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Q9Y5Q5

- CORIN_HUMAN

UniProt

Q9Y5Q5 - CORIN_HUMAN

Protein

Atrial natriuretic peptide-converting enzyme

Gene

CORIN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      Previous versions | rss
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    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.
    Isoform 2: has weaker endopeptidase activity compared to isoform 1.

    Enzyme regulationi

    Inhibited in a dose-dependent manner by non-specific trypsin-like serine protease inhibitors including benzamidine.

    Kineticsi

    1. KM=1.28 mM for pyroGlu-Phe-Lys-pNA.HCl1 Publication
    2. KM=3.52 mM for pyroGlu-Pro-Arg-pNA.HCl1 Publication
    3. KM=2.95 mM for H-D-Pro-Phe-Arg-pNA.2HCl1 Publication
    4. KM=1.92 mM for Bz-Ile-Glu-(gamma-OR)-Gly-Arg-pNA.HCl1 Publication
    5. KM=16 mM for pyroGlu-Gly-Arg-pNA.HCl1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei164 – 1652Cleavage; by autolysis
    Sitei427 – 4282Cleavage; by autolysis
    Sitei801 – 8022CleavageCurated
    Active sitei843 – 8431Charge relay systemBy similarity
    Active sitei892 – 8921Charge relay systemBy similarity
    Active sitei985 – 9851Charge relay system

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: UniProtKB
    2. serine-type exopeptidase activity Source: InterPro

    GO - Biological processi

    1. female pregnancy Source: UniProtKB
    2. peptide hormone processing Source: UniProtKB
    3. proteolysis Source: GOC
    4. regulation of blood pressure Source: UniProtKB
    5. regulation of renal sodium excretion Source: UniProtKB
    6. regulation of systemic arterial blood pressure by atrial natriuretic peptide Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Protein family/group databases

    MEROPSiS01.019.

    Names & Taxonomyi

    Protein namesi
    Gene namesi
    Name:CORIN
    Synonyms:CRN, TMPRSS10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:19012. CORIN.

    Subcellular locationi

    Cell membrane 3 Publications; Single-pass type II membrane protein 3 Publications
    Note: May easily detached from the endothelial cell membrane.
    Isoform 2 : Cell membrane; Single-pass type II membrane protein
    Note: Less efficiently targeted to the cell membrane compared to isoform 1.
    Chain Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment : Secreted
    Note: Soluble form produced following cleavage by ADAM10.
    Chain Atrial natriuretic peptide-converting enzyme, 160 kDa soluble fragment : Secreted
    Note: Soluble form produced following autocatalytic cleavage.
    Chain Atrial natriuretic peptide-converting enzyme, 100 kDa soluble fragment : Secreted
    Note: Soluble form produced following autocatalytic cleavage.

    GO - Cellular componenti

    1. cell surface Source: Ensembl
    2. extracellular region Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. integral component of plasma membrane Source: UniProtKB
    5. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Pre-eclampsia/eclampsia 5 (PEE5) [MIM:614595]: A hypertensive disorder of pregnancy characterized by new hypertension (blood pressure 140/90 or greater) presenting after 20 weeks' gestation with clinically relevant proteinuria. It impacts 2 individuals, the mother and her child, both of whom can be severely affected. Preeclampsia is one of the causes of maternal mortality and morbidity worldwide.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti317 – 3171K → E in PEE5. 1 Publication
    VAR_067795
    Natural varianti472 – 4721S → G in PEE5. 1 Publication
    VAR_067797

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi26 – 261D → A: Impairs cell membrane targeting; when associated with A-30. 1 Publication
    Mutagenesisi30 – 301M → A: Impairs cell membrane targeting; when associated with A-26. 1 Publication
    Mutagenesisi134 – 1341R → A: Does not affect autocatalytic cleavage. 1 Publication
    Mutagenesisi164 – 1641R → A: Affects autocatalytic cleavage and production of Atrial natriuretic peptide-converting enzyme, 160 kDa soluble fragment. 1 Publication
    Mutagenesisi180 – 1801R → A: Does not affect autocatalytic cleavage. 1 Publication
    Mutagenesisi213 – 2131R → A: Does not affect autocatalytic cleavage. 1 Publication
    Mutagenesisi239 – 2391R → A: Does not affect autocatalytic cleavage. 1 Publication
    Mutagenesisi244 – 2441R → A: Does not affect autocatalytic cleavage. 1 Publication
    Mutagenesisi427 – 4271R → A: Affects autocatalytic cleavage and production of Atrial natriuretic peptide-converting enzyme, 100 kDa soluble fragment. 1 Publication
    Mutagenesisi801 – 8011R → A: Loss of activity towards NPPA. 2 Publications
    Mutagenesisi985 – 9851S → A: Loss of activity towards NPPA. 3 Publications

    Organism-specific databases

    MIMi614595. phenotype.
    PharmGKBiPA134972424.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 801Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragmentCuratedPRO_0000417986
    Chaini1 – 10421042Atrial natriuretic peptide-converting enzymePRO_0000088673Add
    BLAST
    Chaini1 – 801801Atrial natriuretic peptide-converting enzyme, N-terminal propeptideCuratedPRO_0000391765Add
    BLAST
    Chaini165 – 801637Atrial natriuretic peptide-converting enzyme, 160 kDa soluble fragmentCuratedPRO_0000417984Add
    BLAST
    Chaini428 – 801374Atrial natriuretic peptide-converting enzyme, 100 kDa soluble fragmentCuratedPRO_0000417985Add
    BLAST
    Chaini802 – 1042241Atrial natriuretic peptide-converting enzyme, activated protease fragmentCuratedPRO_0000391766Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi80 – 801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi135 – 1351N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi139 ↔ 199By similarity
    Glycosylationi141 – 1411N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi147 ↔ 192By similarity
    Disulfide bondi183 ↔ 223By similarity
    Disulfide bondi212 ↔ 256By similarity
    Disulfide bondi216 ↔ 240By similarity
    Glycosylationi231 – 2311N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi245 – 2451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi251 – 2511N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi269 ↔ 282By similarity
    Disulfide bondi277 ↔ 295By similarity
    Disulfide bondi289 ↔ 304By similarity
    Glycosylationi305 – 3051N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi306 ↔ 318By similarity
    Disulfide bondi313 ↔ 331By similarity
    Glycosylationi320 – 3201N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi325 ↔ 340By similarity
    Disulfide bondi342 ↔ 355By similarity
    Disulfide bondi350 ↔ 368By similarity
    Disulfide bondi362 ↔ 377By similarity
    Glycosylationi376 – 3761N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi379 ↔ 392By similarity
    Disulfide bondi387 ↔ 405By similarity
    Disulfide bondi399 ↔ 414By similarity
    Glycosylationi413 – 4131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi446 – 4461N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi451 – 4511N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi455 ↔ 518By similarity
    Disulfide bondi463 ↔ 511By similarity
    Glycosylationi469 – 4691N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi502 ↔ 540By similarity
    Disulfide bondi529 ↔ 570By similarity
    Disulfide bondi533 ↔ 557By similarity
    Glycosylationi567 – 5671N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi580 ↔ 592By similarity
    Disulfide bondi587 ↔ 605By similarity
    Disulfide bondi599 ↔ 614By similarity
    Disulfide bondi616 ↔ 630By similarity
    Disulfide bondi624 ↔ 643By similarity
    Disulfide bondi637 ↔ 652By similarity
    Glycosylationi651 – 6511N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi655 ↔ 667By similarity
    Disulfide bondi662 ↔ 680By similarity
    Disulfide bondi674 ↔ 689By similarity
    Glycosylationi697 – 6971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi761 – 7611N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi790 ↔ 912Interchain (between N-terminal propeptide and activated protease fragment chains)1 Publication
    Disulfide bondi828 ↔ 844By similarity
    Disulfide bondi926 ↔ 991By similarity
    Disulfide bondi955 ↔ 970By similarity
    Disulfide bondi981 ↔ 1010By similarity
    Glycosylationi1022 – 10221N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated; required for processing and activation.2 Publications
    Activated through proteolytic processing by a trypsin-like protease; cleaved into a N-terminal propeptide and an activated corin protease fragment. Different soluble forms are produced by cleavage and autocatalytic cleavage: Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment is produced by cleavage by ADAM10, while 160 kDa and 100 kDa soluble fragments are produced by autocatalytic cleavage. Cleavage by ADAM10 to produce soluble 180 kDa soluble fragment takes place after the transmembrane region and before FZ 1.
    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 soluble fragments (100 kDa, 160 kDa and 180 kDa fragments).

    Keywords - PTMi

    Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiQ9Y5Q5.
    PRIDEiQ9Y5Q5.

    PTM databases

    PhosphoSiteiQ9Y5Q5.

    Expressioni

    Tissue specificityi

    Highly expressed in heart. Expressed in heart myocytes. Also expressed in pregnant uterus. Detected in blood, in plasma as well as in serum (at protein level).3 Publications

    Gene expression databases

    ArrayExpressiQ9Y5Q5.
    BgeeiQ9Y5Q5.
    CleanExiHS_CORIN.
    GenevestigatoriQ9Y5Q5.

