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Database: UniProt
Entry: T1E438_CROHD
LinkDB: T1E438_CROHD
Original site: T1E438_CROHD 
ID   T1E438_CROHD            Unreviewed;       563 AA.
AC   T1E438;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Sorting nexin {ECO:0000256|PIRNR:PIRNR027744};
OS   Crotalus horridus (Timber rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=35024 {ECO:0000313|EMBL:JAA95548.1};
RN   [1] {ECO:0000313|EMBL:JAA95548.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Venom gland {ECO:0000313|EMBL:JAA95548.1};
RX   PubMed=23758969; DOI=10.1186/1471-2164-14-394;
RA   Rokyta D.R., Wray K.P., Margres M.J.;
RT   "The genesis of an exceptionally lethal venom in the timber rattlesnake
RT   (Crotalus horridus) revealed through comparative venom-gland
RT   transcriptomics.";
RL   BMC Genomics 14:394-394(2013).
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; GAAZ01002395; JAA95548.1; -; mRNA.
DR   AlphaFoldDB; T1E438; -.
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          65..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..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;  64424 MW;  168397D2EE97FBE4 CRC64;
     MAFQARALYD FQSENKEEIS IRENEELVLF SEKSLDGWLQ GTNSRGETGL FPASYVEILR
     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
     PPYSYDALNN AISHTGKTYE MVGEMFAEQP KNDLFLMLDS LSLYQGLLSN FPDIIHLQKG
     AFAKVKESQR MSDEGKMDQE EADGIRKRCR VVGFALQAEM NYFHERRILD FKKMMQSYIR
     EQIVFYQRVS QKLEETLRRY DNL
//
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