ID A0A3P8Z6E3_ESOLU Unreviewed; 611 AA.
AC A0A3P8Z6E3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Sorting nexin {ECO:0000256|PIRNR:PIRNR027744};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000024381.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000024381.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000024381.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3P8Z6E3; -.
DR STRING; 8010.ENSELUP00000024381; -.
DR Ensembl; ENSELUT00000035809.2; ENSELUP00000024381.2; ENSELUG00000023146.2.
DR GeneTree; ENSGT00940000157724; -.
DR InParanoid; A0A3P8Z6E3; -.
DR OMA; MGVNYCL; -.
DR Proteomes; UP000265140; LG13.
DR Bgee; ENSELUG00000023146; Expressed in stomach and 14 other cell types or tissues.
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; cd07286; PX_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; 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:UP000265140};
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 246..356
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 131..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 282
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 284
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 322
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 611 AA; 68623 MW; 92B75050F054943E CRC64;
MALKARVLYD FNSENPGEIS VKENEIVTLY SEQDIEGWLE GSNTKGERGL FPASYVEVVK
SDTGTTLNNN STSGDTYQGS RYSNIPAGGF AEPTSYKIQN QTDNLTKTPA TSPGFTAFSP
PIPVQQQHVY QASQGSDDDW DDDWDDSSTV ADEPGVVGGR YSGDLDSNGP ATYRVSTSSV
SRGSNAQQAK SSATVSRNLN RFSTFVKSGG EAFVLGEAAG FVKDGDKICV VMGQYGPEWQ
ENPYPFACTI DDPTKQTKFK GMKSYIAYKL TPTHTQTQVN RRYKHFDWLY ARLVEKFPVI
SVPHIPEKQA TGRFEEDFIS KRRKGLIWWM NHMTSHPVLS KCDVFQHFLT CNSTDEKAWK
QGKRKAERDE MVGANFFLTI STPSGPSLDL IEVESKIDGF RAFTKKMDES VVQVNATTNE
FARKQITWFK KEYQKVGQAF RVLGQAFELD QQAYSLGLNQ AIAFTGEAYD AVGEYFAEQP
KQDVDPLMDL LQLYQGHLAN YPDIIHVQKG ALTKVKESQK HVEEGKMDTP QAEGVKERCN
IISFATLAEI QHFHQIRVRD FKAQMQQYLT EQIGFFQKIT GKLEEALQNF SAFPFYTERG
CLSMKTRGSC V
//
