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SNX30_DANRE
ID   SNX30_DANRE             Reviewed;         430 AA.
AC   Q566W7;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Sorting nexin-30;
GN   Name=snx30; ORFNames=zgc:112424;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the regulation of endocytosis and in several
CC       stages of intracellular trafficking. Together with snx4, involved in
CC       autophagosome assembly. {ECO:0000250|UniProtKB:Q5VWJ9}.
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane
CC       {ECO:0000250|UniProtKB:Q5VWJ9}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:O95219}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:O95219}.
CC   -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR   EMBL; BC093298; AAH93298.1; -; mRNA.
DR   RefSeq; NP_001017798.1; NM_001017798.1.
DR   AlphaFoldDB; Q566W7; -.
DR   SMR; Q566W7; -.
DR   STRING; 7955.ENSDARP00000050176; -.
DR   PaxDb; Q566W7; -.
DR   PRIDE; Q566W7; -.
DR   GeneID; 550496; -.
DR   KEGG; dre:550496; -.
DR   CTD; 401548; -.
DR   ZFIN; ZDB-GENE-050417-330; snx30.
DR   eggNOG; KOG2273; Eukaryota.
DR   InParanoid; Q566W7; -.
DR   OrthoDB; 947320at2759; -.
DR   PhylomeDB; Q566W7; -.
DR   PRO; PR:Q566W7; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR   GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR   GO; GO:2000786; P:positive regulation of autophagosome assembly; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR   GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
DR   Gene3D; 1.20.1270.60; -; 1.
DR   Gene3D; 3.30.1520.10; -; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR028649; SNX30.
DR   PANTHER; PTHR45949:SF1; PTHR45949:SF1; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF103657; SSF103657; 1.
DR   SUPFAM; SSF64268; SSF64268; 1.
DR   PROSITE; PS50195; PX; 1.
PE   2: Evidence at transcript level;
KW   Endosome; Membrane; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..430
FT                   /note="Sorting nexin-30"
FT                   /id="PRO_0000284535"
FT   DOMAIN          80..201
FT                   /note="PX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT   DOMAIN          223..428
FT                   /note="BAR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         123
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-3-phosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58088"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UR97"
FT   BINDING         125
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-3-phosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58088"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UR97"
FT   BINDING         153
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-3-phosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58088"
FT                   /evidence="ECO:0000250|UniProtKB:Q96L94"
FT   BINDING         167
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-3-phosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58088"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P4T1"
SQ   SEQUENCE   430 AA;  49470 MW;  6924F8A9025CEA59 CRC64;
     MSNGGTPRSL PSSGQKSIQE ICHPLSAEES ARSRSPDVLN PGEKDLSLPN GTPVDTSSPA
     SSSSLLNRLQ LDDDLDAETR DLFVTVDDPK KHVSTMETYI TYRVCTKTTR TEFDLPEYSV
     RRRYQDFDWL RIKLEDSQPT HLIPPLPEKF VMKGVVDRFS EEFVETRRKA LDKFLKRVAD
     HPVLSFNEHF NAFLSAKDLN KRQGLALLTK MGESVKYVTG GYKLRGRPVE FAAMGEYLDM
     FTQKLGTIDR IAQRIIKEQT EFLMELREYG PVYSSWSSFE EDLHEPLEGV SGCVSNCSSA
     LEELTEDMSE DFLPVLREYV LYIESMKNVL KKRDQVQAEY ETKLEAVVFR EDKKTPMPTD
     VEKCQDRVEC FNADLKADWD RWQNNKRQDF RQLLTGMADK NIQYYEKCLA AWESLIPLLQ
     DKQDAKGETN
 
 
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