GenomeNet

Database: UniProt/TrEMBL
Entry: F1NYM0_CHICK
LinkDB: F1NYM0_CHICK
Original site: F1NYM0_CHICK 
ID   F1NYM0_CHICK            Unreviewed;      1281 AA.
AC   F1NYM0; J7GZN9;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 2.
DT   25-APR-2018, entry version 59.
DE   RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
GN   Name=ACE {ECO:0000313|EMBL:AFP83450.1,
GN   ECO:0000313|Ensembl:ENSGALP00000039731};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00000039731, ECO:0000313|Proteomes:UP000000539};
RN   [1] {ECO:0000313|Ensembl:ENSGALP00000039731, ECO:0000313|Proteomes:UP000000539}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000039731,
RC   ECO:0000313|Proteomes:UP000000539};
RX   PubMed=15592404; DOI=10.1038/nature03154;
RG   International Chicken Genome Sequencing Consortium;
RA   Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C.,
RA   Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E.,
RA   Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W.,
RA   Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A., Kremitzki C.,
RA   Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E.,
RA   Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J.,
RA   Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M.,
RA   Paton B., Smith J., Morrice D., Daniels L., Tempest H.G.,
RA   Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V.,
RA   Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J.,
RA   van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J.,
RA   Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H.,
RA   Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA   Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA   Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA   Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S.,
RA   Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J.,
RA   Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H.,
RA   Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C.,
RA   Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C.,
RA   Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P.,
RA   King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S.,
RA   Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S.,
RA   Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S.,
RA   Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z.,
RA   Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J.,
RA   Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z.,
RA   Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA   Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA   Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J.,
RA   Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G.,
RA   Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D.,
RA   Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G.,
RA   Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A.,
RA   Mardis E.R., Wilson R.K.;
RT   "Sequence and comparative analysis of the chicken genome provide
RT   unique perspectives on vertebrate evolution.";
RL   Nature 432:695-716(2004).
RN   [2] {ECO:0000313|Ensembl:ENSGALP00000039731}
RP   IDENTIFICATION.
RC   STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000039731};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:AFP83450.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Peng J., Zhang H.;
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361144};
CC       Note=Binds 2 Zn(2+) ions per subunit.
CC       {ECO:0000256|RuleBase:RU361144};
CC   -!- SIMILARITY: Belongs to the peptidase M2 family.
CC       {ECO:0000256|RuleBase:RU361144}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AADN04000381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; JX218994; AFP83450.1; -; mRNA.
DR   RefSeq; NP_001161204.1; NM_001167732.1.
DR   UniGene; Gga.3781; -.
DR   Ensembl; ENSGALT00000040528; ENSGALP00000039731; ENSGALG00000000498.
DR   GeneID; 419953; -.
DR   KEGG; gga:419953; -.
DR   CTD; 1636; -.
DR   eggNOG; KOG3690; Eukaryota.
DR   eggNOG; ENOG410XPJ3; LUCA.
DR   GeneTree; ENSGT00520000055576; -.
DR   KO; K01283; -.
DR   OMA; VTMEQLF; -.
DR   OrthoDB; EOG091G033S; -.
DR   TreeFam; TF312861; -.
DR   Reactome; R-GGA-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR   Proteomes; UP000000539; Chromosome 27.
DR   Bgee; ENSGALG00000000498; -.
DR   GO; GO:0005768; C:endosome; ISA:AgBase.
DR   GO; GO:0009897; C:external side of plasma membrane; ISA:AgBase.
DR   GO; GO:0070062; C:extracellular exosome; ISA:AgBase.
DR   GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR   GO; GO:0016021; C:integral component of membrane; IDA:AgBase.
DR   GO; GO:0005764; C:lysosome; ISA:AgBase.
DR   GO; GO:0005886; C:plasma membrane; ISA:AgBase.
DR   GO; GO:0003779; F:actin binding; ISS:AgBase.
DR   GO; GO:0031711; F:bradykinin receptor binding; ISA:AgBase.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031404; F:chloride ion binding; ISA:AgBase.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:AgBase.
DR   GO; GO:0008144; F:drug binding; ISA:AgBase.
DR   GO; GO:0004175; F:endopeptidase activity; ISA:AgBase.
DR   GO; GO:0008238; F:exopeptidase activity; ISA:AgBase.
DR   GO; GO:0070573; F:metallodipeptidase activity; ISS:AgBase.
DR   GO; GO:0008237; F:metallopeptidase activity; ISA:AgBase.
DR   GO; GO:0051019; F:mitogen-activated protein kinase binding; ISA:AgBase.
DR   GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; ISA:AgBase.
DR   GO; GO:0008241; F:peptidyl-dipeptidase activity; ISA:AgBase.
DR   GO; GO:0008240; F:tripeptidyl-peptidase activity; ISA:AgBase.
