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Q9Y5Q5 (CORIN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length1042 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.10 Ref.11

Isoform 2:has weaker endopeptidase activity compared to isoform 1. Ref.5 Ref.10 Ref.11

Enzyme regulation

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

Subcellular location

Cell membrane; Single-pass type II membrane protein. Note: May easily detached from the endothelial cell membrane. Ref.8 Ref.9 Ref.10

Isoform 2: Cell membrane; Single-pass type II membrane protein. Note: Less efficiently targeted to the cell membrane compared to isoform 1. Ref.8 Ref.9 Ref.10

Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment: Secreted. Note: Soluble form produced following cleavage by ADAM10. Ref.8 Ref.9 Ref.10

Atrial natriuretic peptide-converting enzyme, 160 kDa soluble fragment: Secreted. Note: Soluble form produced following autocatalytic cleavage.

Atrial natriuretic peptide-converting enzyme, 100 kDa soluble fragment: Secreted. Note: Soluble form produced following autocatalytic cleavage.

Tissue specificity

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). Ref.1 Ref.8 Ref.11

Domain

The DDNN motif is required for targeting to the cell membrane and enzyme activation (Ref.10).

Post-translational modification

N-glycosylated; required for processing and activation. Ref.7 Ref.10

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. Ref.7 Ref.9

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).

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11

Miscellaneous

Initially named CORIN due to its abundant expression in the heart (Ref.1).

Sequence similarities

Belongs to the peptidase S1 family.

Contains 2 FZ (frizzled) domains.

Contains 7 LDL-receptor class A domains.

Contains 1 peptidase S1 domain.

Contains 1 SRCR domain.

Biophysicochemical properties

Kinetic parameters:

KM=1.28 mM for pyroGlu-Phe-Lys-pNA.HCl Ref.6

KM=3.52 mM for pyroGlu-Pro-Arg-pNA.HCl

KM=2.95 mM for H-D-Pro-Phe-Arg-pNA.2HCl

KM=1.92 mM for Bz-Ile-Glu-(gamma-OR)-Gly-Arg-pNA.HCl

KM=16 mM for pyroGlu-Gly-Arg-pNA.HCl

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal-anchor
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
Protease
Serine protease
   PTMAutocatalytic cleavage
Disulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfemale pregnancy

Inferred from mutant phenotype Ref.11. Source: UniProtKB

peptide hormone processing

Inferred from direct assay Ref.5Ref.10. Source: UniProtKB

proteolysis

Inferred from direct assay Ref.10. Source: GOC

regulation of blood pressure

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of renal sodium excretion

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of systemic arterial blood pressure by atrial natriuretic peptide

Inferred from mutant phenotype Ref.11. Source: UniProtKB

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

integral component of plasma membrane

Inferred from direct assay Ref.10. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionscavenger receptor activity

Inferred from electronic annotation. Source: InterPro

serine-type endopeptidase activity

Inferred from direct assay Ref.5Ref.10. Source: UniProtKB

serine-type exopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y5Q5-1)

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.
Isoform 2 (identifier: Q9Y5Q5-2)

Also known as: E1a; hE1a;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10421042Atrial natriuretic peptide-converting enzyme
PRO_0000088673
Chain1 – 801801Atrial natriuretic peptide-converting enzyme, N-terminal propeptide Probable
PRO_0000391765
Chain165 – 801637Atrial natriuretic peptide-converting enzyme, 160 kDa soluble fragment Probable
PRO_0000417984
Chain428 – 801374Atrial natriuretic peptide-converting enzyme, 100 kDa soluble fragment Probable
PRO_0000417985
Chain? – 801Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment ProbablePRO_0000417986
Chain802 – 1042241Atrial natriuretic peptide-converting enzyme, activated protease fragment Probable
PRO_0000391766

