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Q3UQ28

- PXDN_MOUSE

UniProt

Q3UQ28 - PXDN_MOUSE

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Protein

Peroxidasin homolog

Gene

Pxdn

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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.By similarity

Catalytic activityi

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

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei823 – 8231Heme (covalent; via 2 links)By similarity
Active sitei824 – 8241Proton acceptorPROSITE-ProRule annotation
Metal bindingi825 – 8251CalciumPROSITE-ProRule annotation
Metal bindingi904 – 9041CalciumPROSITE-ProRule annotation
Metal bindingi906 – 9061Calcium; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi908 – 9081CalciumPROSITE-ProRule annotation
Metal bindingi910 – 9101CalciumPROSITE-ProRule annotation
Sitei974 – 9741Transition state stabilizerPROSITE-ProRule annotation
Binding sitei977 – 9771Heme (covalent; via 2 links)By similarity
Metal bindingi1071 – 10711Iron (heme axial ligand)PROSITE-ProRule annotation

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: Ensembl
  2. heme binding Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. peroxidase activity Source: UniProtKB

GO - Biological processi

  1. extracellular matrix organization Source: UniProtKB
  2. hydrogen peroxide catabolic process Source: UniProtKB
  3. oxidation-reduction process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxidasin homolog (EC:1.11.1.7)
Gene namesi
Name:Pxdn
Synonyms:Kiaa0230
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:1916925. Pxdn.

Subcellular locationi

Secretedextracellular spaceextracellular matrix 1 Publication
Note: Enriched in the peritubular space of fibrotic kidneys.

GO - Cellular componenti

  1. endoplasmic reticulum Source: Ensembl
  2. extracellular matrix Source: UniProtKB
  3. extracellular space Source: UniProtKB
  4. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 14751452Peroxidasin homologPRO_0000319620Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi264 ↔ 314By similarity
Disulfide bondi360 ↔ 409By similarity
Disulfide bondi451 ↔ 499By similarity
Disulfide bondi543 ↔ 591By similarity
Glycosylationi637 – 6371N-linked (GlcNAc...)Sequence Analysis
Glycosylationi696 – 6961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi716 – 7161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi728 – 7281N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi729 ↔ 745By similarity
Disulfide bondi844 ↔ 854By similarity
Disulfide bondi848 ↔ 872By similarity
Disulfide bondi956 ↔ 967By similarity
Modified residuei1173 – 11731PhosphotyrosineBy similarity
Disulfide bondi1174 ↔ 1231By similarity
Glycosylationi1175 – 11751N-linked (GlcNAc...)Sequence Analysis
Modified residuei1177 – 11771PhosphoserineBy similarity
Disulfide bondi1272 ↔ 1298By similarity
Glycosylationi1277 – 12771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1364 – 13641N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ3UQ28.
PaxDbiQ3UQ28.
PRIDEiQ3UQ28.

PTM databases

PhosphoSiteiQ3UQ28.

Expressioni

Tissue specificityi

Highly expressed in the cardiovascular system. In the embryo, expressed in the corneal epithelial layer. In the adult eyes, expressed in the corneal and lens epithelium.2 Publications

Developmental stagei

Expressed in all embryonic tissues at 10 dpc. Detected at 7 dpc.2 Publications

Gene expression databases

BgeeiQ3UQ28.
CleanExiMM_PXDN.
ExpressionAtlasiQ3UQ28. baseline and differential.
GenevestigatoriQ3UQ28.

Interactioni

Protein-protein interaction databases

BioGridi213608. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ3UQ28.
SMRiQ3UQ28. Positions 27-673, 735-1311.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 6037LRRNTAdd
BLAST
Repeati84 – 10522LRR 1Add
BLAST
Repeati108 – 12922LRR 2Add
BLAST
Repeati132 – 15322LRR 3Add
BLAST
Repeati156 – 17722LRR 4Add
BLAST
Domaini189 – 24254LRRCTAdd
BLAST
Domaini243 – 32987Ig-like C2-type 1Add
BLAST
Domaini339 – 42587Ig-like C2-type 2Add
BLAST
Domaini430 – 51788Ig-like C2-type 3Add
BLAST
Domaini518 – 60790Ig-like C2-type 4Add
BLAST
Domaini1409 – 146759VWFCPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peroxidase family. XPO subfamily.PROSITE-ProRule annotation
Contains 4 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated
Contains 1 LRRNT domain.Curated
Contains 1 VWFC domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Leucine-rich repeat, Repeat, Signal

Phylogenomic databases

eggNOGiNOG262194.
GeneTreeiENSGT00550000074325.
HOGENOMiHOG000016084.
HOVERGENiHBG108312.
InParanoidiQ3UQ28.
OMAiEPVITWN.
OrthoDBiEOG7D2FD6.
TreeFamiTF314316.

