GenomeNet

Database: UniProt
Entry: F6W4P8_MONDO
LinkDB: F6W4P8_MONDO
Original site: F6W4P8_MONDO 
ID   F6W4P8_MONDO            Unreviewed;      1488 AA.
AC   F6W4P8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 2.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Peroxidasin {ECO:0000313|Ensembl:ENSMODP00000017876.3};
GN   Name=PXDN {ECO:0000313|Ensembl:ENSMODP00000017876.3};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000017876.3, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000017876.3, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA   Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA   Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA   Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA   Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA   Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA   Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA   Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA   VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA   Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT   coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000017876.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_001381381.2; XM_001381344.4.
DR   STRING; 13616.ENSMODP00000017876; -.
DR   Ensembl; ENSMODT00000018205.3; ENSMODP00000017876.3; ENSMODG00000014304.4.
DR   GeneID; 100032348; -.
DR   KEGG; mdo:100032348; -.
DR   CTD; 7837; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   GeneTree; ENSGT00940000157666; -.
DR   HOGENOM; CLU_006087_0_1_1; -.
DR   InParanoid; F6W4P8; -.
DR   OMA; QHFKCAK; -.
DR   OrthoDB; 4560at2759; -.
DR   TreeFam; TF314316; -.
DR   Proteomes; UP000002280; Chromosome 1.
DR   Bgee; ENSMODG00000014304; Expressed in extraembryonic membrane and 20 other cell types or tissues.
DR   GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IEA:Ensembl.
DR   GO; GO:0020037; F:heme binding; IEA:Ensembl.
DR   GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043237; F:laminin-1 binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR   GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR   GO; GO:0070831; P:basement membrane assembly; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IEA:Ensembl.
DR   GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR   GO; GO:0001654; P:eye development; IEA:Ensembl.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:Ensembl.
DR   GO; GO:0070207; P:protein homotrimerization; IEA:Ensembl.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd05745; Ig3_Peroxidasin; 1.
DR   CDD; cd05746; Ig4_Peroxidasin; 1.
DR   CDD; cd09826; peroxidasin_like; 1.
DR   Gene3D; 6.20.200.20; -; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR047018; Peroxidasin_Ig-like3.
DR   InterPro; IPR034828; Peroxidasin_Ig-like4.
DR   InterPro; IPR034824; Peroxidasin_peroxidase.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR   PANTHER; PTHR11475:SF75; PEROXIDASIN HOMOLOG; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   Pfam; PF07679; I-set; 3.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF00093; VWC; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 4.
DR   SMART; SM00369; LRR_TYP; 5.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00214; VWC; 1.
DR   SUPFAM; SSF57603; FnI-like domain; 1.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 4.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS50835; IG_LIKE; 4.
DR   PROSITE; PS51450; LRR; 2.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
DR   PROSITE; PS01208; VWFC_1; 1.
DR   PROSITE; PS50184; VWFC_2; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR619791-2};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR619791-2};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002280};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..1488
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5023906025"
FT   DOMAIN          253..339
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          349..435
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          440..527
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          528..617
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1420..1478
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   COILED          1396..1423
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         1081
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
SQ   SEQUENCE   1488 AA;  167142 MW;  5B8143B0CB348E0A CRC64;
     MAPFRASTPR SLLLLLLCWS AGVFVGVSPQ LGSSSGGGGN GGCPSRCLCF RTTVRCMHLM
     LESVPSVSPQ TSILDLRFNR IREIQPGTFK RLKNLNTLLL NNNQIKRIPS GSFEDLENLK
     YLYLYKNEIQ SIDRQAFKGL ASLEQLYLHF NQIETLDPES FNHLPKLERL FLHNNRIAHL
     VPGTFSHLNS MKRLRLDSNA LHCDCEILWL ADLLKTYAES GNAQAAATCE YPRRIQGRSV
     ATITPEELNC ERPRITSEPQ DVDVTSGNTV YFTCRAEGNP KPEIIWLRNN NELSMKTDSR
     LNLLDDGTLM IQNTQETDQG IYQCMAKNVA GEVKTQEVTL RYFGSPARPS FVIQPQNTEV
     LVGESVTLEC SATGHPLPRI TWTKGDRTPL PTDPRVNITP SGGLYIEKVI QEDSGEYICF
     AANNVDSIHA TAYIIVQAVP HFTVTPQDRV VIEGQTVDFQ CEAQGYPQPV IAWTKGGSQL
     SVDRRHLVLS SGTLRISSVA LHDQGQYECQ AVNIIGSQRV AVHLTVQPRV TPVFASIPRD
     MTVEVGTNVQ IPCSSQGEPE PVITWNKDGV QVTESGKFHI NPEGFLTIND VGPADEGRYE
     CVARNTIGYS SVSMVLSVNV PDVSRNGDPF VATSIVEAIA TVDRAINSTR THLFDSRPRS
     PNDLLALFRY PRDPYTVEQA RAGEIFERTL QLIQEHVQHG LMVDLNGTSY HYNDLVSPQY
     LSLIANLSGC TAHRRVNNCS DMCFHQKYRT HDGTCNNLQH PMWGASLTAF ERLLKSVYEN
     GFNLPRGINP NRLYNGFPLP MPRLVSTTLI GTESITPDEQ FTHMTMQWGQ FLDHDLDSTV
     VALSQARFSD GQHCSSVCTN DPPCFSVMIP PNDPRVRNGA RCMFFVRSSP VCGSGMTSLL
     MNSVYPREQI NQLTSYIDAS NVYGSSDHEA REIRDLASHR GLLRQGIVQR SGKPLLPFAT
     GPPTECMRDE NESPIPCFLA GDHRANEQLG LTSMHTLWFR EHNRIATELL KLNPHWDGDT
     IYYETRKIVG AEIQHITYNH WLPKIFGEVG MKMLGEYKGY DPSVNSGIFN AFATAAFRFG
     HTLINPILYR LDENFEPIPQ GHIPLHKAFF SPFRIVNEGG IDPLLRGLFG VAGKMRVPTQ
     LLNTELTERL FSMAHTVALD LAAINIQRGR DHGIPPYHDF RVYCNLSSAS TFEDLRNEIK
     NPHIREKLQG LYGSPLNIDL FPALMVEDLV PGSRLGPTLM CLLSTQFKRL RDGDRLWYEN
     PGVFSPAQLT QIKQTSLARI LCDNSDNITH VQRDVFRVAE FPHGYSSCDE IPKVDLRMWQ
     DCCEDCRTRG QFNVFSYHFR GRRSLEFSYQ EDKPAKRTKA RKILSTVKQS QPFNNFTSSS
     DEHMNVPATN DFKEFVLEMQ KTITGLRKQI KKLESRLSKT ECTDEKGKSY SSNEKWKRDS
     CTVCECKDGQ ITCFVESCQP ADCPAPVKIK GECCPVCLKN TVSKPKKP
//
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