Regions

Topological domain1 – 4545Cytoplasmic Potential
Transmembrane46 – 6621Helical; Signal-anchor for type II membrane protein; Potential
Topological domain67 – 1042976Extracellular Potential
Domain134 – 259126FZ 1
Domain268 – 30437LDL-receptor class A 1
Domain305 – 34036LDL-receptor class A 2
Domain341 – 37737LDL-receptor class A 3
Domain378 – 41538LDL-receptor class A 4
Domain450 – 573124FZ 2
Domain579 – 61436LDL-receptor class A 5
Domain615 – 65339LDL-receptor class A 6
Domain654 – 68936LDL-receptor class A 7
Domain690 – 801112SRCR
Domain802 – 1035234Peptidase S1
Motif26 – 294DDNN motif

Sites

Active site8431Charge relay system By similarity
Active site8921Charge relay system By similarity
Active site9851Charge relay system
Site164 – 1652Cleavage; by autolysis
Site427 – 4282Cleavage; by autolysis
Site801 – 8022Cleavage Probable

Amino acid modifications

Glycosylation801N-linked (GlcNAc...) Potential
Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation1351N-linked (GlcNAc...) Potential
Glycosylation1411N-linked (GlcNAc...) Potential
Glycosylation2311N-linked (GlcNAc...) Potential
Glycosylation2451N-linked (GlcNAc...) Potential
Glycosylation2511N-linked (GlcNAc...) Potential
Glycosylation3051N-linked (GlcNAc...) Potential
Glycosylation3201N-linked (GlcNAc...) Potential
Glycosylation3761N-linked (GlcNAc...) Potential
Glycosylation4131N-linked (GlcNAc...) Potential
Glycosylation4461N-linked (GlcNAc...) Potential
Glycosylation4511N-linked (GlcNAc...) Potential
Glycosylation4691N-linked (GlcNAc...) Potential
Glycosylation5671N-linked (GlcNAc...) Potential
Glycosylation6511N-linked (GlcNAc...) Potential
Glycosylation6971N-linked (GlcNAc...) Potential
Glycosylation7611N-linked (GlcNAc...) Potential
Glycosylation10221N-linked (GlcNAc...) Potential
Disulfide bond139 ↔ 199 By similarity
Disulfide bond147 ↔ 192 By similarity
Disulfide bond183 ↔ 223 By similarity
Disulfide bond212 ↔ 256 By similarity
Disulfide bond216 ↔ 240 By similarity
Disulfide bond269 ↔ 282 By similarity
Disulfide bond277 ↔ 295 By similarity
Disulfide bond289 ↔ 304 By similarity
Disulfide bond306 ↔ 318 By similarity
Disulfide bond313 ↔ 331 By similarity
Disulfide bond325 ↔ 340 By similarity
Disulfide bond342 ↔ 355 By similarity
Disulfide bond350 ↔ 368 By similarity
Disulfide bond362 ↔ 377 By similarity
Disulfide bond379 ↔ 392 By similarity
Disulfide bond387 ↔ 405 By similarity
Disulfide bond399 ↔ 414 By similarity
Disulfide bond455 ↔ 518 By similarity
Disulfide bond463 ↔ 511 By similarity
Disulfide bond502 ↔ 540 By similarity
Disulfide bond529 ↔ 570 By similarity
Disulfide bond533 ↔ 557 By similarity
Disulfide bond580 ↔ 592 By similarity
Disulfide bond587 ↔ 605 By similarity
Disulfide bond599 ↔ 614 By similarity
Disulfide bond616 ↔ 630 By similarity
Disulfide bond624 ↔ 643 By similarity
Disulfide bond637 ↔ 652 By similarity
Disulfide bond655 ↔ 667 By similarity
Disulfide bond662 ↔ 680 By similarity
Disulfide bond674 ↔ 689 By similarity
Disulfide bond790 ↔ 912Interchain (between N-terminal propeptide and activated protease fragment chains) Probable
Disulfide bond828 ↔ 844 By similarity
Disulfide bond926 ↔ 991 By similarity
Disulfide bond955 ↔ 970 By similarity
Disulfide bond981 ↔ 1010 By similarity