    Interactioni

    Protein-protein interaction databases

    BioGridi115937. 1 interaction.
    STRINGi9606.ENSP00000273857.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y5Q5.
    SMRiQ9Y5Q5. Positions 138-441, 455-701, 788-1034.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4545CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini67 – 1042976ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei46 – 6621Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini134 – 259126FZ 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini268 – 30437LDL-receptor class A 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini305 – 34036LDL-receptor class A 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini341 – 37737LDL-receptor class A 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini378 – 41538LDL-receptor class A 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini450 – 573124FZ 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini579 – 61436LDL-receptor class A 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini615 – 65339LDL-receptor class A 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini654 – 68936LDL-receptor class A 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini690 – 801112SRCRAdd
    BLAST
    Domaini802 – 1035234Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi26 – 294DDNN motif

    Domaini

    The DDNN motif is required for targeting to the cell membrane and enzyme activation.1 Publication

    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.Curated

    Keywords - Domaini

    Repeat, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5640.
    HOGENOMiHOG000060148.
    HOVERGENiHBG051079.
    InParanoidiQ9Y5Q5.
    KOiK09614.
    OMAiHHVCADG.
    OrthoDBiEOG75B84T.
    PhylomeDBiQ9Y5Q5.
    TreeFamiTF351678.

    Family and domain databases

    Gene3Di1.10.2000.10. 2 hits.
    4.10.400.10. 6 hits.
    InterProiIPR020067. Frizzled_dom.
    IPR023415. LDLR_class-A_CS.
    IPR002172. LDrepeatLR_classA_rpt.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR017052. Peptidase_S1A_corin.
    IPR017448. SRCR-like_dom.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF01392. Fz. 2 hits.
    PF00057. Ldl_recept_a. 6 hits.
    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.
    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. Align

    Isoform 1 (identifier: Q9Y5Q5-1) [UniParc]FASTAAdd to Basket

    Also known as: E1, hE1

    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

    MKQSPALAPE ERCRRAGSPK PVLRADDNNM GNGCSQKLAT ANLLRFLLLV     50
    LIPCICALVL LLVILLSYVG TLQKVYFKSN GSEPLVTDGE IQGSDVILTN 100
    TIYNQSTVVS TAHPDQHVPA WTTDASLPGD QSHRNTSACM NITHSQCQML 150
    PYHATLTPLL SVVRNMEMEK FLKFFTYLHR LSCYQHIMLF GCTLAFPECI 200
    IDGDDSHGLL PCRSFCEAAK EGCESVLGMV NYSWPDFLRC SQFRNQTESS 250
    NVSRICFSPQ QENGKQLLCG RGENFLCASG ICIPGKLQCN GYNDCDDWSD 300
    EAHCNCSENL FHCHTGKCLN YSLVCDGYDD CGDLSDEQNC DCNPTTEHRC 350
    GDGRCIAMEW VCDGDHDCVD KSDEVNCSCH SQGLVECRNG QCIPSTFQCD 400
    GDEDCKDGSD EENCSVIQTS CQEGDQRCLY NPCLDSCGGS SLCDPNNSLN 450
    NCSQCEPITL ELCMNLPYNS TSYPNYFGHR TQKEASISWE SSLFPALVQT 500
    NCYKYLMFFS CTILVPKCDV NTGEHIPPCR ALCEHSKERC ESVLGIVGLQ 550
    WPEDTDCSQF PEENSDNQTC LMPDEYVEEC SPSHFKCRSG QCVLASRRCD 600
    GQADCDDDSD EENCGCKERD LWECPSNKQC LKHTVICDGF PDCPDYMDEK 650
    NCSFCQDDEL ECANHACVSR DLWCDGEADC SDSSDEWDCV TLSINVNSSS 700
    FLMVHRAATE HHVCADGWQE ILSQLACKQM GLGEPSVTKL IQEQEKEPRW 750
    LTLHSNWESL NGTTLHELLV NGQSCESRSK ISLLCTKQDC GRRPAARMNK 800
    RILGGRTSRP GRWPWQCSLQ SEPSGHICGC VLIAKKWVLT VAHCFEGREN 850
    AAVWKVVLGI NNLDHPSVFM QTRFVKTIIL HPRYSRAVVD YDISIVELSE 900
    DISETGYVRP VCLPNPEQWL EPDTYCYITG WGHMGNKMPF KLQEGEVRII 950
    SLEHCQSYFD MKTITTRMIC AGYESGTVDS CMGDSGGPLV CEKPGGRWTL 1000
    FGLTSWGSVC FSKVLGPGVY SNVSYFVEWI KRQIYIQTFL LN 1042
    Length:1,042
    Mass (Da):116,486
    Last modified:January 11, 2011 - v2
    Checksum:iA3F1CB8EBB676F78
    GO
    Isoform 2 (identifier: Q9Y5Q5-2) [UniParc]FASTAAdd to Basket

    Also known as: E1a, hE1a

    The sequence of this isoform differs from the canonical sequence as follows:
         1-29: Missing.

