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Q3UQ28 (PXDN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxidasin homolog
EC=1.11.1.7
Gene names
Name:Pxdn
Synonyms:Kiaa0230
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length1475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Displays low peroxidase activity and is likely to participate in H2O2 metabolism and peroxidative reactions in the cardiovascular system By similarity. Plays a role in extracellular matrix formation.

Catalytic activity

2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Binds 1 heme B (iron-protoporphyrin IX) group covalently per subunit By similarity.

Subcellular location

Secreted › extracellular space › extracellular matrix. Note: Enriched in the peritubular space of fibrotic kidneys. Ref.5

Tissue specificity

Highly expressed in the cardiovascular system. Ref.4

Developmental stage

Expressed in all embryonic tissues at 10 dpc. Detected at 7 dpc. Ref.4 Ref.6

Sequence similarities

Belongs to the peroxidase family. XPO subfamily.

Contains 4 Ig-like C2-type (immunoglobulin-like) domains.

Contains 4 LRR (leucine-rich) repeats.

Contains 1 LRRCT domain.

Contains 1 LRRNT domain.

Contains 1 VWFC domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 14751452Peroxidasin homolog
PRO_0000319620

Regions

Domain24 – 6037LRRNT
Repeat84 – 10522LRR 1
Repeat108 – 12922LRR 2
Repeat132 – 15322LRR 3
Repeat156 – 17722LRR 4
Domain189 – 24254LRRCT
Domain243 – 32987Ig-like C2-type 1
Domain339 – 42587Ig-like C2-type 2
Domain430 – 51788Ig-like C2-type 3
Domain518 – 60790Ig-like C2-type 4
Domain1409 – 146759VWFC

Sites

Active site8241Proton acceptor By similarity
Metal binding8251Calcium By similarity
Metal binding9041Calcium By similarity
Metal binding9061Calcium; via carbonyl oxygen By similarity
Metal binding9081Calcium By similarity
Metal binding9101Calcium By similarity
Metal binding10711Iron (heme axial ligand) By similarity
Binding site8231Heme (covalent; via 2 links) By similarity
Binding site9771Heme (covalent; via 2 links) By similarity
Site9741Transition state stabilizer By similarity

Amino acid modifications

Modified residue11731Phosphotyrosine By similarity
Modified residue11771Phosphoserine By similarity
Glycosylation6371N-linked (GlcNAc...) Potential
Glycosylation6961N-linked (GlcNAc...) Potential
Glycosylation7161N-linked (GlcNAc...) Potential
Glycosylation7281N-linked (GlcNAc...) Potential
Glycosylation11751N-linked (GlcNAc...) Potential
Glycosylation12771N-linked (GlcNAc...) Potential
Glycosylation13641N-linked (GlcNAc...) Potential
Disulfide bond264 ↔ 314 By similarity
Disulfide bond360 ↔ 409 By similarity
Disulfide bond451 ↔ 499 By similarity
Disulfide bond543 ↔ 591 By similarity
Disulfide bond729 ↔ 745 By similarity
Disulfide bond844 ↔ 854 By similarity
Disulfide bond848 ↔ 872 By similarity
Disulfide bond956 ↔ 967 By similarity
Disulfide bond1174 ↔ 1231 By similarity
Disulfide bond1272 ↔ 1298 By similarity

Experimental info

Sequence conflict5491P → Q in BAE25216. Ref.1
Sequence conflict12981C → R in AAI12914. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q3UQ28 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 7F49A5B0D4CDBEB6

FASTA1,475165,103
        10         20         30         40         50         60 
MAVRPTRRCL LALLLCFAWW AMAVVASKQG AGCPSRCLCF RTTVRCMHLL LEAVPAVAPQ 

        70         80         90        100        110        120 
TSILDLRFNR IREIQPGAFR RLRSLNTLLL NNNQIKKIPN GAFEDLENLK YLYLYKNEIQ 

