ID   PXDNL_HUMAN             Reviewed;        1463 AA.
AC   A1KZ92; B5ME43; B6CGZ3; H0YBM9; Q6ZMR2; Q96LH9;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 3.
DT   27-MAR-2024, entry version 137.
DE   RecName: Full=Probable oxidoreductase PXDNL {ECO:0000305};
DE            EC=1.-.-.- {ECO:0000305|PubMed:24253521};
DE   AltName: Full=Cardiac peroxidase;
DE   AltName: Full=Inactive peroxidasin-like protein {ECO:0000305|PubMed:24253521};
DE   AltName: Full=Polysomal ribonuclease 1;
DE            Short=PRM1;
DE   AltName: Full=Vascular peroxidase 2;
DE   Flags: Precursor;
GN   Name=PXDNL {ECO:0000312|HGNC:HGNC:26359}; Synonyms=VPO2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-981.
RX   PubMed=18929642; DOI=10.1016/j.freeradbiomed.2008.09.009;
RA   Cheng G., Salerno J.C., Cao Z., Pagano P.J., Lambeth J.D.;
RT   "Identification and characterization of VPO1, a new animal heme-containing
RT   peroxidase.";
RL   Free Radic. Biol. Med. 45:1682-1694(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS VAL-981; LYS-1399 AND
RP   GLU-1452.
RC   TISSUE=Heart;
RA   Sum A., Peterfi Z., Geiszt M.;
RT   "Identification of a novel peroxidase in heart.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 735-1463 (ISOFORM 2), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 894-1463 (ISOFORM 1), AND VARIANT VAL-981.
RC   TISSUE=Pericardium, and Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 752-1463, AND VARIANT
RP   VAL-981.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION (ISOFORM PMR1), AND SUBCELLULAR LOCATION.
RX   PubMed=12923263; DOI=10.1261/rna.5720303;
RA   Bremer K.A., Stevens A., Schoenberg D.R.;
RT   "An endonuclease activity similar to Xenopus PMR1 catalyzes the degradation
RT   of normal and nonsense-containing human beta-globin mRNA in erythroid
RT   cells.";
RL   RNA 9:1157-1167(2003).
RN   [7]
RP   ALTERNATIVE SPLICING (ISOFORM PMR1), FUNCTION, TISSUE SPECIFICITY,
RP   PHOSPHORYLATION, AND INTERACTION WITH SRC.
RX   PubMed=22543864; DOI=10.1261/rna.031369.111;
RA   Gu S.Q., Bakthavachalu B., Han J., Patil D.P., Otsuka Y., Guda C.,
RA   Schoenberg D.R.;
RT   "Identification of the human PMR1 mRNA endonuclease as an alternatively
RT   processed product of the gene for peroxidasin-like protein.";
RL   RNA 18:1186-1196(2012).
RN   [8]
RP   FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH PXDN,
RP   AND INDUCTION.
RX   PubMed=24253521; DOI=10.1093/cvr/cvt256;
RA   Peterfi Z., Toth Z.E., Kovacs H.A., Lazar E., Sum A., Donko A.,
RA   Sirokmany G., Shah A.M., Geiszt M.;
RT   "Peroxidasin-like protein: a novel peroxidase homologue in the human
RT   heart.";
RL   Cardiovasc. Res. 101:393-399(2014).
CC   -!- FUNCTION: Probable oxidoreductase (Probable). Lacks peroxidase activity
CC       (PubMed:24253521). Inhibits the peroxidase activity of PXDN through its
CC       interaction (PubMed:24253521). {ECO:0000269|PubMed:24253521,
CC       ECO:0000305|PubMed:24253521}.
CC   -!- FUNCTION: [Isoform PMR1]: Endonuclease selectively degrading some
CC       target mRNAs while they are engaged by translating ribosomes, among
CC       which albumin and beta-globin mRNAs. {ECO:0000269|PubMed:22543864}.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00298};
CC   -!- SUBUNIT: Interacts with PXDN; this interaction inhibits the peroxidase
CC       activity of PXDN. {ECO:0000269|PubMed:24253521}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24253521}.
CC       Endoplasmic reticulum {ECO:0000269|PubMed:24253521}. Cell membrane
CC       {ECO:0000269|PubMed:24253521}.
