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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
 
 
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