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A1KZ92 (PXDNL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxidasin-like protein

EC=1.11.1.7
Alternative name(s):
Cardiac peroxidase
Vascular peroxidase 2
polysomal ribonuclease 1
Short name=PRM1
Gene names
Name:PXDNL
Synonyms:VPO2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1463 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Isoform PMR1:Endonuclease selectively degrading some target mRNAs while they are engaged by translating ribosomes, among which albumin and beta-globin mRNAs. Ref.6 Ref.7

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 Potential Ref.6.

Isoform PMR1: Cytoplasm. Note: Associates with polysomes. Ref.6

Tissue specificity

the 57 kDa isoform PMR1 is the only form detected at protein levels in human cell lines. Ref.7

Post-translational modification

Phosphorylation by SRC on tyrosine residues is required for targeting to polysomes.

Sequence similarities

Belongs to the peroxidase family. XPO subfamily.

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

Contains 5 LRR (leucine-rich) repeats.

Contains 1 LRRCT domain.

Contains 1 LRRNT domain.

Contains 1 VWFC domain.

Sequence caution

The sequence AAX70929.1 differs from that shown. Reason: Frameshift at positions 127 and 132.

The sequence BAB71713.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAD18663.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence EAW86707.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: A1KZ92-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: A1KZ92-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1302-1316: CRSRGQFRAVTQESQ → KQAGGTPEAGRVYRC
     1317-1463: Missing.
Note: No experimental confirmation available.
Isoform PMR1 (identifier: A1KZ92-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-801: Missing.
     1302-1463: CRSRGQFRAV...GMPSDSPEKR → KQAGGTPEAGRVYRC

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 14631440Peroxidasin-like protein
PRO_0000330731

Regions

Domain24 – 5027LRRNT
Repeat51 – 7222LRR 1
Repeat75 – 9622LRR 2
Repeat99 – 12022LRR 3
Repeat123 – 14422LRR 4
Repeat147 – 16822LRR 5
Domain180 – 23354LRRCT
Domain234 – 32289Ig-like C2-type 1
Domain330 – 41485Ig-like C2-type 2
Domain419 – 50486Ig-like C2-type 3
Domain507 – 59690Ig-like C2-type 4
Domain1393 – 145159VWFC

Sites

Active site8121Proton acceptor By similarity
Metal binding8131Calcium By similarity
Metal binding8911Calcium By similarity
Metal binding8931Calcium; via carbonyl oxygen By similarity
Metal binding8951Calcium By similarity
Metal binding8971Calcium By similarity
Metal binding10571Iron (heme axial ligand) By similarity
Site9601Transition state stabilizer By similarity

Amino acid modifications

Glycosylation3871N-linked (GlcNAc...) Potential
Disulfide bond255 ↔ 305 By similarity
Disulfide bond351 ↔ 398 By similarity
Disulfide bond440 ↔ 488 By similarity
Disulfide bond532 ↔ 580 By similarity
Disulfide bond718 ↔ 734 By similarity
Disulfide bond832 ↔ 842 By similarity
Disulfide bond836 ↔ 859 By similarity
Disulfide bond944 ↔ 953 By similarity
Disulfide bond1160 ↔ 1217 By similarity
Disulfide bond1258 ↔ 1284 By similarity

Natural variations

Alternative sequence1 – 801801Missing in isoform PMR1.
VSP_044240
Alternative sequence1302 – 1463162CRSRG…SPEKR → KQAGGTPEAGRVYRC in isoform PMR1.
VSP_044241
Alternative sequence1302 – 131615CRSRG…TQESQ → KQAGGTPEAGRVYRC in isoform 2.
VSP_033070
Alternative sequence1317 – 1463147Missing in isoform 2.
VSP_033071
Natural variant3431I → T.
Corresponds to variant rs7833909 [ dbSNP | Ensembl ].
VAR_050488
Natural variant5831R → Q.
Corresponds to variant rs16916235 [ dbSNP | Ensembl ].
VAR_050489
Natural variant6161D → A.
Corresponds to variant rs16916207 [ dbSNP | Ensembl ].
VAR_050490
Natural variant9811M → V. Ref.1 Ref.2 Ref.4 Ref.5
Corresponds to variant rs2977020 [ dbSNP | Ensembl ].
VAR_050491
Natural variant13271V → D.
Corresponds to variant rs11774588 [ dbSNP | Ensembl ].
VAR_050492
Natural variant13991R → K. Ref.2
Corresponds to variant rs7827446 [ dbSNP | Ensembl ].
VAR_050493
Natural variant14521D → E. Ref.2
Corresponds to variant rs1052704 [ dbSNP | Ensembl ].
VAR_050494