Family and domain databases

Gene3Di1.10.640.10. 2 hits.
2.60.40.10. 4 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
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]
PfamiPF03098. An_peroxidase. 1 hit.
PF07679. I-set. 4 hits.
PF00560. LRR_1. 1 hit.
PF13855. LRR_8. 1 hit.
PF00093. VWC. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SMARTiSM00408. IGc2. 4 hits.
SM00369. LRR_TYP. 4 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS50835. IG_LIKE. 4 hits.
PS51450. LRR. 5 hits.
PS50292. PEROXIDASE_3. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3UQ28 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVRPTRRCL LALLLCFAWW AMAVVASKQG AGCPSRCLCF RTTVRCMHLL
60 70 80 90 100
LEAVPAVAPQ TSILDLRFNR IREIQPGAFR RLRSLNTLLL NNNQIKKIPN
110 120 130 140 150
GAFEDLENLK YLYLYKNEIQ SIDRQAFKGL ASLEQLYLHF NQIETLDPES
160 170 180 190 200
FQHLPKLERL FLHNNRITHL VPGTFSQLES MKRLRLDSNA LHCDCEILWL
210 220 230 240 250
ADLLKTYAQS GNAQAAATCE YPRRIQGRSV ATITPEELNC ERPRITSEPQ
260 270 280 290 300
DADVTSGNTV YFTCRAEGNP KPEIIWLRNN NELSMKTDSR LNLLDDGTLM
310 320 330 340 350
IQNTQEADEG VYQCMAKNVA GEAKTQEVTL RYLGSPARPT FVIQPQNTEV
360 370 380 390 400
LVGESVTLEC SATGHPLPQI TWTRGDRTPL PIDPRVNITP SGGLYIQNVA
410 420 430 440 450
QSDSGEYTCF ASNSVDSIHA TAFIIVQALP QFTVTPQSRV VIEGQTVDFQ
460 470 480 490 500
CAAKGHPQPV IAWTKGGSQL SVDRRHLVLS SGTLRISGVA LHDQGQYECQ
510 520 530 540 550
AVNIIGSQKV VAHLTVQPRV TPVFASIPSD MTVEVGTNVQ LPCSSQGEPE
560 570 580 590 600
PAITWNKDGV QVTESGKFHI SPEGFLTIND VGTADAGRYE CVARNTIGYA
610 620 630 640 650
SVSMVLSVNV PDVSRNGDPY VATSIVEAIA TVDRAINSTR THLFDSRPRS
660 670 680 690 700
PNDLLALFRY PRDPYTVGQA RAGEIFERTL QLIQEHVQHG LMVDLNGTSY
710 720 730 740 750
HYNDLVSPQY LSLIANLSGC TAHRRVNNCS DMCFHQKYRT HDGTCNNLQH
760 770 780 790 800
PMWGASLTAF ERLLKAVYEN GFNTPRGINS QRQYNGHVLP MPRLVSTTLI
810 820 830 840 850
GTEVITPDEQ FTHMLMQWGQ FLDHDLDSTV VALSQARFSD GQHCSSVCSN
860 870 880 890 900
DPPCFSVMIP PNDPRVRSGA RCMFFVRSSP VCGSGMTSLL MNSVYPREQI
910 920 930 940 950
NQLTSYIDAS NVYGSTDHEA RSIRDLASHR GLLRQGIVQR SGKPLLPFAT
960 970 980 990 1000
GPPTECMRDE NESPIPCFLA GDHRANEQLG LTSMHTLWFR EHNRIAAELL
1010 1020 1030 1040 1050
KLNPHWDGDT VYHETRKIVG AEIQHITYRH WLPKILGEVG MKMLGEYRGY
1060 1070 1080 1090 1100
DPSVNAGIFN AFATAAFRFG HTLINPLLYR LDENFEPIPQ GHVPLHKAFF
1110 1120 1130 1140 1150
SPFRIVNEGG IDPLLRGLFG VAGKMRIPSQ LLNTELTERL FSMAHTVALD
1160 1170 1180 1190 1200
LAAINIQRGR DHGIPPYHDY RVYCNLSAAY TFEDLKNEIK SPVIREKLQR
1210 1220 1230 1240 1250
LYGSTLNIDL FPALMVEDLV PGSRLGPTLM CLLSTQFRRL RDGDRLWYEN
1260 1270 1280 1290 1300
PGVFSPAQLT QLKQTSLARI LCDNSDNITR VQQDVFRVAE FPHGYSSCED
1310 1320 1330 1340 1350
IPRVDLRVWQ DCCEDCRTRG QFNAFSYHFR GRRSLEFSYE DDKPTKRARW
1360 1370 1380 1390 1400
RKALSVKHGK HLSNATSATH EHLEGPATND LKEFVLEMQK IITDLRKQIN
1410 1420 1430 1440 1450
SLESRLSTTE CVDDSGESHG GNTKWKKDPC TVCECKNGQI TCFVEACQPA
1460 1470
ACPQPVKVEG ACCPVCLKNT AEEKP
Length:1,475
Mass (Da):165,103
Last modified:July 27, 2011 - v2
Checksum:i7F49A5B0D4CDBEB6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti549 – 5491P → Q in BAE25216. (PubMed:16141072)Curated
Sequence conflicti1298 – 12981C → R in AAI12914. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK142872 mRNA. Translation: BAE25216.1.
AC159626 Genomic DNA. No translation available.
AC165078 Genomic DNA. No translation available.
BC112913 mRNA. Translation: AAI12914.1.
CCDSiCCDS25856.1.
RefSeqiNP_852060.2. NM_181395.2.
UniGeneiMm.251774.

Genome annotation databases

EnsembliENSMUST00000122328; ENSMUSP00000113703; ENSMUSG00000020674.
GeneIDi69675.
KEGGimmu:69675.
UCSCiuc007ngl.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK142872 mRNA. Translation: BAE25216.1 .
AC159626 Genomic DNA. No translation available.
AC165078 Genomic DNA. No translation available.
BC112913 mRNA. Translation: AAI12914.1 .
CCDSi CCDS25856.1.
RefSeqi NP_852060.2. NM_181395.2.
UniGenei Mm.251774.

3D structure databases

ProteinModelPortali Q3UQ28.
SMRi Q3UQ28. Positions 27-673, 735-1311.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 213608. 1 interaction.

PTM databases

PhosphoSitei Q3UQ28.

Proteomic databases

MaxQBi Q3UQ28.
PaxDbi Q3UQ28.
PRIDEi Q3UQ28.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000122328 ; ENSMUSP00000113703 ; ENSMUSG00000020674 .
GeneIDi 69675.
KEGGi mmu:69675.
UCSCi uc007ngl.2. mouse.

Organism-specific databases

CTDi 7837.
MGIi MGI:1916925. Pxdn.
Rougei Search...

Phylogenomic databases

eggNOGi NOG262194.
GeneTreei ENSGT00550000074325.
HOGENOMi HOG000016084.
HOVERGENi HBG108312.
InParanoidi Q3UQ28.
OMAi EPVITWN.
OrthoDBi EOG7D2FD6.
TreeFami TF314316.

Miscellaneous databases

NextBioi 330062.
PROi Q3UQ28.
SOURCEi Search...

Gene expression databases

Bgeei Q3UQ28.
CleanExi MM_PXDN.
ExpressionAtlasi Q3UQ28. baseline and differential.
Genevestigatori Q3UQ28.

Family and domain databases

Gene3Di 1.10.640.10. 2 hits.
2.60.40.10. 4 hits.
InterProi IPR000483. Cys-rich_flank_reg_C.
IPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
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 ]
Pfami PF03098. An_peroxidase. 1 hit.
PF07679. I-set. 4 hits.
PF00560. LRR_1. 1 hit.
PF13855. LRR_8. 1 hit.
PF00093. VWC. 1 hit.
[Graphical view ]
PRINTSi PR00457. ANPEROXIDASE.
SMARTi SM00408. IGc2. 4 hits.
SM00369. LRR_TYP. 4 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view ]
SUPFAMi SSF48113. SSF48113. 1 hit.
PROSITEi PS50835. IG_LIKE. 4 hits.
PS51450. LRR. 5 hits.
PS50292. PEROXIDASE_3. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.
  7. Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiPXDN_MOUSE
AccessioniPrimary (citable) accession number: Q3UQ28
Secondary accession number(s): A4FU83, E9QNQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3