl:ENSLAFP00000018870.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000018870.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000018870.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000018870.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000018870.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000018870.1};
RG Ensembl;
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 AlphaFoldDB; G3TTG2; -.
DR STRING; 9785.ENSLAFP00000018870; -.
DR Ensembl; ENSLAFT00000031243.1; ENSLAFP00000018870.1; ENSLAFG00000009231.3.
DR eggNOG; KOG2528; Eukaryota.
DR GeneTree; ENSGT00940000157724; -.
DR HOGENOM; CLU_021494_1_0_1; -.
DR InParanoid; G3TTG2; -.
DR OMA; MGVNYCL; -.
DR TreeFam; TF314082; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:Ensembl.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:Ensembl.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl.
DR GO; GO:0036089; P:cleavage furrow formation; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0016197; P:endosomal transport; IEA:Ensembl.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:Ensembl.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd07670; BAR_SNX18; 1.
DR CDD; cd07286; PX_SNX18; 1.
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; IPR035703; SNX18_PX.
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 3: Inferred from homology;
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:UP000007646};
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 272..382
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 61..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..112
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 308
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 310
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 348
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 620 AA; 68461 MW; 3B3AAE2ED1FC2D6E CRC64;
MALRARALYD FRSENPGEIS LREHEVLSLC SEQDIEGWLE GVNSRGDRGL FPASYVQVIR
GPEPGPAGDG GAGAPARYAN VPPGGFEPLP AAPPASFKPS QQTPPPSTFQ PPGAGFPYGG
GALQPSPQQL YGGGGGYQAS QGSDDDWDDE WDDTSTVADE PGALGSGAYP DFDGSSSGAG
GAAGRYRLST RSDLSLGSRR STAPTHHPQH HPSGAKSSAT VSRNLNRFST FVKSGGEAFV
LGEASGFVKD GDKLCVVLGP YGPEWQENPY PFQCTIDDPT KQTKFKGMKS YISYKLVPTH
TQVPVHRRYK HFDWLYARLA EKFPVISVPH LPEKQATGRF EEDFISKRRK GLIWWMNHMA
SHPVLAQCDV FQHFLTCPSS TDEKAWKQGK RKAEKDEMVG ANFFLTLSTP PAAALDLQEV
ESKIDGFKSF TKKMDDSALQ LNHTANEFAR KQVTGFKKEY QKVGQSFRGL SQAFELDQQA
FSAGLNQAIA FTGDAYDAIG ELFADQPRQD LDPVMDLLAL YQGHLANFPD IIHVQKGALT
KVKESRRHVE EGKMEVQKAD GIQDRCNTIS FATLAEIHHF HQIRVRDFKS QMQHFLQQQI
IFFQKVTQKL EEALHKYDSV
//
