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Atrial natriuretic peptide-converting enzyme (EC 3.4.21.-) (Corin) (Pro-ANP-converting enzyme) [Cleaved into: Atrial natriuretic peptide-converting enzyme, N-terminal propeptide; Atrial natriuretic peptide-converting enzyme, activated protease fragment; Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment]

 CORIN_RAT               Reviewed;        1111 AA.
Q80YN4; D3ZN44; F1LS60;
02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
13-JUN-2012, sequence version 2.
23-MAY-2018, entry version 115.
RecName: Full=Atrial natriuretic peptide-converting enzyme;
EC=3.4.21.-;
AltName: Full=Corin;
AltName: Full=Pro-ANP-converting enzyme;
Contains:
RecName: Full=Atrial natriuretic peptide-converting enzyme, N-terminal propeptide;
Contains:
RecName: Full=Atrial natriuretic peptide-converting enzyme, activated protease fragment;
Contains:
RecName: Full=Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment;
Name=Corin;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
STRAIN=Sprague-Dawley;
PubMed=15155264; DOI=10.1152/ajpheart.00947.2003;
Langenickel T.H., Pagel I., Buttgereit J., Tenner K., Lindner M.,
Dietz R., Willenbrock R., Bader M.;
"Rat corin gene: molecular cloning and reduced expression in
experimental heart failure.";
Am. J. Physiol. 287:H1516-H1521(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[3]
FUNCTION, ACTIVATION, PROTEOLYTIC PROCESSING, MUTAGENESIS OF ARG-866;
ASN-968 AND ASN-1087, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
PubMed=17660514; DOI=10.1074/jbc.M703687200;
Liao X., Wang W., Chen S., Wu Q.;
"Role of glycosylation in corin zymogen activation.";
J. Biol. Chem. 282:27728-27735(2007).
[4]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20613715; DOI=10.1038/ki.2010.197;
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.;
"Decreased renal corin expression contributes to sodium retention in
proteinuric kidney diseases.";
Kidney Int. 78:650-659(2010).
-!- 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.
{ECO:0000269|PubMed:17660514, ECO:0000269|PubMed:20613715}.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
protein. Cytoplasmic vesicle.
-!- SUBCELLULAR LOCATION: Atrial natriuretic peptide-converting
enzyme, 180 kDa soluble fragment: Secreted {ECO:0000250}.
Note=Soluble form produced following cleavage by ADAM10.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Specifically expressed in heart. Also detected
in kidney, aorta, brain and testis. In kidney, present in
epithelial cells, with segmental expression in the proximal
tubule, thick ascending limb, connecting tubule, and throughout
the collecting duct (at protein level).
{ECO:0000269|PubMed:15155264}.
-!- INDUCTION: Down-regulated upon experimental heart failure.
{ECO:0000269|PubMed:15155264}.
-!- PTM: N-glycosylated; required for processing and activation.
{ECO:0000269|PubMed:17660514}.
-!- PTM: 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 (Probable). {ECO:0000305|PubMed:17660514}.
-!- PTM: 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 (Probable).
{ECO:0000305}.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-----------------------------------------------------------------------
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EMBL; AY251285; AAO86772.1; -; mRNA.
EMBL; AC121481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_872279.1; NM_182473.1.
UniGene; Rn.211679; -.
SMR; Q80YN4; -.
STRING; 10116.ENSRNOP00000061602; -.
MEROPS; S01.019; -.
PaxDb; Q80YN4; -.
PRIDE; Q80YN4; -.
GeneID; 289596; -.
KEGG; rno:289596; -.
UCSC; RGD:727887; rat.
CTD; 10699; -.
RGD; 727887; Corin.
eggNOG; KOG3577; Eukaryota.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
HOGENOM; HOG000060148; -.
HOVERGEN; HBG051079; -.
InParanoid; Q80YN4; -.
KO; K09614; -.
PRO; PR:Q80YN4; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0007565; P:female pregnancy; ISS:UniProtKB.
GO; GO:0016486; P:peptide hormone processing; ISS:UniProtKB.
GO; GO:0008217; P:regulation of blood pressure; IMP:UniProtKB.
GO; GO:0035813; P:regulation of renal sodium excretion; IMP:UniProtKB.
GO; GO:0003050; P:regulation of systemic arterial blood pressure by atrial natriuretic peptide; ISS:UniProtKB.
CDD; cd00112; LDLa; 7.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 1.10.2000.10; -; 2.
