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Q9Y5Q5

- CORIN_HUMAN

UniProt

Q9Y5Q5 - CORIN_HUMAN

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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

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
Complete GO annotation...

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-KW
  3. integral component of membrane Source: UniProtKB-KW
  4. integral component of plasma membrane Source: UniProtKB
  5. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

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

BgeeiQ9Y5Q5.
CleanExiHS_CORIN.
ExpressionAtlasiQ9Y5Q5. baseline and differential.
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.
GeneTreeiENSGT00760000119008.
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

        10         20         30         40         50
MKQSPALAPE ERCRRAGSPK PVLRADDNNM GNGCSQKLAT ANLLRFLLLV
60 70 80 90 100
LIPCICALVL LLVILLSYVG TLQKVYFKSN GSEPLVTDGE IQGSDVILTN
110 120 130 140 150
TIYNQSTVVS TAHPDQHVPA WTTDASLPGD QSHRNTSACM NITHSQCQML
160 170 180 190 200
PYHATLTPLL SVVRNMEMEK FLKFFTYLHR LSCYQHIMLF GCTLAFPECI
210 220 230 240 250
IDGDDSHGLL PCRSFCEAAK EGCESVLGMV NYSWPDFLRC SQFRNQTESS
260 270 280 290 300
NVSRICFSPQ QENGKQLLCG RGENFLCASG ICIPGKLQCN GYNDCDDWSD
310 320 330 340 350
EAHCNCSENL FHCHTGKCLN YSLVCDGYDD CGDLSDEQNC DCNPTTEHRC
360 370 380 390 400
GDGRCIAMEW VCDGDHDCVD KSDEVNCSCH SQGLVECRNG QCIPSTFQCD
410 420 430 440 450
GDEDCKDGSD EENCSVIQTS CQEGDQRCLY NPCLDSCGGS SLCDPNNSLN
460 470 480 490 500
NCSQCEPITL ELCMNLPYNS TSYPNYFGHR TQKEASISWE SSLFPALVQT
510 520 530 540 550
NCYKYLMFFS CTILVPKCDV NTGEHIPPCR ALCEHSKERC ESVLGIVGLQ
560 570 580 590 600
WPEDTDCSQF PEENSDNQTC LMPDEYVEEC SPSHFKCRSG QCVLASRRCD
610 620 630 640 650
GQADCDDDSD EENCGCKERD LWECPSNKQC LKHTVICDGF PDCPDYMDEK
660 670 680 690 700
NCSFCQDDEL ECANHACVSR DLWCDGEADC SDSSDEWDCV TLSINVNSSS
710 720 730 740 750
FLMVHRAATE HHVCADGWQE ILSQLACKQM GLGEPSVTKL IQEQEKEPRW
760 770 780 790 800
LTLHSNWESL NGTTLHELLV NGQSCESRSK ISLLCTKQDC GRRPAARMNK
810 820 830 840 850
RILGGRTSRP GRWPWQCSLQ SEPSGHICGC VLIAKKWVLT VAHCFEGREN
860 870 880 890 900
AAVWKVVLGI NNLDHPSVFM QTRFVKTIIL HPRYSRAVVD YDISIVELSE
910 920 930 940 950
DISETGYVRP VCLPNPEQWL EPDTYCYITG WGHMGNKMPF KLQEGEVRII
960 970 980 990 1000
SLEHCQSYFD MKTITTRMIC AGYESGTVDS CMGDSGGPLV CEKPGGRWTL
1010 1020 1030 1040
FGLTSWGSVC FSKVLGPGVY SNVSYFVEWI KRQIYIQTFL LN
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.
GeneTreei ENSGT00760000119008.
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

Bgeei Q9Y5Q5.
CleanExi HS_CORIN.
ExpressionAtlasi Q9Y5Q5. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 138 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