Experimental info

Sequence conflict7811R → G in BAD18663. Ref.4
Sequence conflict8331S → N in BAD18663. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: F6FE8200892CCCAE

FASTA1,463163,686
        10         20         30         40         50         60 
MEPRLFCWTT LFLLAGWCLP GLPCPSRCLC FKSTVRCMHL MLDHIPQVPQ QTTVLDLRFN 

        70         80         90        100        110        120 
RIREIPGSAF KKLKNLNTLL LNNNHIRKIS RNAFEGLENL LYLYLYKNEI HALDKQTFKG 

       130        140        150        160        170        180 
LISLEHLYIH FNQLEMLQPE TFGDLLRLER LFLHNNKLSK IPAGSFSNLD SLKRLRLDSN 

       190        200        210        220        230        240 
ALVCDCDLMW LGELLQGFAQ HGHTQAAATC EYPRRLHGRA VASVTVEEFN CQSPRITFEP 

       250        260        270        280        290        300 
QDVEVPSGNT VYFTCRAEGN PKPEIIWIHN NHSLDLEDDT RLNVFDDGTL MIRNTRESDQ 

       310        320        330        340        350        360 
GVYQCMARNS AGEAKTQSAM LRYSSLPAKP SFVIQPQDTE VLIGTSTTLE CMATGHPHPL 

       370        380        390        400        410        420 
ITWTRDNGLE LDGSRHVATS SGLYLQNITQ RDHGRFTCHA NNSHGTVQAA ANIIVQAPPQ 

       430        440        450        460        470        480 
FTVTPKDQVV LEEHAVEWLC EADGNPPPVI VWTKTGGQLP VEGQHTVLSS GTLRIDRAAQ 

       490        500        510        520        530        540 
HDQGQYECQA VSSLGVKKVS VQLTVKPKAL AVFTQLPQDT SVEVGKNINI SCHAQGEPQP 

       550        560        570        580        590        600 
IITWNKEGVQ ITESGKFHVD DEGTLTIYDA GFPDQGRYEC VARNSFGLAV TNMFLTVTAI 

       610        620        630        640        650        660 
QGRQAGDDFV ESSILDAVQR VDSAINSTRR HLFSQKPHTS SDLLAQFHYP RDPLIVEMAR 

       670        680        690        700        710        720 
AGEIFEHTLQ LIRERVKQGL TVDLEGKEFR YNDLVSPRSL SLIANLSGCT ARRPLPNCSN 

       730        740        750        760        770        780 
RCFHAKYRAH DGTCNNLQQP TWGAALTAFA RLLQPAYRDG IRAPRGLGLP VGSRQPLPPP 

       790        800        810        820        830        840 
RLVATVWARA AAVTPDHSYT RMLMHWGWFL EHDLDHTVPA LSTARFSDGR PCSSVCTNDP 

       850        860        870        880        890        900 
PCFPMNTRHA DPRGTHAPCM LFARSSPACA SGRPSATVDS VYAREQINQQ TAYIDGSNVY 

       910        920        930        940        950        960 
GSSERESQAL RDPSVPRGLL KTGFPWPPSG KPLLPFSTGP PTECARQEQE SPCFLAGDHR 

       970        980        990       1000       1010       1020 
ANEHLALAAM HTLWFREHNR MATELSALNP HWEGNTVYQE ARKIVGAELQ HITYSHWLPK 

      1030       1040       1050       1060       1070       1080 
VLGDPGTRML RGYRGYNPNV NAGIINSFAT AAFRFGHTLI NPILYRLNAT LGEISEGHLP 

      1090       1100       1110       1120       1130       1140 
FHKALFSPSR IIKEGGIDPV LRGLFGVAAK WRAPSYLLSP ELTQRLFSAA YSAAVDSAAT 

      1150       1160       1170       1180       1190       1200 
IIQRGRDHGI PPYVDFRVFC NLTSVKNFED LQNEIKDSEI RQKLRKLYGS PGDIDLWPAL 

      1210       1220       1230       1240       1250       1260 
MVEDLIPGTR VGPTLMCLFV TQFQRLRDGD RFWYENPGVF TPAQLTQLKQ ASLSRVLCDN 

      1270       1280       1290       1300       1310       1320 
GDSIQQVQAD VFVKAEYPQD YLNCSEIPKV DLRVWQDCCA DCRSRGQFRA VTQESQKKRS 

      1330       1340       1350       1360       1370       1380 
AQYSYPVDKD MELSHLRSRQ QDKIYVGEDA RNVTVLAKTK FSQDFSTFAA EIQETITALR 

      1390       1400       1410       1420       1430       1440 
EQINKLEARL RQAGCTDVRG VPRKAEERWM KEDCTHCICE SGQVTCVVEI CPPAPCPSPE 

      1450       1460 
LVKGTCCPVC RDRGMPSDSP EKR 

« Hide

Isoform 2 [UniParc].