InterPro; IPR017052; Corin.
InterPro; IPR020067; Frizzled_dom.
InterPro; IPR036790; Frizzled_dom_sf.
InterPro; IPR036055; LDL_receptor-like_sf.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001190; SRCR.
InterPro; IPR017448; SRCR-like_dom.
InterPro; IPR036772; SRCR-like_dom_sf.
InterPro; IPR001254; Trypsin_dom.
Pfam; PF01392; Fz; 2.
Pfam; PF00057; Ldl_recept_a; 6.
Pfam; PF15494; SRCR_2; 1.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF036376; Corin; 1.
PRINTS; PR00261; LDLRECEPTOR.
SMART; SM00063; FRI; 2.
SMART; SM00192; LDLa; 7.
SMART; SM00202; SR; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF56487; SSF56487; 1.
SUPFAM; SSF57424; SSF57424; 7.
SUPFAM; SSF63501; SSF63501; 2.
PROSITE; PS50038; FZ; 2.
PROSITE; PS01209; LDLRA_1; 6.
PROSITE; PS50068; LDLRA_2; 7.
PROSITE; PS00420; SRCR_1; 1.
PROSITE; PS50287; SRCR_2; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytoplasmic vesicle; Disulfide bond;
Glycoprotein; Hydrolase; Membrane; Protease; Reference proteome;
Repeat; Secreted; Serine protease; Signal-anchor; Transmembrane;
Transmembrane helix; Zymogen.
CHAIN 1 1111 Atrial natriuretic peptide-converting
enzyme.
/FTId=PRO_0000391762.
CHAIN 1 866 Atrial natriuretic peptide-converting
enzyme, N-terminal propeptide.
{ECO:0000305}.
/FTId=PRO_0000391763.
CHAIN ? 866 Atrial natriuretic peptide-converting
enzyme, 180 kDa soluble fragment.
{ECO:0000250}.
/FTId=PRO_0000417988.
CHAIN 867 1111 Atrial natriuretic peptide-converting
enzyme, activated protease fragment.
{ECO:0000305}.
/FTId=PRO_0000391764.
TOPO_DOM 1 112 Cytoplasmic. {ECO:0000255}.
TRANSMEM 113 133 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 134 1111 Extracellular. {ECO:0000255}.
DOMAIN 199 325 FZ 1. {ECO:0000255|PROSITE-
ProRule:PRU00090}.
DOMAIN 334 371 LDL-receptor class A 1.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 371 407 LDL-receptor class A 2.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 407 444 LDL-receptor class A 3.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 444 481 LDL-receptor class A 4.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 516 639 FZ 2. {ECO:0000255|PROSITE-
ProRule:PRU00090}.
DOMAIN 645 681 LDL-receptor class A 5.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 681 719 LDL-receptor class A 6.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 720 756 LDL-receptor class A 7.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 756 851 SRCR. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 867 1100 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
MOTIF 93 96 DDNN motif.
ACT_SITE 908 908 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
ACT_SITE 957 957 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
ACT_SITE 1050 1050 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
SITE 866 867 Cleavage. {ECO:0000305}.
CARBOHYD 147 147 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 409 409 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 535 535 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 763 763 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 204 264 {ECO:0000250}.
DISULFID 212 257 {ECO:0000250}.
DISULFID 248 288 {ECO:0000250}.
DISULFID 277 322 {ECO:0000250}.
DISULFID 281 305 {ECO:0000250}.
DISULFID 335 348 {ECO:0000250}.
DISULFID 343 361 {ECO:0000250}.
DISULFID 355 370 {ECO:0000250}.
DISULFID 372 384 {ECO:0000250}.
DISULFID 379 397 {ECO:0000250}.
DISULFID 391 406 {ECO:0000250}.
DISULFID 408 421 {ECO:0000250}.
DISULFID 416 434 {ECO:0000250}.
DISULFID 428 443 {ECO:0000250}.
DISULFID 445 458 {ECO:0000250}.
DISULFID 453 471 {ECO:0000250}.
DISULFID 465 480 {ECO:0000250}.
DISULFID 521 584 {ECO:0000250}.
DISULFID 529 577 {ECO:0000250}.
DISULFID 568 606 {ECO:0000250}.
DISULFID 595 636 {ECO:0000250}.
DISULFID 599 623 {ECO:0000250}.
DISULFID 646 658 {ECO:0000250}.
DISULFID 653 671 {ECO:0000250}.
