PEX13_MOUSE
ID PEX13_MOUSE Reviewed; 405 AA.
AC Q9D0K1; Q3U5T1; Q8CCJ5; Q8CCW5; Q99MM2; Q9EPK1;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Peroxisomal membrane protein PEX13;
DE AltName: Full=Peroxin-13;
GN Name=Pex13;
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].
RC STRAIN=129/SvJ;
RX PubMed=11829486; DOI=10.1006/geno.2002.6697;
RA Bjoerkman J., Gould S.J., Crane D.I.;
RT "Pex13, the mouse ortholog of the human peroxisome biogenesis disorder
RT PEX13 gene: gene structure, tissue expression, and localization of the
RT protein to peroxisomes.";
RL Genomics 79:162-168(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Van Veldhoven P.P.;
RT "Cloning of mouse peroxins.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, Cerebellum, Embryo, 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [7]
RP STRUCTURE BY NMR OF 267-347.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SH3 domain of mouse peroxisomal biogenesis
RT factor 13.";
RL Submitted (JAN-2006) to the PDB data bank.
CC -!- FUNCTION: Component of the peroxisomal translocation machinery with
CC PEX14 and PEX17. Functions as a docking factor for the predominantly
CC cytoplasmic PTS1 receptor (PAS10/PEX5). Involved in the import of PTS1
CC and PTS2 proteins (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PEX19. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peroxin-13 family. {ECO:0000305}.
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DR EMBL; AF329877; AAK15313.2; -; mRNA.
DR EMBL; AJ304506; CAC20705.1; -; mRNA.
DR EMBL; AK011355; BAB27563.1; -; mRNA.
DR EMBL; AK029099; BAC26296.1; -; mRNA.
DR EMBL; AK029336; BAC26402.1; -; mRNA.
DR EMBL; AK031710; BAC27526.1; -; mRNA.
DR EMBL; AK031975; BAC27635.1; -; mRNA.
DR EMBL; AK032650; BAC27971.1; -; mRNA.
DR EMBL; AK153438; BAE31995.1; -; mRNA.
DR EMBL; AK169148; BAE40927.1; -; mRNA.
DR EMBL; BC023683; AAH23683.1; -; mRNA.
DR CCDS; CCDS24478.1; -.
DR RefSeq; NP_076140.2; NM_023651.4.
DR PDB; 1WXU; NMR; -; A=267-346.
DR PDBsum; 1WXU; -.
DR AlphaFoldDB; Q9D0K1; -.
DR SMR; Q9D0K1; -.
DR STRING; 10090.ENSMUSP00000020523; -.
DR iPTMnet; Q9D0K1; -.
DR PhosphoSitePlus; Q9D0K1; -.
DR EPD; Q9D0K1; -.
DR MaxQB; Q9D0K1; -.
DR PaxDb; Q9D0K1; -.
DR PeptideAtlas; Q9D0K1; -.
DR PRIDE; Q9D0K1; -.
DR ProteomicsDB; 301792; -.
DR Antibodypedia; 30577; 118 antibodies from 31 providers.
DR DNASU; 72129; -.
DR Ensembl; ENSMUST00000020523; ENSMUSP00000020523; ENSMUSG00000020283.
DR GeneID; 72129; -.
DR KEGG; mmu:72129; -.
DR UCSC; uc007ifj.1; mouse.
DR CTD; 5194; -.
DR MGI; MGI:1919379; Pex13.
DR VEuPathDB; HostDB:ENSMUSG00000020283; -.
DR eggNOG; KOG3875; Eukaryota.
DR GeneTree; ENSGT00390000016883; -.
DR HOGENOM; CLU_045457_0_0_1; -.
DR InParanoid; Q9D0K1; -.
DR OMA; QPKIRGW; -.
DR OrthoDB; 1085263at2759; -.
DR PhylomeDB; Q9D0K1; -.
DR TreeFam; TF327117; -.
DR Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR Reactome; R-MMU-9603798; Class I peroxisomal membrane protein import.
DR BioGRID-ORCS; 72129; 8 hits in 72 CRISPR screens.
DR ChiTaRS; Pex13; mouse.
DR EvolutionaryTrace; Q9D0K1; -.
DR PRO; PR:Q9D0K1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9D0K1; protein.
DR Bgee; ENSMUSG00000020283; Expressed in seminiferous tubule of testis and 252 other tissues.
DR ExpressionAtlas; Q9D0K1; baseline and differential.
DR Genevisible; Q9D0K1; MM.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; ISO:MGI.
DR GO; GO:1990429; C:peroxisomal importomer complex; IBA:GO_Central.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:MGI.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0000268; F:peroxisome targeting sequence binding; TAS:MGI.
DR GO; GO:0021795; P:cerebral cortex cell migration; IMP:MGI.
DR GO; GO:0001561; P:fatty acid alpha-oxidation; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0060152; P:microtubule-based peroxisome localization; IMP:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; IMP:MGI.
DR GO; GO:0001967; P:suckling behavior; IMP:MGI.
DR InterPro; IPR007223; Peroxin-13_N.
DR InterPro; IPR035463; Pex13.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR19332; PTHR19332; 1.
DR Pfam; PF04088; Peroxin-13_N; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Peroxisome; Phosphoprotein; Protein transport;
KW Reference proteome; SH3 domain; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..405
FT /note="Peroxisomal membrane protein PEX13"
FT /id="PRO_0000240662"
FT TOPO_DOM 1..235
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 274..338
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT CONFLICT 177
FT /note="F -> C (in Ref. 2; CAC20705)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="M -> K (in Ref. 3; BAC27635)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="L -> I (in Ref. 2; CAC20705)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="G -> S (in Ref. 2; CAC20705)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="D -> N (in Ref. 3; BAE31995)"
FT /evidence="ECO:0000305"
FT CONFLICT 239..241
FT /note="FLF -> ILS (in Ref. 2; CAC20705)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="E -> G (in Ref. 3; BAE31995)"
FT /evidence="ECO:0000305"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:1WXU"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:1WXU"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:1WXU"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:1WXU"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:1WXU"
FT STRAND 316..324
FT /evidence="ECO:0007829|PDB:1WXU"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:1WXU"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:1WXU"
FT TURN 343..346
FT /evidence="ECO:0007829|PDB:1WXU"
SQ SEQUENCE 405 AA; 44610 MW; 4ABF0463211AA466 CRC64;
MASQPPPPPK PWESRRIPGA GPGPGSGPGP TYQSADLGPT LLTRPGQPTL TRVPPPILPR
PSQQTGSNNV NTFRPAYSSF SSGYGAYGNS FYGSYSPYSY GYNGLGFNRL RVDDLPPSRF
VQQAEESSRG AFQSIESIVH AFASVSMMMD ATFSAVYNSF RAVLDVANHF SRLKIHFTKV
FSAFALVRTI RYLYRRLQWM MGLRRGSENE DLWAESEGTV ACLSAEDQAT NSAKSWPIFL
FFAVILGGPY LIWKLLSTHN DEVTDNTNWA SGEDDHVVAR AEYDFVAVSD EEISFRAGDM
LNLALKEQQP KVRGWLLASL DGQTTGLIPA NYVKILGKRR GRKTIESSTM LKQQQSFTNP
TLIKGVTTTN PLDEQEAAFE SVFVETNKVS SAPDSTGKNG DKQDL