Checksum: B9FD640C9FF6E1FF
Show »

FASTA1,316146,935
Isoform PMR1 [UniParc].

Checksum: 5A872CB698D94326
Show »

FASTA51557,461

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-981.
[2]"Identification of a novel peroxidase in heart."
Sum A., Peterfi Z., Geiszt M.
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS VAL-981; LYS-1399 AND GLU-1452.
Tissue: Heart.
[3]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 735-1463 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 894-1463 (ISOFORM 1), VARIANT VAL-981.
Tissue: Pericardium and Testis.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 752-1463, VARIANT VAL-981.
[6]"An endonuclease activity similar to Xenopus PMR1 catalyzes the degradation of normal and nonsense-containing human beta-globin mRNA in erythroid cells."
Bremer K.A., Stevens A., Schoenberg D.R.
RNA 9:1157-1167(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION (ISOFORM PMR1), SUBCELLULAR LOCATION.
[7]"Identification of the human PMR1 mRNA endonuclease as an alternatively processed product of the gene for peroxidasin-like protein."
Gu S.Q., Bakthavachalu B., Han J., Patil D.P., Otsuka Y., Guda C., Schoenberg D.R.
RNA 18:1186-1196(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM PMR1), FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH SRC.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EU170240 mRNA. Translation: ABX24517.1.
AY877349 mRNA. Translation: AAX70929.1. Frameshift.
AC090186 Genomic DNA. No translation available.
AC103958 Genomic DNA. No translation available.
AC107374 Genomic DNA. No translation available.
AC011128 Genomic DNA. No translation available.
AC012413 Genomic DNA. No translation available.
AK058200 mRNA. Translation: BAB71713.1. Different initiation.
AK131524 mRNA. Translation: BAD18663.1. Different initiation.
CH471068 Genomic DNA. Translation: EAW86707.1. Sequence problems.
CCDSCCDS47855.1. [A1KZ92-1]
RefSeqNP_653252.3. NM_144651.4.
UniGeneHs.444882.

3D structure databases

ProteinModelPortalA1KZ92.
SMRA1KZ92. Positions 21-599, 708-1297.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid126492. 2 interactions.
STRING9606.ENSP00000348645.

Protein family/group databases

MEROPSI43.001.
PeroxiBase5398. HsPxd02.
5827. HsPxd03.

PTM databases

PhosphoSiteA1KZ92.

Proteomic databases

PaxDbA1KZ92.
PRIDEA1KZ92.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356297; ENSP00000348645; ENSG00000147485. [A1KZ92-1]
ENST00000543296; ENSP00000444865; ENSG00000147485. [A1KZ92-2]
GeneID137902.
KEGGhsa:137902.
UCSCuc003xqu.4. human. [A1KZ92-1]

Organism-specific databases

CTD137902.
GeneCardsGC08M052232.
HGNCHGNC:26359. PXDNL.
HPAHPA007919.
neXtProtNX_A1KZ92.
PharmGKBPA142671110.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG262194.
HOGENOMHOG000016084.
HOVERGENHBG108312.
OMARNTRESD.
PhylomeDBA1KZ92.
TreeFamTF314316.

Gene expression databases

ArrayExpressA1KZ92.
BgeeA1KZ92.
CleanExHS_PXDNL.
GenevestigatorA1KZ92.

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.
PF13855. LRR_8. 2 hits.
PF00093. VWC. 1 hit.
[Graphical view]
PRINTSPR00457. ANPEROXIDASE.
SMARTSM00408. IGc2. 4 hits.
SM00369. LRR_TYP. 3 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
SUPFAMSSF48113. SSF48113. 1 hit.
PROSITEPS50835. IG_LIKE. 4 hits.
PS51450. LRR. 6 hits.
PS50292. PEROXIDASE_3. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi137902.
NextBio83705.
PROA1KZ92.

Entry information

Entry namePXDNL_HUMAN
AccessionPrimary (citable) accession number: A1KZ92
Secondary accession number(s): B5ME43 expand/collapse secondary AC list , B6CGZ3, H0YBM9, Q6ZMR2, Q96LH9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 72 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM