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Protein

Atrial natriuretic peptide-converting enzyme

Gene

Corin

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Serine-type endopeptidase involved in atrial natriuretic peptide hormone (NPPA) processing. Converts through proteolytic cleavage the non-functional propeptide NPPA into the active hormone, thereby regulating blood pressure in heart and promoting natriuresis, diuresis and vasodilation. Proteolytic cleavage of pro-NPPA also plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus. Also acts as a regulator of sodium reabsorption in kidney. May also process pro-NPPB the B-type natriuretic peptide.5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei910 – 9101Charge relay systemBy similarity
Active sitei959 – 9591Charge relay systemBy similarity
Active sitei1052 – 10521Charge relay systemBy similarity

GO - Molecular functioni

  • scavenger receptor activity Source: InterPro
  • serine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  • female pregnancy Source: UniProtKB
  • neuron differentiation Source: MGI
  • peptide hormone processing Source: UniProtKB
  • regulation of blood pressure Source: UniProtKB
  • regulation of renal sodium excretion Source: UniProtKB
  • regulation of systemic arterial blood pressure by atrial natriuretic peptide Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

ReactomeiR-MMU-5578768. Physiological factors.

Protein family/group databases

MEROPSiS01.019.

Names & Taxonomyi

Protein namesi
Recommended name:
Atrial natriuretic peptide-converting enzyme (EC:3.4.21.-)
Alternative name(s):
Corin
Low density lipoprotein receptor-related protein 4
Pro-ANP-converting enzyme
Cleaved into the following 3 chains:
Gene namesi
Name:Corin
Synonyms:Crn, Lrp4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1349451. Corin.

Subcellular locationi

Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment :
  • Secreted By similarity

  • Note: Soluble form produced following cleavage by ADAM10.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 112112CytoplasmicSequence analysisAdd
BLAST
Transmembranei113 – 13321Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini134 – 1113980ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: MGI
  • extracellular region Source: UniProtKB-SubCell
  • integral component of plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Disruption phenotypei

