| Tag | Content |
|---|
| CPLM ID | CPLM-018784 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Peroxidasin homolog |
Protein Synonyms/Alias | Melanoma-associated antigen MG50; Vascular peroxidase 1; p53-responsive gene 2 protein |
Gene Name | PXDN |
Gene Synonyms/Alias | KIAA0230; MG50; PRG2; VPO; VPO1 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 99 | LLNNNQIKRIPSGAF | ubiquitination | [1] | | 289 | NNNELSMKTDSRLNL | ubiquitination | [1] | | 740 | SDMCFHQKYRTHDGT | ubiquitination | [1] | | 768 | TAFERLLKSVYENGF | ubiquitination | [1] | | 1100 | QDHLPLHKAFFSPFR | ubiquitination | [1] | | 1241 | CLLSTQFKRLRDGDR | ubiquitination | [1] |
|
Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] |
Functional Description | Displays low peroxidase activity and is likely to participate in H(2)O(2) metabolism and peroxidative reactions in the cardiovascular system. Plays a role in extracellular matrix formation. |
Sequence Annotation | DOMAIN 27 63 LRRNT.
REPEAT 87 108 LRR 1.
REPEAT 111 132 LRR 2.
REPEAT 135 156 LRR 3.
REPEAT 159 180 LRR 4.
DOMAIN 192 245 LRRCT.
DOMAIN 246 332 Ig-like C2-type 1.
DOMAIN 342 428 Ig-like C2-type 2.
DOMAIN 433 520 Ig-like C2-type 3.
DOMAIN 521 610 Ig-like C2-type 4.
DOMAIN 1413 1471 VWFC.
ACT_SITE 827 827 Proton acceptor (By similarity).
METAL 828 828 Calcium (By similarity).
METAL 907 907 Calcium (By similarity).
METAL 909 909 Calcium; via carbonyl oxygen (By
METAL 911 911 Calcium (By similarity).
METAL 913 913 Calcium (By similarity).
METAL 1074 1074 Iron (heme axial ligand) (By similarity).
BINDING 826 826 Heme (covalent; via 2 links) (By
BINDING 980 980 Heme (covalent; via 2 links) (By
MOD_RES 1176 1176 Phosphotyrosine.
MOD_RES 1180 1180 Phosphoserine.
CARBOHYD 640 640 N-linked (GlcNAc...) (Potential).
CARBOHYD 699 699 N-linked (GlcNAc...) (Potential).
CARBOHYD 719 719 N-linked (GlcNAc...) (Potential).
CARBOHYD 731 731 N-linked (GlcNAc...) (Potential).
CARBOHYD 865 865 N-linked (GlcNAc...) (Potential).
CARBOHYD 1178 1178 N-linked (GlcNAc...).
CARBOHYD 1280 1280 N-linked (GlcNAc...) (Potential).
CARBOHYD 1368 1368 N-linked (GlcNAc...) (Potential).
CARBOHYD 1425 1425 N-linked (GlcNAc...) (Potential).
DISULFID 267 317 By similarity.
DISULFID 363 412 By similarity.
DISULFID 454 502 By similarity.
DISULFID 546 594 By similarity.
DISULFID 732 748 By similarity.
DISULFID 847 857 By similarity.
DISULFID 851 875 By similarity.
DISULFID 959 970 By similarity.
DISULFID 1177 1234 By similarity.