DR   GO; GO:0008270; F:zinc ion binding; ISA:AgBase.
DR   GO; GO:0050435; P:amyloid-beta metabolic process; ISA:AgBase.
DR   GO; GO:0050482; P:arachidonic acid secretion; ISA:AgBase.
DR   GO; GO:0008283; P:cell proliferation; IMP:AgBase.
DR   GO; GO:0042447; P:hormone catabolic process; ISA:AgBase.
DR   GO; GO:0001822; P:kidney development; ISA:AgBase.
DR   GO; GO:0043171; P:peptide catabolic process; ISA:AgBase.
DR   GO; GO:0060319; P:primitive erythrocyte differentiation; IMP:AgBase.
DR   GO; GO:0060177; P:regulation of angiotensin metabolic process; ISA:AgBase.
DR   GO; GO:0003081; P:regulation of systemic arterial blood pressure by renin-angiotensin; ISA:AgBase.
DR   CDD; cd06461; M2_ACE; 2.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; PTHR10514; 2.
DR   Pfam; PF01401; Peptidase_M2; 2.
DR   PRINTS; PR00791; PEPDIPTASEA.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase {ECO:0000256|RuleBase:RU361144};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000539};
KW   Glycoprotein {ECO:0000256|RuleBase:RU361144};
KW   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:UP000000539};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU361144}.
FT   SIGNAL        1     17       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        18   1281       Angiotensin-converting enzyme.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5014303362.
SQ   SEQUENCE   1281 AA;  147239 MW;  8D601B3C85D0A709 CRC64;
     MPAALGLLLP WLSLVGALQP GLEPPQSDPT EAGAVFFASE YNSTAEIVLF RSVSASWEYN
     TNLTTANAAL QVEASLEEQN FTELWGKKAK ELYGNIWSNF SDPQLKKIIG SIQTLGPSNL
     PLDKRQQYNT ILSDMDKIYS TAKVCLDNGT CWDLEPDISD IMATSRSYKK LLYAWEGWHN
     AAGNPLRAKY QEFVTLSNEA YQMDGFEDTG SYWRSWYDST TFEDDLEHLY NQLEPLYLNL
     HAFVRRKLYD RYGPKYINLK GPIPAHLLGN MWAQQWNNIY DLMVPYPDKP NLDVTNTMVN
     QGWNATHMFR VSEEFFTSLG LLEMPPEFWE KSMLEKPADG REVVCHASAW DFYNRKDFRI
     KQCTTVTMEQ LFTVHHEMGH VQYYLQYKDQ PVSFRGGANP GFHEAIGDVL SLSVSTPSHL
     QKIGLLSSAV EDEESNINYL LKMALEKIAF LPFGYLIDQW RWNVFSGRTP PSRYNYDWWY
     LRTKYQGICA PVSRNESNFD PGAKYHIPGN TPYIRYFVSF ILQFQFHKAL CQAANHTGPL
     HTCDIYMSKE AGAKLREVLK AGSSKSWQEI LFNLTGTDKM DAGALLEYFS PVTTWLQEQN
     NKTNEVLGWP EFDWRPPIPE GYPEGIDKIV DEAQAKEFLS EYNSTAEVVW NAYTEASWEY
     NTNITDHNKE VMLEKNLAMS KHTIEYGMRA RQFDPSDFQD ETVTRILNKL SVLERAALPE
     DELKEYNTLL SDMETTYSVA KVCRENNTCH PLDPDLTDIL ATSRDYNELL FAWKGWRDAS
     GAKIKDKYKR YVELSNKAAV LNGYTDNGAY WRSLYETPTF EEDLERLYLQ LQPLYLNLHA
     YVRRALYNKY GAEHISLKGP IPAHLLGNMW AQSWSNIFDL VMPFPDATKV DATPAMKQQG
     WTPKMMFEES DRFFTSLGLI PMPQEFWDKS MIEKPADGRE VVCHASAWDF YNRKDFRIKQ
     CTVVNMDDLI TVHHEMGHVQ YFLQYMDQPI SFRDGANPGF HEAIGDVMAL SVSTPKHLHS
     INLLDQVTEN EESDINYLMS IALDKIAFLP FGYLMDQWRW KVFDGRIKED EYNQQWWNLR
     LKYQGLCPPV PRSEDDFDPG AKFHIPANVP YIRYFVSFVI QFQFHQALCK AAGHTGPLHT
     CDIYQSKEAG KLLGDAMKLG FSKPWPEAMQ LITGQPNMSA EALMSYFEPL MTWLVKKNTE
     NGEVLGWPEY SWTPYAVTEF HAATDTADFL GMSVGTKQAT AGAWVLLALA LVFLITSIFL
     GVKLFSSRRK AFKSSSEMEL K
//
DBGET integrated database retrieval system