ID A0A287AGB0_PIG Unreviewed; 1113 AA.
AC A0A287AGB0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 18-JUN-2025, entry version 44.
DE RecName: Full=Atrial natriuretic peptide-converting enzyme {ECO:0000256|ARBA:ARBA00068301};
DE AltName: Full=Corin {ECO:0000256|ARBA:ARBA00077383};
DE AltName: Full=Pro-ANP-converting enzyme {ECO:0000256|ARBA:ARBA00082201};
GN Name=CORIN {ECO:0000313|Ensembl:ENSSSCP00000042872.2,
GN ECO:0000313|VGNC:VGNC:86911};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000042872.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000042872.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000042872.2};
RX PubMed=32543654;
RA Warr A., Affara N., Aken B., Beiki H., Bickhart D.M., Billis K., Chow W.,
RA Eory L., Finlayson H.A., Flicek P., Giron C.G., Griffin D.K., Hall R.,
RA Hannum G., Hourlier T., Howe K., Hume D.A., Izuogu O., Kim K., Koren S.,
RA Liu H., Manchanda N., Martin F.J., Nonneman D.J., O'Connor R.E.,
RA Phillippy A.M., Rohrer G.A., Rosen B.D., Rund L.A., Sargent C.A.,
RA Schook L.B., Schroeder S.G., Schwartz A.S., Skinner B.M., Talbot R.,
RA Tseng E., Tuggle C.K., Watson M., Smith T.P.L., Archibald A.L.;
RT "An improved pig reference genome sequence to enable pig genetics and
RT genomics research.";
RL Gigascience 9:0-0(2020).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000042872.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the LDLR family.
CC {ECO:0000256|ARBA:ARBA00009939}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR RefSeq; XP_020956230.1; XM_021100571.1.
DR AlphaFoldDB; A0A287AGB0; -.
DR SMR; A0A287AGB0; -.
DR FunCoup; A0A287AGB0; 296.
DR STRING; 9823.ENSSSCP00000042872; -.
DR GlyGen; A0A287AGB0; 1 site.
DR PaxDb; 9823-ENSSSCP00000009394; -.
DR Ensembl; ENSSSCT00000048072.2; ENSSSCP00000042872.2; ENSSSCG00000008813.5.
DR GeneID; 100738048; -.
DR VGNC; VGNC:86911; CORIN.
DR GeneTree; ENSGT00940000157103; -.
DR InParanoid; A0A287AGB0; -.
DR OrthoDB; 7863416at2759; -.
DR Reactome; R-SSC-5578768; Physiological factors.
DR Proteomes; UP000008227; Chromosome 8.
DR Bgee; ENSSSCG00000008813; Expressed in heart left ventricle and 22 other cell types or tissues.
DR ExpressionAtlas; A0A287AGB0; baseline and differential.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:Ensembl.
DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR GO; GO:0016486; P:peptide hormone processing; IEA:Ensembl.
DR GO; GO:0035813; P:regulation of renal sodium excretion; IEA:Ensembl.
DR GO; GO:0003050; P:regulation of systemic arterial blood pressure by atrial natriuretic peptide; IEA:Ensembl.
DR CDD; cd07445; CRD_corin_1; 1.
DR CDD; cd07888; CRD_corin_2; 1.
DR CDD; cd00112; LDLa; 7.
DR CDD; cd00190; Tryp_SPc; 1.
DR FunFam; 1.10.2000.10:FF:000013; atrial natriuretic peptide-converting enzyme; 1.
DR FunFam; 2.40.10.10:FF:000015; Atrial natriuretic peptide-converting enzyme; 1.
DR FunFam; 4.10.400.10:FF:000083; Atrial natriuretic peptide-converting enzyme; 1.
DR FunFam; 4.10.400.10:FF:000103; Atrial natriuretic peptide-converting enzyme; 1.
DR FunFam; 1.10.2000.10:FF:000011; Corin, serine peptidase; 1.
DR FunFam; 4.10.400.10:FF:000042; Corin, serine peptidase; 1.
DR FunFam; 4.10.400.10:FF:000054; Corin, serine peptidase; 1.
DR FunFam; 4.10.400.10:FF:000024; Low-density lipoprotein RecePtor related; 1.