Natural variations

Alternative sequence1 – 2929Missing in isoform 2.
VSP_043952
Natural variant131C → Y. Ref.1 Ref.3
Corresponds to variant rs2289433 [ dbSNP | Ensembl ].
VAR_038000
Natural variant3171K → E in PEE5. Ref.11
VAR_067795
Natural variant4441D → G.
Corresponds to variant rs13105608 [ dbSNP | Ensembl ].
VAR_067796
Natural variant4721S → G in PEE5. Ref.11
VAR_067797
Natural variant5251H → R. Ref.1 Ref.3 Ref.12
Corresponds to variant rs11934749 [ dbSNP | Ensembl ].
VAR_038001

Experimental info

Mutagenesis261D → A: Impairs cell membrane targeting; when associated with A-30. Ref.10
Mutagenesis301M → A: Impairs cell membrane targeting; when associated with A-26. Ref.10
Mutagenesis1341R → A: Does not affect autocatalytic cleavage. Ref.9
Mutagenesis1641R → A: Affects autocatalytic cleavage and production of Atrial natriuretic peptide-converting enzyme, 160 kDa soluble fragment. Ref.9
Mutagenesis1801R → A: Does not affect autocatalytic cleavage. Ref.9
Mutagenesis2131R → A: Does not affect autocatalytic cleavage. Ref.9
Mutagenesis2391R → A: Does not affect autocatalytic cleavage. Ref.9
Mutagenesis2441R → A: Does not affect autocatalytic cleavage. Ref.9
Mutagenesis4271R → A: Affects autocatalytic cleavage and production of Atrial natriuretic peptide-converting enzyme, 100 kDa soluble fragment. Ref.9
Mutagenesis8011R → A: Loss of activity towards NPPA. Ref.6 Ref.9
Mutagenesis9851S → A: Loss of activity towards NPPA. Ref.5 Ref.6 Ref.9
Sequence conflict8541W → R in AAF21966. Ref.4
Sequence conflict8761K → R in AAF21966. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (E1) (hE1) [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: A3F1CB8EBB676F78

FASTA1,042116,486
        10         20         30         40         50         60 
MKQSPALAPE ERCRRAGSPK PVLRADDNNM GNGCSQKLAT ANLLRFLLLV LIPCICALVL 

        70         80         90        100        110        120 
LLVILLSYVG TLQKVYFKSN GSEPLVTDGE IQGSDVILTN TIYNQSTVVS TAHPDQHVPA 

       130        140        150        160        170        180 
WTTDASLPGD QSHRNTSACM NITHSQCQML PYHATLTPLL SVVRNMEMEK FLKFFTYLHR 

       190        200        210        220        230        240 
LSCYQHIMLF GCTLAFPECI IDGDDSHGLL PCRSFCEAAK EGCESVLGMV NYSWPDFLRC 

       250        260        270        280        290        300 
SQFRNQTESS NVSRICFSPQ QENGKQLLCG RGENFLCASG ICIPGKLQCN GYNDCDDWSD 

       310        320        330        340        350        360 
EAHCNCSENL FHCHTGKCLN YSLVCDGYDD CGDLSDEQNC DCNPTTEHRC GDGRCIAMEW 

       370        380        390        400        410        420 
VCDGDHDCVD KSDEVNCSCH SQGLVECRNG QCIPSTFQCD GDEDCKDGSD EENCSVIQTS 

       430        440        450        460        470        480 
CQEGDQRCLY NPCLDSCGGS SLCDPNNSLN NCSQCEPITL ELCMNLPYNS TSYPNYFGHR 

       490        500        510        520        530        540 
TQKEASISWE SSLFPALVQT NCYKYLMFFS CTILVPKCDV NTGEHIPPCR ALCEHSKERC 

       550        560        570        580        590        600 
ESVLGIVGLQ WPEDTDCSQF PEENSDNQTC LMPDEYVEEC SPSHFKCRSG QCVLASRRCD 

       610        620        630        640        650        660 
GQADCDDDSD EENCGCKERD LWECPSNKQC LKHTVICDGF PDCPDYMDEK NCSFCQDDEL 

