PXDNL_HUMAN
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 03-AUG-2022, entry version 129.
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;
CC Evidence={ECO:0000255|PROSITE-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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 22.
DR IntAct; A1KZ92; 4.
DR STRING; 9606.ENSP00000348645; -.
DR PeroxiBase; 5398; HsPxd02.
DR PeroxiBase; 5827; HsPxd03.
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; A1KZ92; -.
DR PeptideAtlas; A1KZ92; -.
DR PRIDE; 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 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; FHRKYRA; -.
DR OrthoDB; 276568at2759; -.
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 1067 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 94 other tissues.
DR ExpressionAtlas; A1KZ92; baseline and differential.
DR Genevisible; A1KZ92; HS.
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: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; 1.10.640.10; -; 1.
DR Gene3D; 2.60.40.10; -; 4.
DR Gene3D; 3.80.10.10; -; 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; IPR029610; PXDNL.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR11475:SF38; PTHR11475:SF38; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF07679; I-set; 3.
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; SSF48113; SSF48113; 1.
DR SUPFAM; SSF48726; SSF48726; 4.
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.
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
