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Database: UniProt
Entry: A0A091RAJ6_MERNU
LinkDB: A0A091RAJ6_MERNU
Original site: A0A091RAJ6_MERNU 
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
//
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