       670        680        690        700        710        720 
ECANHACVSR DLWCDGEADC SDSSDEWDCV TLSINVNSSS FLMVHRAATE HHVCADGWQE 

       730        740        750        760        770        780 
ILSQLACKQM GLGEPSVTKL IQEQEKEPRW LTLHSNWESL NGTTLHELLV NGQSCESRSK 

       790        800        810        820        830        840 
ISLLCTKQDC GRRPAARMNK RILGGRTSRP GRWPWQCSLQ SEPSGHICGC VLIAKKWVLT 

       850        860        870        880        890        900 
VAHCFEGREN AAVWKVVLGI NNLDHPSVFM QTRFVKTIIL HPRYSRAVVD YDISIVELSE 

       910        920        930        940        950        960 
DISETGYVRP VCLPNPEQWL EPDTYCYITG WGHMGNKMPF KLQEGEVRII SLEHCQSYFD 

       970        980        990       1000       1010       1020 
MKTITTRMIC AGYESGTVDS CMGDSGGPLV CEKPGGRWTL FGLTSWGSVC FSKVLGPGVY 

      1030       1040 
SNVSYFVEWI KRQIYIQTFL LN 

« Hide

Isoform 2 (E1a) (hE1a) [UniParc].

Checksum: F4084E8B3AFFFDB8
Show »

FASTA1,013113,297

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS3477.1. [Q9Y5Q5-1]
RefSeqNP_001265514.1. NM_001278585.1.
NP_006578.2. NM_006587.3. [Q9Y5Q5-1]
UniGeneHs.518618.
Hs.604887.

3D structure databases

ProteinModelPortalQ9Y5Q5.
SMRQ9Y5Q5. Positions 138-441, 455-701, 788-1034.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115937. 1 interaction.
STRING9606.ENSP00000273857.

Protein family/group databases

MEROPSS01.019.

PTM databases

PhosphoSiteQ9Y5Q5.

Polymorphism databases

DMDM317373348.

Proteomic databases

PaxDbQ9Y5Q5.
PRIDEQ9Y5Q5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000273857; ENSP00000273857; ENSG00000145244. [Q9Y5Q5-1]
GeneID10699.
KEGGhsa:10699.
UCSCuc003gxm.3. human. [Q9Y5Q5-1]

Organism-specific databases

CTD10699.
GeneCardsGC04M047596.
H-InvDBHIX0024555.
HGNCHGNC:19012. CORIN.
MIM605236. gene.
614595. phenotype.
neXtProtNX_Q9Y5Q5.
PharmGKBPA134972424.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000060148.
HOVERGENHBG051079.
InParanoidQ9Y5Q5.
KOK09614.
OMAHHVCADG.
OrthoDBEOG75B84T.
PhylomeDBQ9Y5Q5.
TreeFamTF351678.

Gene expression databases

ArrayExpressQ9Y5Q5.
BgeeQ9Y5Q5.
CleanExHS_CORIN.
GenevestigatorQ9Y5Q5.

Family and domain databases

Gene3D1.10.2000.10. 2 hits.
4.10.400.10. 6 hits.
InterProIPR020067. 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]
PfamPF01392. Fz. 2 hits.
PF00057. Ldl_recept_a. 6 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF036376. Corin. 1 hit.
PRINTSPR00261. LDLRECEPTOR.
SMARTSM00063. FRI. 2 hits.
SM00192. LDLa. 7 hits.
SM00202. SR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF56487. SSF56487. 1 hit.
SSF57424. SSF57424. 7 hits.
SSF63501. SSF63501. 2 hits.
PROSITEPS50038. 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]
ProtoNetSearch...

Other

ChiTaRSCORIN. human.
GeneWikiCORIN.
GenomeRNAi10699.
NextBio40661.
PROQ9Y5Q5.
SOURCESearch...

Entry information

Entry nameCORIN_HUMAN
AccessionPrimary (citable) accession number: Q9Y5Q5
Secondary accession number(s): B0ZBE3 expand/collapse secondary AC list , Q2TBD2, Q4W5E5, Q4W5G6, Q9UHY2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM