LOCUS NP_057643 626 aa linear PRI 18-DEC-2022
DEFINITION PEX5-related protein isoform 1 [Homo sapiens].
ACCESSION NP_057643
VERSION NP_057643.1
DBSOURCE REFSEQ: accession NM_016559.3
KEYWORDS RefSeq; MANE Select.
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 626)
AUTHORS Chen AS, Liu H, Wu Y, Luo S, Patz EF Jr, Glass C, Su L, Du M,
Christiani DC and Wei Q.
TITLE Genetic variants in DDO and PEX5L in peroxisome-related pathways
predict non-small cell lung cancer survival
JOURNAL Mol Carcinog 61 (7), 619-628 (2022)
PUBMED 35502931
REMARK GeneRIF: Genetic variants in DDO and PEX5L in peroxisome-related
pathways predict non-small cell lung cancer survival.
REFERENCE 2 (residues 1 to 626)
AUTHORS Lyman KA, Han Y, Heuermann RJ, Cheng X, Kurz JE, Lyman RE, Van
Veldhoven PP and Chetkovich DM.
TITLE Allostery between two binding sites in the ion channel subunit
TRIP8b confers binding specificity to HCN channels
JOURNAL J Biol Chem 292 (43), 17718-17730 (2017)
PUBMED 28887304
REMARK GeneRIF: allosteric coupling of the TRIP8b TPR domains both
promotes binding to HCN channels and limits binding to type 1
peroxisomal targeting signal substrates.
REFERENCE 3 (residues 1 to 626)
AUTHORS Bankston JR, DeBerg HA, Stoll S and Zagotta WN.
TITLE Mechanism for the inhibition of the cAMP dependence of HCN ion
channels by the auxiliary subunit TRIP8b
JOURNAL J Biol Chem 292 (43), 17794-17803 (2017)
PUBMED 28864772
REMARK GeneRIF: TRIP8b competes with a portion of the cAMP-binding site or
distorts the binding site by making interactions with the binding
pocket, thus acting predominantly as a competitive antagonist that
inhibits the cyclic-nucleotide dependence of HCN channels.
REFERENCE 4 (residues 1 to 626)
AUTHORS Kunze M, Malkani N, Maurer-Stroh S, Wiesinger C, Schmid JA and
Berger J.
TITLE Mechanistic insights into PTS2-mediated peroxisomal protein import:
the co-receptor PEX5L drastically increases the interaction
strength between the cargo protein and the receptor PEX7
JOURNAL J Biol Chem 290 (8), 4928-4940 (2015)
PUBMED 25538232
REMARK GeneRIF: the sequential formation of a highly stable trimeric
complex involving cargo protein, PEX7 and PEX5L stabilizes cargo
binding and is a prerequisite for PTS2-mediated peroxisomal import.
REFERENCE 5 (residues 1 to 626)
AUTHORS Saponaro A, Pauleta SR, Cantini F, Matzapetakis M, Hammann C,
Donadoni C, Hu L, Thiel G, Banci L, Santoro B and Moroni A.
TITLE Structural basis for the mutual antagonism of cAMP and TRIP8b in
regulating HCN channel function
JOURNAL Proc Natl Acad Sci U S A 111 (40), 14577-14582 (2014)
PUBMED 25197093
REMARK GeneRIF: Data show that Rab8b-interacting protein TRIP8b does not
compete with cyclic AMP for the same binding region of
hyperpolarization activated cyclic nucleotide gated potassium
channel 2 (HCN2).
REFERENCE 6 (residues 1 to 626)
AUTHORS Han Y, Noam Y, Lewis AS, Gallagher JJ, Wadman WJ, Baram TZ and
Chetkovich DM.
TITLE Trafficking and gating of hyperpolarization-activated cyclic
nucleotide-gated channels are regulated by interaction with
tetratricopeptide repeat-containing Rab8b-interacting protein
(TRIP8b) and cyclic AMP at distinct sites
JOURNAL J Biol Chem 286 (23), 20823-20834 (2011)
PUBMED 21504900
REMARK GeneRIF: increasing cAMP levels in cells antagonized the
up-regulation of HCN1 channels mediated by a TRIP8b construct
binding the CNBD exclusively.
