ID   RANB9_DANRE             Reviewed;         597 AA.
AC   A1L252;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Ran-binding protein 9;
DE            Short=RanBP9;
GN   Name=ranbp9; ORFNames=zgc:158650;
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 (DEC-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}.
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DR   EMBL; BC129352; AAI29353.1; -; mRNA.
DR   RefSeq; NP_001074040.1; NM_001080571.2.
DR   AlphaFoldDB; A1L252; -.
DR   SMR; A1L252; -.
DR   STRING; 7955.ENSDARP00000081043; -.
DR   PaxDb; A1L252; -.
DR   PeptideAtlas; A1L252; -.
DR   GeneID; 558976; -.
DR   KEGG; dre:558976; -.
DR   CTD; 10048; -.
DR   ZFIN; ZDB-GENE-021030-5; ranbp9.
DR   eggNOG; KOG1477; Eukaryota.
DR   InParanoid; A1L252; -.
DR   OrthoDB; 1106989at2759; -.
DR   PhylomeDB; A1L252; -.
DR   Reactome; R-DRE-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-DRE-8851805; MET activates RAS signaling.
DR   PRO; PR:A1L252; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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   GO; GO:0060041; P:retina development in camera-type eye; IMP:ZFIN.
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..597
FT                   /note="Ran-binding protein 9"
FT                   /id="PRO_0000305233"
FT   DOMAIN          29..216
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   DOMAIN          247..279
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT   DOMAIN          285..342
FT                   /note="CTLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT   REGION          343..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          389..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          437..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..375
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        437..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   597 AA;  65582 MW;  BA54B711AF02A1E0 CRC64;
     MSGPSSGCGF LMSVVVHGDL ALNEQEKELN QRLRRLYPAV NEQETPLPRS WSPKDKFSYI
     GLSQNNLRVH YKGHGKTPKD AASVRATHPI PAACGVYYFE VKIISKGRDG YMGIGLSAQG
     VNMNRLPGWD KHSYGYHGDD GHSFCSSGTG QPYGPTFTTG DVIGCCVNLI NNTCFYTKNG
     HSLGIAFTDL PPNLYPTVGL QTPGEVVDAN FGQHPFVFDI EDYMREWRTK IQSQIDRFPI
     GEREGEWQAM IQKMVASYLV HHSYCATAEA FAKSTDQAVH EELASIKNRQ KIQKLVLSGR
     MGEAIETTQQ LYPSLLERNP DLLFMLKVRQ FIEMVNGTDS EVRCLGGRSP KSQDSYPGSP
     RLFNSPVHKP SSSQAYQTGF DSNYCNGVSS SKGHTSAHSH KSCPPTLSSP ELGVLNGSRG
     QQTIVSSEVE MEVDHFSNGV SESSSNGFLN GSSTHGTEQE DCDADMEVDS TQSKRQLCGG
     SQAAIERMIQ FGRELQSMSE HLRRERGKNS ANKKMLKDAF SLLAYSDPWN SPVGYQLDSI
     QREPVCSTLN SAILETHNLP KQPPLALAMG QAAQCLSLMA RTGSGSCAFA SVDDYLH