ID T1E5N7_CROHD Unreviewed; 444 AA.
AC T1E5N7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 22-FEB-2023, entry version 27.
DE SubName: Full=Sorting nexin-8 {ECO:0000313|EMBL:JAA96332.1};
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:JAA96332.1};
RN [1] {ECO:0000313|EMBL:JAA96332.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Venom gland {ECO:0000313|EMBL:JAA96332.1};
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).
RN [2] {ECO:0000313|EMBL:JAG43703.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Venom gland {ECO:0000313|EMBL:JAG43703.1};
RX PubMed=25727380; DOI=10.1016/j.toxicon.2015.02.015;
RA Rokyta D.R., Wray K.P., McGivern J.J., Margres M.J.;
RT "The transcriptomic and proteomic basis for the evolution of a novel venom
RT phenotype within the Timber Rattlesnake (Crotalus horridus).";
RL Toxicon 98:34-48(2015).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004287};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883}.
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DR EMBL; GAAZ01001611; JAA96332.1; -; mRNA.
DR EMBL; GBKC01002367; JAG43703.1; -; Transcribed_RNA.
DR AlphaFoldDB; T1E5N7; -.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:InterPro.
DR CDD; cd07597; BAR_SNX8; 1.
DR CDD; cd06866; PX_SNX8_Mvp1p_like; 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 InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR028662; SNX8/Mvp1.
DR InterPro; IPR035704; SNX8/Mvp1_PX.
DR InterPro; IPR045734; Snx8_BAR_dom.
DR PANTHER; PTHR46571; SORTING NEXIN-8; 1.
DR PANTHER; PTHR46571:SF1; SORTING NEXIN-8; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF19566; Snx8_BAR_dom; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50195; PX; 1.
PE 2: Evidence at transcript level;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 52..160
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 50772 MW; 5C468954F9B34ADD CRC64;
MDRDEGPEAS PGGAAEVGEP PVSDPKDPEE PRMQKPPGSP LVLPHTLQEL LSKDIVQVQL
IPEKKGLFLK HVEYEVSSKR FRCSVYRRYN DFVVFHEMLL QKFPYRMVPG LPPKRMLGAD
REFIETRRRA LKRFINLVAR HPPFSEDVLL KFFLSFSGSD VQNKLRELVQ GVGDEFMNCQ
FAMQAKEYLP TDIQIQFAAS RELIRNIYNS FYKLRDRTER IASRAVDNAS DLLLFGKELS
ALGSDTTPLP SWAALNSSAW GNLKQALKGL SVEFAMLADK AVQQGKQEEN DVVEKLNLFL
DLLQSYKDLC ERHENGVLHK HQRALHKYSM MKKQMMSATV QNKEPDSVEQ LESRIVEQEN
AILTMEQRNY FSLYCLHQET QLIHIYLPLT SHILGAFVNS QIQGHKEMST VWNELKPKLS
CLFAGTSSVL MLPLSAQEEN FLPS
//
