ID A0A195ETY3_9HYME Unreviewed; 938 AA.
AC A0A195ETY3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Atrial natriuretic peptide-converting enzyme {ECO:0000313|EMBL:KYN31367.1};
GN ORFNames=ALC56_14248 {ECO:0000313|EMBL:KYN31367.1};
OS Trachymyrmex septentrionalis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=34720 {ECO:0000313|EMBL:KYN31367.1, ECO:0000313|Proteomes:UP000078541};
RN [1] {ECO:0000313|EMBL:KYN31367.1, ECO:0000313|Proteomes:UP000078541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN31367.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN31367.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex septentrionalis WGS genome.";
RL Submitted (MAR-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:PRU00196}.
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DR EMBL; KQ981979; KYN31367.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A195ETY3; -.
DR STRING; 34720.A0A195ETY3; -.
DR Proteomes; UP000078541; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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:UniProtKB-KW.
DR CDD; cd07066; CRD_FZ; 1.
DR CDD; cd00112; LDLa; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
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; IPR001314; Peptidase_S1A.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF7; HYALIN; 1.
DR Pfam; PF01392; Fz; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00192; LDLa; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 2.
DR SUPFAM; SSF56487; SRCR-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 2.
DR PROSITE; PS50287; SRCR_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000078541};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 259..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 312..441
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 557..603
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 673..925
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 114..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 462..480
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 474..489
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 529..547
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 541..556
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 938 AA; 105547 MW; 22503DBA0CFA11D9 CRC64;
MALPRREIFQ KDELKYATIL TSGRERRSKF EELQAASKNL ERRLHEDDDY CRRQEMDRRI
NKDKPPRYED LEGIPHDLDK RYHGEQRSLE QQQQHSIMRS KYESDMERAR NILQHNLRKE
RTGNEKLEKL PKATQTNLPP PLSAICQSPV PKPISVRQDS NVSSDSFSQT SSPSYTSKTM
EAPLLPHKHG KVPDRALVSE PDNSSGRPIT KSTSTPASLQ TIVRMHAGNN SSLHHKIIRD
MTGSHYVTTG RLRFRFVQVL LNAVVLLAIA GGLAAYFKTY PENDFKLENR TIYTAVIPIP
ESTRFVIEDK NPAPGVCLPI IVTFCQQHKV PYNYTVFPNY MGNFGQREAQ HELELYDAVV
DVRCYELAAL FLCSVFVPKC GSRGRVVRPC RSLCFRIFSK SISETKRRCG FFLKVFGLSL
PDYLECELFP ENPSSDECIG HHEVIEAARR AEKPVCTSGF QCDGTRCIPF DWRCDGHLDC
SDHSDEIGCG NCNSTTSSSE PVSSAFGQIV LSKGSSTKST LSTKSSLHCG ERRCMSASHI
CDGVMDCPWG QDERYCLKLS HRNGDVGEGR LEVYHAEMGK FMPACVSHWE PTTSPQEVCA
MLGYKGTVSN GTKLMNDSLS IVLSSEYRNK NLLKQFQGCI KDREPYPMVK LTCVDYACGR
RRSVYGNVRV KRIVGGVESA PGDWPFLAAL LGGPEQIFYC AGVLIADQWV LTASHCVGNH
SEVSGWTIQL GITRRLSHTY LGQKLKVKRV IPHPYYNLGV AHDNDVALFQ LEKRVQYHEH
LRPVCLPTAD TNLTPDTNCT VIGWGKKNDT DFQLLSHRLL SASEYEPAVN EVVVPILPRH
LCNSWLAYKE LNVTDGMICA GYADGGKDAC QGDSGGPLLC QDKEDKDRWF VGGIVSWGIK
CAHPKLPGVY AYVPKYVTWI QKEMSKYSEY NSRSNGKM
//
