ID R0L4W7_ANAPL Unreviewed; 1021 AA.
AC R0L4W7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Atrial natriuretic peptide-converting enzyme {ECO:0000313|EMBL:EOA95302.1};
DE Flags: Fragment;
GN ORFNames=Anapl_14094 {ECO:0000313|EMBL:EOA95302.1};
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839 {ECO:0000313|EMBL:EOA95302.1, ECO:0000313|Proteomes:UP000296049};
RN [1] {ECO:0000313|Proteomes:UP000296049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23749191; DOI=10.1038/ng.2657;
RA Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., Gan S.,
RA Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., Fairley S.,
RA Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., Lee T.,
RA Kim K.W., Sheng Z., An Y., Searle S., Herrero J., Groenen M.A.,
RA Crooijmans R.P., Faraut T., Cai Q., Webster R.G., Aldridge J.R.,
RA Warren W.C., Bartschat S., Kehr S., Marz M., Stadler P.F., Smith J.,
RA Kraus R.H., Zhao Y., Ren L., Fei J., Morisson M., Kaiser P., Griffin D.K.,
RA Rao M., Pitel F., Wang J., Li N.;
RT "The duck genome and transcriptome provide insight into an avian influenza
RT virus reservoir species.";
RL Nat. Genet. 45:776-783(2013).
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}.
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DR EMBL; KB744333; EOA95302.1; -; Genomic_DNA.
DR AlphaFoldDB; R0L4W7; -.
DR HOGENOM; CLU_010853_0_0_1; -.
DR Proteomes; UP000296049; 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; cd07445; CRD_corin_1; 1.
DR CDD; cd07888; CRD_corin_2; 1.
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; 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; IPR017448; SRCR-like_dom.
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; 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; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 2.
DR SUPFAM; SSF57424; LDL receptor-like module; 7.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000296049};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 113..239
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 427..550
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 781..1014
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 822
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036376-50"
FT ACT_SITE 871
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036376-50"
FT ACT_SITE 964
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036376-50"
FT DISULFID 118..179
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 126..172
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 196..220
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 257..275
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 269..284
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 286..298
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 293..311
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 305..320
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 330..348
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 342..357
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 367..385
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 379..394
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 479..517
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 506..547
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 510..534
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 557..569
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 564..582
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 576..591
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 614..629
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 632..644
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 639..657
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 651..666
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EOA95302.1"
FT NON_TER 1021
FT /evidence="ECO:0000313|EMBL:EOA95302.1"
SQ SEQUENCE 1021 AA; 114087 MW; 020C59227A68DC87 CRC64;
VLGADEDNMG DGCSQKLASA KFLRLLLLIL IPCICALILL LVILLTFVGV LEKTCFYSNG
SEVLTVNGDI ETSDVLLPNM VENSSTTNPT VDLSTWTPAW TTTPLSHIGQ MNKNSSACIN
ITNSQCQMLP YNYTTLTSVL SIVKNIEMEK FLKFFSYLSR LSCYQHIMLF GCSLALPECI
SDGDDSQSLL PCRTFCEAAK EGCEPVLGMV NASWPEFLKC SQFHNQTEND TMERVCFSPY
QEKGKQSLCG GEESFLCASG ICIPGKLQCN GYNDCDDWSD EIHCNCSDDV FRCNTGKCLN
YTFVCDGYDD CGDLSDEQNC DCNPLTHHQC GDGRCITADW VCDGDHDCID KSDEINCSCH
SQGLVECKNG QCIPSAFQCD GDNDCKDGSD EENCSESQTL CQEGDQRCTS CPDTCGTSLC
EMKNSQINCS QCEPITLELC MNLPYNYTSY PNYLGHRTQK EASVSWESSL FPALVQTNCY
KYLMFFACTI LVPKCDPNTN HRIPPCRTLC VQSKERCESV LGIVGLQWPE DTDCTQFPDE
NSDNQTCLTP DEGVEECSPS HFKCRSGRCV LASRRCDGQA DCEDDSDEDS CGCGERGLWE
CPLKKMCIKH TMICDGFPDC PDMMDEKNCS FCEEHELECA NHECVPRELW CDGQADCSDS
SDEWDCVTLS KNMNSLMFLT IHRSAADNHV CADEWQENLS QLACNQMGLG GPPTTEIVLE
DEEIQHQKWL NLHPDWKNKN ASTLHALLVN GQICRSRSKV ALLCTKEDCG RRPAARMNKR
ILGGRTSRPG RWPWQCSLQS EPSGHICGCV LIAKRWVLTV AHCFEGRENA AVWKVVFGIS
NLDHPSSFMQ TRLVKTIILH PRYNRAVVDY DISIVELDED INETSYVRPV CLPSKEQLVQ
PDTYCYITGW GHMGNKMPFK LQEGEVRIIS LEQCQSYFDM KTITSRMLCA GYESGTVDSC
MGDSGGPLVC EQPAGRWTLF GLTSWGSVCF SKVLGPGVYS NVSHFIEWIE RQIYIHTFLL
N
//