CC   -!- SUBCELLULAR LOCATION: [Isoform PMR1]: Cytoplasm. Note=Associates with
CC       polysomes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=A1KZ92-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A1KZ92-2; Sequence=VSP_033070, VSP_033071;
CC       Name=PMR1;
CC         IsoId=A1KZ92-3; Sequence=VSP_044240, VSP_044241;
CC   -!- TISSUE SPECIFICITY: the 57 kDa isoform PMR1 is the only form detected
CC       at protein levels in human cell lines (PubMed:22543864). Expressed in
CC       heart (PubMed:24253521). {ECO:0000269|PubMed:22543864,
CC       ECO:0000269|PubMed:24253521}.
CC   -!- INDUCTION: Increased by Angiotensin-2. {ECO:0000269|PubMed:24253521}.
CC   -!- PTM: Phosphorylation by SRC on tyrosine residues is required for
CC       targeting to polysomes. {ECO:0000269|PubMed:22543864}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00298}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAX70929.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAB71713.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAD18663.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=EAW86707.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; EU170240; ABX24517.1; -; mRNA.
DR   EMBL; AY877349; AAX70929.1; ALT_FRAME; mRNA.
DR   EMBL; AC090186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC103958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC107374; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC011128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC012413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK058200; BAB71713.1; ALT_INIT; mRNA.
DR   EMBL; AK131524; BAD18663.1; ALT_INIT; mRNA.
DR   EMBL; CH471068; EAW86707.1; ALT_SEQ; Genomic_DNA.
DR   CCDS; CCDS47855.1; -. [A1KZ92-1]
DR   RefSeq; NP_653252.3; NM_144651.4. [A1KZ92-1]
DR   AlphaFoldDB; A1KZ92; -.
DR   SMR; A1KZ92; -.
DR   BioGRID; 126492; 23.
DR   IntAct; A1KZ92; 4.
DR   STRING; 9606.ENSP00000348645; -.
DR   PeroxiBase; 5398; HsPxd02.
DR   PeroxiBase; 5827; HsPxd03.
DR   GlyCosmos; A1KZ92; 1 site, No reported glycans.
DR   GlyGen; A1KZ92; 1 site.
DR   iPTMnet; A1KZ92; -.
DR   PhosphoSitePlus; A1KZ92; -.
DR   BioMuta; PXDNL; -.
DR   EPD; A1KZ92; -.
DR   jPOST; A1KZ92; -.
DR   MassIVE; A1KZ92; -.
DR   MaxQB; A1KZ92; -.
DR   PaxDb; 9606-ENSP00000348645; -.
DR   PeptideAtlas; A1KZ92; -.
DR   ProteomicsDB; 126; -. [A1KZ92-1]
DR   ProteomicsDB; 127; -. [A1KZ92-2]
DR   ProteomicsDB; 36775; -.
DR   DNASU; 137902; -.
DR   Ensembl; ENST00000356297.5; ENSP00000348645.4; ENSG00000147485.13. [A1KZ92-1]
DR   GeneID; 137902; -.
DR   KEGG; hsa:137902; -.
DR   MANE-Select; ENST00000356297.5; ENSP00000348645.4; NM_144651.5; NP_653252.4.
DR   UCSC; uc003xqu.5; human. [A1KZ92-1]
DR   AGR; HGNC:26359; -.
DR   CTD; 137902; -.
DR   DisGeNET; 137902; -.
DR   GeneCards; PXDNL; -.
DR   HGNC; HGNC:26359; PXDNL.
DR   HPA; ENSG00000147485; Tissue enriched (heart).
DR   neXtProt; NX_A1KZ92; -.
DR   OpenTargets; ENSG00000147485; -.
DR   PharmGKB; PA142671110; -.
DR   VEuPathDB; HostDB:ENSG00000147485; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   GeneTree; ENSGT00940000163562; -.
DR   HOGENOM; CLU_006087_0_1_1; -.
DR   InParanoid; A1KZ92; -.
DR   OMA; DCVARNS; -.
DR   OrthoDB; 4560at2759; -.
DR   PhylomeDB; A1KZ92; -.
DR   TreeFam; TF314316; -.
DR   BRENDA; 1.11.1.7; 2681.
DR   PathwayCommons; A1KZ92; -.
DR   SignaLink; A1KZ92; -.
DR   BioGRID-ORCS; 137902; 11 hits in 1144 CRISPR screens.
DR   ChiTaRS; PXDNL; human.
DR   GenomeRNAi; 137902; -.
DR   Pharos; A1KZ92; Tbio.