       130        140        150        160        170        180 
SIDRQAFKGL ASLEQLYLHF NQIETLDPES FQHLPKLERL FLHNNRITHL VPGTFSQLES 

       190        200        210        220        230        240 
MKRLRLDSNA LHCDCEILWL ADLLKTYAQS GNAQAAATCE YPRRIQGRSV ATITPEELNC 

       250        260        270        280        290        300 
ERPRITSEPQ DADVTSGNTV YFTCRAEGNP KPEIIWLRNN NELSMKTDSR LNLLDDGTLM 

       310        320        330        340        350        360 
IQNTQEADEG VYQCMAKNVA GEAKTQEVTL RYLGSPARPT FVIQPQNTEV LVGESVTLEC 

       370        380        390        400        410        420 
SATGHPLPQI TWTRGDRTPL PIDPRVNITP SGGLYIQNVA QSDSGEYTCF ASNSVDSIHA 

       430        440        450        460        470        480 
TAFIIVQALP QFTVTPQSRV VIEGQTVDFQ CAAKGHPQPV IAWTKGGSQL SVDRRHLVLS 

       490        500        510        520        530        540 
SGTLRISGVA LHDQGQYECQ AVNIIGSQKV VAHLTVQPRV TPVFASIPSD MTVEVGTNVQ 

       550        560        570        580        590        600 
LPCSSQGEPE PAITWNKDGV QVTESGKFHI SPEGFLTIND VGTADAGRYE CVARNTIGYA 

       610        620        630        640        650        660 
SVSMVLSVNV PDVSRNGDPY VATSIVEAIA TVDRAINSTR THLFDSRPRS PNDLLALFRY 

       670        680        690        700        710        720 
PRDPYTVGQA RAGEIFERTL QLIQEHVQHG LMVDLNGTSY HYNDLVSPQY LSLIANLSGC 

       730        740        750        760        770        780 
TAHRRVNNCS DMCFHQKYRT HDGTCNNLQH PMWGASLTAF ERLLKAVYEN GFNTPRGINS 

       790        800        810        820        830        840 
QRQYNGHVLP MPRLVSTTLI GTEVITPDEQ FTHMLMQWGQ FLDHDLDSTV VALSQARFSD 

       850        860        870        880        890        900 
GQHCSSVCSN DPPCFSVMIP PNDPRVRSGA RCMFFVRSSP VCGSGMTSLL MNSVYPREQI 

       910        920        930        940        950        960 
NQLTSYIDAS NVYGSTDHEA RSIRDLASHR GLLRQGIVQR SGKPLLPFAT GPPTECMRDE 

       970        980        990       1000       1010       1020 
NESPIPCFLA GDHRANEQLG LTSMHTLWFR EHNRIAAELL KLNPHWDGDT VYHETRKIVG 

      1030       1040       1050       1060       1070       1080 
AEIQHITYRH WLPKILGEVG MKMLGEYRGY DPSVNAGIFN AFATAAFRFG HTLINPLLYR 

      1090       1100       1110       1120       1130       1140 
LDENFEPIPQ GHVPLHKAFF SPFRIVNEGG IDPLLRGLFG VAGKMRIPSQ LLNTELTERL 

      1150       1160       1170       1180       1190       1200 
FSMAHTVALD LAAINIQRGR DHGIPPYHDY RVYCNLSAAY TFEDLKNEIK SPVIREKLQR 

      1210       1220       1230       1240       1250       1260 
LYGSTLNIDL FPALMVEDLV PGSRLGPTLM CLLSTQFRRL RDGDRLWYEN PGVFSPAQLT 

      1270       1280       1290       1300       1310       1320 
QLKQTSLARI LCDNSDNITR VQQDVFRVAE FPHGYSSCED IPRVDLRVWQ DCCEDCRTRG 

      1330       1340       1350       1360       1370       1380 
QFNAFSYHFR GRRSLEFSYE DDKPTKRARW RKALSVKHGK HLSNATSATH EHLEGPATND 