DISULFID 665 680 {ECO:0000250}.
DISULFID 682 696 {ECO:0000250}.
DISULFID 690 709 {ECO:0000250}.
DISULFID 703 718 {ECO:0000250}.
DISULFID 721 733 {ECO:0000250}.
DISULFID 728 746 {ECO:0000250}.
DISULFID 740 755 {ECO:0000250}.
DISULFID 855 977 Interchain (between N-terminal propeptide
and activated protease fragment chains).
{ECO:0000255|PROSITE-ProRule:PRU00090,
ECO:0000255|PROSITE-ProRule:PRU00124,
ECO:0000255|PROSITE-ProRule:PRU00196,
ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 893 909 {ECO:0000250}.
DISULFID 991 1056 {ECO:0000250}.
DISULFID 1020 1035 {ECO:0000250}.
MUTAGEN 866 866 R->A: Impairs proteolytic processing and
activation.
{ECO:0000269|PubMed:17660514}.
MUTAGEN 968 968 N->S: Prevents proteolytic processing and
activation; when associated with S-1087.
{ECO:0000269|PubMed:17660514}.
MUTAGEN 1087 1087 N->S: Prevents proteolytic processing and
activation; when associated with S-968.
{ECO:0000269|PubMed:17660514}.
CONFLICT 178 178 P -> S (in Ref. 1; AAO86772).
{ECO:0000305}.
CONFLICT 320 320 R -> T (in Ref. 1; AAO86772).
{ECO:0000305}.
CONFLICT 1048 1048 I -> G (in Ref. 1; AAO86772).
{ECO:0000305}.
SEQUENCE 1111 AA; 122757 MW; 44A738ACA6E0AC16 CRC64;
MGRVSFNVRV SSVRRARCSC PGRCYLSCRV PPTTALHALN GFGRAGVLGE TAGGTVGLGP
SGTRGFLSGS KFQASGSLKD CFGAPPAPDV LRADSSVGEG CPQKLVTANL LRFLLLVLIP
CICALIVLLA ILLSFVGTLK KVYFKSNDSE PLVTDGEVRV PGVIHVNRYE NTGAPSMPPS
QSIPAWTPRA PSLEDQSHGN TSTCVNITHR QCQILPYHST LAPLLPIVKN MDTEKFLKFF
TYLHRLGCYQ HILLFGCSLA FPKCIVDGDD RHGLLPCRSF CEAAKEGCES VLGMVNSSWP
DSLRCSQFRY HTENNSDASR ICFSLQQEHG KQSLCGGGES FLCTSGLCIS KKLQCNGYND
CDDWSDEAHC NCSEDLFHCG TGKCLHHSLV CDGYDDCGDL SDEQNCDCNL TKEHRCGDGR
CIAAEWVCDG DHDCVDKSDE VNCSCPSQGL VECRSGQCIP STFQCDGDED CKDGSDEENC
SDRPTPCPGG DRGCLDSSCV ESCAGSSLCD SDSSLSNCSH CEPITLELCM NLPYNLTHYP
NYLGHRTQKE ASISWESALF PALVQTNCYK YLMFFACTIL VPKCDVNTGQ RVPPCRLLCE
HSKERCESVL GIVGLQWPED TDCSQFPEQS SDNQTCLLPN EDVEECSPSH FKCRSGRCVL
GSRRCDGQAD CDDDSDEENC GCKERDLWEC PLNKQCLKHT LICDGFPDCS DSMDEKNCSF
CQDDELECAN HECVPRDLWC DGWTDCSDSS DEWGCVTLSK NGNSSSFLTV HRSARDHHVC
ADGWQETLSQ LACRQMGLGE PSVTELVQGQ EGQQWLRLHS SWENLNGSTL QELLVHRRSC
PSGSEISLLC TKQDCGRRPA ARMNKRILGG RTSRPGRWPW QCSLQSEPSG HICGCVLIAK
KWVLTVAHCF EGREDADVWK VVFGINNLDH PSGFMQTRFV KTILLHPRYS RAVVDYDISV
VELSDDINET SYVRPVCLPS PREFLEPDTY CYITGWGHMG NKMPFKLQEG EVRIIPLEQC
QSYFDMKTIT NRMICAGYES GTVDSCMIDS GGPLVCERPG GQWTLFGLTS WGSVCFSKVL
GPGVYSNVSY FVDWIERQIY IQTFLQKKSQ G


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