ID L8HYS1_9CETA Unreviewed; 576 AA.
AC L8HYS1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
DE Flags: Fragment;
GN ORFNames=M91_00463 {ECO:0000313|EMBL:ELR49345.1};
OS Bos mutus (wild yak).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=72004 {ECO:0000313|EMBL:ELR49345.1, ECO:0000313|Proteomes:UP000011080};
RN [1] {ECO:0000313|EMBL:ELR49345.1, ECO:0000313|Proteomes:UP000011080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yakQH1 {ECO:0000313|Proteomes:UP000011080};
RX PubMed=22751099; DOI=10.1038/ng.2343;
RA Qiu Q., Zhang G., Ma T., Qian W., Wang J., Ye Z., Cao C., Hu Q., Kim J.,
RA Larkin D.M., Auvil L., Capitanu B., Ma J., Lewin H.A., Qian X., Lang Y.,
RA Zhou R., Wang L., Wang K., Xia J., Liao S., Pan S., Lu X., Hou H., Wang Y.,
RA Zang X., Yin Y., Ma H., Zhang J., Wang Z., Zhang Y., Zhang D., Yonezawa T.,
RA Hasegawa M., Zhong Y., Liu W., Zhang Y., Huang Z., Zhang S., Long R.,
RA Yang H., Wang J., Lenstra J.A., Cooper D.N., Wu Y., Wang J., Shi P.,
RA Wang J., Liu J.;
RT "The yak genome and adaptation to life at high altitude.";
RL Nat. Genet. 44:946-949(2012).
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}.
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DR EMBL; JH882455; ELR49345.1; -; Genomic_DNA.
DR AlphaFoldDB; L8HYS1; -.
DR STRING; 72004.ENSBMUP00000033052; -.
DR MEROPS; M02.004; -.
DR Proteomes; UP000011080; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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; IEA:UniProtKB-KW.
DR GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06461; M2_ACE; 1.
DR Gene3D; 1.10.1370.30; -; 1.
DR InterPro; IPR001548; Peptidase_M2.
DR PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR PANTHER; PTHR10514:SF41; ANGIOTENSIN-CONVERTING ENZYME-LIKE PROTEIN ACE3; 1.
DR Pfam; PF01401; Peptidase_M2; 1.
DR PRINTS; PR00791; PEPDIPTASEA.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 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 Reference proteome {ECO:0000313|Proteomes:UP000011080};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|RuleBase:RU361144}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ELR49345.1"
FT NON_TER 576
FT /evidence="ECO:0000313|EMBL:ELR49345.1"
SQ SEQUENCE 576 AA; 67151 MW; 14BBFBDF7E7B8AB4 CRC64;
LPGQLTPISF SADQLYNETV AKAFLEFYER TAQVVWNQFM AAAWNYVTNI TKKNQEEMLY
KDVEKSQHTL YFGTRARMFK IANFQDSDVK RMLSKLLNVD KAALPKEELR EYNEILAYME
TTYSMAQVCL NEGPCLPLEP DLEEVMATSR DQKELLWAWQ GWRDAVGRQL RMTFERYVQL
SNKAAKLNGY QDMGALWRSK YESDTLQEDL EQLFQELQPL YLNLHAYVRR ALYRFYGPEL
IDLRGPIPAH VLGNMWAQSW VNILDLALPF PEKPPEDITK IMQGQHWKPE KMFQEAEKFF
TSMGLLSTPP EFWKNSMMER PTDGREVECH ASAWDFYNGK DFRIKKCTEV TIEDLLSIFH
QMGHIQYFLQ YKNLSVIFRA GANPAFEEAM GSVVTLSASS HKHLLNRGLL SQQHQDKEEE
VNFLMSVALE KIAFIPFAYL MDLFRWKVFD GTIEKDVYNQ EWWNLRLKYQ GLCPPIPRTE
EDFDPGAKFH ISASLPYIRY FLSLVLQFQF HEALCKASGH MGPLHRCDIY NSKEAGKLLE
DVLKLGSSKP WPEVLEKMTG ETKVSTKALM TYFKPL
//