DR   PRO; PR:A1KZ92; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; A1KZ92; Protein.
DR   Bgee; ENSG00000147485; Expressed in cardiac muscle of right atrium and 96 other cell types or tissues.
DR   ExpressionAtlas; A1KZ92; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR   GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; ISS:UniProtKB.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; ISS:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
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; IPR034824; Peroxidasin_peroxidase.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR   PANTHER; PTHR11475:SF38; OXIDOREDUCTASE PXDNL-RELATED; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   Pfam; PF07679; I-set; 3.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF13855; LRR_8; 2.
DR   Pfam; PF00093; VWC; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 4.
DR   SMART; SM00369; LRR_TYP; 6.
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; 6.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
DR   PROSITE; PS01208; VWFC_1; 1.
DR   PROSITE; PS50184; VWFC_2; 1.
DR   Genevisible; A1KZ92; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell membrane; Cytoplasm; Disulfide bond;
KW   Endonuclease; Endoplasmic reticulum; Glycoprotein; Heme; Hydrolase;
KW   Immunoglobulin domain; Iron; Leucine-rich repeat; Membrane; Metal-binding;
KW   Nuclease; Oxidoreductase; Phosphoprotein; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..1463
FT                   /note="Probable oxidoreductase PXDNL"
FT                   /id="PRO_0000330731"
FT   DOMAIN          24..50
FT                   /note="LRRNT"
FT   REPEAT          51..72
FT                   /note="LRR 1"
FT   REPEAT          75..96
FT                   /note="LRR 2"
FT   REPEAT          99..120
FT                   /note="LRR 3"
FT   REPEAT          123..144
FT                   /note="LRR 4"
FT   REPEAT          147..168
FT                   /note="LRR 5"
FT   DOMAIN          180..233
FT                   /note="LRRCT"
FT   DOMAIN          234..322
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          330..414
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          419..504
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          507..596
FT                   /note="Ig-like C2-type 4"
FT   DOMAIN          1393..1451
FT                   /note="VWFC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   ACT_SITE        812
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   BINDING         813
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   BINDING         891
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   BINDING         893
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   BINDING         895
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   BINDING         897
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   BINDING         1057
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:0000255|PROSITE-ProRule:PRU00298"
FT   SITE            960
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   CARBOHYD        387
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        255..305
FT                   /evidence="ECO:0000250"
FT   DISULFID        351..398
FT                   /evidence="ECO:0000250"
FT   DISULFID        440..488
FT                   /evidence="ECO:0000250"
FT   DISULFID        532..580
FT                   /evidence="ECO:0000250"
FT   DISULFID        718..734
FT                   /evidence="ECO:0000250"
FT   DISULFID        832..842
FT                   /evidence="ECO:0000250"
FT   DISULFID        836..859
FT                   /evidence="ECO:0000250"
FT   DISULFID        944..953
FT                   /evidence="ECO:0000250"
FT   DISULFID        1160..1217
FT                   /evidence="ECO:0000250"
FT   DISULFID        1258..1284