Mice develop normally, are viable and fertile but develop hypertension. They display increased body weight associated with impaired maturation of pro-NPPA which can be restored by injection of Corin. Spontaneous and salt-sensitive hypertension exacerbated during pregnancy is also noticed. A cardiac hypertrophy is also detected together with a decline in cardiac function later in life (PubMed:15637153). Blood pressure on a high-salt diet is significantly increased: knockout mice show an impairment of urinary sodium excretion and an increase in body weight, but no elevation of plasma renin or serum aldosterone levels (PubMed:22418978). Conditional knockout mice which express Corin in heart only do not display any visible phenotype in non-pregnant mice. In contrast, pregnant conditional knockout mice develop high blood pressure and proteinuria, characteristics of pre-eclampsia. In these mice, trophoblast invasion and uterine spiral artery remodeling are markedly impaired (PubMed:22437503).3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 867Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragmentBy similarityPRO_0000417987
Chaini1 – 11131113Atrial natriuretic peptide-converting enzymePRO_0000088674Add
BLAST
Chaini1 – 867867Atrial natriuretic peptide-converting enzyme, N-terminal propeptideBy similarityPRO_0000391767Add
BLAST
Chaini868 – 1113246Atrial natriuretic peptide-converting enzyme, activated protease fragmentBy similarityPRO_0000391768Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi147 – 1471N-linked (GlcNAc...)Sequence analysis
Glycosylationi202 – 2021N-linked (GlcNAc...)Sequence analysis
Disulfide bondi206 ↔ 266By similarity
Glycosylationi208 – 2081N-linked (GlcNAc...)Sequence analysis
Disulfide bondi214 ↔ 259By similarity
Disulfide bondi250 ↔ 290By similarity
Disulfide bondi279 ↔ 324By similarity
Disulfide bondi283 ↔ 307By similarity
Glycosylationi298 – 2981N-linked (GlcNAc...)Sequence analysis
Glycosylationi317 – 3171N-linked (GlcNAc...)Sequence analysis
Disulfide bondi337 ↔ 350By similarity
Disulfide bondi345 ↔ 363By similarity
Disulfide bondi357 ↔ 372By similarity
Glycosylationi373 – 3731N-linked (GlcNAc...)Sequence analysis
Disulfide bondi374 ↔ 386By similarity
Disulfide bondi381 ↔ 399By similarity
Disulfide bondi393 ↔ 408By similarity
Disulfide bondi410 ↔ 423By similarity
Glycosylationi411 – 4111N-linked (GlcNAc...)Sequence analysis
Disulfide bondi418 ↔ 436By similarity
Disulfide bondi430 ↔ 445By similarity
Glycosylationi444 – 4441N-linked (GlcNAc...)Sequence analysis
Disulfide bondi447 ↔ 460By similarity
Disulfide bondi455 ↔ 473By similarity
Disulfide bondi467 ↔ 482By similarity
Glycosylationi481 – 4811N-linked (GlcNAc...)Sequence analysis
Glycosylationi519 – 5191N-linked (GlcNAc...)Sequence analysis
Disulfide bondi523 ↔ 586By similarity
Disulfide bondi531 ↔ 579By similarity
Glycosylationi537 – 5371N-linked (GlcNAc...)Sequence analysis
Disulfide bondi570 ↔ 608By similarity
Disulfide bondi597 ↔ 638By similarity
Disulfide bondi601 ↔ 625By similarity
Glycosylationi635 – 6351N-linked (GlcNAc...)Sequence analysis
Disulfide bondi648 ↔ 660By similarity
Disulfide bondi655 ↔ 673By similarity
Disulfide bondi667 ↔ 682By similarity
Disulfide bondi684 ↔ 698By similarity
Disulfide bondi692 ↔ 711By similarity
Disulfide bondi705 ↔ 720By similarity
Glycosylationi719 – 7191N-linked (GlcNAc...)Sequence analysis
Disulfide bondi723 ↔ 735By similarity
Disulfide bondi730 ↔ 748By similarity
Disulfide bondi742 ↔ 757By similarity
Glycosylationi765 – 7651N-linked (GlcNAc...)Sequence analysis
Disulfide bondi782 ↔ 884By similarity
Glycosylationi828 – 8281N-linked (GlcNAc...)Sequence analysis
Disulfide bondi857 ↔ 979Interchain (between N-terminal propeptide and activated protease fragment chains)PROSITE-ProRule annotation
Disulfide bondi895 ↔ 911By similarity
Glycosylationi970 – 9701N-linked (GlcNAc...)Sequence analysis
Disulfide bondi993 ↔ 1058By similarity
Disulfide bondi1022 ↔ 1037By similarity
Disulfide bondi1048 ↔ 1077By similarity
Glycosylationi1089 – 10891N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated; required for processing and activation.By similarity
Activated through proteolytic processing by a trypsin-like protease; cleaved into a N-terminal propeptide and an activated corin protease fragment. Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment is produced by cleavage by ADAM10. Cleavage by ADAM10 to produce soluble 180 kDa soluble fragment takes place after the transmembrane region and before FZ 1 (By similarity).By similarity
A disulfide bond links the activated corin protease fragment and the N-terminal propeptide. The disulfide bond also links the activated corin protease fragment with Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei868 – 8692CleavageBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ9Z319.
PRIDEiQ9Z319.

PTM databases

iPTMnetiQ9Z319.
PhosphoSiteiQ9Z319.

Expressioni

Tissue specificityi

Highly expressed in heart. Also expressed in pregnant uterus.1 Publication

Gene expression databases

BgeeiQ9Z319.
CleanExiMM_CORIN.
ExpressionAtlasiQ9Z319. baseline and differential.
GenevisibleiQ9Z319. MM.

Interactioni

Protein-protein interaction databases

MINTiMINT-4998561.
STRINGi10090.ENSMUSP00000005352.

Structurei

3D structure databases

ProteinModelPortaliQ9Z319.
SMRiQ9Z319. Positions 206-639, 644-754, 767-803, 842-1101.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini201 – 327127FZ 1PROSITE-ProRule annotationAdd
BLAST
Domaini336 – 37237LDL-receptor class A 1PROSITE-ProRule annotationAdd
BLAST
Domaini373 – 40836LDL-receptor class A 2PROSITE-ProRule annotationAdd
BLAST
Domaini409 – 44537LDL-receptor class A 3PROSITE-ProRule annotationAdd
BLAST
Domaini446 – 48338LDL-receptor class A 4PROSITE-ProRule annotationAdd
BLAST
Domaini518 – 641124FZ 2PROSITE-ProRule annotationAdd
BLAST
Domaini647 – 68236LDL-receptor class A 5PROSITE-ProRule annotationAdd
BLAST
Domaini683 – 72139LDL-receptor class A 6PROSITE-ProRule annotationAdd
BLAST
Domaini722 – 75736LDL-receptor class A 7PROSITE-ProRule annotationAdd
BLAST
Domaini758 – 85396SRCRPROSITE-ProRule annotationAdd
BLAST
Domaini869 – 1102234Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 2 FZ (frizzled) domains.PROSITE-ProRule annotation
Contains 7 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
Contains 1 SRCR domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3577. Eukaryota.
KOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00840000129691.
HOGENOMiHOG000060148.
HOVERGENiHBG051079.
InParanoidiQ9Z319.
KOiK09614.
OMAiHHVCADG.
OrthoDBiEOG75B84T.
TreeFamiTF351678.

Family and domain databases

Gene3Di1.10.2000.10. 2 hits.
3.10.250.10. 1 hit.
4.10.400.10. 6 hits.
InterProiIPR017052. Corin.
IPR020067. Frizzled_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR009003. Peptidase_S1_PA.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR001254. Trypsin_dom.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF01392. Fz. 2 hits.
PF00057. Ldl_recept_a. 6 hits.
PF15494. SRCR_2. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF036376. Corin. 1 hit.
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00063. FRI. 2 hits.
SM00192. LDLa. 7 hits.
SM00202. SR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF56487. SSF56487. 1 hit.
SSF57424. SSF57424. 7 hits.
SSF63501. SSF63501. 2 hits.
PROSITEiPS50038. FZ. 2 hits.
PS01209. LDLRA_1. 6 hits.
PS50068. LDLRA_2. 7 hits.
PS00420. SRCR_1. 1 hit.
PS50287. SRCR_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Z319-1) [UniParc]FASTAAdd to basket

Also known as: E1a, mE1a

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.

« Hide

        10         20         30         40         50
MGRVSFSVRV SSVRRARCSC PGRCYLSCRV PPTTALRALN GLGCAGVPGE
60 70 80 90 100
TAGGAVGPGP LGTRGFLSGS KFQAPGSWKD CFGAPPAPDV LRADRSVGEG
110 120 130 140 150
CPQKLVTANL LRFLLLVLIP CICALIVLLA ILLSFVGTLK RVYFKSNDSE
160 170 180 190 200
PLVTDGEARV PGVIPVNTVY YENTGAPSLP PSQSTPAWTP RAPSPEDQSH
210 220 230 240 250
RNTSTCMNIT HSQCQILPYH STLAPLLPIV KNMDMEKFLK FFTYLHRLSC
260 270 280 290 300
YQHILLFGCS LAFPECVVDG DDRHGLLPCR SFCEAAKEGC ESVLGMVNSS
310 320 330 340 350
WPDSLRCSQF RDHTETNSSV RKSCFSLQQE HGKQSLCGGG ESFLCTSGLC
360 370 380 390 400
VPKKLQCNGY NDCDDWSDEA HCNCSKDLFH CGTGKCLHYS LLCDGYDDCG
410 420 430 440 450
DLSDEQNCDC NLTKEHRCGD GRCIAAEWVC DGDHDCVDKS DEVNCSCHSQ
460 470 480 490 500
GLVECRSGQC IPSTFQCDGD EDCKDGSDEE NCSDSQTPCP EGEQGCLGSS
510 520 530 540 550
CVESCAGSSL CDSDSSLSNC SQCEPITLEL CMNLPYNHTH YPNYLGHRTQ
560 570 580 590 600
KEASISWESS LFPALVQTNC YKYLMFFACT ILVPKCDVNT GQRIPPCRLL
610 620 630 640 650
CEHSKERCES VLGIVGLQWP EDTDCNQFPE ESSDNQTCLL PNEDVEECSP
660 670 680 690 700
SHFKCRSGRC VLGSRRCDGQ ADCDDDSDEE NCGCKERALW ECPFNKQCLK
710 720 730 740 750
HTLICDGFPD CPDSMDEKNC SFCQDNELEC ANHECVPRDL WCDGWVDCSD
760 770 780 790 800
SSDEWGCVTL SKNGNSSSLL TVHKSAKEHH VCADGWRETL SQLACKQMGL
810 820 830 840 850
GEPSVTKLIP GQEGQQWLRL YPNWENLNGS TLQELLVYRH SCPSRSEISL
860 870 880 890 900
LCSKQDCGRR PAARMNKRIL GGRTSRPGRW PWQCSLQSEP SGHICGCVLI
910 920 930 940 950
AKKWVLTVAH CFEGREDADV WKVVFGINNL DHPSGFMQTR FVKTILLHPR
960 970 980 990 1000
YSRAVVDYDI SVVELSDDIN ETSYVRPVCL PSPEEYLEPD TYCYITGWGH
1010 1020 1030 1040 1050
MGNKMPFKLQ EGEVRIIPLE QCQSYFDMKT ITNRMICAGY ESGTVDSCMG
1060 1070 1080 1090 1100
DSGGPLVCER PGGQWTLFGL TSWGSVCFSK VLGPGVYSNV SYFVGWIERQ
1110
IYIQTFLQKK SQG
Length:1,113
Mass (Da):123,006
Last modified:July 27, 2011 - v2
Checksum:iD6D002204779F8EA
GO
Isoform 2 (identifier: Q9Z319-2) [UniParc]FASTAAdd to basket

Also known as: E1, mE1

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: MGRVSFSVRV...DCFGAPPAPD → MFTKRPPALAPEEYSRRADAPKR

Show »
Length:1,047
Mass (Da):116,697
Checksum:i2C434D652014A34D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti402 – 4021L → P in BAA34371 (PubMed:9756624).Curated
Sequence conflicti456 – 4561R → T in BAA34371 (PubMed:9756624).Curated
Sequence conflicti497 – 4971L → F in BAA34371 (PubMed:9756624).Curated
Sequence conflicti535 – 5351P → L in BAA34371 (PubMed:9756624).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8989MGRVS…PPAPD → MFTKRPPALAPEEYSRRADA PKR in isoform 2. 1 PublicationVSP_043953Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013874 mRNA. Translation: BAA34371.1.
AC129608 Genomic DNA. No translation available.
AC161529 Genomic DNA. No translation available.
CH466524 Genomic DNA. Translation: EDL37819.1.
BC093485 mRNA. Translation: AAH93485.1.
BC138339 mRNA. Translation: AAI38340.1.
BC138340 mRNA. Translation: AAI38341.1.
CCDSiCCDS19330.1. [Q9Z319-1]
CCDS51513.1. [Q9Z319-2]
PIRiJE0315.
RefSeqiNP_001116228.1. NM_001122756.1. [Q9Z319-2]
NP_058565.2. NM_016869.3. [Q9Z319-1]
UniGeneiMm.332425.

Genome annotation databases

EnsembliENSMUST00000005352; ENSMUSP00000005352; ENSMUSG00000005220. [Q9Z319-1]
ENSMUST00000167460; ENSMUSP00000127389; ENSMUSG00000005220. [Q9Z319-2]
GeneIDi53419.
KEGGimmu:53419.
UCSCiuc008xrj.2. mouse. [Q9Z319-1]
uc008xrk.2. mouse. [Q9Z319-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013874 mRNA. Translation: BAA34371.1.
AC129608 Genomic DNA. No translation available.
AC161529 Genomic DNA. No translation available.
CH466524 Genomic DNA. Translation: EDL37819.1.
BC093485 mRNA. Translation: AAH93485.1.
BC138339 mRNA. Translation: AAI38340.1.
BC138340 mRNA. Translation: AAI38341.1.
CCDSiCCDS19330.1. [Q9Z319-1]
CCDS51513.1. [Q9Z319-2]
PIRiJE0315.
RefSeqiNP_001116228.1. NM_001122756.1. [Q9Z319-2]
NP_058565.2. NM_016869.3. [Q9Z319-1]
UniGeneiMm.332425.

3D structure databases

ProteinModelPortaliQ9Z319.
SMRiQ9Z319. Positions 206-639, 644-754, 767-803, 842-1101.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4998561.
STRINGi10090.ENSMUSP00000005352.

Protein family/group databases

MEROPSiS01.019.

PTM databases

iPTMnetiQ9Z319.
PhosphoSiteiQ9Z319.

Proteomic databases

PaxDbiQ9Z319.
PRIDEiQ9Z319.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005352; ENSMUSP00000005352; ENSMUSG00000005220. [Q9Z319-1]
ENSMUST00000167460; ENSMUSP00000127389; ENSMUSG00000005220. [Q9Z319-2]
GeneIDi53419.
KEGGimmu:53419.
UCSCiuc008xrj.2. mouse. [Q9Z319-1]
uc008xrk.2. mouse. [Q9Z319-2]

Organism-specific databases

CTDi10699.
MGIiMGI:1349451. Corin.

