RANB9_XENTR
ID RANB9_XENTR Reviewed; 548 AA.
AC Q28FM1;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Ran-binding protein 9;
DE Short=RanBP9;
DE AltName: Full=Ran-binding protein 10;
DE Short=RanBP10;
DE AltName: Full=Ran-binding protein M;
DE Short=RanBPM;
GN Name=ranbp9; Synonyms=ranbp10, ranbpm; ORFNames=TNeu108a21.1;
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=Neurula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May act as scaffolding protein, and as adapter protein to
CC couple membrane receptors to intracellular signaling pathways. Acts as
CC a mediator of cell spreading and actin cytoskeleton rearrangement. Core
CC component of the CTLH E3 ubiquitin-protein ligase complex that mediates
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. {ECO:0000250|UniProtKB:Q96S59}.
CC -!- SUBUNIT: Identified in the CTLH complex that contains at least MAEA,
CC RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9
CC and/or RANBP10. {ECO:0000250|UniProtKB:Q96S59}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P69566}. Cell
CC membrane {ECO:0000250|UniProtKB:P69566}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P69566}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P69566}. Nucleus {ECO:0000250|UniProtKB:P69566}.
CC Note=Predominantly cytoplasmic. {ECO:0000250|UniProtKB:P69566}.
CC -!- SIMILARITY: Belongs to the RANBP9/10 family. {ECO:0000305}.
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; CR761896; CAJ83297.1; -; mRNA.
DR RefSeq; NP_001037977.1; NM_001044512.1.
DR AlphaFoldDB; Q28FM1; -.
DR SMR; Q28FM1; -.
DR STRING; 8364.ENSXETP00000020490; -.
DR PaxDb; Q28FM1; -.
DR GeneID; 733762; -.
DR KEGG; xtr:733762; -.
DR CTD; 10048; -.
DR Xenbase; XB-GENE-494852; ranbp9.
DR eggNOG; KOG1477; Eukaryota.
DR HOGENOM; CLU_009129_4_1_1; -.
DR InParanoid; Q28FM1; -.
DR OMA; GRDGXWD; -.
DR OrthoDB; 1106989at2759; -.
DR PhylomeDB; Q28FM1; -.
DR TreeFam; TF331658; -.
DR Reactome; R-XTR-5673001; RAF/MAP kinase cascade.
DR Reactome; R-XTR-8851805; MET activates RAS signaling.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
DR ExpressionAtlas; Q28FM1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR CDD; cd12909; SPRY_RanBP9_10; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035782; SPRY_RanBP9/10.
DR Pfam; PF10607; CLTH; 1.
DR Pfam; PF08513; LisH; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00757; CRA; 1.
DR SMART; SM00668; CTLH; 1.
DR SMART; SM00667; LisH; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Membrane; Nucleus; Reference proteome.
FT CHAIN 1..548
FT /note="Ran-binding protein 9"
FT /id="PRO_0000305235"
FT DOMAIN 2..189
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT DOMAIN 217..249
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 255..312
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 548 AA; 60403 MW; ED08C495FC4479C7 CRC64;
MSSPPLHGLS SGGHLSRDPP PRSWSPRDKC SYLGLSHGNL RVHYKGHGKT SKDAASVRST
HPIPAACGIF YFEVKIISKG RDGYMGIGLS TQGVNLSRLP GWDKHSYGYH GDDGHSFCSS
GTGQPYGPTF TTGDVIGCCV NLIDNTCFYT KNGHSLGIAF TDLPPNLYPT VGLQTPGEVV
DANFGQSPFV FDIEDYIREW RTKIQAQIER FPVGGEWQSM IQRMVSSYLV HHGYCSTAEA
FAKSTDQTVQ EELASIKNRQ RIQKLVLSGR MGEAIETTQQ LYPSLLERNP NLLFTLKVRQ
FIEMVNGTDS EVRCLGNRSL KSLDGCSGSD SNCSNGIISN KAHQTHCHSK SQSSNLNVTE
LNSINMTMSH QLNSYSSNDV EMETDHYSNG FSASTSNGFL NGSSRHEPEL EECDTEMEVD
TSHGRRQLCG GSQAAVERMI CFGRELQAMS EQLRRERGKN ATNKNMLKDA FSLLAYSDPW
NSPVGYQLDP IQREHVCSSL NSAILDIHNL PKQPPLSLAL EQASQCLEMM AQCGIGSCAF
ARVADYLH