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Database: UniProt
Entry: A0A287AGB0_PIG
LinkDB: A0A287AGB0_PIG
Original site: A0A287AGB0_PIG 
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
//
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