PEX5R_MOUSE
ID PEX5R_MOUSE Reviewed; 567 AA.
AC Q8C437; Q8CA31; Q9DAA1; Q9JMB9;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=PEX5-related protein;
DE AltName: Full=PEX2-related protein;
DE AltName: Full=PEX5-like protein;
DE AltName: Full=Peroxin-5-related protein;
DE AltName: Full=Tetratricopeptide repeat-containing Rab8b-interacting protein;
DE Short=Pex5Rp;
DE Short=TRIP8b;
GN Name=Pex5l; Synonyms=Pex2, Pex5r, Pxr2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RA Sano H., Snider J., Ohta M.;
RT "A novel peroxisomal targeting signal 1 receptor-like gene, PXR2,
RT preferentially expressed in brain.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Hippocampus, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; SER-202; SER-386 AND
RP SER-388, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, AND INTERACTION WITH HCN3.
RX DOI=10.1074/jbc.M112.434803;
RA Cao-Ehlker X., Zong X., Hammelmann V., Gruner C., Fenske S., Michalakis S.,
RA Wahl-Schott C., Biel M.;
RT "Up-regulation of hyperpolarization-activated cyclic nucleotide-gated
RT channel 3 (HCN3) by specific interaction with K+ channel tetramerization
RT domain-containing protein 3 (KCTD3).";
RL J. Biol. Chem. 288:7580-7589(2013).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 206-567 IN COMPLEX WITH HCN2,
RP FUNCTION, AND SUBUNIT.
RX PubMed=22550182; DOI=10.1073/pnas.1201997109;
RA Bankston J.R., Camp S.S., DiMaio F., Lewis A.S., Chetkovich D.M.,
RA Zagotta W.N.;
RT "Structure and stoichiometry of an accessory subunit TRIP8b interaction
RT with hyperpolarization-activated cyclic nucleotide-gated channels.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:7899-7904(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:22550182, ECO:0000269|Ref.5}.
CC -!- SUBUNIT: Interacts with RAB8B (By similarity). Forms an obligate 4:4
CC complex with HCN2 (PubMed:22550182). Interacts with HCN3 (Ref.5).
CC {ECO:0000250|UniProtKB:Q8IYB4, ECO:0000250|UniProtKB:Q925N3,
CC ECO:0000269|PubMed:22550182, ECO:0000269|Ref.5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Note=Some fraction is
CC membrane associated via its interaction with RAB8B. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8C437-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q8C437-3; Sequence=VSP_010439;
CC Name=4;
CC IsoId=Q8C437-4; Sequence=VSP_010437;
CC -!- SIMILARITY: Belongs to the peroxisomal targeting signal receptor
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC38781.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB032591; BAA92877.1; -; mRNA.
DR EMBL; AK006035; BAB24376.1; -; mRNA.
DR EMBL; AK083141; BAC38781.1; ALT_INIT; mRNA.
DR CCDS; CCDS17302.1; -. [Q8C437-3]
DR CCDS; CCDS50888.1; -. [Q8C437-4]
DR CCDS; CCDS50889.1; -. [Q8C437-1]
DR RefSeq; NP_001156988.1; NM_001163516.3.
DR RefSeq; NP_001156989.1; NM_001163517.3. [Q8C437-4]
DR PDB; 4EQF; X-ray; 3.00 A; A=206-567.
DR PDBsum; 4EQF; -.
DR AlphaFoldDB; Q8C437; -.
DR SMR; Q8C437; -.
DR BioGRID; 208454; 45.
DR IntAct; Q8C437; 44.
DR STRING; 10090.ENSMUSP00000103861; -.
DR iPTMnet; Q8C437; -.
DR PhosphoSitePlus; Q8C437; -.
DR MaxQB; Q8C437; -.
DR PaxDb; Q8C437; -.
DR PRIDE; Q8C437; -.
DR ProteomicsDB; 288039; -. [Q8C437-1]
DR ProteomicsDB; 288040; -. [Q8C437-3]
DR ProteomicsDB; 288041; -. [Q8C437-4]
DR ABCD; Q8C437; 5 sequenced antibodies.
DR Antibodypedia; 54548; 47 antibodies from 17 providers.
DR DNASU; 58869; -.
DR Ensembl; ENSMUST00000108221; ENSMUSP00000103856; ENSMUSG00000027674. [Q8C437-4]
DR GeneID; 58869; -.
DR KEGG; mmu:58869; -.
DR UCSC; uc008owt.3; mouse. [Q8C437-1]
DR CTD; 51555; -.
DR MGI; MGI:1916672; Pex5l.
DR VEuPathDB; HostDB:ENSMUSG00000027674; -.
DR eggNOG; KOG1125; Eukaryota.
DR GeneTree; ENSGT00940000155931; -.
DR HOGENOM; CLU_013516_1_0_1; -.
DR InParanoid; Q8C437; -.
DR OrthoDB; 588648at2759; -.
DR PhylomeDB; Q8C437; -.
DR BioGRID-ORCS; 58869; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Pex5l; mouse.
