CORIN_MOUSE
ID CORIN_MOUSE Reviewed; 1113 AA.
AC Q9Z319; B2RRC6; Q566K6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Atrial natriuretic peptide-converting enzyme;
DE EC=3.4.21.-;
DE AltName: Full=Corin;
DE AltName: Full=Low density lipoprotein receptor-related protein 4;
DE AltName: Full=Pro-ANP-converting enzyme;
DE Contains:
DE RecName: Full=Atrial natriuretic peptide-converting enzyme, N-terminal propeptide;
DE Contains:
DE RecName: Full=Atrial natriuretic peptide-converting enzyme, activated protease fragment;
DE Contains:
DE RecName: Full=Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment;
GN Name=Corin; Synonyms=Crn, Lrp4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9756624; DOI=10.1093/oxfordjournals.jbchem.a022180;
RA Tomita Y., Kim D.-H., Magoori K., Fujino T., Yamamoto T.T.;
RT "A novel low-density lipoprotein receptor-related protein with type II
RT membrane protein-like structure is abundant in heart.";
RL J. Biochem. 124:784-789(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Head;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION.
RX PubMed=11884416; DOI=10.1074/jbc.m201503200;
RA Wu F., Yan W., Pan J., Morser J., Wu Q.;
RT "Processing of pro-atrial natriuretic peptide by corin in cardiac
RT myocytes.";
RL J. Biol. Chem. 277:16900-16905(2002).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15637153; DOI=10.1073/pnas.0407234102;
RA Chan J.C., Knudson O., Wu F., Morser J., Dole W.P., Wu Q.;
RT "Hypertension in mice lacking the proatrial natriuretic peptide convertase
RT corin.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:785-790(2005).
RN [7]
RP FUNCTION.
RX PubMed=20613715; DOI=10.1038/ki.2010.197;
RA Polzin D., Kaminski H.J., Kastner C., Wang W., Kramer S., Gambaryan S.,
RA Russwurm M., Peters H., Wu Q., Vandewalle A., Bachmann S., Theilig F.;
RT "Decreased renal corin expression contributes to sodium retention in
RT proteinuric kidney diseases.";
RL Kidney Int. 78:650-659(2010).
RN [8]
RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
RX PubMed=21518754; DOI=10.1074/jbc.m110.217570;
RA Qi X., Jiang J., Zhu M., Wu Q.;
RT "Human corin isoforms with different cytoplasmic tails that alter cell
RT surface targeting.";
RL J. Biol. Chem. 286:20963-20969(2011).
RN [9]
RP DISRUPTION IN W-SH MODEL MICE.
RX PubMed=21903139; DOI=10.1016/j.regpep.2011.08.006;
RA Buckley C.L., Stokes A.J.;
RT "Corin-deficient W-sh mice poorly tolerate increased cardiac afterload.";
RL Regul. Pept. 172:44-50(2011).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22418978; DOI=10.1038/ki.2012.41;
RA Wang W., Shen J., Cui Y., Jiang J., Chen S., Peng J., Wu Q.;
RT "Impaired sodium excretion and salt-sensitive hypertension in corin-
RT deficient mice.";
RL Kidney Int. 82:26-33(2012).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22437503; DOI=10.1038/nature10897;
RA Cui Y., Wang W., Dong N., Lou J., Srinivasan D.K., Cheng W., Huang X.,
RA Liu M., Fang C., Peng J., Chen S., Wu S., Liu Z., Dong L., Zhou Y., Wu Q.;
RT "Role of corin in trophoblast invasion and uterine spiral artery
RT remodelling in pregnancy.";
RL Nature 484:246-250(2012).
CC -!- FUNCTION: Serine-type endopeptidase involved in atrial natriuretic
CC peptide (NPPA) processing (PubMed:11884416, PubMed:15637153). Converts
CC through proteolytic cleavage the non-functional propeptide NPPA into
CC the active hormone, thereby regulating blood pressure in heart and
CC promoting natriuresis, diuresis and vasodilation (PubMed:11884416,
CC PubMed:15637153, PubMed:22418978). Proteolytic cleavage of pro-NPPA
CC also plays a role in female pregnancy by promoting trophoblast invasion
CC and spiral artery remodeling in uterus (PubMed:22437503). Also acts as
CC a regulator of sodium reabsorption in kidney (PubMed:20613715,
CC PubMed:22418978). May also process pro-NPPB the B-type natriuretic
CC peptide (By similarity). {ECO:0000250|UniProtKB:Q9Y5Q5,
CC ECO:0000269|PubMed:11884416, ECO:0000269|PubMed:15637153,
CC ECO:0000269|PubMed:20613715, ECO:0000269|PubMed:22418978,
CC ECO:0000269|PubMed:22437503}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Atrial natriuretic peptide-converting enzyme,
CC 180 kDa soluble fragment]: Secreted {ECO:0000250}. Note=Soluble form
CC produced following cleavage by ADAM10. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=E1a, mE1a;
CC IsoId=Q9Z319-1; Sequence=Displayed;
CC Name=2; Synonyms=E1, mE1;
CC IsoId=Q9Z319-2; Sequence=VSP_043953;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart. Also expressed in
CC pregnant uterus. {ECO:0000269|PubMed:22437503}.
CC -!- PTM: N-glycosylated; required for processing and activation.
CC {ECO:0000250}.
CC -!- PTM: Activated through proteolytic processing by a trypsin-like
CC protease; cleaved into a N-terminal propeptide and an activated corin
CC protease fragment. Atrial natriuretic peptide-converting enzyme, 180
CC kDa soluble fragment is produced by cleavage by ADAM10. Cleavage by
CC ADAM10 to produce soluble 180 kDa soluble fragment takes place after
CC the transmembrane region and before FZ 1 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: A disulfide bond links the activated corin protease fragment and
CC the N-terminal propeptide. The disulfide bond also links the activated
CC corin protease fragment with Atrial natriuretic peptide-converting
CC enzyme, 180 kDa soluble fragment (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice develop normally, are viable and fertile but
CC develop hypertension. They display increased body weight associated
CC with impaired maturation of pro-NPPA which can be restored by injection
CC of Corin. Spontaneous and salt-sensitive hypertension exacerbated
CC during pregnancy is also noticed. A cardiac hypertrophy is also
CC detected together with a decline in cardiac function later in life
CC (PubMed:15637153). Blood pressure on a high-salt diet is significantly
CC increased: knockout mice show an impairment of urinary sodium excretion
CC and an increase in body weight, but no elevation of plasma renin or
CC serum aldosterone levels (PubMed:22418978). Conditional knockout mice
CC which express Corin in heart only do not display any visible phenotype
CC in non-pregnant mice. In contrast, pregnant conditional knockout mice
CC develop high blood pressure and proteinuria, characteristics of pre-
CC eclampsia. In these mice, trophoblast invasion and uterine spiral
CC artery remodeling are markedly impaired (PubMed:22437503).
CC {ECO:0000269|PubMed:15637153, ECO:0000269|PubMed:22418978,
CC ECO:0000269|PubMed:22437503}.
CC -!- MISCELLANEOUS: Corin is disrupted in C57BL/6-Kit(W-sh/W-sh) mice, a
CC genetic inversion used as mast cell-deficient model. Phenotypes in
CC C57BL/6-Kit(W-sh/W-sh) mice are mainly due to the absence of Kit, a
CC receptor for mast cell development. The absence of Corin probably leads
CC to immediate significant cardiac hypertrophy and contractile
CC dysfunction in response to pressure overload (PubMed:21903139).
CC {ECO:0000305|PubMed:21903139}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AB013874; BAA34371.1; -; mRNA.
DR EMBL; AC129608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466524; EDL37819.1; -; Genomic_DNA.
DR EMBL; BC093485; AAH93485.1; -; mRNA.
DR EMBL; BC138339; AAI38340.1; -; mRNA.
DR EMBL; BC138340; AAI38341.1; -; mRNA.
DR CCDS; CCDS19330.1; -. [Q9Z319-1]
DR CCDS; CCDS51513.1; -. [Q9Z319-2]
DR PIR; JE0315; JE0315.
DR RefSeq; NP_001116228.1; NM_001122756.1. [Q9Z319-2]
DR RefSeq; NP_058565.2; NM_016869.3. [Q9Z319-1]
DR AlphaFoldDB; Q9Z319; -.
DR SMR; Q9Z319; -.
DR BioGRID; 207313; 9.
DR STRING; 10090.ENSMUSP00000005352; -.
DR MEROPS; S01.019; -.
DR GlyGen; Q9Z319; 17 sites.
DR iPTMnet; Q9Z319; -.
DR PhosphoSitePlus; Q9Z319; -.
DR CPTAC; non-CPTAC-3454; -.
DR PaxDb; Q9Z319; -.
DR PRIDE; Q9Z319; -.
DR ProteomicsDB; 284092; -. [Q9Z319-1]
DR ProteomicsDB; 284093; -. [Q9Z319-2]
DR Antibodypedia; 23775; 342 antibodies from 27 providers.
DR DNASU; 53419; -.
DR Ensembl; ENSMUST00000005352; ENSMUSP00000005352; ENSMUSG00000005220. [Q9Z319-1]
DR Ensembl; ENSMUST00000167460; ENSMUSP00000127389; ENSMUSG00000005220. [Q9Z319-2]
DR GeneID; 53419; -.
DR KEGG; mmu:53419; -.
DR UCSC; uc008xrj.2; mouse. [Q9Z319-1]
DR UCSC; uc008xrk.2; mouse. [Q9Z319-2]
DR CTD; 10699; -.
DR MGI; MGI:1349451; Corin.
DR VEuPathDB; HostDB:ENSMUSG00000005220; -.
DR eggNOG; KOG3577; Eukaryota.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000157103; -.
DR InParanoid; Q9Z319; -.
DR OMA; ELECVNH; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q9Z319; -.
DR TreeFam; TF351678; -.
DR Reactome; R-MMU-5578768; Physiological factors.
DR BioGRID-ORCS; 53419; 1 hit in 78 CRISPR screens.
DR ChiTaRS; Corin; mouse.
DR PRO; PR:Q9Z319; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9Z319; protein.
DR Bgee; ENSMUSG00000005220; Expressed in myocardium of ventricle and 94 other tissues.
DR ExpressionAtlas; Q9Z319; baseline and differential.
DR Genevisible; Q9Z319; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IMP:UniProtKB.
DR GO; GO:0007565; P:female pregnancy; IMP:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; ISO:MGI.
DR GO; GO:0016486; P:peptide hormone processing; IMP:UniProtKB.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:UniProtKB.
DR GO; GO:0035813; P:regulation of renal sodium excretion; IMP:UniProtKB.
DR GO; GO:0003050; P:regulation of systemic arterial blood pressure by atrial natriuretic peptide; IMP:UniProtKB.
DR CDD; cd07445; CRD_corin_1; 1.
DR CDD; cd07888; CRD_corin_2; 1.
DR CDD; cd00112; LDLa; 7.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 1.10.2000.10; -; 2.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 4.10.400.10; -; 7.
DR InterPro; IPR017052; Corin.
DR InterPro; IPR041762; Corin_CRD_1.
DR InterPro; IPR041763; Corin_CRD_2.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF01392; Fz; 2.
DR Pfam; PF00057; Ldl_recept_a; 6.
DR Pfam; PF15494; SRCR_2; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF036376; Corin; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00063; FRI; 2.
DR SMART; SM00192; LDLa; 7.
DR SMART; SM00202; SR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56487; SSF56487; 1.
DR SUPFAM; SSF57424; SSF57424; 7.
DR SUPFAM; SSF63501; SSF63501; 2.
DR PROSITE; PS50038; FZ; 2.
DR PROSITE; PS01209; LDLRA_1; 6.
DR PROSITE; PS50068; LDLRA_2; 7.
DR PROSITE; PS00420; SRCR_1; 1.
DR PROSITE; PS50287; SRCR_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Hydrolase; Membrane; Protease; Reference proteome; Repeat; Secreted;
KW Serine protease; Signal-anchor; Transmembrane; Transmembrane helix;
KW Zymogen.
FT CHAIN 1..1113
FT /note="Atrial natriuretic peptide-converting enzyme"
FT /id="PRO_0000088674"
FT CHAIN 1..867
FT /note="Atrial natriuretic peptide-converting enzyme, N-
FT terminal propeptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000391767"
FT CHAIN ?..867
FT /note="Atrial natriuretic peptide-converting enzyme, 180
FT kDa soluble fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000417987"
FT CHAIN 868..1113
FT /note="Atrial natriuretic peptide-converting enzyme,
FT activated protease fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000391768"
FT TOPO_DOM 1..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..1113
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 201..327
FT /note="FZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DOMAIN 336..372
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 373..408
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 409..445
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 446..483
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 518..641
FT /note="FZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DOMAIN 647..682
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 683..721
FT /note="LDL-receptor class A 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 722..757
FT /note="LDL-receptor class A 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 758..853
FT /note="SRCR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 869..1102
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 176..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 910
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 959
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 1052
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT SITE 868..869
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 635
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 719
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 765
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 828
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 970
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1089
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 206..266
FT /evidence="ECO:0000250"
FT DISULFID 214..259
FT /evidence="ECO:0000250"
FT DISULFID 250..290
FT /evidence="ECO:0000250"
FT DISULFID 279..324
FT /evidence="ECO:0000250"
FT DISULFID 283..307
FT /evidence="ECO:0000250"
FT DISULFID 337..350
FT /evidence="ECO:0000250"
FT DISULFID 345..363
FT /evidence="ECO:0000250"
FT DISULFID 357..372
FT /evidence="ECO:0000250"
FT DISULFID 374..386
FT /evidence="ECO:0000250"
FT DISULFID 381..399
FT /evidence="ECO:0000250"
FT DISULFID 393..408
FT /evidence="ECO:0000250"
FT DISULFID 410..423
FT /evidence="ECO:0000250"
FT DISULFID 418..436
FT /evidence="ECO:0000250"
FT DISULFID 430..445
