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SNX30_XENTR
ID   SNX30_XENTR             Reviewed;         446 AA.
AC   Q28E02;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Sorting nexin-30;
GN   Name=snx30; ORFNames=TEgg065l16.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) 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; CR848512; CAJ81312.1; -; mRNA.
DR   RefSeq; NP_001016905.1; NM_001016905.2.
DR   AlphaFoldDB; Q28E02; -.
DR   SMR; Q28E02; -.
DR   STRING; 8364.ENSXETP00000004753; -.
DR   PaxDb; Q28E02; -.
DR   PRIDE; Q28E02; -.
DR   GeneID; 549659; -.
DR   KEGG; xtr:549659; -.
DR   CTD; 401548; -.
DR   Xenbase; XB-GENE-944717; snx30.
DR   eggNOG; KOG2273; Eukaryota.
DR   HOGENOM; CLU_040655_1_0_1; -.
DR   InParanoid; Q28E02; -.
DR   OMA; FIWLRQK; -.
DR   OrthoDB; 947320at2759; -.
DR   PhylomeDB; Q28E02; -.
DR   TreeFam; TF328543; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000002230; Expressed in egg cell and 14 other tissues.
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; IPR004148; BAR_dom.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR028649; SNX30.
DR   PANTHER; PTHR45949:SF1; PTHR45949:SF1; 1.
DR   Pfam; PF03114; BAR; 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..446
FT                   /note="Sorting nexin-30"
FT                   /id="PRO_0000284537"
FT   DOMAIN          98..219
FT                   /note="PX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT   DOMAIN          243..446
FT                   /note="BAR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT   REGION          1..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..84
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         141
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         143
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         171
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         185
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   446 AA;  50959 MW;  5139CBB3EB5EE420 CRC64;
     MSGSSTPKSL PTSGQQSLHD IKHPLSCSPS AEDDAAGENG AVIIESPSPD LPNTEPSSLA
     DKDLSLPNGT PADTSSPASS SSLLNRLQLD DDLDGETRDL FVTVDDPKKH VCTMETYITY
     RVSTKTTRTE FDLPEYSIRR RYQDFDWLRN KLEETQPTHF IPPLPEKFVV KGVVDRFSEE
     FVETRRKALD KFLKRIADHP VLSFNEHFNV FLTAKDLNSH KKQGITLLSK MGESVRYVTS
     GYKLRNRPVE FATITDYLDT FQLKLGTIDR IAQRIIKEEV EYLMELREYG PVYSTWSGLE
     RELNEPLEGV SACVGNCSTA LEELTEDMSE DFLPVIREYM LYSESMKTVL KKRDQVQAEY
     EAKAEAAALK REERSTVPTD VEKCQDKVEC FNADLKADMD RWQNNKRQDF RQLLMGMADK
     NIQYYEKCLT AWESIIPLLQ DKQEPK
 
 
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