REFERENCE 7 (residues 1 to 626)
AUTHORS Sim X, Ong RT, Suo C, Tay WT, Liu J, Ng DP, Boehnke M, Chia KS,
Wong TY, Seielstad M, Teo YY and Tai ES.
TITLE Transferability of type 2 diabetes implicated loci in multi-ethnic
cohorts from Southeast Asia
JOURNAL PLoS Genet 7 (4), e1001363 (2011)
PUBMED 21490949
REFERENCE 8 (residues 1 to 626)
AUTHORS Zolles G, Wenzel D, Bildl W, Schulte U, Hofmann A, Muller CS,
Thumfart JO, Vlachos A, Deller T, Pfeifer A, Fleischmann BK, Roeper
J, Fakler B and Klocker N.
TITLE Association with the auxiliary subunit PEX5R/Trip8b controls
responsiveness of HCN channels to cAMP and adrenergic stimulation
JOURNAL Neuron 62 (6), 814-825 (2009)
PUBMED 19555650
REFERENCE 9 (residues 1 to 626)
AUTHORS Fransen M, Amery L, Hartig A, Brees C, Rabijns A, Mannaerts GP and
Van Veldhoven PP.
TITLE Comparison of the PTS1- and Rab8b-binding properties of Pex5p and
Pex5Rp/TRIP8b
JOURNAL Biochim Biophys Acta 1783 (5), 864-873 (2008)
PUBMED 18346465
REFERENCE 10 (residues 1 to 626)
AUTHORS Amery L, Sano H, Mannaerts GP, Snider J, Van Looy J, Fransen M and
Van Veldhoven PP.
TITLE Identification of PEX5p-related novel peroxisome-targeting signal 1
(PTS1)-binding proteins in mammals
JOURNAL Biochem J 357 (Pt 3), 635-646 (2001)
PUBMED 11463335
COMMENT VALIDATED REFSEQ: This record has undergone validation or
preliminary review. The reference sequence was derived from
DA772743.1, AB032593.1 and AC007687.17.
Transcript Variant: This variant (1) encodes isoform 1.
Sequence Note: This RefSeq record was created from transcript and
genomic sequence data to make the sequence consistent with the
reference genome assembly. The genomic coordinates used for the
transcript record were based on transcript alignments.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
Transcript exon combination :: SRR1660805.210180.1,
SRR1803615.213003.1 [ECO:0000332]
RNAseq introns :: single sample supports all introns
SAMEA2145743, SAMEA2157437
[ECO:0000348]
##Evidence-Data-END##
##RefSeq-Attributes-START##
MANE Ensembl match :: ENST00000467460.6/ ENSP00000419975.1
RefSeq Select criteria :: based on conservation, expression
##RefSeq-Attributes-END##
FEATURES Location/Qualifiers
source 1..626
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="3"
/map="3q26.33"
Protein 1..626
/product="PEX5-related protein isoform 1"
/note="Pex5p-related protein; PEX5-related protein;
PEX5-like protein; PEX2-related protein; peroxin-5-related
protein; peroxisome biogenesis factor 5-like;
tetratricopeptide repeat-containing Rab8b-interacting
protein; HCN channel auxiliary subunit"
/calculated_mol_wt=69566
Region 1..20
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q8IYB4.2)"
Region 118..167
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q8IYB4.2)"
Region 181..235
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q8IYB4.2)"
Site 205
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:Q8C437; propagated from
UniProtKB/Swiss-Prot (Q8IYB4.2)"
Site 253
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:Q925N3; propagated from
UniProtKB/Swiss-Prot (Q8IYB4.2)"
Site 257