DISULFID 1275 1301 By similarity. |
Keyword | Alternative splicing; Calcium; Complete proteome; Disulfide bond; Extracellular matrix; Glycoprotein; Heme; Hydrogen peroxide; Immunoglobulin domain; Iron; Leucine-rich repeat; Metal-binding; Oxidoreductase; Peroxidase; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Secreted; Signal. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1479 AA |
Protein Sequence | MAKRSRGPGR RCLLALVLFC AWGTLAVVAQ KPGAGCPSRC LCFRTTVRCM HLLLEAVPAV 60
APQTSILDLR FNRIREIQPG AFRRLRNLNT LLLNNNQIKR IPSGAFEDLE NLKYLYLYKN 120
EIQSIDRQAF KGLASLEQLY LHFNQIETLD PDSFQHLPKL ERLFLHNNRI THLVPGTFNH 180
LESMKRLRLD SNTLHCDCEI LWLADLLKTY AESGNAQAAA ICEYPRRIQG RSVATITPEE 240
LNCERPRITS EPQDADVTSG NTVYFTCRAE GNPKPEIIWL RNNNELSMKT DSRLNLLDDG 300
TLMIQNTQET DQGIYQCMAK NVAGEVKTQE VTLRYFGSPA RPTFVIQPQN TEVLVGESVT 360
LECSATGHPP PRISWTRGDR TPLPVDPRVN ITPSGGLYIQ NVVQGDSGEY ACSATNNIDS 420
VHATAFIIVQ ALPQFTVTPQ DRVVIEGQTV DFQCEAKGNP PPVIAWTKGG SQLSVDRRHL 480
VLSSGTLRIS GVALHDQGQY ECQAVNIIGS QKVVAHLTVQ PRVTPVFASI PSDTTVEVGA 540
NVQLPCSSQG EPEPAITWNK DGVQVTESGK FHISPEGFLT INDVGPADAG RYECVARNTI 600
GSASVSMVLS VNVPDVSRNG DPFVATSIVE AIATVDRAIN STRTHLFDSR PRSPNDLLAL 660
FRYPRDPYTV EQARAGEIFE RTLQLIQEHV QHGLMVDLNG TSYHYNDLVS PQYLNLIANL 720
SGCTAHRRVN NCSDMCFHQK YRTHDGTCNN LQHPMWGASL TAFERLLKSV YENGFNTPRG 780
INPHRLYNGH ALPMPRLVST TLIGTETVTP DEQFTHMLMQ WGQFLDHDLD STVVALSQAR 840
FSDGQHCSNV CSNDPPCFSV MIPPNDSRAR SGARCMFFVR SSPVCGSGMT SLLMNSVYPR 900
EQINQLTSYI DASNVYGSTE HEARSIRDLA SHRGLLRQGI VQRSGKPLLP FATGPPTECM 960
RDENESPIPC FLAGDHRANE QLGLTSMHTL WFREHNRIAT ELLKLNPHWD GDTIYYETRK 1020
IVGAEIQHIT YQHWLPKILG EVGMRTLGEY HGYDPGINAG IFNAFATAAF RFGHTLVNPL 1080
LYRLDENFQP IAQDHLPLHK AFFSPFRIVN EGGIDPLLRG LFGVAGKMRV PSQLLNTELT 1140
ERLFSMAHTV ALDLAAINIQ RGRDHGIPPY HDYRVYCNLS AAHTFEDLKN EIKNPEIREK 1200
LKRLYGSTLN IDLFPALVVE DLVPGSRLGP TLMCLLSTQF KRLRDGDRLW YENPGVFSPA 1260
QLTQIKQTSL ARILCDNADN ITRVQSDVFR VAEFPHGYGS CDEIPRVDLR VWQDCCEDCR 1320
TRGQFNAFSY HFRGRRSLEF SYQEDKPTKK TRPRKIPSVG RQGEHLSNST SAFSTRSDAS 1380
GTNDFREFVL EMQKTITDLR TQIKKLESRL STTECVDAGG ESHANNTKWK KDACTICECK 1440
DGQVTCFVEA CPPATCAVPV NIPGACCPVC LQKRAEEKP 1479 |
Gene Ontology | GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. GO:0031012; C:extracellular matrix; IDA:UniProtKB. GO:0005615; C:extracellular space; IDA:UniProtKB. GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell. GO:0005201; F:extracellular matrix structural constituent; IDA:UniProtKB. GO:0020037; F:heme binding; IDA:UniProtKB. GO:0005152; F:interleukin-1 receptor antagonist activity; NAS:UniProtKB. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0004601; F:peroxidase activity; IDA:UniProtKB. GO:0030198; P:extracellular matrix organization; IDA:UniProtKB. GO:0042744; P:hydrogen peroxide catabolic process; IDA:UniProtKB. GO:0006955; P:immune response; NAS:UniProtKB. |
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