ID   ACE_RABIT      STANDARD;      PRT;  1310 AA.
AC   P12822; O02852;
DT   01-OCT-1989 (Rel. 12, Created)
DT   01-NOV-1997 (Rel. 35, Last sequence update)
DT   15-JUN-2002 (Rel. 41, Last annotation update)
DE   Angiotensin-converting enzyme, somatic isoform precursor (EC 3.4.15.1)
DE   (ACE) (Dipeptidyl carboxypeptidase I) (Kininase II).
GN   DCP1 OR ACE.
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=Lung;
RX   MEDLINE=92178960; PubMed=1311831;
RA   Thekkumkara T.J., Livingston W. III, Kumar R.S., Sen G.C.;
RT   "Use of alternative polyadenylation sites for tissue-specific
RT   transcription of two angiotensin-converting enzyme mRNAs.";
RL   Nucleic Acids Res. 20:683-687(1992).
RN   [2]
RP   REVISIONS.
RA   Sen G.C.;
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   SEQUENCE OF 1-88 FROM N.A.
RC   TISSUE=Liver;
RX   MEDLINE=91139683; PubMed=1847388;
RA   Kumar R.S., Thekkumkara T.J., Sen G.C.;
RT   "The mRNAs encoding the two angiotensin-converting isozymes are
RT   transcribed from the same gene by a tissue-specific choice of
RT   alternative transcription initiation sites.";
RL   J. Biol. Chem. 266:3854-3862(1991).
RN   [4]
RP   SEQUENCE OF 34-55.
RC   TISSUE=Lung;
RX   MEDLINE=84051289; PubMed=6314908;
RA   Iwata K., Blacher R., Soffer R.L., Lai C.Y.;
RT   "Rabbit pulmonary angiotensin-converting enzyme: the NH2-terminal
RT   fragment with enzymatic activity and its formation from the native
RT   enzyme by NH4OH treatment.";
RL   Arch. Biochem. Biophys. 227:188-201(1983).
CC   -!- FUNCTION: CONVERTS ANGIOTENSIN I TO ANGIOTENSIN II BY RELEASE OF
CC       THE TERMINAL HIS-LEU, THIS RESULTS IN AN INCREASE OF THE
CC       VASOCONSTRICTOR ACTIVITY OF ANGIOTENSIN.
CC   -!- CATALYTIC ACTIVITY: Release of a C-terminal dipeptide,
CC       oligopeptide-|-Xaa-Xbb, when Xaa is not Pro, and Xbb is neither
CC       Asp nor Glu. Converts angiotensin I to angiotensin II.
CC   -!- COFACTOR: BINDS 2 ZINC IONS (BY SIMILARITY).
CC   -!- SUBCELLULAR LOCATION: Type I membrane protein.
CC   -!- ALTERNATIVE PRODUCTS: 2 isoforms; somatic (shown here) and testis-
CC       specific (AC P22968); are produced by alternative splicing.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY M2.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; X62551; CAA44428.1; -.
DR   EMBL; M58579; AAA31151.1; ALT_SEQ.
DR   PIR; A23455; A23455.
DR   PIR; S35484; S35484.
DR   MEROPS; M02.001; -.
DR   MEROPS; M02.004; -.
DR   InterPro; IPR001548; Peptidase_M2.
DR   InterPro; IPR000130; Zn_MTpeptdse.
DR   Pfam; PF01401; Peptidase_M2; 2.
DR   PRINTS; PR00791; PEPDIPTASEA.
DR   ProDom; PD004184; Peptidase_M2; 2.
DR   PROSITE; PS00142; ZINC_PROTEASE; 2.
KW   Hydrolase; Metalloprotease; Carboxypeptidase; Zinc; Dipeptidase;
KW   Glycoprotein; Transmembrane; Repeat; Signal; Alternative splicing.
FT   SIGNAL        1     33
FT   CHAIN        34   1310       ANGIOTENSIN-CONVERTING ENZYME, SOMATIC
FT                                ISOFORM.
FT   DOMAIN       34   1263       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM   1264   1280       POTENTIAL.
FT   DOMAIN     1281   1310       CYTOPLASMIC (POTENTIAL).