    Show »
    Length:1,013
    Mass (Da):113,297
    Checksum:iF4084E8B3AFFFDB8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti854 – 8541W → R in AAF21966. (PubMed:11082206)Curated
    Sequence conflicti876 – 8761K → R in AAF21966. (PubMed:11082206)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti13 – 131C → Y.2 Publications
    Corresponds to variant rs2289433 [ dbSNP | Ensembl ].
    VAR_038000
    Natural varianti317 – 3171K → E in PEE5. 1 Publication
    VAR_067795
    Natural varianti444 – 4441D → G.
    Corresponds to variant rs13105608 [ dbSNP | Ensembl ].
    VAR_067796
    Natural varianti472 – 4721S → G in PEE5. 1 Publication
    VAR_067797
    Natural varianti525 – 5251H → R.3 Publications
    Corresponds to variant rs11934749 [ dbSNP | Ensembl ].
    VAR_038001

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2929Missing in isoform 2. CuratedVSP_043952Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF133845 mRNA. Translation: AAD31850.1.
    AC092597 Genomic DNA. No translation available.
    AC104646 Genomic DNA. Translation: AAY40991.1.
    AC107068 Genomic DNA. Translation: AAY40917.1.
    EU326305 Genomic DNA. Translation: ACA05911.1.
    BC110451 mRNA. Translation: AAI10452.1.
    AF113248 mRNA. Translation: AAF21966.1.
    CCDSiCCDS3477.1. [Q9Y5Q5-1]
    RefSeqiNP_001265514.1. NM_001278585.1.
    NP_006578.2. NM_006587.3. [Q9Y5Q5-1]
    UniGeneiHs.518618.
    Hs.604887.

    Genome annotation databases

    EnsembliENST00000273857; ENSP00000273857; ENSG00000145244. [Q9Y5Q5-1]
    GeneIDi10699.
    KEGGihsa:10699.
    UCSCiuc003gxm.3. human. [Q9Y5Q5-1]

    Polymorphism databases

    DMDMi317373348.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF133845 mRNA. Translation: AAD31850.1 .
    AC092597 Genomic DNA. No translation available.
    AC104646 Genomic DNA. Translation: AAY40991.1 .
    AC107068 Genomic DNA. Translation: AAY40917.1 .
    EU326305 Genomic DNA. Translation: ACA05911.1 .
    BC110451 mRNA. Translation: AAI10452.1 .
    AF113248 mRNA. Translation: AAF21966.1 .
    CCDSi CCDS3477.1. [Q9Y5Q5-1 ]
    RefSeqi NP_001265514.1. NM_001278585.1.
    NP_006578.2. NM_006587.3. [Q9Y5Q5-1 ]
    UniGenei Hs.518618.
    Hs.604887.

    3D structure databases

    ProteinModelPortali Q9Y5Q5.
    SMRi Q9Y5Q5. Positions 138-441, 455-701, 788-1034.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115937. 1 interaction.
    STRINGi 9606.ENSP00000273857.

    Protein family/group databases

    MEROPSi S01.019.

    PTM databases

    PhosphoSitei Q9Y5Q5.

    Polymorphism databases

    DMDMi 317373348.

    Proteomic databases

    PaxDbi Q9Y5Q5.
    PRIDEi Q9Y5Q5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000273857 ; ENSP00000273857 ; ENSG00000145244 . [Q9Y5Q5-1 ]
    GeneIDi 10699.
    KEGGi hsa:10699.
    UCSCi uc003gxm.3. human. [Q9Y5Q5-1 ]

    Organism-specific databases

    CTDi 10699.
    GeneCardsi GC04M047596.
    H-InvDB HIX0024555.
    HGNCi HGNC:19012. CORIN.
    MIMi 605236. gene.
    614595. phenotype.
    neXtProti NX_Q9Y5Q5.
    PharmGKBi PA134972424.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOGENOMi HOG000060148.
    HOVERGENi HBG051079.
    InParanoidi Q9Y5Q5.
    KOi K09614.
    OMAi HHVCADG.
    OrthoDBi EOG75B84T.
    PhylomeDBi Q9Y5Q5.
    TreeFami TF351678.

