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Q3UQ28

- PXDN_MOUSE

UniProt

Q3UQ28 - PXDN_MOUSE

Protein

Peroxidasin homolog

Gene

Pxdn

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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

    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-SubCell

    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.1 Publication

    Developmental stagei

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

    Gene expression databases

    ArrayExpressiQ3UQ28.
    BgeeiQ3UQ28.
    CleanExiMM_PXDN.
    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.

    Q3UQ28-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVRPTRRCL LALLLCFAWW AMAVVASKQG AGCPSRCLCF RTTVRCMHLL     50
    LEAVPAVAPQ TSILDLRFNR IREIQPGAFR RLRSLNTLLL NNNQIKKIPN 100
    GAFEDLENLK YLYLYKNEIQ SIDRQAFKGL ASLEQLYLHF NQIETLDPES 150
    FQHLPKLERL FLHNNRITHL VPGTFSQLES MKRLRLDSNA LHCDCEILWL 200
    ADLLKTYAQS GNAQAAATCE YPRRIQGRSV ATITPEELNC ERPRITSEPQ 250
    DADVTSGNTV YFTCRAEGNP KPEIIWLRNN NELSMKTDSR LNLLDDGTLM 300
    IQNTQEADEG VYQCMAKNVA GEAKTQEVTL RYLGSPARPT FVIQPQNTEV 350
    LVGESVTLEC SATGHPLPQI TWTRGDRTPL PIDPRVNITP SGGLYIQNVA 400
    QSDSGEYTCF ASNSVDSIHA TAFIIVQALP QFTVTPQSRV VIEGQTVDFQ 450
    CAAKGHPQPV IAWTKGGSQL SVDRRHLVLS SGTLRISGVA LHDQGQYECQ 500
    AVNIIGSQKV VAHLTVQPRV TPVFASIPSD MTVEVGTNVQ LPCSSQGEPE 550
    PAITWNKDGV QVTESGKFHI SPEGFLTIND VGTADAGRYE CVARNTIGYA 600
    SVSMVLSVNV PDVSRNGDPY VATSIVEAIA TVDRAINSTR THLFDSRPRS 650
    PNDLLALFRY PRDPYTVGQA RAGEIFERTL QLIQEHVQHG LMVDLNGTSY 700
    HYNDLVSPQY LSLIANLSGC TAHRRVNNCS DMCFHQKYRT HDGTCNNLQH 750
    PMWGASLTAF ERLLKAVYEN GFNTPRGINS QRQYNGHVLP MPRLVSTTLI 800
    GTEVITPDEQ FTHMLMQWGQ FLDHDLDSTV VALSQARFSD GQHCSSVCSN 850
    DPPCFSVMIP PNDPRVRSGA RCMFFVRSSP VCGSGMTSLL MNSVYPREQI 900
    NQLTSYIDAS NVYGSTDHEA RSIRDLASHR GLLRQGIVQR SGKPLLPFAT 950
    GPPTECMRDE NESPIPCFLA GDHRANEQLG LTSMHTLWFR EHNRIAAELL 1000
    KLNPHWDGDT VYHETRKIVG AEIQHITYRH WLPKILGEVG MKMLGEYRGY 1050
    DPSVNAGIFN AFATAAFRFG HTLINPLLYR LDENFEPIPQ GHVPLHKAFF 1100
    SPFRIVNEGG IDPLLRGLFG VAGKMRIPSQ LLNTELTERL FSMAHTVALD 1150
    LAAINIQRGR DHGIPPYHDY RVYCNLSAAY TFEDLKNEIK SPVIREKLQR 1200
    LYGSTLNIDL FPALMVEDLV PGSRLGPTLM CLLSTQFRRL RDGDRLWYEN 1250
    PGVFSPAQLT QLKQTSLARI LCDNSDNITR VQQDVFRVAE FPHGYSSCED 1300
    IPRVDLRVWQ DCCEDCRTRG QFNAFSYHFR GRRSLEFSYE DDKPTKRARW 1350
    RKALSVKHGK HLSNATSATH EHLEGPATND LKEFVLEMQK IITDLRKQIN 1400
    SLESRLSTTE CVDDSGESHG GNTKWKKDPC TVCECKNGQI TCFVEACQPA 1450
    ACPQPVKVEG ACCPVCLKNT AEEKP 1475
    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

    ArrayExpressi Q3UQ28.
    Bgeei Q3UQ28.
    CleanExi MM_PXDN.
    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

    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.

    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 1, 2014
    This is version 93 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