DR FunFam; 4.10.400.10:FF:000056; Terribly reduced optic lobes, isoform AM; 1.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 2.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 7.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR017052; Corin.
DR InterPro; IPR041762; Corin_CRD_1.
DR InterPro; IPR041763; Corin_CRD_2.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF11; ATRIAL NATRIURETIC PEPTIDE-CONVERTING ENZYME ISOFORM X1; 1.
DR Pfam; PF01392; Fz; 2.
DR Pfam; PF00057; Ldl_recept_a; 6.
DR Pfam; PF15494; SRCR_2; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF036376; Corin; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00063; FRI; 2.
DR SMART; SM00192; LDLa; 7.
DR SMART; SM00202; SR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 2.
DR SUPFAM; SSF57424; LDL receptor-like module; 7.
DR SUPFAM; SSF56487; SRCR-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50038; FZ; 2.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 7.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT TRANSMEM 117..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 205..330
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 521..644
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 873..1106
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 914
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036376-50"
FT ACT_SITE 963
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036376-50"
FT ACT_SITE 1056
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036376-50"
FT DISULFID 287..311
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 348..366
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 360..375
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 377..389
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 384..402
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 396..411
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 421..439
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 433..448
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 458..476
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 470..485
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 573..611
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 600..641
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 604..628
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 651..663
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 658..676
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 670..685
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 708..723
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 726..738
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 733..751
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 745..760
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1113 AA; 122647 MW; 5F5E1BAD4EB50940 CRC64;
MGRVSFSARV RSVRRPRSPC QGRCHIPCRG VLTVPLPPGA LHASGGLGSA QAPVEAAERA
VGTSLSRVHG SAAPASPAPS IWKDGAASPA PDVLGADASN MGDGCSQKLA TVNILRFLLL
VLIPCICALI VLLVILLSFV GTLKKAYFKS NGSEPLVTDG EVHVSDGILP NTVPNESTGV
SAVRPTPHIP AWTTDAAFPG DRNHRNTSAC VNITHSQCQM LPYNTTLIPL FPLVKSMEIE
KFLKFFTYLH RLGCYQHILL FGCSLAFPKC VGDGDDSHGL LPCRSFCEAA KEGCESVLGM
VNASWPDFLK CSQFRNQSES SNISRICFSP QQEKEKQLLC GGGESFLCAS GICVPRKLQC
NGYNDCDDWS DEAHCNCSEN LFHCHTGKCL NYSLVCDGYD DCGDLSDEQN CDCNPTEEHR
CGDGRCIAVE WVCDGDHDCV DKSDEVNCSC HSQGLVECRN GQCVPSTFWC DGDEDCKDGS
DEESCSDGQT PCQEGDQRCL YSSCLDSCAG GSLCDPGNSP NNCSQCEPIT LELCMNLPYN
YTNYPNYLGH RTQKEASISW ESSLFPALVQ TNCYKYLMFF ACTILVPKCD EITSQRIPPC
RALCEHSKDR CESVLGIVGL QWPEDTDCSQ FPEENSDNQT CLMPDADVEE CSPSHFKCSS
GRCVLASRRC DGQADCDDDS DEENCGCKER DLWECPSNKQ CLKHTVICDG FPDCPDNMDE
KNCSFCQDDE LECANHECVS RDRWCDGEVD CVDSSDEWDC VTLSENVNSS SLLTAHRSAV
EHHVCADGWQ ETLSQLACKQ MGLGEPSVTK LIQQQEQDQQ WLTLHSGWER LNGTTLHKLL
VEGQSCHSRS KISLLCAKQD CGRRPAARMN KRILGGRTSR PGRWPWQCSL QSEPSGHICG
CVLIAKKWVL TVAHCFEGRE NAAVWKVVFG INNLDHPSTF LQTRLVKSII LHPRYSHTVV
DYDISIVELS EDINETSYVR PVCLPSPEQS LEPDTYCYIT GWGHMGNKMP FKLQEGEVRI
ISLEQCQSYF DMKTITTRMI CAGYESGTVD SCMGDSGGPL VCERPGGQWT LFGLTSWGSV
CFSKVLGPGV YSNVTYFVGW IERQIYIHTF LLN
//