ID J3S963_CROAD Unreviewed; 563 AA.
AC J3S963;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Sorting nexin {ECO:0000256|PIRNR:PIRNR027744};
OS Crotalus adamanteus (Eastern diamondback rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8729 {ECO:0000313|EMBL:AFJ50763.1};
RN [1] {ECO:0000313|EMBL:AFJ50763.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Venom gland {ECO:0000313|EMBL:AFJ50763.1};
RX PubMed=23025625; DOI=10.1186/1471-2164-13-312;
RA Rokyta D.R., Lemmon A.R., Margres M.J., Aronow K.;
RT "The venom-gland transcriptome of the eastern diamondback rattlesnake
RT (Crotalus adamanteus).";
RL BMC Genomics 13:312-312(2012).
RN [2] {ECO:0000313|EMBL:JAI11317.1}
RP NUCLEOTIDE SEQUENCE.
RA Margres M.J., Wray K.P., McGivern J.J., Seavy M., Sanader D., Facente J.,
RA Rokyta D.R.;
RT "The extremes of toxin expression variation revealed in two sympatric snake
RT species.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JU175239; AFJ50763.1; -; mRNA.
DR EMBL; GBEX01003243; JAI11317.1; -; mRNA.
DR AlphaFoldDB; J3S963; -.
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:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:InterPro.
DR CDD; cd07669; BAR_SNX33; 1.
DR CDD; cd11896; SH3_SNX33; 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; IPR037427; SNX33_BAR.
DR InterPro; IPR014536; Snx9_fam.
DR InterPro; IPR019497; Sorting_nexin_WASP-bd-dom.
DR PANTHER; PTHR45827; SORTING NEXIN; 1.
DR PANTHER; PTHR45827:SF3; SORTING NEXIN-33; 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 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 219..329
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 67..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..114
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 255
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 257
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 295
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 563 AA; 64385 MW; EAF297D6BF94DAE6 CRC64;
MAFQARALYD FQSENKEEIS IRENEELVLF SEKSLDGWLQ GTNSRGETGL FPASYVEILC
SRSSSTYTNC SNSPTGSPGN GSSFYVPPSA PSISHQGSFE DDEDDWDDWD DDGTVVEEPR
SGAGTNGHPS PSLSCPRPYA HPNNTGSRAK PSLERQDSIG SSKRGSMVSR NLNRFSSFVR
SGVEAFILGD VPMMGKISEA YYIDMGSKGP QWRSSPHPFL CSVEEPTKQT KFKGIKSYIS
YRLMPSNGNS PVYRRYKHFD WLYNRLLHKF TVISVPHLPE KQATGRFGED FIEKRKRRLI
LWMDHMTSHP ALSQYEGFQH FLTCGDNKQW KMGKRRAEKD EMVGASFLLT LQIPTEHQDL
QDVEDRVDTF KAFNKKMDDS VLQLTSVASE LARKHVGGFR KEFQKLGNAF QAISQAFQMD
PPYSYDALNK AISHTGKTYE MVGEMFAEQP KNDLFLMLDS LSLYQGLLSN FPDIIHLQKG
AFAKVKESQR MSDEGKMDQE EADGIRKRCR VVGFALQAEM NYFHERRILD FKKMMQSYIR
EQIVFYQRVS QKLEETLRRY DNL
//