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:Q925N3; propagated from
UniProtKB/Swiss-Prot (Q8IYB4.2)"
Site 261
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:Q8C437; propagated from
UniProtKB/Swiss-Prot (Q8IYB4.2)"
Region 326..359
/region_name="TPR 1"
/note="propagated from UniProtKB/Swiss-Prot (Q8IYB4.2)"
Site order(330..331,334..335,337,361,364..365,368..369,
371..372,395,398..399,402..403,406)
/site_type="other"
/note="putative protein binding surface [polypeptide
binding]"
/db_xref="CDD:276809"
Region 330..354
/region_name="TPR repeat"
/note="TPR repeat [structural motif]"
/db_xref="CDD:276809"
Region 331..>561
/region_name="PEP_TPR_lipo"
/note="putative PEP-CTERM system TPR-repeat lipoprotein;
TIGR02917"
/db_xref="CDD:274350"
Region 359..389
/region_name="TPR repeat"
/note="TPR repeat [structural motif]"
/db_xref="CDD:276809"
Region 360..393
/region_name="TPR 2"
/note="propagated from UniProtKB/Swiss-Prot (Q8IYB4.2)"
Region 394..422
/region_name="TPR repeat"
/note="TPR repeat [structural motif]"
/db_xref="CDD:276809"
Region 395..427
/region_name="TPR 3"
/note="propagated from UniProtKB/Swiss-Prot (Q8IYB4.2)"
Site 445
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:Q8C437; propagated from
UniProtKB/Swiss-Prot (Q8IYB4.2)"
Site 447
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:Q8C437; propagated from
UniProtKB/Swiss-Prot (Q8IYB4.2)"
Region 474..507
/region_name="TPR 4"
/note="propagated from UniProtKB/Swiss-Prot (Q8IYB4.2)"
Region 474..502
/region_name="TPR repeat"
/note="TPR repeat [structural motif]"
/db_xref="CDD:276809"
Site order(475,478..479,482..483,485,509,512..513,516..517,
519..520,543,546..547,550..551,554)
/site_type="other"
/note="putative protein binding surface [polypeptide
binding]"
/db_xref="CDD:276809"
Region 507..537
/region_name="TPR repeat"
/note="TPR repeat [structural motif]"
/db_xref="CDD:276809"
Region 509..541
/region_name="TPR 5"
/note="propagated from UniProtKB/Swiss-Prot (Q8IYB4.2)"
Region 542..570
/region_name="TPR repeat"
/note="TPR repeat [structural motif]"
/db_xref="CDD:276809"
Region 543..575
/region_name="TPR 6"
/note="propagated from UniProtKB/Swiss-Prot (Q8IYB4.2)"
CDS 1..626
/gene="PEX5L"
/gene_synonym="PEX5R; PEX5RP; PXR2; PXR2B; TRIP8b"
/coded_by="NM_016559.3:339..2219"
/note="isoform 1 is encoded by transcript variant 1"
/db_xref="CCDS:CCDS3236.1"
/db_xref="GeneID:51555"
/db_xref="HGNC:HGNC:30024"
/db_xref="MIM:611058"
ORIGIN
1 myqghmqksk eqgygklssd edleiivdqk qgkgsraadk avamvmkeip reesaeekpl
61 ltmtsqlvne qqesrpllsp siddflcetk seaiarpvts ntavlttgld lldlsepvsq
121 tqtkakksep ssktsslkkk adgsdlistd aeqrgqplrv petssldldi qtqlekwddv
181 kfhgdrntkg hpmaerksss srtgskellw ssehrsqpel sggksalnse saselelvap
241 tqarltkehr wgsallsrnh sleeeferak aavesdtefw dkmqaeweem arrnwisenq
301 eaqnqvtisa sekgyyfhte npfkdwpgaf eeglkrlkeg dlpvtilfme aailqdpgda
361 eawqflgitq aeneneqaai valqrclelq pnnlkalmal avsytntghq qdacdalknw
421 ikqnpkykyl vkskkgspgl trrmskspvd ssvlegvkel yleaahqngd midpdlqtgl
481 gvlfhlsgef nraidafnaa ltvrpedysl wnrlgatlan gdrseeavea ytraleiqpg
541 firsrynlgi scinlgayre avsnfltals lqrksrnqqq vphpaisgni waalrialsl
601 mdqpelfqaa nlgdldvllr afnldp
//