ID C3XRM5_BRAFL Unreviewed; 685 AA.
AC C3XRM5;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
GN ORFNames=BRAFLDRAFT_68301 {ECO:0000313|EMBL:EEN69343.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN69343.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN69343.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN69343.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361144};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU361144};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000256|ARBA:ARBA00001923};
CC -!- SIMILARITY: Belongs to the peptidase M2 family.
CC {ECO:0000256|ARBA:ARBA00008139, ECO:0000256|RuleBase:RU361144}.
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; GG666456; EEN69343.1; -; Genomic_DNA.
DR RefSeq; XP_002613334.1; XM_002613288.1.
DR AlphaFoldDB; C3XRM5; -.
DR MEROPS; M02.004; -.
DR eggNOG; KOG3690; Eukaryota.
DR InParanoid; C3XRM5; -.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
DR GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 1.
DR CDD; cd06461; M2_ACE; 1.
DR Gene3D; 1.10.1370.30; -; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
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 PRINTS; PR00791; PEPDIPTASEA.
DR SMART; SM00192; LDLa; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|RuleBase:RU361144};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW ECO:0000256|RuleBase:RU361144}; Hydrolase {ECO:0000256|RuleBase:RU361144};
KW Metal-binding {ECO:0000256|RuleBase:RU361144};
KW Metalloprotease {ECO:0000256|RuleBase:RU361144};
KW Protease {ECO:0000256|RuleBase:RU361144};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|RuleBase:RU361144}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..685
FT /note="Angiotensin-converting enzyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002933047"
SQ SEQUENCE 685 AA; 78333 MW; 652665F410633545 CRC64;
MARFILHLSI VVVVLFSVPT HCQKKNESEG VIFLEEYDTL AKELQNRAVI AGWNYQTNLT
DENAKKQVEL NLEVAKFAKE AATNASEYDW ENFSNVTVKR LFSMITTLGT AALEDEEKLE
QLNNLLSEME EIYSTGQACE YDDPKTCLDL NPGLEDCMAD STDYNRLLFC WEGWRDAAGR
RLGDLYSQFV ELSNEAVRAD GWNDTGEYWR SWYETADLQQ QLETIYQDLQ PLYQNLHAYV
RRKLINTYGA EMVNAEGPIP AHLLGNMWAQ TWGNIYNLVI PFPDKPSIDV TDEMVRQGYD
ALRMFNLSDE FFREMGQIPM PDSFWDRTMF VRPDDRDVVC HASAWDFYLD NDVRIKMCTK
VNQEDLVTVH HEMGHIEYFL QYAHQPLPFR EGANPGFHEA VGDLLALSVS TPAHLNKVGL
LPELVDDPEV DINFLMQMAL EKIAFLPFGY LIDQWRWRVF DGSTTKDKYN EEWWKLRTQY
QGIVPPVPRN PDKDFDAGSK YHVPANTPYI RYFVSFVIQF QFHEAMCTLS GYTGDLHKCD
ASAGAMKDVA GSRLAEMLRM GKSQPWPEAF EVLTGDREMS AAAILQYFAP LIDWLEKQNE
NETLGWNNGW TPPYDCEGTG GFTCLDGSRC VRPADKCDGI QDCDDNSDED PILCETPNDD
SPRMTSSLVV VFLAVLASTV MTSRN
//