      1390       1400       1410       1420       1430       1440 
LKEFVLEMQK IITDLRKQIN SLESRLSTTE CVDDSGESHG GNTKWKKDPC TVCECKNGQI 

      1450       1460       1470 
TCFVEACQPA ACPQPVKVEG ACCPVCLKNT AEEKP

« Hide

References

« Hide 'large scale' references
[1]"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: Head.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"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] OF 370-1475.
Strain: C57BL/6.
Tissue: Brain.
[4]"Identification and characterization of VPO1, a new animal heme-containing peroxidase."
Cheng G., Salerno J.C., Cao Z., Pagano P.J., Lambeth J.D.
Free Radic. Biol. Med. 45:1682-1694(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[5]"Peroxidasin is secreted and incorporated into the extracellular matrix of myofibroblasts and fibrotic kidney."
Peterfi Z., Donko A., Orient A., Sum A., Prokai A., Molnar B., Vereb Z., Rajnavolgyi E., Kovacs K.J., Muller V., Szabo A.J., Geiszt M.
Am. J. Pathol. 175:725-735(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[6]"Expression pattern of LRR and Ig domain-containing protein (LRRIG protein) in the early mouse embryo."
Homma S., Shimada T., Hikake T., Yaginuma H.
Gene Expr. Patterns 9:1-26(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK142872 mRNA. Translation: BAE25216.1.
AC159626 Genomic DNA. No translation available.
AC165078 Genomic DNA. No translation available.
BC112913 mRNA. Translation: AAI12914.1.
IPIIPI00461384.
RefSeqNP_852060.2. NM_181395.2.
UniGeneMm.251774.

3D structure databases

HSSPHSSP built from PDB template 2FT3 based on UniProtKB P21809.
ProteinModelPortalQ3UQ28.
SMRQ3UQ28. Positions 27-673, 735-1311.
ModBaseSearch...

PTM databases

PhosphoSiteQ3UQ28.

Proteomic databases

PaxDbQ3UQ28.
PRIDEQ3UQ28.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000122328; ENSMUSP00000113703; ENSMUSG00000020674.
GeneID69675.
KEGGmmu:69675.
UCSCuc007ngl.2. mouse.

Organism-specific databases

CTD7837.
MGIMGI:1916925. Pxdn.
RougeSearch...

Phylogenomic databases

eggNOGNOG262194.
GeneTreeENSGT00550000074325.
HOGENOMHOG000016084.
HOVERGENHBG108312.
InParanoidQ3UQ28.
OMAEPVITWN.
OrthoDBEOG4J1179.

Gene expression databases

ArrayExpressQ3UQ28.
BgeeQ3UQ28.
CleanExMM_PXDN.
GenevestigatorQ3UQ28.

Family and domain databases

Gene3D1.10.640.10. 2 hits.
2.60.40.10. 4 hits.
InterProIPR000483. Cys-rich_flank_reg_C.
IPR010255. Haem_peroxidase.
IPR002007. Haem_peroxidase_animal.
IPR019791. Haem_peroxidase_animal_subgr.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
IPR001007. VWF_C.
[Graphical view]
PfamPF03098. An_peroxidase. 1 hit.
PF07679. I-set. 4 hits.
PF00560. LRR_1. 1 hit.
PF00093. VWC. 1 hit.
[Graphical view]
PRINTSPR00457. ANPEROXIDASE.
SMARTSM00408. IGc2. 4 hits.
SM00369. LRR_TYP. 4 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
SUPFAMSSF48113. Peroxidase_super. 1 hit.
PROSITEPS50835. IG_LIKE. 4 hits.
PS51450. LRR. 5 hits.
PS00435. PEROXIDASE_1. False negative.
PS00436. PEROXIDASE_2. False negative.
PS50292. PEROXIDASE_3. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio330062.
SOURCESearch...

Entry information

Entry namePXDN_MOUSE
AccessionPrimary (citable) accession number: Q3UQ28
Secondary accession number(s): A4FU83, E9QNQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents