ID A0A194QVR2_PAPMA Unreviewed; 721 AA.
AC A0A194QVR2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Inactive angiotensin-converting enzyme-related protein {ECO:0000313|EMBL:KPJ07651.1};
GN ORFNames=RR48_11207 {ECO:0000313|EMBL:KPJ07651.1};
OS Papilio machaon (Old World swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=76193 {ECO:0000313|EMBL:KPJ07651.1, ECO:0000313|Proteomes:UP000053240};
RN [1] {ECO:0000313|EMBL:KPJ07651.1, ECO:0000313|Proteomes:UP000053240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ07651.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPJ07651.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
CC -!- SIMILARITY: Belongs to the peptidase M2 family.
CC {ECO:0000256|ARBA:ARBA00008139}.
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DR EMBL; KQ461181; KPJ07651.1; -; Genomic_DNA.
DR RefSeq; XP_014368466.1; XM_014512980.1.
DR AlphaFoldDB; A0A194QVR2; -.
DR GeneID; 106718792; -.
DR KEGG; pmac:106718792; -.
DR InParanoid; A0A194QVR2; -.
DR OrthoDB; 3671409at2759; -.
DR Proteomes; UP000053240; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR InterPro; IPR001548; Peptidase_M2.
DR PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR PANTHER; PTHR10514:SF27; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR Pfam; PF01401; Peptidase_M2; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053240};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..721
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008264661"
FT TRANSMEM 681..701
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 583..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 721 AA; 82752 MW; 4FB387549CCE4496 CRC64;
MRASFTLFSV CLYALLSSGT SSGDDRRWLM SLVDLVELDY EDNCEQRATA SWNELIGAPK
GLAKKLERDK AFGILSRQQT AEVKSAVSPK ALASDDLLKR RVKLLLQPGD TLLEPEQWIR
LVTFGNTALH KLRFATDYYC GTQTNCTLRE LNRNMAKQHD EDVLLRMKNS WEQKLPNQKE
YLEHILPLLR NASKENGYKT VEEYWDSLAE YEGALLKVRE IWDYINPLYV KLHKYIALKL
KGADAVGKPL PVHLLKSLNG DDWSNIIENL LPERADIYQK LHVHLRLQEY GGLKAFKQAE
NLLKFLEIGE IEPEIFAESY FNGSCPTSIV DSCKPNKLRF VTCGDISLVN YIEAHEAVTK
LKYKITSALH SNNTYVLREA TRYSAIYEAI PGFISLLSLN PHTLDRAKLY PLERFNYNPN
YHRLVLQLII ALRDLPKLNY YIAADEWRLK VLTGTIPSSK VAASWKEFRA NFSMLETSDK
DILGDSYVLF NKPFVGKFMG IILKYQIYQS FAEELISDDY DLVKHVMEKN ERLIEPMIRG
FSAKWPEMVS DLLAKRENSL EYTGLTDYFR LLDEYLDNQL DPSTDSNDIA EYVDPPETDV
SQERVPDEND IPINQNNIDL KQIPVDTNGN IMDNVIDTGG DNHNKFSFET STVGVLEIKN
PVATGEHNEE TRPKEASYNT YWWIGISVAL VVIIALVAII ARKRHSHRKQ LERQRRENTV
A
//