DR PRO; PR:Q8C437; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8C437; protein.
DR Bgee; ENSMUSG00000027674; Expressed in retinal neural layer and 108 other tissues.
DR ExpressionAtlas; Q8C437; baseline and differential.
DR Genevisible; Q8C437; MM.
DR GO; GO:0051286; C:cell tip; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0017071; C:intracellular cyclic nucleotide activated cation channel complex; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0005221; F:intracellular cyclic nucleotide activated cation channel activity; ISO:MGI.
DR GO; GO:0005052; F:peroxisome matrix targeting signal-1 binding; ISO:MGI.
DR GO; GO:0000268; F:peroxisome targeting sequence binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0045185; P:maintenance of protein location; IDA:MGI.
DR GO; GO:0051461; P:positive regulation of corticotropin secretion; ISO:MGI.
DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; IBA:GO_Central.
DR GO; GO:0045055; P:regulated exocytosis; ISO:MGI.
DR GO; GO:0043949; P:regulation of cAMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
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 3D-structure; Alternative splicing; Cytoplasm; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..567
FT /note="PEX5-related protein"
FT /id="PRO_0000106318"
FT REPEAT 267..300
FT /note="TPR 1"
FT REPEAT 301..334
FT /note="TPR 2"
FT REPEAT 336..368
FT /note="TPR 3"
FT REPEAT 415..448
FT /note="TPR 4"
FT REPEAT 450..482
FT /note="TPR 5"
FT REPEAT 484..516
FT /note="TPR 6"
FT REGION 56..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q925N3"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q925N3"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..223
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010437"
FT VAR_SEQ 1..6
FT /note="MYQGHM -> MSDSEMDGRTHIPSLLNALLSRNRVMQMSYLKSKEQGYGKLS
FT SDEDLEIIVDQK (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_010439"
FT CONFLICT 62
FT /note="P -> T (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="N -> K (in Ref. 2; BAB24376)"
FT /evidence="ECO:0000305"
FT TURN 263..266
FT /evidence="ECO:0007829|PDB:4EQF"
FT HELIX 270..280
FT /evidence="ECO:0007829|PDB:4EQF"
FT HELIX 283..296
FT /evidence="ECO:0007829|PDB:4EQF"
FT HELIX 301..313
FT /evidence="ECO:0007829|PDB:4EQF"
FT HELIX 317..330
FT /evidence="ECO:0007829|PDB:4EQF"
FT HELIX 335..347
FT /evidence="ECO:0007829|PDB:4EQF"
FT HELIX 351..364
FT /evidence="ECO:0007829|PDB:4EQF"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:4EQF"
FT HELIX 393..408
FT /evidence="ECO:0007829|PDB:4EQF"
FT HELIX 415..428
FT /evidence="ECO:0007829|PDB:4EQF"
FT HELIX 431..444
FT /evidence="ECO:0007829|PDB:4EQF"
FT HELIX 449..461
FT /evidence="ECO:0007829|PDB:4EQF"
FT HELIX 465..478
FT /evidence="ECO:0007829|PDB:4EQF"
FT HELIX 483..496
FT /evidence="ECO:0007829|PDB:4EQF"
FT HELIX 500..514
FT /evidence="ECO:0007829|PDB:4EQF"
FT HELIX 530..542
FT /evidence="ECO:0007829|PDB:4EQF"
FT HELIX 545..552
FT /evidence="ECO:0007829|PDB:4EQF"
FT HELIX 557..559
FT /evidence="ECO:0007829|PDB:4EQF"
FT TURN 560..564
FT /evidence="ECO:0007829|PDB:4EQF"
SQ SEQUENCE 567 AA; 63135 MW; 4955363C5A70FB28 CRC64;
MYQGHMQLVN EQQESRPLLS PSIDDFLCET KSEAIAKPVT SNTAVLTTGL DLLDLSEPVS
QPQTKAKKSE PSSKSSSLKK KADGSDLISA DAEQRAQALR GPETSSLDLD IQTQLEKWDD
VKFHGDRTSK GHLMAERKSC SSRTGSKELL WSAEHRSQPE LSTGKSALNS ESASELELVA
PAQARLTKEH RWGSALLSRN HSLEEEFERA KAAVESDTEF WDKMQAEWEE MARRNWISEN
QEAQNQVTVS ASEKGYYFHT ENPFKDWPGA FEEGLKRLKE GDLPVTILFM EAAILQDPGD
AEAWQFLGIT QAENENEQAA IVALQRCLEL QPNNLKALMA LAVSYTNTSH QQDACEALKN
WIKQNPKYKY LVKNKKGSPG LTRRMSKSPV DSSVLEGVKE LYLEAAHQNG DMIDPDLQTG
LGVLFHLSGE FNRAIDAFNA ALTVRPEDYS LWNRLGATLA NGDRSEEAVE AYTRALEIQP
GFIRSRYNLG ISCINLGAYR EAVSNFLTAL SLQRKSRNQQ QVPHPAISGN IWAALRIALS
LMDQPELFQA ANLGDLDVLL RAFNLDP