FT   REPEAT      232    588
FT   REPEAT      829   1185
FT   METAL       395    395       ZINC 1 (CATALYTIC) (BY SIMILARITY).
FT   ACT_SITE    396    396       1 (BY SIMILARITY).
FT   METAL       399    399       ZINC 1 (CATALYTIC) (BY SIMILARITY).
FT   METAL       992    992       ZINC 2 (CATALYTIC) (BY SIMILARITY).
FT   ACT_SITE    993    993       2 (BY SIMILARITY).
FT   METAL       996    996       ZINC 2 (CATALYTIC) (BY SIMILARITY).
FT   CARBOHYD     59     59       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD     79     79       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    151    151       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    323    323       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    449    449       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    513    513       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    681    681       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    699    699       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    718    718       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    946    946       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD   1195   1195       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CONFLICT     48     48       E -> N (IN REF. 4).
SQ   SEQUENCE   1310 AA;  150405 MW;  04777FAB17981DEA CRC64;
     MGAAPGRRGP RLLRPPPPLL LLLLLLRPPP AALTLDPGLL PGDFAADEAG ARLFASSYNS
     SAEQVLFRST AASWAHDTNI TAENARRQEE EALLSQEFAE AWGKKAKELY DPVWQNFTDP
     ELRRIIGAVR TLGPANLPLA KRQQYNSLLS NMSQIYSTGK VCFPNKTASC WSLDPDLNNI
     LASSRSYAML LFAWEGWHNA VGIPLKPLYQ EFTALSNEAY RQDGFSDTGA YWRSWYDSPT
     FEEDLERIYH QLEPLYLNLH AYVRRVLHRR YGDRYINLRG PIPAHLLGNM WAQSWESIYD
     MVVPFPDKPN LDVTSTMVQK GWNATHMFRV AEEFFTSLGL LPMPPEFWAE SMLEKPEDGR
     EVVCHASAWD FYNRKDFRIK QCTQVTMDQL STVHHEMGHV QYYLQYKDQP VSLRRANPGF
     HEAIGDVLAL SVSTPAHLHK IGLLDHVTND TESDINYLLK MALEKIAFLP FGYLVDQWRW
     GVFSGRTPSS RYNFDWWYLR TKYQGICPPV VRNETHFDAG AKFHIPSVTP YIRYFVSFVL
     QFQFHQALCM EAGHQGPLHQ CDIYQSTRAG AKLRAVLQAG CSRPWQEVLK DMVASDALDA
     QPLLDYFQPV TQWLQEQNER NGEVLGWPEY QWRPPLPNNY PEGIDLVTDE AEASRFVEEY
     DRSFQAVWNE YAEANWNYNT NITTEASKIL LQKNMQIANH TLTYGNWARR FDVSNFQNAT
     SKRIIKKVQD LQRAVLPVKE LEEYNQILLD METIYSVANV CRVDGSCLQL EPDLTNLMAT
     SRKYDELLWV WTSWRDKVGR AILPYFPKYV EFTNKAARLN GYVDAGDSWR SMYETPTLEQ
     DLERLFQELQ PLYLNLHAYV GRALHRHYGA QHINLEGPIP AHLLGNMWAQ TWSNIYDLVA
     PFPSASTMDA TEAMIKQGWT PRRMFEEADK FFISLGLLPV PPEFWNKSML EKPTDGREVV
     CHASAWDFYN GKDFRIKQCT TVNMEDLVVV HHEMGHIQYF MQYKDLPVAL REGANPGFHE
     AIGDVLALSV STPKHLHSIN LLSSEGGGYE HDINFLMKMA LDKIAFIPFS YLVDEWRWRV
     FDGSITKENY NQEWWSLRLK YQGLCPPAPR SQGDFDPGAK FHIPSSVPYI RYFVSFIIQF
     QFHEALCKAA GHTGPLHTCD IYQSKEAGKR LADAMKLGYS KPWPEAMKVI TGQPNMSASA
     MMNYFKPLMD WLLTENGRHG EKLGWPQYTW TPNSARSEGS LPDSGRVNFL GMNLDAQQAR
     VGQWVLLFLG VALLLASLGL TQRLFSIRYQ SLRQPHHGPQ FGSEVELRHS
//