Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9D0K1 (PEX13_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxisomal membrane protein PEX13
Alternative name(s):
Peroxin-13
Gene names
Name:Pex13
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length405 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the peroxisomal translocation machinery with PEX14 and PEX17. Functions as a docking factor for the predominantly cytoplasmic PTS1 receptor (PAS10/PEX5). Involved in the import of PTS1 and PTS2 proteins By similarity.

Subunit structure

Interacts with PEX19 By similarity.

Subcellular location

Peroxisome membrane; Single-pass membrane protein By similarity.

Sequence similarities

Belongs to the peroxin-13 family.

Contains 1 SH3 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 405405Peroxisomal membrane protein PEX13
PRO_0000240662

Regions

Topological domain1 – 235235Lumenal Potential
Transmembrane236 – 25621Helical; Potential
Topological domain257 – 405149Cytoplasmic Potential
Domain274 – 33865SH3
Compositional bias5 – 6157Pro-rich

Amino acid modifications

Modified residue3561Phosphoserine Ref.5

Experimental info

Sequence conflict1771F → C in CAC20705. Ref.2
Sequence conflict2001M → K in BAC27635. Ref.3
Sequence conflict2031L → I in CAC20705. Ref.2
Sequence conflict2061G → S in CAC20705. Ref.2
Sequence conflict2271D → N in BAE31995. Ref.3
Sequence conflict239 – 2413FLF → ILS in CAC20705. Ref.2
Sequence conflict2911E → G in BAE31995. Ref.3

Secondary structure

.................. 405
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9D0K1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 4ABF0463211AA466

FASTA40544,610
        10         20         30         40         50         60 
MASQPPPPPK PWESRRIPGA GPGPGSGPGP TYQSADLGPT LLTRPGQPTL TRVPPPILPR 

        70         80         90        100        110        120 
PSQQTGSNNV NTFRPAYSSF SSGYGAYGNS FYGSYSPYSY GYNGLGFNRL RVDDLPPSRF 

       130        140        150        160        170        180 
VQQAEESSRG AFQSIESIVH AFASVSMMMD ATFSAVYNSF RAVLDVANHF SRLKIHFTKV 

       190        200        210        220        230        240 
FSAFALVRTI RYLYRRLQWM MGLRRGSENE DLWAESEGTV ACLSAEDQAT NSAKSWPIFL 

       250        260        270        280        290        300 
FFAVILGGPY LIWKLLSTHN DEVTDNTNWA SGEDDHVVAR AEYDFVAVSD EEISFRAGDM 

       310        320        330        340        350        360 
LNLALKEQQP KVRGWLLASL DGQTTGLIPA NYVKILGKRR GRKTIESSTM LKQQQSFTNP 

       370        380        390        400 
TLIKGVTTTN PLDEQEAAFE SVFVETNKVS SAPDSTGKNG DKQDL 

« Hide

References

« Hide 'large scale' references
[1]"Pex13, the mouse ortholog of the human peroxisome biogenesis disorder PEX13 gene: gene structure, tissue expression, and localization of the protein to peroxisomes."
Bjoerkman J., Gould S.J., Crane D.I.
Genomics 79:162-168(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 129/SvJ.
[2]"Cloning of mouse peroxins."
Van Veldhoven P.P.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Amnion, Cerebellum, Embryo and Testis.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"Solution structure of the SH3 domain of mouse peroxisomal biogenesis factor 13."
RIKEN structural genomics initiative (RSGI)
Submitted (JAN-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 267-347.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF329877 mRNA. Translation: AAK15313.2.
AJ304506 mRNA. Translation: CAC20705.1.
AK011355 mRNA. Translation: BAB27563.1.
AK029099 mRNA. Translation: BAC26296.1.
AK029336 mRNA. Translation: BAC26402.1.
AK031710 mRNA. Translation: BAC27526.1.
AK031975 mRNA. Translation: BAC27635.1.
AK032650 mRNA. Translation: BAC27971.1.
AK153438 mRNA. Translation: BAE31995.1.
AK169148 mRNA. Translation: BAE40927.1.
BC023683 mRNA. Translation: AAH23683.1.
CCDSCCDS24478.1.
RefSeqNP_076140.2. NM_023651.4.
UniGeneMm.286622.
Mm.29536.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WXUNMR-A267-346[»]
ProteinModelPortalQ9D0K1.
SMRQ9D0K1. Positions 264-347.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9D0K1.

Proteomic databases

PaxDbQ9D0K1.
PRIDEQ9D0K1.

Protocols and materials databases

DNASU72129.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020523; ENSMUSP00000020523; ENSMUSG00000020283.
GeneID72129.
KEGGmmu:72129.
UCSCuc007ifj.1. mouse.

Organism-specific databases

CTD5194.
MGIMGI:1919379. Pex13.

Phylogenomic databases

eggNOGNOG281515.
GeneTreeENSGT00390000016883.
HOGENOMHOG000231374.
HOVERGENHBG053570.
InParanoidQ9D0K1.
KOK13344.
OMAYRRLQWM.
OrthoDBEOG7VX8W3.
PhylomeDBQ9D0K1.
TreeFamTF327117.

Gene expression databases

ArrayExpressQ9D0K1.
BgeeQ9D0K1.
CleanExMM_PEX13.
GenevestigatorQ9D0K1.

Family and domain databases

InterProIPR007223. Peroxin-13_N.
IPR001452. SH3_domain.
[Graphical view]
PfamPF04088. Peroxin-13_N. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9D0K1.
NextBio335514.
PROQ9D0K1.
SOURCESearch...

Entry information

Entry namePEX13_MOUSE
AccessionPrimary (citable) accession number: Q9D0K1
Secondary accession number(s): Q3U5T1 expand/collapse secondary AC list , Q8CCJ5, Q8CCW5, Q99MM2, Q9EPK1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot