ID A0A091KMF5_9GRUI Unreviewed; 836 AA.
AC A0A091KMF5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Atrial natriuretic peptide-converting enzyme {ECO:0000313|EMBL:KFP40663.1};
DE Flags: Fragment;
GN ORFNames=N324_07529 {ECO:0000313|EMBL:KFP40663.1};
OS Chlamydotis macqueenii (Macqueen's bustard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Otididae; Chlamydotis.
OX NCBI_TaxID=187382 {ECO:0000313|EMBL:KFP40663.1, ECO:0000313|Proteomes:UP000053330};
RN [1] {ECO:0000313|EMBL:KFP40663.1, ECO:0000313|Proteomes:UP000053330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N324 {ECO:0000313|EMBL:KFP40663.1};
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:PRU00124}.
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DR EMBL; KK747393; KFP40663.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091KMF5; -.
DR Proteomes; UP000053330; 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 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; 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; 2.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000053330}.
FT DOMAIN 1..54
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 242..365
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 596..829
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 11..35
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 72..90
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 84..99
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 101..113
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 108..126
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 120..135
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 145..163
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 157..172
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 182..200
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 194..209
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 294..332
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 321..362
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 325..349
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 372..384
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 379..397
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 391..406
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 429..444
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 447..459
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 454..472
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 466..481
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP40663.1"
FT NON_TER 836
FT /evidence="ECO:0000313|EMBL:KFP40663.1"
SQ SEQUENCE 836 AA; 93949 MW; EBEE94F68D908760 CRC64;
SRGLLPCRTF CEAAKEGCEP VLGMVNASWP EFLKCSQFQN KTENDTTTRV CFSPHQEKGK
QSLCGGEESF LCASGICIPG KLQCNGYNDC DDWSDEVHCN CSDDVFRCNT GKCLNYTFVC
DGYDDCGDLS DEQNCDCNPV THHQCGDGRC ITADWVCDGD HDCIDKSDEI NCSCHSQGLV
ECRNGQCIPS AFQCDGDNDC KDGSDEENCS ESQTLCQEGD QRCTSCPDPC GTSLCEMRNS
QTNCSQCEPI TLELCMNLPY NYTYYPNYLG HRTQKEASIS WESSLFPALV QTNCYKYLMF
FACTILVPKC DPHTNQRIPP CRTLCVQSKE RCESVLGIVG LQWPEDTDCT QFPDENSDNQ
TCLTPDEDVE ECSPSHFKCR SGRCVLASRR CDGQADCEDD SDEDSCGCRE RGLWECPLKK
LCIKHTMICD GFPDCPDMMD EKNCSFCEES ELECANHECV PREHWCDGQA DCSDSSDEWD
CVTLSKNMNS LMLLTIHRSA ADNHVCADEW QEDLSQLACN QMGLGGPSKT EIVIENEEMH
HQKWLNLHSD WKNKNASTLH ALLVNGQMCR SRSKVALLCT KEDCGRRPAA RMNKRILGGR
TSRPGRWPWQ CSLQSEPSGH ICGCVLIAKR WVLTVAHCFE GRENAAVWKV VFGISNLDHP
SSFMQTRLVK TIILHPRYNR AVVDYDISIV ELNKDINETS YVRPVCLPSK DQLVRPDTYC
YITGWGHMGN KMPFKLQEGE VRIISLEQCQ SYFDMKTITS RMLCAGYESG TVDSCMGDSG
GPLVCEQPAG RWTLFGLTSW GSVCFSKVLG PGVYSNVSHF IEWIERQIYI HTFLLN
//
