RIPL2_DANRE
ID RIPL2_DANRE Reviewed; 195 AA.
AC A4IGC3; A5WUX4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=RILP-like protein 2;
DE AltName: Full=Rab-interacting lysosomal-like protein 2;
GN Name=rilpl2; ORFNames=si:ch211-275j6.7, zgc:162589;
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 GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in cell shape and neuronal morphogenesis, positively
CC regulating the establishment and maintenance of dendritic spines. Plays
CC a role in cellular protein transport (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
CC Cell projection, cilium {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RILPL family. {ECO:0000305}.
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DR EMBL; CR847941; CAN87839.1; -; Genomic_DNA.
DR EMBL; BC135027; AAI35028.1; -; mRNA.
DR RefSeq; NP_001077319.1; NM_001083850.1.
DR AlphaFoldDB; A4IGC3; -.
DR SMR; A4IGC3; -.
DR STRING; 7955.ENSDARP00000030815; -.
DR PaxDb; A4IGC3; -.
DR PeptideAtlas; A4IGC3; -.
DR Ensembl; ENSDART00000028954; ENSDARP00000030815; ENSDARG00000024818.
DR GeneID; 100004718; -.
DR KEGG; dre:100004718; -.
DR CTD; 196383; -.
DR ZFIN; ZDB-GENE-030131-6682; rilpl2.
DR eggNOG; ENOG502S08B; Eukaryota.
DR GeneTree; ENSGT00940000160182; -.
DR HOGENOM; CLU_096533_1_0_1; -.
DR InParanoid; A4IGC3; -.
DR OMA; LEMFEIM; -.
DR OrthoDB; 890179at2759; -.
DR PhylomeDB; A4IGC3; -.
DR PRO; PR:A4IGC3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000024818; Expressed in swim bladder and 20 other tissues.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:GOC.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0003382; P:epithelial cell morphogenesis; ISS:UniProtKB.
DR GO; GO:1903445; P:protein transport from ciliary membrane to plasma membrane; ISS:UniProtKB.
DR InterPro; IPR034743; RH1.
DR InterPro; IPR034744; RH2.
DR InterPro; IPR021563; RILP_dimer.
DR Pfam; PF11461; RILP; 1.
DR PROSITE; PS51776; RH1; 1.
DR PROSITE; PS51777; RH2; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..195
FT /note="RILP-like protein 2"
FT /id="PRO_0000317008"
FT DOMAIN 8..92
FT /note="RH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01112"
FT DOMAIN 115..185
FT /note="RH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01113"
FT COILED 58..149
FT /evidence="ECO:0000255"
FT CONFLICT 86
FT /note="T -> M (in Ref. 2; AAI35028)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="L -> S (in Ref. 2; AAI35028)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="E -> D (in Ref. 2; AAI35028)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="P -> Q (in Ref. 2; AAI35028)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 195 AA; 22412 MW; 57B44365AE83D37E CRC64;
MEGRHDNSPT QAFDKDVLEL TVEDVYDISY VIGRDLLKVN TGGNREISDL QFKIVRVLEM
FETMVNKYNL SLEELRMEMD NMRTETDRVV AEGSSGNINT VGPNKLVVDL KDPNRPRFTM
QELKEVLQER NKLKAQLLVA QEELQLYKSG VLSSQQNMVE VNLETVPQSE PLRSSITEES
KEKSTIQKLF SFRPK
