ID A0A091RAJ6_MERNU Unreviewed; 580 AA.
AC A0A091RAJ6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Atrial natriuretic peptide-converting enzyme {ECO:0000313|EMBL:KFQ35939.1};
DE Flags: Fragment;
GN ORFNames=N331_02307 {ECO:0000313|EMBL:KFQ35939.1};
OS Merops nubicus (Northern carmine bee-eater).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Meropidae; Merops.
OX NCBI_TaxID=57421 {ECO:0000313|EMBL:KFQ35939.1, ECO:0000313|Proteomes:UP000052967};
RN [1] {ECO:0000313|EMBL:KFQ35939.1, ECO:0000313|Proteomes:UP000052967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N331 {ECO:0000313|EMBL:KFQ35939.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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:PRU00196}.
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DR EMBL; KK715207; KFQ35939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091RAJ6; -.
DR Proteomes; UP000052967; 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:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00112; LDLa; 6.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 7.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
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; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24270:SF2; ATRIAL NATRIURETIC PEPTIDE-CONVERTING ENZYME; 1.
DR PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR Pfam; PF01392; Fz; 1.
DR Pfam; PF00057; Ldl_recept_a; 7.
DR Pfam; PF15494; SRCR_2; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00192; LDLa; 7.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
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; 1.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 7.
DR PROSITE; PS50287; SRCR_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW Protease {ECO:0000256|ARBA:ARBA00022825};
KW Reference proteome {ECO:0000313|Proteomes:UP000052967};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 181..304
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 444..562
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 535..580
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 11..29
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 23..38
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 40..52
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 47..65
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 59..74
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 84..102
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 96..111
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 121..139
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 133..148
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 233..271
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 260..301
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 264..288
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 311..323
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 318..336
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 330..345
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 368..383
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 386..398
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 393..411
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 405..420
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ35939.1"
FT NON_TER 580
FT /evidence="ECO:0000313|EMBL:KFQ35939.1"
SQ SEQUENCE 580 AA; 64922 MW; 1426E053185CE79C CRC64;
ALCGGEESFL CASGICIPGK LQCNGYNDCD DWSDEVHCNC SDDVFRCNTG KCLNYTFVCD
GYDDCGDLSD EQNCDCNPVT HHQCGDGRCI TADWVCDGDH DCTDKSDEIN CSCHSQGLVE
CRNGQCIPSA FQCDGDNDCK DGSDEENCSE SQTLCQEGDQ RCTSCPELCG NSLCDMRNSQ
TNCSQCEPIT LELCMNLPYN YTYYPNYLGH RTQKEASISW ESSLFPALVQ TNCYKYLMFF
ACTILVPKCD PHTNQRIPPC RTLCVQSKER CESVLGIVGL QWPEDTDCTQ FPDENSDNQT
CLTPDEDVEE CSPSHFKCRS GRCVLASRRC DGQADCEDDS DEDSCGCRER GLWECPLKKL
CIKHTMICDG FPDCPDMMDE KNCSFCEENE LECANHECVL RELWCDGQAD CSDSSDEWDC
VTLSKNMNSL TFLTIHRSAA DNHVCADEWQ ENLSRLACNQ MGLGGPSKTE IVIENEETQH
QKWLNLQSDW KNKNASTLHA LLVDGQMCRS RSKVALICTK EDCGRRPAAR MAKRILGGRT
SRPGRWPWQC SLQSEPSGHI CGCVLIAKRW VLTVAHCFEG
//