Phylogenomic databases

eggNOGiKOG3577. Eukaryota.
KOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00840000129691.
HOGENOMiHOG000060148.
HOVERGENiHBG051079.
InParanoidiQ9Z319.
KOiK09614.
OMAiHHVCADG.
OrthoDBiEOG75B84T.
TreeFamiTF351678.

Enzyme and pathway databases

ReactomeiR-MMU-5578768. Physiological factors.

Miscellaneous databases

NextBioi310249.
PROiQ9Z319.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z319.
CleanExiMM_CORIN.
ExpressionAtlasiQ9Z319. baseline and differential.
GenevisibleiQ9Z319. MM.

Family and domain databases

Gene3Di1.10.2000.10. 2 hits.
3.10.250.10. 1 hit.
4.10.400.10. 6 hits.
InterProiIPR017052. Corin.
IPR020067. Frizzled_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR009003. Peptidase_S1_PA.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR001254. Trypsin_dom.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF01392. Fz. 2 hits.
PF00057. Ldl_recept_a. 6 hits.
PF15494. SRCR_2. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF036376. Corin. 1 hit.
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00063. FRI. 2 hits.
SM00192. LDLa. 7 hits.
SM00202. SR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF56487. SSF56487. 1 hit.
SSF57424. SSF57424. 7 hits.
SSF63501. SSF63501. 2 hits.
PROSITEiPS50038. FZ. 2 hits.
PS01209. LDLRA_1. 6 hits.
PS50068. LDLRA_2. 7 hits.
PS00420. SRCR_1. 1 hit.
PS50287. SRCR_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel low-density lipoprotein receptor-related protein with type II membrane protein-like structure is abundant in heart."
    Tomita Y., Kim D.-H., Magoori K., Fujino T., Yamamoto T.T.
    J. Biochem. 124:784-789(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Brain and Head.
  5. "Processing of pro-atrial natriuretic peptide by corin in cardiac myocytes."
    Wu F., Yan W., Pan J., Morser J., Wu Q.
    J. Biol. Chem. 277:16900-16905(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Hypertension in mice lacking the proatrial natriuretic peptide convertase corin."
    Chan J.C., Knudson O., Wu F., Morser J., Dole W.P., Wu Q.
    Proc. Natl. Acad. Sci. U.S.A. 102:785-790(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  7. "Decreased renal corin expression contributes to sodium retention in proteinuric kidney diseases."
    Polzin D., Kaminski H.J., Kastner C., Wang W., Kramer S., Gambaryan S., Russwurm M., Peters H., Wu Q., Vandewalle A., Bachmann S., Theilig F.
    Kidney Int. 78:650-659(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Human corin isoforms with different cytoplasmic tails that alter cell surface targeting."
    Qi X., Jiang J., Zhu M., Wu Q.
    J. Biol. Chem. 286:20963-20969(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
  9. "Corin-deficient W-sh mice poorly tolerate increased cardiac afterload."
    Buckley C.L., Stokes A.J.
    Regul. Pept. 172:44-50(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION IN W-SH MODEL MICE.
  10. "Impaired sodium excretion and salt-sensitive hypertension in corin-deficient mice."
    Wang W., Shen J., Cui Y., Jiang J., Chen S., Peng J., Wu Q.
    Kidney Int. 82:26-33(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  11. "Role of corin in trophoblast invasion and uterine spiral artery remodelling in pregnancy."
    Cui Y., Wang W., Dong N., Lou J., Srinivasan D.K., Cheng W., Huang X., Liu M., Fang C., Peng J., Chen S., Wu S., Liu Z., Dong L., Zhou Y., Wu Q.
    Nature 484:246-250(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiCORIN_MOUSE
AccessioniPrimary (citable) accession number: Q9Z319
Secondary accession number(s): B2RRC6, Q566K6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Corin is disrupted in C57BL/6-Kit(W-sh/W-sh) mice, a genetic inversion used as mast cell-deficient model. Phenotypes in C57BL/6-Kit(W-sh/W-sh) mice are mainly due to the absence of Kit, a receptor for mast cell development. The absence of Corin probably leads to immediate significant cardiac hypertrophy and contractile dysfunction in response to pressure overload (PubMed:21903139).1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.