PEX5R_RAT
ID PEX5R_RAT Reviewed; 602 AA.
AC Q925N3;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=PEX5-related protein;
DE AltName: Full=PEX5-like protein;
DE AltName: Full=Peroxin-5-related protein;
DE AltName: Full=TPR-containing Rab8b-interacting protein;
DE AltName: Full=Tetratricopeptide repeat-containing Rab8b-interacting protein;
DE Short=Pex5Rp;
DE Short=TRIP8b;
GN Name=Pex5l; Synonyms=Pex2, Pex5r, Trip8b;
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 [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH RAB8B.
RC TISSUE=Brain;
RX PubMed=11278749; DOI=10.1074/jbc.m010798200;
RA Chen S., Liang M.C., Chia J.N., Ngsee J.K., Ting A.E.;
RT "Rab8b and its interacting partner TRIP8b are involved in regulated
RT secretion in AtT20 cells.";
RL J. Biol. Chem. 276:13209-13216(2001).
RN [2]
RP FUNCTION.
RX PubMed=19555650; DOI=10.1016/j.neuron.2009.05.008;
RA Zolles G., Wenzel D., Bildl W., Schulte U., Hofmann A., Muller C.S.,
RA Thumfart J.O., Vlachos A., Deller T., Pfeifer A., Fleischmann B.K.,
RA Roeper J., Fakler B., Klocker N.;
RT "Association with the auxiliary subunit PEX5R/Trip8b controls
RT responsiveness of HCN channels to cAMP and adrenergic stimulation.";
RL Neuron 62:814-825(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229; SER-233; SER-237 AND
RP SER-423, AND IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: Accessory subunit of hyperpolarization-activated cyclic
CC nucleotide-gated (HCN) channels, regulating their cell-surface
CC expression and cyclic nucleotide dependence.
CC {ECO:0000269|PubMed:19555650}.
CC -!- SUBUNIT: Forms an obligate 4:4 complex with HCN2 (By similarity).
CC Interacts with RAB8B (PubMed:11278749). Interacts with HCN3 (By
CC similarity). {ECO:0000250|UniProtKB:Q8C437,
CC ECO:0000269|PubMed:11278749}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11278749}. Membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Some
CC fraction is membrane associated via its interaction with RAB8B.
CC -!- TISSUE SPECIFICITY: Brain specific. {ECO:0000269|PubMed:11278749}.
CC -!- SIMILARITY: Belongs to the peroxisomal targeting signal receptor
CC family. {ECO:0000305}.
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DR EMBL; AF324454; AAK38580.1; -; mRNA.
DR RefSeq; NP_775175.1; NM_173152.1.
DR AlphaFoldDB; Q925N3; -.
DR SMR; Q925N3; -.
DR BioGRID; 251927; 2.
DR STRING; 10116.ENSRNOP00000015200; -.
DR iPTMnet; Q925N3; -.
DR PhosphoSitePlus; Q925N3; -.
DR jPOST; Q925N3; -.
DR PaxDb; Q925N3; -.
DR PRIDE; Q925N3; -.
DR ABCD; Q925N3; 5 sequenced antibodies.
DR GeneID; 286937; -.
DR KEGG; rno:286937; -.
DR UCSC; RGD:708407; rat.
DR CTD; 51555; -.
DR RGD; 708407; Pex5l.
DR eggNOG; KOG1125; Eukaryota.
DR InParanoid; Q925N3; -.
DR OrthoDB; 588648at2759; -.
DR PhylomeDB; Q925N3; -.
DR PRO; PR:Q925N3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0051286; C:cell tip; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0017071; C:intracellular cyclic nucleotide activated cation channel complex; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0005221; F:intracellular cyclic nucleotide activated cation channel activity; IDA:UniProtKB.
DR GO; GO:0005052; F:peroxisome matrix targeting signal-1 binding; ISO:RGD.
DR GO; GO:0000268; F:peroxisome targeting sequence binding; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; IPI:RGD.
DR GO; GO:0045185; P:maintenance of protein location; ISO:RGD.
DR GO; GO:0051461; P:positive regulation of corticotropin secretion; IDA:RGD.
DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; IBA:GO_Central.
DR GO; GO:0045055; P:regulated exocytosis; IDA:RGD.
DR GO; GO:0043949; P:regulation of cAMP-mediated signaling; IDA:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR024111; PEX5/PEX5L.
DR InterPro; IPR024112; PEX5L_vertebrates.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR10130; PTHR10130; 1.
DR PANTHER; PTHR10130:SF1; PTHR10130:SF1; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW TPR repeat.
FT CHAIN 1..602
FT /note="PEX5-related protein"
FT /id="PRO_0000106319"
FT REPEAT 302..335
FT /note="TPR 1"
FT REPEAT 336..369
FT /note="TPR 2"
FT REPEAT 371..403
FT /note="TPR 3"
FT REPEAT 450..483
FT /note="TPR 4"
FT REPEAT 485..517
FT /note="TPR 5"
FT REPEAT 519..551
FT /note="TPR 6"
FT REGION 94..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C437"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C437"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 602 AA; 66872 MW; 5B8841F2AE1D558F CRC64;
MYQGHMQGKG SRAADKAVAM VMKEIPREES AEEKPLLTMT SQLVNEQQES RPLLSPSIDD
FLCETKSEAI AKPVTSNTAV LTTGLDLLDL SEPVSQTQTK AKKSESSSKS SSLKKKADGS
DLISADAEQR AQALRGPETS SLDLDIQTQL EKWDDVKFHG DRTSKGHLMA ERKSCSSRAG
SKELLWSSEH RSQPELSTGK SALNSESASE LELVAPAQAR LTKEHRWGSA LLSRNHSLEE
EFERAKAAVE SDTEFWDKMQ AEWEEMARRN WISENQEAQN QVTVSASEKG YYFHTENPFK
DWPGAFEEGL KRLKEGDLPV TILFMEAAIL QDPGNAEAWQ FLGITQAENE NEQAAIVALQ
RCLELQPNNL KALMALAVSY TNTSHQQDAC EALKNWIKQN PKYKYLVKNK KGSPGLTRRM
SKSPVDSSVL EGVKDLYLEA AHQNGDMIDP DLQTGLGVLF HLSGEFNRAI DAFNAALTVR
PEDYSLWNRL GATLANGDRS EEAVEAYTRA LEIQPGFIRS RYNLGISCIN LGAYREAVSN
FLTALSLQRK SRNQQQVPHP AISGNIWAAL RIALSLMDQP ELFQAANLGD LDVLLRAFNL
DP
