ID A0A1V4JFZ2_PATFA Unreviewed; 1067 AA.
AC A0A1V4JFZ2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Atrial natriuretic peptide-converting enzyme {ECO:0000313|EMBL:OPJ71086.1};
GN Name=CORIN {ECO:0000313|EMBL:OPJ71086.1};
GN ORFNames=AV530_017382 {ECO:0000313|EMBL:OPJ71086.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ71086.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ71086.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ71086.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ71086.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ71086.1}.
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DR EMBL; LSYS01007721; OPJ71086.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4JFZ2; -.
DR STRING; 372326.A0A1V4JFZ2; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0016486; P:peptide hormone processing; IEA:InterPro.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:InterPro.
DR CDD; cd00112; LDLa; 6.
DR CDD; cd00190; Tryp_SPc; 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; 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; IPR017448; SRCR-like_dom.
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:SF9; ATRIAL NATRIURETIC PEPTIDE-CONVERTING ENZYME ISOFORM X1; 1.
DR Pfam; PF01392; Fz; 1.
DR Pfam; PF00057; Ldl_recept_a; 6.
DR Pfam; PF15494; SRCR_2; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF036376; Corin; 3.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00192; LDLa; 7.
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 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 186..330
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 473..596
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 827..1060
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 78..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 868
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036376-50"
FT ACT_SITE 917
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036376-50"
FT ACT_SITE 1010
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036376-50"
FT DISULFID 191..252
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 199..245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 303..321
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 315..330
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 332..344
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 339..357
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 351..366
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 376..394
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 388..403
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 413..431
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 425..440
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 525..563
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 552..593
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 556..580
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 603..615
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 610..628
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 622..637
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 660..675
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 678..690
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 685..703
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 697..712
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1067 AA; 119246 MW; AF35DE1FB75BFE79 CRC64;
MGDGCSQKLA SAKFLRLLLL ILIPCICALI LLLVILLTFV GVLEKACFYS NGSEVLTVNG
DIETSDVLLP NMVENSSKTD PTMDLSTQPS SWTTTPSSHI DQMNKNSSIF RNTFQQESFA
LTTQASPHPT YDAALAEESE DDTQIFSTAE EVTLWSTHAS FSNTDRIATL PVLSPTHPSV
SQNMDQRKSA CINITNSQCQ MLPYNYTTVT SVLSIVKNVE MEKFLKFFSY LNRLSCYQHI
MLFGCSLALP ECISDGDDRL YGKIYVSTLL TMEEQRKRFC AAGYTLDVFD CYALCGGEES
FLCASGICIP GKLQCNGYND CDDWSDEVHC NCSDDVFRCN TGKCLNYTFV CDGYDDCGDL
SDEQNCDCNP ATHHQCGDGR CVTADWVCDG DHDCIDKSDE INCSCHSQGL VECRNGQCIP
SAFQCDGDND CKDGSDEENC SESQTLCQGG DQRCDSCPDP CGTSLCEMRN SQTNCSQCEP
ITLELCMNLP YNYTYYPNYL GHRTQKEASV SWESSLFPAL VQTNCYKYLM FFACTILVPK
CDPHTNQRIP PCRTLCVQSK ERCESVLGIV GLQWPEDTDC SQFPDEKSDN QTCLTPDEDV
EECSPSHFKC RSGRCVLASR RCDGQADCED DSDEDSCGCG ERGLWECPFK KLCIKHTMIC
DGFPDCPDMM DEKNCSLCEE SEVECANHQC VPRELWCDGQ PDCSDSSDEW DCVTLSKTKN
SLMFLTVHRS AADNHVCADD WQESLSQLAC NQMGLGGPSK TDIVIDSEET QHQKWLNLHS
DWKNKNASTL HALLVSGQLC RSRSKVALFC TKEDCGRRPA ARMNKRILGG RTSRPGRWPW
QCSLQSEPSG HICGCVLIAK RWVLTVAHCF EGRENAAVWK VVFGISNLDQ PSGFMQTRLV
KTIILHPRYN RAVVDYDISI VELDEDINET SYVRPVCLPS RDQLVRPDTY CYITGWGHMG
NKMPFKLQEG EVRIISLEQC QSYFDMKPIT SRMLCAGYES GTVDSCMGDS GGPLVCEQPA
GRWTLFGLTS WGSVCFSKVL GPGVYSNVSH FIEWIERQIY IHTFLLN
//