    Miscellaneous databases

    ChiTaRSi CORIN. human.
    GeneWikii CORIN.
    GenomeRNAii 10699.
    NextBioi 40661.
    PROi Q9Y5Q5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y5Q5.
    Bgeei Q9Y5Q5.
    CleanExi HS_CORIN.
    Genevestigatori Q9Y5Q5.

    Family and domain databases

    Gene3Di 1.10.2000.10. 2 hits.
    4.10.400.10. 6 hits.
    InterProi IPR020067. Frizzled_dom.
    IPR023415. LDLR_class-A_CS.
    IPR002172. LDrepeatLR_classA_rpt.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR017052. Peptidase_S1A_corin.
    IPR017448. SRCR-like_dom.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF01392. Fz. 2 hits.
    PF00057. Ldl_recept_a. 6 hits.
    PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036376. Corin. 1 hit.
    PRINTSi PR00261. LDLRECEPTOR.
    SMARTi SM00063. FRI. 2 hits.
    SM00192. LDLa. 7 hits.
    SM00202. SR. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF56487. SSF56487. 1 hit.
    SSF57424. SSF57424. 7 hits.
    SSF63501. SSF63501. 2 hits.
    PROSITEi PS50038. FZ. 2 hits.
    PS01209. LDLRA_1. 6 hits.
    PS50068. LDLRA_2. 7 hits.
    PS00420. SRCR_1. 1 hit.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Corin, a mosaic transmembrane serine protease encoded by a novel cDNA from human heart."
      Yan W., Sheng N., Seto M., Morser J., Wu Q.
      J. Biol. Chem. 274:14926-14935(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANTS TYR-13 AND ARG-525.
      Tissue: Heart.
    2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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] (ISOFORM 1), VARIANTS TYR-13 AND ARG-525.
    4. "Localization of the mosaic transmembrane serine protease corin to heart myocytes."
      Hooper J.D., Scarman A.L., Clarke B.E., Normyle J.F., Antalis T.M.
      Eur. J. Biochem. 267:6931-6937(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 734-1040.
      Tissue: Heart.
    5. "Corin, a transmembrane cardiac serine protease, acts as a pro-atrial natriuretic peptide-converting enzyme."
      Yan W., Wu F., Morser J., Wu Q.
      Proc. Natl. Acad. Sci. U.S.A. 97:8525-8529(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF SER-985.
    6. "Functional analysis of the transmembrane domain and activation cleavage of human corin: design and characterization of a soluble corin."
      Knappe S., Wu F., Masikat M.R., Morser J., Wu Q.
      J. Biol. Chem. 278:52363-52370(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVATION, MUTAGENESIS OF ARG-801 AND SER-985, BIOPHYSICOCHEMICAL PROPERTIES.
    7. "Role of glycosylation in corin zymogen activation."
      Liao X., Wang W., Chen S., Wu Q.
      J. Biol. Chem. 282:27728-27735(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, GLYCOSYLATION, DISULFIDE BONDS.
    8. "Enzyme-linked immunoabsorbent assay for detection of human serine protease corin in blood."
      Peleg A., Jaffe A.S., Hasin Y.
      Clin. Chim. Acta 409:85-89(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    9. "Ectodomain shedding and autocleavage of the cardiac membrane protease corin."
      Jiang J., Wu S., Wang W., Chen S., Peng J., Zhang X., Wu Q.
      J. Biol. Chem. 286:10066-10072(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, MUTAGENESIS OF ARG-134; ARG-164; ARG-180; ARG-213; ARG-239; ARG-244; ARG-427; ARG-801 AND SER-985.
    10. "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), FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF ASP-26 AND MET-30.
    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, INVOLVEMENT IN PEE5, TISSUE SPECIFICITY, VARIANTS PEE5 GLU-317 AND GLY-472.
    12. "An integrated genetic and functional analysis of the role of type II transmembrane serine proteases (TMPRSSs) in hearing loss."
      Guipponi M., Toh M.-Y., Tan J., Park D., Hanson K., Ballana E., Kwong D., Cannon P.Z.F., Wu Q., Gout A., Delorenzi M., Speed T.P., Smith R.J.H., Dahl H.-H.M., Petersen M., Teasdale R.D., Estivill X., Park W.J., Scott H.S.
      Hum. Mutat. 29:130-141(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ARG-525.

    Entry informationi

    Entry nameiCORIN_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y5Q5
    Secondary accession number(s): B0ZBE3
    , Q2TBD2, Q4W5E5, Q4W5G6, Q9UHY2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 137 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Initially named CORIN due to its abundant expression in the heart.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3