FT /evidence="ECO:0000250"
FT DISULFID 447..460
FT /evidence="ECO:0000250"
FT DISULFID 455..473
FT /evidence="ECO:0000250"
FT DISULFID 467..482
FT /evidence="ECO:0000250"
FT DISULFID 523..586
FT /evidence="ECO:0000250"
FT DISULFID 531..579
FT /evidence="ECO:0000250"
FT DISULFID 570..608
FT /evidence="ECO:0000250"
FT DISULFID 597..638
FT /evidence="ECO:0000250"
FT DISULFID 601..625
FT /evidence="ECO:0000250"
FT DISULFID 648..660
FT /evidence="ECO:0000250"
FT DISULFID 655..673
FT /evidence="ECO:0000250"
FT DISULFID 667..682
FT /evidence="ECO:0000250"
FT DISULFID 684..698
FT /evidence="ECO:0000250"
FT DISULFID 692..711
FT /evidence="ECO:0000250"
FT DISULFID 705..720
FT /evidence="ECO:0000250"
FT DISULFID 723..735
FT /evidence="ECO:0000250"
FT DISULFID 730..748
FT /evidence="ECO:0000250"
FT DISULFID 742..757
FT /evidence="ECO:0000250"
FT DISULFID 782..884
FT /evidence="ECO:0000250"
FT DISULFID 857..979
FT /note="Interchain (between N-terminal propeptide and
FT activated protease fragment chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090,
FT ECO:0000255|PROSITE-ProRule:PRU00124, ECO:0000255|PROSITE-
FT ProRule:PRU00196, ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 895..911
FT /evidence="ECO:0000250"
FT DISULFID 993..1058
FT /evidence="ECO:0000250"
FT DISULFID 1022..1037
FT /evidence="ECO:0000250"
FT DISULFID 1048..1077
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..89
FT /note="MGRVSFSVRVSSVRRARCSCPGRCYLSCRVPPTTALRALNGLGCAGVPGETA
FT GGAVGPGPLGTRGFLSGSKFQAPGSWKDCFGAPPAPD -> MFTKRPPALAPEEYSRRA
FT DAPKR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043953"
FT CONFLICT 402
FT /note="L -> P (in Ref. 1; BAA34371)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="R -> T (in Ref. 1; BAA34371)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="L -> F (in Ref. 1; BAA34371)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="P -> L (in Ref. 1; BAA34371)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1113 AA; 123006 MW; D6D002204779F8EA CRC64;
MGRVSFSVRV SSVRRARCSC PGRCYLSCRV PPTTALRALN GLGCAGVPGE TAGGAVGPGP
LGTRGFLSGS KFQAPGSWKD CFGAPPAPDV LRADRSVGEG CPQKLVTANL LRFLLLVLIP
CICALIVLLA ILLSFVGTLK RVYFKSNDSE PLVTDGEARV PGVIPVNTVY YENTGAPSLP
PSQSTPAWTP RAPSPEDQSH RNTSTCMNIT HSQCQILPYH STLAPLLPIV KNMDMEKFLK
FFTYLHRLSC YQHILLFGCS LAFPECVVDG DDRHGLLPCR SFCEAAKEGC ESVLGMVNSS
WPDSLRCSQF RDHTETNSSV RKSCFSLQQE HGKQSLCGGG ESFLCTSGLC VPKKLQCNGY
NDCDDWSDEA HCNCSKDLFH CGTGKCLHYS LLCDGYDDCG DLSDEQNCDC NLTKEHRCGD
GRCIAAEWVC DGDHDCVDKS DEVNCSCHSQ GLVECRSGQC IPSTFQCDGD EDCKDGSDEE
NCSDSQTPCP EGEQGCLGSS CVESCAGSSL CDSDSSLSNC SQCEPITLEL CMNLPYNHTH
YPNYLGHRTQ KEASISWESS LFPALVQTNC YKYLMFFACT ILVPKCDVNT GQRIPPCRLL
CEHSKERCES VLGIVGLQWP EDTDCNQFPE ESSDNQTCLL PNEDVEECSP SHFKCRSGRC
VLGSRRCDGQ ADCDDDSDEE NCGCKERALW ECPFNKQCLK HTLICDGFPD CPDSMDEKNC
SFCQDNELEC ANHECVPRDL WCDGWVDCSD SSDEWGCVTL SKNGNSSSLL TVHKSAKEHH
VCADGWRETL SQLACKQMGL GEPSVTKLIP GQEGQQWLRL YPNWENLNGS TLQELLVYRH
SCPSRSEISL LCSKQDCGRR PAARMNKRIL GGRTSRPGRW PWQCSLQSEP SGHICGCVLI
AKKWVLTVAH CFEGREDADV WKVVFGINNL DHPSGFMQTR FVKTILLHPR YSRAVVDYDI
SVVELSDDIN ETSYVRPVCL PSPEEYLEPD TYCYITGWGH MGNKMPFKLQ EGEVRIIPLE
QCQSYFDMKT ITNRMICAGY ESGTVDSCMG DSGGPLVCER PGGQWTLFGL TSWGSVCFSK
VLGPGVYSNV SYFVGWIERQ IYIQTFLQKK SQG
