RIPL1_RAT
ID RIPL1_RAT Reviewed; 406 AA.
AC D3ZUQ0;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=RILP-like protein 1;
DE AltName: Full=GAPDH's competitor of SIAH1 protein enhances life;
DE Short=GOSPEL;
DE AltName: Full=Rab-interacting lysosomal-like protein 1;
GN Name=Rilpl1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-289.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH GAPDH,
RP S-NITROSYLATION AT CYS-47, AND MUTAGENESIS OF CYS-47.
RX PubMed=19607794; DOI=10.1016/j.neuron.2009.05.024;
RA Sen N., Hara M.R., Ahmad A.S., Cascio M.B., Kamiya A., Ehmsen J.T.,
RA Agrawal N., Hester L., Dore S., Snyder S.H., Sawa A.;
RT "GOSPEL: a neuroprotective protein that binds to GAPDH upon S-
RT nitrosylation.";
RL Neuron 63:81-91(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=30398148; DOI=10.7554/elife.40202;
RA Dhekne H.S., Yanatori I., Gomez R.C., Tonelli F., Diez F., Schuele B.,
RA Steger M., Alessi D.R., Pfeffer S.R.;
RT "A pathway for Parkinson's Disease LRRK2 kinase to block primary cilia and
RT Sonic hedgehog signaling in the brain.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Plays a role in the regulation of cell shape and polarity (By
CC similarity). Plays a role in cellular protein transport, including
CC protein transport away from primary cilia (By similarity).
CC Neuroprotective protein, which acts by sequestring GAPDH in the cytosol
CC and prevent the apoptotic function of GAPDH in the nucleus
CC (PubMed:19607794). Competes with SIAH1 for binding GAPDH
CC (PubMed:19607794). Does not regulate lysosomal morphology and
CC distribution (By similarity). Binds to RAB10 following LRRK2-mediated
CC RAB10 phosphorylation which leads to inhibition of ciliogenesis (By
CC similarity). {ECO:0000250|UniProtKB:Q5EBL4,
CC ECO:0000250|UniProtKB:Q9JJC6, ECO:0000269|PubMed:19607794}.
CC -!- SUBUNIT: Interacts (when S-nitrosylated) with GAPDH (PubMed:19607794).
CC Interacts with RAB8A; interaction is dependent on the phosphorylation
CC of 'Thr-72' of RAB8A (By similarity). Interacts with RAB10 and RAB12;
CC the interaction is dependent on the phosphorylation of 'Thr-73' of
CC RAB10, and 'Ser-105' of RAB12 (By similarity).
CC {ECO:0000250|UniProtKB:Q5EBL4, ECO:0000269|PubMed:19607794}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19607794}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriole {ECO:0000269|PubMed:30398148}. Cytoplasm, cytoskeleton,
CC cilium basal body {ECO:0000269|PubMed:30398148}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, brain
CC and lung (at protein level). {ECO:0000269|PubMed:19607794}.
CC -!- PTM: S-nitrosylation is required for the interaction with GAPDH.
CC {ECO:0000269|PubMed:19607794}.
CC -!- SIMILARITY: Belongs to the RILPL family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CK357616; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CK600354; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CK357616; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CK600354; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001178594.1; NM_001191665.1.
DR AlphaFoldDB; D3ZUQ0; -.
DR SMR; D3ZUQ0; -.
DR BioGRID; 257870; 2.
DR STRING; 10116.ENSRNOP00000001401; -.
DR iPTMnet; D3ZUQ0; -.
DR PhosphoSitePlus; D3ZUQ0; -.
DR jPOST; D3ZUQ0; -.
DR PaxDb; D3ZUQ0; -.
DR PeptideAtlas; D3ZUQ0; -.
DR PRIDE; D3ZUQ0; -.
DR GeneID; 304469; -.
DR KEGG; rno:304469; -.
DR UCSC; RGD:1307973; rat.
DR CTD; 353116; -.
DR RGD; 1307973; Rilpl1.
DR VEuPathDB; HostDB:ENSRNOG00000001055; -.
DR eggNOG; ENOG502QR9G; Eukaryota.
DR HOGENOM; CLU_044133_3_0_1; -.
DR InParanoid; D3ZUQ0; -.
DR OMA; NHELHGA; -.
DR OrthoDB; 890179at2759; -.
DR PhylomeDB; D3ZUQ0; -.
DR TreeFam; TF313489; -.
DR PRO; PR:D3ZUQ0; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001055; Expressed in skeletal muscle tissue and 20 other tissues.
DR ExpressionAtlas; D3ZUQ0; baseline and differential.
DR Genevisible; D3ZUQ0; RN.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
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; IDA:UniProtKB.
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 GO; GO:1901214; P:regulation of neuron death; IDA:UniProtKB.
DR InterPro; IPR019143; JNK/Rab-associated_protein-1_N.
DR InterPro; IPR034743; RH1.
DR InterPro; IPR034744; RH2.
DR InterPro; IPR021563; RILP_dimer.
DR Pfam; PF09744; Jnk-SapK_ap_N; 1.
DR Pfam; PF11461; RILP; 1.
DR PROSITE; PS51776; RH1; 1.
DR PROSITE; PS51777; RH2; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Protein transport; Reference proteome; S-nitrosylation;
KW Transport.
FT CHAIN 1..406
FT /note="RILP-like protein 1"
FT /id="PRO_0000403768"
FT DOMAIN 10..97
FT /note="RH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01112"
FT DOMAIN 294..359
FT /note="RH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01113"
FT REGION 255..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 76..258
FT /evidence="ECO:0000255"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 47
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:19607794"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5EBL4"
FT MUTAGEN 47
FT /note="C->S: Abolishes S-nitrosylation and subsequent
FT interaction with GAPDH."
FT /evidence="ECO:0000269|PubMed:19607794"
FT CONFLICT 276
FT /note="E -> D (in Ref. 2; CK357616)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 406 AA; 47330 MW; 7216BF52CF49CEE4 CRC64;
MEEPLGSPPA ALSALEKNVA ELTVMDVYDI ASLVGHEFER VIDQHGCEAI ARLMPKVVRV
LEILEVLVSR HHVAPELDEL RLELDRLRVE RMDRIEKERK HQKELELVED VWRGEAQDLL
SQIAQLQEEN KQLMTNLNHK DVGFSEEELQ KHEGMSERER QVMKRLKEVV DKQRDEIRAK
DRELVLKNED VEALQQQQTR LMKINHDLRH RVTVVEAQGK ALIEQKVELE ADLQTKEQEM
GSLRAELGKL RERLQGEHSQ NGEEEEAEIP PQPDGEESIS DAEKAALDLK DPNRPRFTLQ
ELRDVLHERN ELKSKVFLLQ EELAYYKSEE IEEENRIPQP PPITHPRTSP QPESGIKRLF
SFFSRDKRRL ANTQRPTHIH ESFGQWAITH RDDGYTEQGQ EALQHL