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..801
FT                   /note="Missing (in isoform PMR1)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_044240"
FT   VAR_SEQ         1302..1463
FT                   /note="CRSRGQFRAVTQESQKKRSAQYSYPVDKDMELSHLRSRQQDKIYVGEDARNV
FT                   TVLAKTKFSQDFSTFAAEIQETITALREQINKLEARLRQAGCTDVRGVPRKAEERWMKE
FT                   DCTHCICESGQVTCVVEICPPAPCPSPELVKGTCCPVCRDRGMPSDSPEKR -> KQAG
FT                   GTPEAGRVYRC (in isoform PMR1)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_044241"
FT   VAR_SEQ         1302..1316
FT                   /note="CRSRGQFRAVTQESQ -> KQAGGTPEAGRVYRC (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_033070"
FT   VAR_SEQ         1317..1463
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_033071"
FT   VARIANT         343
FT                   /note="I -> T (in dbSNP:rs7833909)"
FT                   /id="VAR_050488"
FT   VARIANT         583
FT                   /note="R -> Q (in dbSNP:rs16916235)"
FT                   /id="VAR_050489"
FT   VARIANT         616
FT                   /note="D -> A (in dbSNP:rs16916207)"
FT                   /id="VAR_050490"
FT   VARIANT         981
FT                   /note="M -> V (in dbSNP:rs2977020)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:18929642, ECO:0000269|Ref.2,
FT                   ECO:0000269|Ref.5"
FT                   /id="VAR_050491"
FT   VARIANT         1327
FT                   /note="V -> D (in dbSNP:rs11774588)"
FT                   /id="VAR_050492"
FT   VARIANT         1399
FT                   /note="R -> K (in dbSNP:rs7827446)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_050493"
FT   VARIANT         1452
FT                   /note="D -> E (in dbSNP:rs1052704)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_050494"
FT   CONFLICT        781
FT                   /note="R -> G (in Ref. 4; BAD18663)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        833
FT                   /note="S -> N (in Ref. 4; BAD18663)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1463 AA;  163686 MW;  F6FE8200892CCCAE CRC64;
     MEPRLFCWTT LFLLAGWCLP GLPCPSRCLC FKSTVRCMHL MLDHIPQVPQ QTTVLDLRFN
     RIREIPGSAF KKLKNLNTLL LNNNHIRKIS RNAFEGLENL LYLYLYKNEI HALDKQTFKG
     LISLEHLYIH FNQLEMLQPE TFGDLLRLER LFLHNNKLSK IPAGSFSNLD SLKRLRLDSN
     ALVCDCDLMW LGELLQGFAQ HGHTQAAATC EYPRRLHGRA VASVTVEEFN CQSPRITFEP
     QDVEVPSGNT VYFTCRAEGN PKPEIIWIHN NHSLDLEDDT RLNVFDDGTL MIRNTRESDQ
     GVYQCMARNS AGEAKTQSAM LRYSSLPAKP SFVIQPQDTE VLIGTSTTLE CMATGHPHPL
     ITWTRDNGLE LDGSRHVATS SGLYLQNITQ RDHGRFTCHA NNSHGTVQAA ANIIVQAPPQ
     FTVTPKDQVV LEEHAVEWLC EADGNPPPVI VWTKTGGQLP VEGQHTVLSS GTLRIDRAAQ
     HDQGQYECQA VSSLGVKKVS VQLTVKPKAL AVFTQLPQDT SVEVGKNINI SCHAQGEPQP
     IITWNKEGVQ ITESGKFHVD DEGTLTIYDA GFPDQGRYEC VARNSFGLAV TNMFLTVTAI
     QGRQAGDDFV ESSILDAVQR VDSAINSTRR HLFSQKPHTS SDLLAQFHYP RDPLIVEMAR
     AGEIFEHTLQ LIRERVKQGL TVDLEGKEFR YNDLVSPRSL SLIANLSGCT ARRPLPNCSN
     RCFHAKYRAH DGTCNNLQQP TWGAALTAFA RLLQPAYRDG IRAPRGLGLP VGSRQPLPPP
     RLVATVWARA AAVTPDHSYT RMLMHWGWFL EHDLDHTVPA LSTARFSDGR PCSSVCTNDP
     PCFPMNTRHA DPRGTHAPCM LFARSSPACA SGRPSATVDS VYAREQINQQ TAYIDGSNVY
     GSSERESQAL RDPSVPRGLL KTGFPWPPSG KPLLPFSTGP PTECARQEQE SPCFLAGDHR
     ANEHLALAAM HTLWFREHNR MATELSALNP HWEGNTVYQE ARKIVGAELQ HITYSHWLPK
     VLGDPGTRML RGYRGYNPNV NAGIINSFAT AAFRFGHTLI NPILYRLNAT LGEISEGHLP
     FHKALFSPSR IIKEGGIDPV LRGLFGVAAK WRAPSYLLSP ELTQRLFSAA YSAAVDSAAT
     IIQRGRDHGI PPYVDFRVFC NLTSVKNFED LQNEIKDSEI RQKLRKLYGS PGDIDLWPAL
     MVEDLIPGTR VGPTLMCLFV TQFQRLRDGD RFWYENPGVF TPAQLTQLKQ ASLSRVLCDN
     GDSIQQVQAD VFVKAEYPQD YLNCSEIPKV DLRVWQDCCA DCRSRGQFRA VTQESQKKRS
     AQYSYPVDKD MELSHLRSRQ QDKIYVGEDA RNVTVLAKTK FSQDFSTFAA EIQETITALR
     EQINKLEARL RQAGCTDVRG VPRKAEERWM KEDCTHCICE SGQVTCVVEI CPPAPCPSPE
     LVKGTCCPVC RDRGMPSDSP EKR
//